data_9BMH
# 
_entry.id   9BMH 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9BMH         pdb_00009bmh 10.2210/pdb9bmh/pdb 
WWPDB D_1000283526 ?            ?                   
EMDB  EMD-44699    ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1  'Structure model' 1 0 2025-04-23 ? 
2  'EM metadata'     1 0 2025-04-23 ? 
3  'Additional map'  1 0 2025-04-23 1 
4  FSC               1 0 2025-04-23 ? 
5  'Half map'        1 0 2025-04-23 1 
6  'Half map'        1 0 2025-04-23 2 
7  Image             1 0 2025-04-23 ? 
8  Mask              1 0 2025-04-23 1 
9  'Primary map'     1 0 2025-04-23 ? 
10 'Structure model' 1 1 2025-04-30 ? 
# 
loop_
_pdbx_audit_revision_details.ordinal 
_pdbx_audit_revision_details.revision_ordinal 
_pdbx_audit_revision_details.data_content_type 
_pdbx_audit_revision_details.provider 
_pdbx_audit_revision_details.type 
_pdbx_audit_revision_details.description 
_pdbx_audit_revision_details.details 
1 1 'Structure model' repository 'Initial release' ? ? 
2 2 'EM metadata'     repository 'Initial release' ? ? 
3 3 'Additional map'  repository 'Initial release' ? ? 
4 4 FSC               repository 'Initial release' ? ? 
5 5 'Half map'        repository 'Initial release' ? ? 
6 6 'Half map'        repository 'Initial release' ? ? 
7 7 Image             repository 'Initial release' ? ? 
8 8 Mask              repository 'Initial release' ? ? 
9 9 'Primary map'     repository 'Initial release' ? ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 10 'Structure model' 'Data collection'     
2 10 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 10 'Structure model' citation        
2 10 'Structure model' citation_author 
3 10 'Structure model' em_admin        
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 10 'Structure model' '_citation.country'                 
2 10 'Structure model' '_citation.journal_abbrev'          
3 10 'Structure model' '_citation.journal_id_CSD'          
4 10 'Structure model' '_citation.journal_id_ISSN'         
5 10 'Structure model' '_citation.pdbx_database_id_DOI'    
6 10 'Structure model' '_citation.pdbx_database_id_PubMed' 
7 10 'Structure model' '_citation.title'                   
8 10 'Structure model' '_citation.year'                    
9 10 'Structure model' '_em_admin.last_update'             
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9BMH 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-02 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        'State-4 of motor domain from full-length human dynein-1 in 5mM ATPVi' 
_pdbx_database_related.db_id          EMD-44699 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              jack.zhang@yale.edu 
_pdbx_contact_author.name_first         Jack 
_pdbx_contact_author.name_last          Zhang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8617-2855 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Chai, P.'  1 0000-0001-9702-978X 
'Zhang, K.' 2 0000-0001-8617-2855 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Nat.Struct.Mol.Biol. 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1545-9985 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'The mechanochemical cycle of reactive full-length human dynein 1.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41594-025-01543-3 
_citation.pdbx_database_id_PubMed   40263469 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Chai, P.'       1 0000-0001-9702-978X 
primary 'Yang, J.'       2 ?                   
primary 'Geohring, I.C.' 3 ?                   
primary 'Markus, S.M.'   4 0000-0002-3098-0236 
primary 'Wang, Y.'       5 0000-0002-8020-3937 
primary 'Zhang, K.'      6 0000-0001-8617-2855 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Cytoplasmic dynein 1 heavy chain 1' 533083.250 1 ? ? ? ? 
2 non-polymer syn 'ADP ORTHOVANADATE'                  544.156    1 ? ? ? ? 
3 non-polymer syn "ADENOSINE-5'-TRIPHOSPHATE"          507.181    1 ? ? ? ? 
4 non-polymer syn "ADENOSINE-5'-DIPHOSPHATE"           427.201    2 ? ? ? ? 
5 non-polymer syn 'MAGNESIUM ION'                      24.305     2 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Cytoplasmic dynein heavy chain 1,Dynein heavy chain,cytosolic' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MSEPGGGGGEDGSAGLEVSAVQNVADVSVLQKHLRKLVPLLLEDGGEAPAALEAALEEKSALEQMRKFLSDPQVHTVLVE
RSTLKEDVGDEGEEEKEFISYNINIDIHYGVKSNSLAFIKRTPVIDADKPVSSQLRVLTLSEDSPYETLHSFISNAVAPF
FKSYIRESGKADRDGDKMAPSVEKKIAELEMGLLHLQQNIEIPEISLPIHPMITNVAKQCYERGEKPKVTDFGDKVEDPT
FLNQLQSGVNRWIREIQKVTKLDRDPASGTALQEISFWLNLERALYRIQEKRESPEVLLTLDILKHGKRFHATVSFDTDT
GLKQALETVNDYNPLMKDFPLNDLLSATELDKIRQALVAIFTHLRKIRNTKYPIQRALRLVEAISRDLSSQLLKVLGTRK
LMHVAYEEFEKVMVACFEVFQTWDDEYEKLQVLLRDIVKRKREENLKMVWRINPAHRKLQARLDQMRKFRRQHEQLRAVI
VRVLRPQVTAVAQQNQGEVPEPQDMKVAEVLFDAADANAIEEVNLAYENVKEVDGLDVSKEGTEAWEAAMKRYDERIDRV
ETRITARLRDQLGTAKNANEMFRIFSRFNALFVRPHIRGAIREYQTQLIQRVKDDIESLHDKFKVQYPQSQACKMSHVRD
LPPVSGSIIWAKQIDRQLTAYMKRVEDVLGKGWENHVEGQKLKQDGDSFRMKLNTQEIFDDWARKVQQRNLGVSGRIFTI
ESTRVRGRTGNVLKLKVNFLPEIITLSKEVRNLKWLGFRVPLAIVNKAHQANQLYPFAISLIESVRTYERTCEKVEERNT
ISLLVAGLKKEVQALIAEGIALVWESYKLDPYVQRLAETVFNFQEKVDDLLIIEEKIDLEVRSLETCMYDHKTFSEILNR
VQKAVDDLNLHSYSNLPIWVNKLDMEIERILGVRLQAGLRAWTQVLLGQAEDKAEVDMDTDAPQVSHKPGGEPKIKNVVH
ELRITNQVIYLNPPIEECRYKLYQEMFAWKMVVLSLPRIQSQRYQVGVHYELTEEEKFYRNALTRMPDGPVALEESYSAV
MGIVSEVEQYVKVWLQYQCLWDMQAENIYNRLGEDLNKWQALLVQIRKARGTFDNAETKKEFGPVVIDYGKVQSKVNLKY
DSWHKEVLSKFGQMLGSNMTEFHSQISKSRQELEQHSVDTASTSDAVTFITYVQSLKRKIKQFEKQVELYRNGQRLLEKQ
RFQFPPSWLYIDNIEGEWGAFNDIMRRKDSAIQQQVANLQMKIVQEDRAVESRTTDLLTDWEKTKPVTGNLRPEEALQAL
TIYEGKFGRLKDDREKCAKAKEALELTDTGLLSGSEERVQVALEELQDLKGVWSELSKVWEQIDQMKEQPWVSVQPRKLR
QNLDALLNQLKSFPARLRQYASYEFVQRLLKGYMKINMLVIELKSEALKDRHWKQLMKRLHVNWVVSELTLGQIWDVDLQ
KNEAIVKDVLLVAQGEMALEEFLKQIREVWNTYELDLVNYQNKCRLIRGWDDLFNKVKEHINSVSAMKLSPYYKVFEEDA
LSWEDKLNRIMALFDVWIDVQRRWVYLEGIFTGSADIKHLLPVETQRFQSISTEFLALMKKVSKSPLVMDVLNIQGVQRS
LERLADLLGKIQKALGEYLERERSSFPRFYFVGDEDLLEIIGNSKNVAKLQKHFKKMFAGVSSIILNEDNSVVLGISSRE
GEEVMFKTPVSITEHPKINEWLTLVEKEMRVTLAKLLAESVTEVEIFGKATSIDPNTYITWIDKYQAQLVVLSAQIAWSE
NVETALSSMGGGGDAAPLHSVLSNVEVTLNVLADSVLMEQPPLRRRKLEHLITELVHQRDVTRSLIKSKIDNAKSFEWLS
QMRFYFDPKQTDVLQQLSIQMANAKFNYGFEYLGVQDKLVQTPLTDRCYLTMTQALEARLGGSPFGPAGTGKTESVKALG
HQLGRFVLVFNCDETFDFQAMGRIFVGLCQVGAWGCFDEFNRLEERMLSAVSQQVQCIQEALREHSNPNYDKTSAPITCE
LLNKQVKVSPDMAIFITMNPGYAGRSNLPDNLKKLFRSLAMTKPDRQLIAQVMLYSQGFRTAEVLANKIVPFFKLCDEQL
SSQSHYDFGLRALKSVLVSAGNVKRERIQKIKREKEERGEAVDEGEIAENLPEQEILIQSVCETMVPKLVAEDIPLLFSL
LSDVFPGVQYHRGEMTALREELKKVCQEMYLTYGDGEEVGGMWVEKVLQLYQITQINHGLMMVGPSGSGKSMAWRVLLKA
LERLEGVEGVAHIIDPKAISKDHLYGTLDPNTREWTDGLFTHVLRKIIDSVRGELQKRQWIVFDGDVDPEWVENLNSVLD
DNKLLTLPNGERLSLPPNVRIMFEVQDLKYATLATVSRCGMVWFSEDVLSTDMIFNNFLARLRSIPLDEGEDEAQRRRKG
KEDEGEEAASPMLQIQRDAATIMQPYFTSNGLVTKALEHAFQLEHIMDLTRLRCLGSLFSMLHQACRNVAQYNANHPDFP
MQIEQLERYIQRYLVYAILWSLSGDSRLKMRAELGEYIRRITTVPLPTAPNIPIIDYEVSISGEWSPWQAKVPQIEVETH
KVAAPDVVVPTLDTVRHEALLYTWLAEHKPLVLCGPPGSGKTMTLFSALRALPDMEVVGLNFSSATTPELLLKTFDHYCE
YRRTPNGVVLAPVQLGKWLVLFCDEINLPDMDKYGTQRVISFIRQMVEHGGFYRTSDQTWVKLERIQFVGACNPPTDPGR
KPLSHRFLRHVPVVYVDYPGPASLTQIYGTFNRAMLRLIPSLRTYAEPLTAAMVEFYTMSQERFTQDTQPHYIYSPREMT
RWVRGIFEALRPLETLPVEGLIRIWAHEALRLFQDRLVEDEERRWTDENIDTVALKHFPNIDREKAMSRPILYSNWLSKD
YIPVDQEELRDYVKARLKVFYEEELDVPLVLFNEVLDHVLRIDRIFRQPQGHLLLIGVSGAGKTTLSRFVAWMNGLSVYQ
IKVHRKYTGEDFDEDLRTVLRRSGCKNEKIAFIMDESNVLDSGFLERMNTLLANGEVPGLFEGDEYATLMTQCKEGAQKE
GLMLDSHEELYKWFTSQVIRNLHVVFTMNPSSEGLKDRAATSPALFNRCVLNWFGDWSTEALYQVGKEFTSKMDLEKPNY
IVPDYMPVVYDKLPQPPSHREAIVNSCVFVHQTLHQANARLAKRGGRTMAITPRHYLDFINHYANLFHEKRSELEEQQMH
LNVGLRKIKETVDQVEELRRDLRIKSQELEVKNAAANDKLKKMVKDQQEAEKKKVMSQEIQEQLHKQQEVIADKQMSVKE
DLDKVEPAVIEAQNAVKSIKKQHLVEVRSMANPPAAVKLALESICLLLGESTTDWKQIRSIIMRENFIPTIVNFSAEEIS
DAIREKMKKNYMSNPSYNYEIVNRASLACGPMVKWAIAQLNYADMLKRVEPLRNELQKLEDDAKDNQQKANEVEQMIRDL
EASIARYKEEYAVLISEAQAIKADLAAVEAKVNRSTALLKSLSAERERWEKTSETFKNQMSTIAGDCLLSAAFIAYAGYF
DQQMRQNLFTTWSHHLQQANIQFRTDIARTEYLSNADERLRWQASSLPADDLCTENAIMLKRFNRYPLIIDPSGQATEFI
MNEYKDRKITRTSFLDDAFRKNLESALRFGNPLLVQDVESYDPVLNPVLNREVRRTGGRVLITLGDQDIDLSPSFVIFLS
TRDPTVEFPPDLCSRVTFVNFTVTRSSLQSQCLNEVLKAERPDVDEKRSDLLKLQGEFQLRLRQLEKSLLQALNEVKGRI
LDDDTIITTLENLKREAAEVTRKVEETDIVMQEVETVSQQYLPLSTACSSIYFTMESLKQIHFLYQYSLQFFLDIYHNVL
YENPNLKGVTDHTQRLSIITKDLFQVAFNRVARGMLHQDHITFAMLLARIKLKGTVGEPTYDAEFQHFLRGNEIVLSAGS
TPRIQGLTVEQAEAVVRLSCLPAFKDLIAKVQADEQFGIWLDSSSPEQTVPYLWSEETPATPIGQAIHRLLLIQAFRPDR
LLAMAHMFVSTNLGESFMSIMEQPLDLTHIVGTEVKPNTPVLMCSVPGYDASGHVEDLAAEQNTQITSIAIGSAEGFNQA
DKAINTAVKSGRWVMLKNVHLAPGWLMQLEKKLHSLQPHACFRLFLTMEINPKVPVNLLRAGRIFVFEPPPGVKANMLRT
FSSIPVSRICKSPNERARLYFLLAWFHAIIQERLRYAPLGWSKKYEFGESDLRSACDTVDTWLDDTAKGRQNISPDKIPW
SALKTLMAQSIYGGRVDNEFDQRLLNTFLERLFTTRSFDSEFKLACKVDGHKDIQMPDGIRREEFVQWVELLPDTQTPSW
LGLPNNAERVLLTTQGVDMISKMLKMQMLEDEDDLAYAETEKKTRTDSTSDGRPAWMRTLHTTASNWLHLIPQTLSHLKR
TVENIKDPLFRFFEREVKMGAKLLQDVRQDLADVVQVCEGKKKQTNYLRTLINELVKGILPRSWSHYTVPAGMTVIQWVS
DFSERIKQLQNISLAAASGGAKELKNIHVCLGGLFVPEAYITATRQYVAQANSWSLEELCLEVNVTTSQGATLDACSFGV
TGLKLQGATCNNNKLSLSNAISTALPLTQLRWVKQTNTEKKASVVTLPVYLNFTRADLIFTVDFEIATKEDPRSFYERGV
AVLCTE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSEPGGGGGEDGSAGLEVSAVQNVADVSVLQKHLRKLVPLLLEDGGEAPAALEAALEEKSALEQMRKFLSDPQVHTVLVE
RSTLKEDVGDEGEEEKEFISYNINIDIHYGVKSNSLAFIKRTPVIDADKPVSSQLRVLTLSEDSPYETLHSFISNAVAPF
FKSYIRESGKADRDGDKMAPSVEKKIAELEMGLLHLQQNIEIPEISLPIHPMITNVAKQCYERGEKPKVTDFGDKVEDPT
FLNQLQSGVNRWIREIQKVTKLDRDPASGTALQEISFWLNLERALYRIQEKRESPEVLLTLDILKHGKRFHATVSFDTDT
GLKQALETVNDYNPLMKDFPLNDLLSATELDKIRQALVAIFTHLRKIRNTKYPIQRALRLVEAISRDLSSQLLKVLGTRK
LMHVAYEEFEKVMVACFEVFQTWDDEYEKLQVLLRDIVKRKREENLKMVWRINPAHRKLQARLDQMRKFRRQHEQLRAVI
VRVLRPQVTAVAQQNQGEVPEPQDMKVAEVLFDAADANAIEEVNLAYENVKEVDGLDVSKEGTEAWEAAMKRYDERIDRV
ETRITARLRDQLGTAKNANEMFRIFSRFNALFVRPHIRGAIREYQTQLIQRVKDDIESLHDKFKVQYPQSQACKMSHVRD
LPPVSGSIIWAKQIDRQLTAYMKRVEDVLGKGWENHVEGQKLKQDGDSFRMKLNTQEIFDDWARKVQQRNLGVSGRIFTI
ESTRVRGRTGNVLKLKVNFLPEIITLSKEVRNLKWLGFRVPLAIVNKAHQANQLYPFAISLIESVRTYERTCEKVEERNT
ISLLVAGLKKEVQALIAEGIALVWESYKLDPYVQRLAETVFNFQEKVDDLLIIEEKIDLEVRSLETCMYDHKTFSEILNR
VQKAVDDLNLHSYSNLPIWVNKLDMEIERILGVRLQAGLRAWTQVLLGQAEDKAEVDMDTDAPQVSHKPGGEPKIKNVVH
ELRITNQVIYLNPPIEECRYKLYQEMFAWKMVVLSLPRIQSQRYQVGVHYELTEEEKFYRNALTRMPDGPVALEESYSAV
MGIVSEVEQYVKVWLQYQCLWDMQAENIYNRLGEDLNKWQALLVQIRKARGTFDNAETKKEFGPVVIDYGKVQSKVNLKY
DSWHKEVLSKFGQMLGSNMTEFHSQISKSRQELEQHSVDTASTSDAVTFITYVQSLKRKIKQFEKQVELYRNGQRLLEKQ
RFQFPPSWLYIDNIEGEWGAFNDIMRRKDSAIQQQVANLQMKIVQEDRAVESRTTDLLTDWEKTKPVTGNLRPEEALQAL
TIYEGKFGRLKDDREKCAKAKEALELTDTGLLSGSEERVQVALEELQDLKGVWSELSKVWEQIDQMKEQPWVSVQPRKLR
QNLDALLNQLKSFPARLRQYASYEFVQRLLKGYMKINMLVIELKSEALKDRHWKQLMKRLHVNWVVSELTLGQIWDVDLQ
KNEAIVKDVLLVAQGEMALEEFLKQIREVWNTYELDLVNYQNKCRLIRGWDDLFNKVKEHINSVSAMKLSPYYKVFEEDA
LSWEDKLNRIMALFDVWIDVQRRWVYLEGIFTGSADIKHLLPVETQRFQSISTEFLALMKKVSKSPLVMDVLNIQGVQRS
LERLADLLGKIQKALGEYLERERSSFPRFYFVGDEDLLEIIGNSKNVAKLQKHFKKMFAGVSSIILNEDNSVVLGISSRE
GEEVMFKTPVSITEHPKINEWLTLVEKEMRVTLAKLLAESVTEVEIFGKATSIDPNTYITWIDKYQAQLVVLSAQIAWSE
NVETALSSMGGGGDAAPLHSVLSNVEVTLNVLADSVLMEQPPLRRRKLEHLITELVHQRDVTRSLIKSKIDNAKSFEWLS
QMRFYFDPKQTDVLQQLSIQMANAKFNYGFEYLGVQDKLVQTPLTDRCYLTMTQALEARLGGSPFGPAGTGKTESVKALG
HQLGRFVLVFNCDETFDFQAMGRIFVGLCQVGAWGCFDEFNRLEERMLSAVSQQVQCIQEALREHSNPNYDKTSAPITCE
LLNKQVKVSPDMAIFITMNPGYAGRSNLPDNLKKLFRSLAMTKPDRQLIAQVMLYSQGFRTAEVLANKIVPFFKLCDEQL
SSQSHYDFGLRALKSVLVSAGNVKRERIQKIKREKEERGEAVDEGEIAENLPEQEILIQSVCETMVPKLVAEDIPLLFSL
LSDVFPGVQYHRGEMTALREELKKVCQEMYLTYGDGEEVGGMWVEKVLQLYQITQINHGLMMVGPSGSGKSMAWRVLLKA
LERLEGVEGVAHIIDPKAISKDHLYGTLDPNTREWTDGLFTHVLRKIIDSVRGELQKRQWIVFDGDVDPEWVENLNSVLD
DNKLLTLPNGERLSLPPNVRIMFEVQDLKYATLATVSRCGMVWFSEDVLSTDMIFNNFLARLRSIPLDEGEDEAQRRRKG
KEDEGEEAASPMLQIQRDAATIMQPYFTSNGLVTKALEHAFQLEHIMDLTRLRCLGSLFSMLHQACRNVAQYNANHPDFP
MQIEQLERYIQRYLVYAILWSLSGDSRLKMRAELGEYIRRITTVPLPTAPNIPIIDYEVSISGEWSPWQAKVPQIEVETH
KVAAPDVVVPTLDTVRHEALLYTWLAEHKPLVLCGPPGSGKTMTLFSALRALPDMEVVGLNFSSATTPELLLKTFDHYCE
YRRTPNGVVLAPVQLGKWLVLFCDEINLPDMDKYGTQRVISFIRQMVEHGGFYRTSDQTWVKLERIQFVGACNPPTDPGR
KPLSHRFLRHVPVVYVDYPGPASLTQIYGTFNRAMLRLIPSLRTYAEPLTAAMVEFYTMSQERFTQDTQPHYIYSPREMT
RWVRGIFEALRPLETLPVEGLIRIWAHEALRLFQDRLVEDEERRWTDENIDTVALKHFPNIDREKAMSRPILYSNWLSKD
YIPVDQEELRDYVKARLKVFYEEELDVPLVLFNEVLDHVLRIDRIFRQPQGHLLLIGVSGAGKTTLSRFVAWMNGLSVYQ
IKVHRKYTGEDFDEDLRTVLRRSGCKNEKIAFIMDESNVLDSGFLERMNTLLANGEVPGLFEGDEYATLMTQCKEGAQKE
GLMLDSHEELYKWFTSQVIRNLHVVFTMNPSSEGLKDRAATSPALFNRCVLNWFGDWSTEALYQVGKEFTSKMDLEKPNY
IVPDYMPVVYDKLPQPPSHREAIVNSCVFVHQTLHQANARLAKRGGRTMAITPRHYLDFINHYANLFHEKRSELEEQQMH
LNVGLRKIKETVDQVEELRRDLRIKSQELEVKNAAANDKLKKMVKDQQEAEKKKVMSQEIQEQLHKQQEVIADKQMSVKE
DLDKVEPAVIEAQNAVKSIKKQHLVEVRSMANPPAAVKLALESICLLLGESTTDWKQIRSIIMRENFIPTIVNFSAEEIS
DAIREKMKKNYMSNPSYNYEIVNRASLACGPMVKWAIAQLNYADMLKRVEPLRNELQKLEDDAKDNQQKANEVEQMIRDL
EASIARYKEEYAVLISEAQAIKADLAAVEAKVNRSTALLKSLSAERERWEKTSETFKNQMSTIAGDCLLSAAFIAYAGYF
DQQMRQNLFTTWSHHLQQANIQFRTDIARTEYLSNADERLRWQASSLPADDLCTENAIMLKRFNRYPLIIDPSGQATEFI
MNEYKDRKITRTSFLDDAFRKNLESALRFGNPLLVQDVESYDPVLNPVLNREVRRTGGRVLITLGDQDIDLSPSFVIFLS
TRDPTVEFPPDLCSRVTFVNFTVTRSSLQSQCLNEVLKAERPDVDEKRSDLLKLQGEFQLRLRQLEKSLLQALNEVKGRI
LDDDTIITTLENLKREAAEVTRKVEETDIVMQEVETVSQQYLPLSTACSSIYFTMESLKQIHFLYQYSLQFFLDIYHNVL
YENPNLKGVTDHTQRLSIITKDLFQVAFNRVARGMLHQDHITFAMLLARIKLKGTVGEPTYDAEFQHFLRGNEIVLSAGS
TPRIQGLTVEQAEAVVRLSCLPAFKDLIAKVQADEQFGIWLDSSSPEQTVPYLWSEETPATPIGQAIHRLLLIQAFRPDR
LLAMAHMFVSTNLGESFMSIMEQPLDLTHIVGTEVKPNTPVLMCSVPGYDASGHVEDLAAEQNTQITSIAIGSAEGFNQA
DKAINTAVKSGRWVMLKNVHLAPGWLMQLEKKLHSLQPHACFRLFLTMEINPKVPVNLLRAGRIFVFEPPPGVKANMLRT
FSSIPVSRICKSPNERARLYFLLAWFHAIIQERLRYAPLGWSKKYEFGESDLRSACDTVDTWLDDTAKGRQNISPDKIPW
SALKTLMAQSIYGGRVDNEFDQRLLNTFLERLFTTRSFDSEFKLACKVDGHKDIQMPDGIRREEFVQWVELLPDTQTPSW
LGLPNNAERVLLTTQGVDMISKMLKMQMLEDEDDLAYAETEKKTRTDSTSDGRPAWMRTLHTTASNWLHLIPQTLSHLKR
TVENIKDPLFRFFEREVKMGAKLLQDVRQDLADVVQVCEGKKKQTNYLRTLINELVKGILPRSWSHYTVPAGMTVIQWVS
DFSERIKQLQNISLAAASGGAKELKNIHVCLGGLFVPEAYITATRQYVAQANSWSLEELCLEVNVTTSQGATLDACSFGV
TGLKLQGATCNNNKLSLSNAISTALPLTQLRWVKQTNTEKKASVVTLPVYLNFTRADLIFTVDFEIATKEDPRSFYERGV
AVLCTE
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ADP ORTHOVANADATE'         AOV 
3 "ADENOSINE-5'-TRIPHOSPHATE" ATP 
4 "ADENOSINE-5'-DIPHOSPHATE"  ADP 
5 'MAGNESIUM ION'             MG  
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1    MET n 
1 2    SER n 
1 3    GLU n 
1 4    PRO n 
1 5    GLY n 
1 6    GLY n 
1 7    GLY n 
1 8    GLY n 
1 9    GLY n 
1 10   GLU n 
1 11   ASP n 
1 12   GLY n 
1 13   SER n 
1 14   ALA n 
1 15   GLY n 
1 16   LEU n 
1 17   GLU n 
1 18   VAL n 
1 19   SER n 
1 20   ALA n 
1 21   VAL n 
1 22   GLN n 
1 23   ASN n 
1 24   VAL n 
1 25   ALA n 
1 26   ASP n 
1 27   VAL n 
1 28   SER n 
1 29   VAL n 
1 30   LEU n 
1 31   GLN n 
1 32   LYS n 
1 33   HIS n 
1 34   LEU n 
1 35   ARG n 
1 36   LYS n 
1 37   LEU n 
1 38   VAL n 
1 39   PRO n 
1 40   LEU n 
1 41   LEU n 
1 42   LEU n 
1 43   GLU n 
1 44   ASP n 
1 45   GLY n 
1 46   GLY n 
1 47   GLU n 
1 48   ALA n 
1 49   PRO n 
1 50   ALA n 
1 51   ALA n 
1 52   LEU n 
1 53   GLU n 
1 54   ALA n 
1 55   ALA n 
1 56   LEU n 
1 57   GLU n 
1 58   GLU n 
1 59   LYS n 
1 60   SER n 
1 61   ALA n 
1 62   LEU n 
1 63   GLU n 
1 64   GLN n 
1 65   MET n 
1 66   ARG n 
1 67   LYS n 
1 68   PHE n 
1 69   LEU n 
1 70   SER n 
1 71   ASP n 
1 72   PRO n 
1 73   GLN n 
1 74   VAL n 
1 75   HIS n 
1 76   THR n 
1 77   VAL n 
1 78   LEU n 
1 79   VAL n 
1 80   GLU n 
1 81   ARG n 
1 82   SER n 
1 83   THR n 
1 84   LEU n 
1 85   LYS n 
1 86   GLU n 
1 87   ASP n 
1 88   VAL n 
1 89   GLY n 
1 90   ASP n 
1 91   GLU n 
1 92   GLY n 
1 93   GLU n 
1 94   GLU n 
1 95   GLU n 
1 96   LYS n 
1 97   GLU n 
1 98   PHE n 
1 99   ILE n 
1 100  SER n 
1 101  TYR n 
1 102  ASN n 
1 103  ILE n 
1 104  ASN n 
1 105  ILE n 
1 106  ASP n 
1 107  ILE n 
1 108  HIS n 
1 109  TYR n 
1 110  GLY n 
1 111  VAL n 
1 112  LYS n 
1 113  SER n 
1 114  ASN n 
1 115  SER n 
1 116  LEU n 
1 117  ALA n 
1 118  PHE n 
1 119  ILE n 
1 120  LYS n 
1 121  ARG n 
1 122  THR n 
1 123  PRO n 
1 124  VAL n 
1 125  ILE n 
1 126  ASP n 
1 127  ALA n 
1 128  ASP n 
1 129  LYS n 
1 130  PRO n 
1 131  VAL n 
1 132  SER n 
1 133  SER n 
1 134  GLN n 
1 135  LEU n 
1 136  ARG n 
1 137  VAL n 
1 138  LEU n 
1 139  THR n 
1 140  LEU n 
1 141  SER n 
1 142  GLU n 
1 143  ASP n 
1 144  SER n 
1 145  PRO n 
1 146  TYR n 
1 147  GLU n 
1 148  THR n 
1 149  LEU n 
1 150  HIS n 
1 151  SER n 
1 152  PHE n 
1 153  ILE n 
1 154  SER n 
1 155  ASN n 
1 156  ALA n 
1 157  VAL n 
1 158  ALA n 
1 159  PRO n 
1 160  PHE n 
1 161  PHE n 
1 162  LYS n 
1 163  SER n 
1 164  TYR n 
1 165  ILE n 
1 166  ARG n 
1 167  GLU n 
1 168  SER n 
1 169  GLY n 
1 170  LYS n 
1 171  ALA n 
1 172  ASP n 
1 173  ARG n 
1 174  ASP n 
1 175  GLY n 
1 176  ASP n 
1 177  LYS n 
1 178  MET n 
1 179  ALA n 
1 180  PRO n 
1 181  SER n 
1 182  VAL n 
1 183  GLU n 
1 184  LYS n 
1 185  LYS n 
1 186  ILE n 
1 187  ALA n 
1 188  GLU n 
1 189  LEU n 
1 190  GLU n 
1 191  MET n 
1 192  GLY n 
1 193  LEU n 
1 194  LEU n 
1 195  HIS n 
1 196  LEU n 
1 197  GLN n 
1 198  GLN n 
1 199  ASN n 
1 200  ILE n 
1 201  GLU n 
1 202  ILE n 
1 203  PRO n 
1 204  GLU n 
1 205  ILE n 
1 206  SER n 
1 207  LEU n 
1 208  PRO n 
1 209  ILE n 
1 210  HIS n 
1 211  PRO n 
1 212  MET n 
1 213  ILE n 
1 214  THR n 
1 215  ASN n 
1 216  VAL n 
1 217  ALA n 
1 218  LYS n 
1 219  GLN n 
1 220  CYS n 
1 221  TYR n 
1 222  GLU n 
1 223  ARG n 
1 224  GLY n 
1 225  GLU n 
1 226  LYS n 
1 227  PRO n 
1 228  LYS n 
1 229  VAL n 
1 230  THR n 
1 231  ASP n 
1 232  PHE n 
1 233  GLY n 
1 234  ASP n 
1 235  LYS n 
1 236  VAL n 
1 237  GLU n 
1 238  ASP n 
1 239  PRO n 
1 240  THR n 
1 241  PHE n 
1 242  LEU n 
1 243  ASN n 
1 244  GLN n 
1 245  LEU n 
1 246  GLN n 
1 247  SER n 
1 248  GLY n 
1 249  VAL n 
1 250  ASN n 
1 251  ARG n 
1 252  TRP n 
1 253  ILE n 
1 254  ARG n 
1 255  GLU n 
1 256  ILE n 
1 257  GLN n 
1 258  LYS n 
1 259  VAL n 
1 260  THR n 
1 261  LYS n 
1 262  LEU n 
1 263  ASP n 
1 264  ARG n 
1 265  ASP n 
1 266  PRO n 
1 267  ALA n 
1 268  SER n 
1 269  GLY n 
1 270  THR n 
1 271  ALA n 
1 272  LEU n 
1 273  GLN n 
1 274  GLU n 
1 275  ILE n 
1 276  SER n 
1 277  PHE n 
1 278  TRP n 
1 279  LEU n 
1 280  ASN n 
1 281  LEU n 
1 282  GLU n 
1 283  ARG n 
1 284  ALA n 
1 285  LEU n 
1 286  TYR n 
1 287  ARG n 
1 288  ILE n 
1 289  GLN n 
1 290  GLU n 
1 291  LYS n 
1 292  ARG n 
1 293  GLU n 
1 294  SER n 
1 295  PRO n 
1 296  GLU n 
1 297  VAL n 
1 298  LEU n 
1 299  LEU n 
1 300  THR n 
1 301  LEU n 
1 302  ASP n 
1 303  ILE n 
1 304  LEU n 
1 305  LYS n 
1 306  HIS n 
1 307  GLY n 
1 308  LYS n 
1 309  ARG n 
1 310  PHE n 
1 311  HIS n 
1 312  ALA n 
1 313  THR n 
1 314  VAL n 
1 315  SER n 
1 316  PHE n 
1 317  ASP n 
1 318  THR n 
1 319  ASP n 
1 320  THR n 
1 321  GLY n 
1 322  LEU n 
1 323  LYS n 
1 324  GLN n 
1 325  ALA n 
1 326  LEU n 
1 327  GLU n 
1 328  THR n 
1 329  VAL n 
1 330  ASN n 
1 331  ASP n 
1 332  TYR n 
1 333  ASN n 
1 334  PRO n 
1 335  LEU n 
1 336  MET n 
1 337  LYS n 
1 338  ASP n 
1 339  PHE n 
1 340  PRO n 
1 341  LEU n 
1 342  ASN n 
1 343  ASP n 
1 344  LEU n 
1 345  LEU n 
1 346  SER n 
1 347  ALA n 
1 348  THR n 
1 349  GLU n 
1 350  LEU n 
1 351  ASP n 
1 352  LYS n 
1 353  ILE n 
1 354  ARG n 
1 355  GLN n 
1 356  ALA n 
1 357  LEU n 
1 358  VAL n 
1 359  ALA n 
1 360  ILE n 
1 361  PHE n 
1 362  THR n 
1 363  HIS n 
1 364  LEU n 
1 365  ARG n 
1 366  LYS n 
1 367  ILE n 
1 368  ARG n 
1 369  ASN n 
1 370  THR n 
1 371  LYS n 
1 372  TYR n 
1 373  PRO n 
1 374  ILE n 
1 375  GLN n 
1 376  ARG n 
1 377  ALA n 
1 378  LEU n 
1 379  ARG n 
1 380  LEU n 
1 381  VAL n 
1 382  GLU n 
1 383  ALA n 
1 384  ILE n 
1 385  SER n 
1 386  ARG n 
1 387  ASP n 
1 388  LEU n 
1 389  SER n 
1 390  SER n 
1 391  GLN n 
1 392  LEU n 
1 393  LEU n 
1 394  LYS n 
1 395  VAL n 
1 396  LEU n 
1 397  GLY n 
1 398  THR n 
1 399  ARG n 
1 400  LYS n 
1 401  LEU n 
1 402  MET n 
1 403  HIS n 
1 404  VAL n 
1 405  ALA n 
1 406  TYR n 
1 407  GLU n 
1 408  GLU n 
1 409  PHE n 
1 410  GLU n 
1 411  LYS n 
1 412  VAL n 
1 413  MET n 
1 414  VAL n 
1 415  ALA n 
1 416  CYS n 
1 417  PHE n 
1 418  GLU n 
1 419  VAL n 
1 420  PHE n 
1 421  GLN n 
1 422  THR n 
1 423  TRP n 
1 424  ASP n 
1 425  ASP n 
1 426  GLU n 
1 427  TYR n 
1 428  GLU n 
1 429  LYS n 
1 430  LEU n 
1 431  GLN n 
1 432  VAL n 
1 433  LEU n 
1 434  LEU n 
1 435  ARG n 
1 436  ASP n 
1 437  ILE n 
1 438  VAL n 
1 439  LYS n 
1 440  ARG n 
1 441  LYS n 
1 442  ARG n 
1 443  GLU n 
1 444  GLU n 
1 445  ASN n 
1 446  LEU n 
1 447  LYS n 
1 448  MET n 
1 449  VAL n 
1 450  TRP n 
1 451  ARG n 
1 452  ILE n 
1 453  ASN n 
1 454  PRO n 
1 455  ALA n 
1 456  HIS n 
1 457  ARG n 
1 458  LYS n 
1 459  LEU n 
1 460  GLN n 
1 461  ALA n 
1 462  ARG n 
1 463  LEU n 
1 464  ASP n 
1 465  GLN n 
1 466  MET n 
1 467  ARG n 
1 468  LYS n 
1 469  PHE n 
1 470  ARG n 
1 471  ARG n 
1 472  GLN n 
1 473  HIS n 
1 474  GLU n 
1 475  GLN n 
1 476  LEU n 
1 477  ARG n 
1 478  ALA n 
1 479  VAL n 
1 480  ILE n 
1 481  VAL n 
1 482  ARG n 
1 483  VAL n 
1 484  LEU n 
1 485  ARG n 
1 486  PRO n 
1 487  GLN n 
1 488  VAL n 
1 489  THR n 
1 490  ALA n 
1 491  VAL n 
1 492  ALA n 
1 493  GLN n 
1 494  GLN n 
1 495  ASN n 
1 496  GLN n 
1 497  GLY n 
1 498  GLU n 
1 499  VAL n 
1 500  PRO n 
1 501  GLU n 
1 502  PRO n 
1 503  GLN n 
1 504  ASP n 
1 505  MET n 
1 506  LYS n 
1 507  VAL n 
1 508  ALA n 
1 509  GLU n 
1 510  VAL n 
1 511  LEU n 
1 512  PHE n 
1 513  ASP n 
1 514  ALA n 
1 515  ALA n 
1 516  ASP n 
1 517  ALA n 
1 518  ASN n 
1 519  ALA n 
1 520  ILE n 
1 521  GLU n 
1 522  GLU n 
1 523  VAL n 
1 524  ASN n 
1 525  LEU n 
1 526  ALA n 
1 527  TYR n 
1 528  GLU n 
1 529  ASN n 
1 530  VAL n 
1 531  LYS n 
1 532  GLU n 
1 533  VAL n 
1 534  ASP n 
1 535  GLY n 
1 536  LEU n 
1 537  ASP n 
1 538  VAL n 
1 539  SER n 
1 540  LYS n 
1 541  GLU n 
1 542  GLY n 
1 543  THR n 
1 544  GLU n 
1 545  ALA n 
1 546  TRP n 
1 547  GLU n 
1 548  ALA n 
1 549  ALA n 
1 550  MET n 
1 551  LYS n 
1 552  ARG n 
1 553  TYR n 
1 554  ASP n 
1 555  GLU n 
1 556  ARG n 
1 557  ILE n 
1 558  ASP n 
1 559  ARG n 
1 560  VAL n 
1 561  GLU n 
1 562  THR n 
1 563  ARG n 
1 564  ILE n 
1 565  THR n 
1 566  ALA n 
1 567  ARG n 
1 568  LEU n 
1 569  ARG n 
1 570  ASP n 
1 571  GLN n 
1 572  LEU n 
1 573  GLY n 
1 574  THR n 
1 575  ALA n 
1 576  LYS n 
1 577  ASN n 
1 578  ALA n 
1 579  ASN n 
1 580  GLU n 
1 581  MET n 
1 582  PHE n 
1 583  ARG n 
1 584  ILE n 
1 585  PHE n 
1 586  SER n 
1 587  ARG n 
1 588  PHE n 
1 589  ASN n 
1 590  ALA n 
1 591  LEU n 
1 592  PHE n 
1 593  VAL n 
1 594  ARG n 
1 595  PRO n 
1 596  HIS n 
1 597  ILE n 
1 598  ARG n 
1 599  GLY n 
1 600  ALA n 
1 601  ILE n 
1 602  ARG n 
1 603  GLU n 
1 604  TYR n 
1 605  GLN n 
1 606  THR n 
1 607  GLN n 
1 608  LEU n 
1 609  ILE n 
1 610  GLN n 
1 611  ARG n 
1 612  VAL n 
1 613  LYS n 
1 614  ASP n 
1 615  ASP n 
1 616  ILE n 
1 617  GLU n 
1 618  SER n 
1 619  LEU n 
1 620  HIS n 
1 621  ASP n 
1 622  LYS n 
1 623  PHE n 
1 624  LYS n 
1 625  VAL n 
1 626  GLN n 
1 627  TYR n 
1 628  PRO n 
1 629  GLN n 
1 630  SER n 
1 631  GLN n 
1 632  ALA n 
1 633  CYS n 
1 634  LYS n 
1 635  MET n 
1 636  SER n 
1 637  HIS n 
1 638  VAL n 
1 639  ARG n 
1 640  ASP n 
1 641  LEU n 
1 642  PRO n 
1 643  PRO n 
1 644  VAL n 
1 645  SER n 
1 646  GLY n 
1 647  SER n 
1 648  ILE n 
1 649  ILE n 
1 650  TRP n 
1 651  ALA n 
1 652  LYS n 
1 653  GLN n 
1 654  ILE n 
1 655  ASP n 
1 656  ARG n 
1 657  GLN n 
1 658  LEU n 
1 659  THR n 
1 660  ALA n 
1 661  TYR n 
1 662  MET n 
1 663  LYS n 
1 664  ARG n 
1 665  VAL n 
1 666  GLU n 
1 667  ASP n 
1 668  VAL n 
1 669  LEU n 
1 670  GLY n 
1 671  LYS n 
1 672  GLY n 
1 673  TRP n 
1 674  GLU n 
1 675  ASN n 
1 676  HIS n 
1 677  VAL n 
1 678  GLU n 
1 679  GLY n 
1 680  GLN n 
1 681  LYS n 
1 682  LEU n 
1 683  LYS n 
1 684  GLN n 
1 685  ASP n 
1 686  GLY n 
1 687  ASP n 
1 688  SER n 
1 689  PHE n 
1 690  ARG n 
1 691  MET n 
1 692  LYS n 
1 693  LEU n 
1 694  ASN n 
1 695  THR n 
1 696  GLN n 
1 697  GLU n 
1 698  ILE n 
1 699  PHE n 
1 700  ASP n 
1 701  ASP n 
1 702  TRP n 
1 703  ALA n 
1 704  ARG n 
1 705  LYS n 
1 706  VAL n 
1 707  GLN n 
1 708  GLN n 
1 709  ARG n 
1 710  ASN n 
1 711  LEU n 
1 712  GLY n 
1 713  VAL n 
1 714  SER n 
1 715  GLY n 
1 716  ARG n 
1 717  ILE n 
1 718  PHE n 
1 719  THR n 
1 720  ILE n 
1 721  GLU n 
1 722  SER n 
1 723  THR n 
1 724  ARG n 
1 725  VAL n 
1 726  ARG n 
1 727  GLY n 
1 728  ARG n 
1 729  THR n 
1 730  GLY n 
1 731  ASN n 
1 732  VAL n 
1 733  LEU n 
1 734  LYS n 
1 735  LEU n 
1 736  LYS n 
1 737  VAL n 
1 738  ASN n 
1 739  PHE n 
1 740  LEU n 
1 741  PRO n 
1 742  GLU n 
1 743  ILE n 
1 744  ILE n 
1 745  THR n 
1 746  LEU n 
1 747  SER n 
1 748  LYS n 
1 749  GLU n 
1 750  VAL n 
1 751  ARG n 
1 752  ASN n 
1 753  LEU n 
1 754  LYS n 
1 755  TRP n 
1 756  LEU n 
1 757  GLY n 
1 758  PHE n 
1 759  ARG n 
1 760  VAL n 
1 761  PRO n 
1 762  LEU n 
1 763  ALA n 
1 764  ILE n 
1 765  VAL n 
1 766  ASN n 
1 767  LYS n 
1 768  ALA n 
1 769  HIS n 
1 770  GLN n 
1 771  ALA n 
1 772  ASN n 
1 773  GLN n 
1 774  LEU n 
1 775  TYR n 
1 776  PRO n 
1 777  PHE n 
1 778  ALA n 
1 779  ILE n 
1 780  SER n 
1 781  LEU n 
1 782  ILE n 
1 783  GLU n 
1 784  SER n 
1 785  VAL n 
1 786  ARG n 
1 787  THR n 
1 788  TYR n 
1 789  GLU n 
1 790  ARG n 
1 791  THR n 
1 792  CYS n 
1 793  GLU n 
1 794  LYS n 
1 795  VAL n 
1 796  GLU n 
1 797  GLU n 
1 798  ARG n 
1 799  ASN n 
1 800  THR n 
1 801  ILE n 
1 802  SER n 
1 803  LEU n 
1 804  LEU n 
1 805  VAL n 
1 806  ALA n 
1 807  GLY n 
1 808  LEU n 
1 809  LYS n 
1 810  LYS n 
1 811  GLU n 
1 812  VAL n 
1 813  GLN n 
1 814  ALA n 
1 815  LEU n 
1 816  ILE n 
1 817  ALA n 
1 818  GLU n 
1 819  GLY n 
1 820  ILE n 
1 821  ALA n 
1 822  LEU n 
1 823  VAL n 
1 824  TRP n 
1 825  GLU n 
1 826  SER n 
1 827  TYR n 
1 828  LYS n 
1 829  LEU n 
1 830  ASP n 
1 831  PRO n 
1 832  TYR n 
1 833  VAL n 
1 834  GLN n 
1 835  ARG n 
1 836  LEU n 
1 837  ALA n 
1 838  GLU n 
1 839  THR n 
1 840  VAL n 
1 841  PHE n 
1 842  ASN n 
1 843  PHE n 
1 844  GLN n 
1 845  GLU n 
1 846  LYS n 
1 847  VAL n 
1 848  ASP n 
1 849  ASP n 
1 850  LEU n 
1 851  LEU n 
1 852  ILE n 
1 853  ILE n 
1 854  GLU n 
1 855  GLU n 
1 856  LYS n 
1 857  ILE n 
1 858  ASP n 
1 859  LEU n 
1 860  GLU n 
1 861  VAL n 
1 862  ARG n 
1 863  SER n 
1 864  LEU n 
1 865  GLU n 
1 866  THR n 
1 867  CYS n 
1 868  MET n 
1 869  TYR n 
1 870  ASP n 
1 871  HIS n 
1 872  LYS n 
1 873  THR n 
1 874  PHE n 
1 875  SER n 
1 876  GLU n 
1 877  ILE n 
1 878  LEU n 
1 879  ASN n 
1 880  ARG n 
1 881  VAL n 
1 882  GLN n 
1 883  LYS n 
1 884  ALA n 
1 885  VAL n 
1 886  ASP n 
1 887  ASP n 
1 888  LEU n 
1 889  ASN n 
1 890  LEU n 
1 891  HIS n 
1 892  SER n 
1 893  TYR n 
1 894  SER n 
1 895  ASN n 
1 896  LEU n 
1 897  PRO n 
1 898  ILE n 
1 899  TRP n 
1 900  VAL n 
1 901  ASN n 
1 902  LYS n 
1 903  LEU n 
1 904  ASP n 
1 905  MET n 
1 906  GLU n 
1 907  ILE n 
1 908  GLU n 
1 909  ARG n 
1 910  ILE n 
1 911  LEU n 
1 912  GLY n 
1 913  VAL n 
1 914  ARG n 
1 915  LEU n 
1 916  GLN n 
1 917  ALA n 
1 918  GLY n 
1 919  LEU n 
1 920  ARG n 
1 921  ALA n 
1 922  TRP n 
1 923  THR n 
1 924  GLN n 
1 925  VAL n 
1 926  LEU n 
1 927  LEU n 
1 928  GLY n 
1 929  GLN n 
1 930  ALA n 
1 931  GLU n 
1 932  ASP n 
1 933  LYS n 
1 934  ALA n 
1 935  GLU n 
1 936  VAL n 
1 937  ASP n 
1 938  MET n 
1 939  ASP n 
1 940  THR n 
1 941  ASP n 
1 942  ALA n 
1 943  PRO n 
1 944  GLN n 
1 945  VAL n 
1 946  SER n 
1 947  HIS n 
1 948  LYS n 
1 949  PRO n 
1 950  GLY n 
1 951  GLY n 
1 952  GLU n 
1 953  PRO n 
1 954  LYS n 
1 955  ILE n 
1 956  LYS n 
1 957  ASN n 
1 958  VAL n 
1 959  VAL n 
1 960  HIS n 
1 961  GLU n 
1 962  LEU n 
1 963  ARG n 
1 964  ILE n 
1 965  THR n 
1 966  ASN n 
1 967  GLN n 
1 968  VAL n 
1 969  ILE n 
1 970  TYR n 
1 971  LEU n 
1 972  ASN n 
1 973  PRO n 
1 974  PRO n 
1 975  ILE n 
1 976  GLU n 
1 977  GLU n 
1 978  CYS n 
1 979  ARG n 
1 980  TYR n 
1 981  LYS n 
1 982  LEU n 
1 983  TYR n 
1 984  GLN n 
1 985  GLU n 
1 986  MET n 
1 987  PHE n 
1 988  ALA n 
1 989  TRP n 
1 990  LYS n 
1 991  MET n 
1 992  VAL n 
1 993  VAL n 
1 994  LEU n 
1 995  SER n 
1 996  LEU n 
1 997  PRO n 
1 998  ARG n 
1 999  ILE n 
1 1000 GLN n 
1 1001 SER n 
1 1002 GLN n 
1 1003 ARG n 
1 1004 TYR n 
1 1005 GLN n 
1 1006 VAL n 
1 1007 GLY n 
1 1008 VAL n 
1 1009 HIS n 
1 1010 TYR n 
1 1011 GLU n 
1 1012 LEU n 
1 1013 THR n 
1 1014 GLU n 
1 1015 GLU n 
1 1016 GLU n 
1 1017 LYS n 
1 1018 PHE n 
1 1019 TYR n 
1 1020 ARG n 
1 1021 ASN n 
1 1022 ALA n 
1 1023 LEU n 
1 1024 THR n 
1 1025 ARG n 
1 1026 MET n 
1 1027 PRO n 
1 1028 ASP n 
1 1029 GLY n 
1 1030 PRO n 
1 1031 VAL n 
1 1032 ALA n 
1 1033 LEU n 
1 1034 GLU n 
1 1035 GLU n 
1 1036 SER n 
1 1037 TYR n 
1 1038 SER n 
1 1039 ALA n 
1 1040 VAL n 
1 1041 MET n 
1 1042 GLY n 
1 1043 ILE n 
1 1044 VAL n 
1 1045 SER n 
1 1046 GLU n 
1 1047 VAL n 
1 1048 GLU n 
1 1049 GLN n 
1 1050 TYR n 
1 1051 VAL n 
1 1052 LYS n 
1 1053 VAL n 
1 1054 TRP n 
1 1055 LEU n 
1 1056 GLN n 
1 1057 TYR n 
1 1058 GLN n 
1 1059 CYS n 
1 1060 LEU n 
1 1061 TRP n 
1 1062 ASP n 
1 1063 MET n 
1 1064 GLN n 
1 1065 ALA n 
1 1066 GLU n 
1 1067 ASN n 
1 1068 ILE n 
1 1069 TYR n 
1 1070 ASN n 
1 1071 ARG n 
1 1072 LEU n 
1 1073 GLY n 
1 1074 GLU n 
1 1075 ASP n 
1 1076 LEU n 
1 1077 ASN n 
1 1078 LYS n 
1 1079 TRP n 
1 1080 GLN n 
1 1081 ALA n 
1 1082 LEU n 
1 1083 LEU n 
1 1084 VAL n 
1 1085 GLN n 
1 1086 ILE n 
1 1087 ARG n 
1 1088 LYS n 
1 1089 ALA n 
1 1090 ARG n 
1 1091 GLY n 
1 1092 THR n 
1 1093 PHE n 
1 1094 ASP n 
1 1095 ASN n 
1 1096 ALA n 
1 1097 GLU n 
1 1098 THR n 
1 1099 LYS n 
1 1100 LYS n 
1 1101 GLU n 
1 1102 PHE n 
1 1103 GLY n 
1 1104 PRO n 
1 1105 VAL n 
1 1106 VAL n 
1 1107 ILE n 
1 1108 ASP n 
1 1109 TYR n 
1 1110 GLY n 
1 1111 LYS n 
1 1112 VAL n 
1 1113 GLN n 
1 1114 SER n 
1 1115 LYS n 
1 1116 VAL n 
1 1117 ASN n 
1 1118 LEU n 
1 1119 LYS n 
1 1120 TYR n 
1 1121 ASP n 
1 1122 SER n 
1 1123 TRP n 
1 1124 HIS n 
1 1125 LYS n 
1 1126 GLU n 
1 1127 VAL n 
1 1128 LEU n 
1 1129 SER n 
1 1130 LYS n 
1 1131 PHE n 
1 1132 GLY n 
1 1133 GLN n 
1 1134 MET n 
1 1135 LEU n 
1 1136 GLY n 
1 1137 SER n 
1 1138 ASN n 
1 1139 MET n 
1 1140 THR n 
1 1141 GLU n 
1 1142 PHE n 
1 1143 HIS n 
1 1144 SER n 
1 1145 GLN n 
1 1146 ILE n 
1 1147 SER n 
1 1148 LYS n 
1 1149 SER n 
1 1150 ARG n 
1 1151 GLN n 
1 1152 GLU n 
1 1153 LEU n 
1 1154 GLU n 
1 1155 GLN n 
1 1156 HIS n 
1 1157 SER n 
1 1158 VAL n 
1 1159 ASP n 
1 1160 THR n 
1 1161 ALA n 
1 1162 SER n 
1 1163 THR n 
1 1164 SER n 
1 1165 ASP n 
1 1166 ALA n 
1 1167 VAL n 
1 1168 THR n 
1 1169 PHE n 
1 1170 ILE n 
1 1171 THR n 
1 1172 TYR n 
1 1173 VAL n 
1 1174 GLN n 
1 1175 SER n 
1 1176 LEU n 
1 1177 LYS n 
1 1178 ARG n 
1 1179 LYS n 
1 1180 ILE n 
1 1181 LYS n 
1 1182 GLN n 
1 1183 PHE n 
1 1184 GLU n 
1 1185 LYS n 
1 1186 GLN n 
1 1187 VAL n 
1 1188 GLU n 
1 1189 LEU n 
1 1190 TYR n 
1 1191 ARG n 
1 1192 ASN n 
1 1193 GLY n 
1 1194 GLN n 
1 1195 ARG n 
1 1196 LEU n 
1 1197 LEU n 
1 1198 GLU n 
1 1199 LYS n 
1 1200 GLN n 
1 1201 ARG n 
1 1202 PHE n 
1 1203 GLN n 
1 1204 PHE n 
1 1205 PRO n 
1 1206 PRO n 
1 1207 SER n 
1 1208 TRP n 
1 1209 LEU n 
1 1210 TYR n 
1 1211 ILE n 
1 1212 ASP n 
1 1213 ASN n 
1 1214 ILE n 
1 1215 GLU n 
1 1216 GLY n 
1 1217 GLU n 
1 1218 TRP n 
1 1219 GLY n 
1 1220 ALA n 
1 1221 PHE n 
1 1222 ASN n 
1 1223 ASP n 
1 1224 ILE n 
1 1225 MET n 
1 1226 ARG n 
1 1227 ARG n 
1 1228 LYS n 
1 1229 ASP n 
1 1230 SER n 
1 1231 ALA n 
1 1232 ILE n 
1 1233 GLN n 
1 1234 GLN n 
1 1235 GLN n 
1 1236 VAL n 
1 1237 ALA n 
1 1238 ASN n 
1 1239 LEU n 
1 1240 GLN n 
1 1241 MET n 
1 1242 LYS n 
1 1243 ILE n 
1 1244 VAL n 
1 1245 GLN n 
1 1246 GLU n 
1 1247 ASP n 
1 1248 ARG n 
1 1249 ALA n 
1 1250 VAL n 
1 1251 GLU n 
1 1252 SER n 
1 1253 ARG n 
1 1254 THR n 
1 1255 THR n 
1 1256 ASP n 
1 1257 LEU n 
1 1258 LEU n 
1 1259 THR n 
1 1260 ASP n 
1 1261 TRP n 
1 1262 GLU n 
1 1263 LYS n 
1 1264 THR n 
1 1265 LYS n 
1 1266 PRO n 
1 1267 VAL n 
1 1268 THR n 
1 1269 GLY n 
1 1270 ASN n 
1 1271 LEU n 
1 1272 ARG n 
1 1273 PRO n 
1 1274 GLU n 
1 1275 GLU n 
1 1276 ALA n 
1 1277 LEU n 
1 1278 GLN n 
1 1279 ALA n 
1 1280 LEU n 
1 1281 THR n 
1 1282 ILE n 
1 1283 TYR n 
1 1284 GLU n 
1 1285 GLY n 
1 1286 LYS n 
1 1287 PHE n 
1 1288 GLY n 
1 1289 ARG n 
1 1290 LEU n 
1 1291 LYS n 
1 1292 ASP n 
1 1293 ASP n 
1 1294 ARG n 
1 1295 GLU n 
1 1296 LYS n 
1 1297 CYS n 
1 1298 ALA n 
1 1299 LYS n 
1 1300 ALA n 
1 1301 LYS n 
1 1302 GLU n 
1 1303 ALA n 
1 1304 LEU n 
1 1305 GLU n 
1 1306 LEU n 
1 1307 THR n 
1 1308 ASP n 
1 1309 THR n 
1 1310 GLY n 
1 1311 LEU n 
1 1312 LEU n 
1 1313 SER n 
1 1314 GLY n 
1 1315 SER n 
1 1316 GLU n 
1 1317 GLU n 
1 1318 ARG n 
1 1319 VAL n 
1 1320 GLN n 
1 1321 VAL n 
1 1322 ALA n 
1 1323 LEU n 
1 1324 GLU n 
1 1325 GLU n 
1 1326 LEU n 
1 1327 GLN n 
1 1328 ASP n 
1 1329 LEU n 
1 1330 LYS n 
1 1331 GLY n 
1 1332 VAL n 
1 1333 TRP n 
1 1334 SER n 
1 1335 GLU n 
1 1336 LEU n 
1 1337 SER n 
1 1338 LYS n 
1 1339 VAL n 
1 1340 TRP n 
1 1341 GLU n 
1 1342 GLN n 
1 1343 ILE n 
1 1344 ASP n 
1 1345 GLN n 
1 1346 MET n 
1 1347 LYS n 
1 1348 GLU n 
1 1349 GLN n 
1 1350 PRO n 
1 1351 TRP n 
1 1352 VAL n 
1 1353 SER n 
1 1354 VAL n 
1 1355 GLN n 
1 1356 PRO n 
1 1357 ARG n 
1 1358 LYS n 
1 1359 LEU n 
1 1360 ARG n 
1 1361 GLN n 
1 1362 ASN n 
1 1363 LEU n 
1 1364 ASP n 
1 1365 ALA n 
1 1366 LEU n 
1 1367 LEU n 
1 1368 ASN n 
1 1369 GLN n 
1 1370 LEU n 
1 1371 LYS n 
1 1372 SER n 
1 1373 PHE n 
1 1374 PRO n 
1 1375 ALA n 
1 1376 ARG n 
1 1377 LEU n 
1 1378 ARG n 
1 1379 GLN n 
1 1380 TYR n 
1 1381 ALA n 
1 1382 SER n 
1 1383 TYR n 
1 1384 GLU n 
1 1385 PHE n 
1 1386 VAL n 
1 1387 GLN n 
1 1388 ARG n 
1 1389 LEU n 
1 1390 LEU n 
1 1391 LYS n 
1 1392 GLY n 
1 1393 TYR n 
1 1394 MET n 
1 1395 LYS n 
1 1396 ILE n 
1 1397 ASN n 
1 1398 MET n 
1 1399 LEU n 
1 1400 VAL n 
1 1401 ILE n 
1 1402 GLU n 
1 1403 LEU n 
1 1404 LYS n 
1 1405 SER n 
1 1406 GLU n 
1 1407 ALA n 
1 1408 LEU n 
1 1409 LYS n 
1 1410 ASP n 
1 1411 ARG n 
1 1412 HIS n 
1 1413 TRP n 
1 1414 LYS n 
1 1415 GLN n 
1 1416 LEU n 
1 1417 MET n 
1 1418 LYS n 
1 1419 ARG n 
1 1420 LEU n 
1 1421 HIS n 
1 1422 VAL n 
1 1423 ASN n 
1 1424 TRP n 
1 1425 VAL n 
1 1426 VAL n 
1 1427 SER n 
1 1428 GLU n 
1 1429 LEU n 
1 1430 THR n 
1 1431 LEU n 
1 1432 GLY n 
1 1433 GLN n 
1 1434 ILE n 
1 1435 TRP n 
1 1436 ASP n 
1 1437 VAL n 
1 1438 ASP n 
1 1439 LEU n 
1 1440 GLN n 
1 1441 LYS n 
1 1442 ASN n 
1 1443 GLU n 
1 1444 ALA n 
1 1445 ILE n 
1 1446 VAL n 
1 1447 LYS n 
1 1448 ASP n 
1 1449 VAL n 
1 1450 LEU n 
1 1451 LEU n 
1 1452 VAL n 
1 1453 ALA n 
1 1454 GLN n 
1 1455 GLY n 
1 1456 GLU n 
1 1457 MET n 
1 1458 ALA n 
1 1459 LEU n 
1 1460 GLU n 
1 1461 GLU n 
1 1462 PHE n 
1 1463 LEU n 
1 1464 LYS n 
1 1465 GLN n 
1 1466 ILE n 
1 1467 ARG n 
1 1468 GLU n 
1 1469 VAL n 
1 1470 TRP n 
1 1471 ASN n 
1 1472 THR n 
1 1473 TYR n 
1 1474 GLU n 
1 1475 LEU n 
1 1476 ASP n 
1 1477 LEU n 
1 1478 VAL n 
1 1479 ASN n 
1 1480 TYR n 
1 1481 GLN n 
1 1482 ASN n 
1 1483 LYS n 
1 1484 CYS n 
1 1485 ARG n 
1 1486 LEU n 
1 1487 ILE n 
1 1488 ARG n 
1 1489 GLY n 
1 1490 TRP n 
1 1491 ASP n 
1 1492 ASP n 
1 1493 LEU n 
1 1494 PHE n 
1 1495 ASN n 
1 1496 LYS n 
1 1497 VAL n 
1 1498 LYS n 
1 1499 GLU n 
1 1500 HIS n 
1 1501 ILE n 
1 1502 ASN n 
1 1503 SER n 
1 1504 VAL n 
1 1505 SER n 
1 1506 ALA n 
1 1507 MET n 
1 1508 LYS n 
1 1509 LEU n 
1 1510 SER n 
1 1511 PRO n 
1 1512 TYR n 
1 1513 TYR n 
1 1514 LYS n 
1 1515 VAL n 
1 1516 PHE n 
1 1517 GLU n 
1 1518 GLU n 
1 1519 ASP n 
1 1520 ALA n 
1 1521 LEU n 
1 1522 SER n 
1 1523 TRP n 
1 1524 GLU n 
1 1525 ASP n 
1 1526 LYS n 
1 1527 LEU n 
1 1528 ASN n 
1 1529 ARG n 
1 1530 ILE n 
1 1531 MET n 
1 1532 ALA n 
1 1533 LEU n 
1 1534 PHE n 
1 1535 ASP n 
1 1536 VAL n 
1 1537 TRP n 
1 1538 ILE n 
1 1539 ASP n 
1 1540 VAL n 
1 1541 GLN n 
1 1542 ARG n 
1 1543 ARG n 
1 1544 TRP n 
1 1545 VAL n 
1 1546 TYR n 
1 1547 LEU n 
1 1548 GLU n 
1 1549 GLY n 
1 1550 ILE n 
1 1551 PHE n 
1 1552 THR n 
1 1553 GLY n 
1 1554 SER n 
1 1555 ALA n 
1 1556 ASP n 
1 1557 ILE n 
1 1558 LYS n 
1 1559 HIS n 
1 1560 LEU n 
1 1561 LEU n 
1 1562 PRO n 
1 1563 VAL n 
1 1564 GLU n 
1 1565 THR n 
1 1566 GLN n 
1 1567 ARG n 
1 1568 PHE n 
1 1569 GLN n 
1 1570 SER n 
1 1571 ILE n 
1 1572 SER n 
1 1573 THR n 
1 1574 GLU n 
1 1575 PHE n 
1 1576 LEU n 
1 1577 ALA n 
1 1578 LEU n 
1 1579 MET n 
1 1580 LYS n 
1 1581 LYS n 
1 1582 VAL n 
1 1583 SER n 
1 1584 LYS n 
1 1585 SER n 
1 1586 PRO n 
1 1587 LEU n 
1 1588 VAL n 
1 1589 MET n 
1 1590 ASP n 
1 1591 VAL n 
1 1592 LEU n 
1 1593 ASN n 
1 1594 ILE n 
1 1595 GLN n 
1 1596 GLY n 
1 1597 VAL n 
1 1598 GLN n 
1 1599 ARG n 
1 1600 SER n 
1 1601 LEU n 
1 1602 GLU n 
1 1603 ARG n 
1 1604 LEU n 
1 1605 ALA n 
1 1606 ASP n 
1 1607 LEU n 
1 1608 LEU n 
1 1609 GLY n 
1 1610 LYS n 
1 1611 ILE n 
1 1612 GLN n 
1 1613 LYS n 
1 1614 ALA n 
1 1615 LEU n 
1 1616 GLY n 
1 1617 GLU n 
1 1618 TYR n 
1 1619 LEU n 
1 1620 GLU n 
1 1621 ARG n 
1 1622 GLU n 
1 1623 ARG n 
1 1624 SER n 
1 1625 SER n 
1 1626 PHE n 
1 1627 PRO n 
1 1628 ARG n 
1 1629 PHE n 
1 1630 TYR n 
1 1631 PHE n 
1 1632 VAL n 
1 1633 GLY n 
1 1634 ASP n 
1 1635 GLU n 
1 1636 ASP n 
1 1637 LEU n 
1 1638 LEU n 
1 1639 GLU n 
1 1640 ILE n 
1 1641 ILE n 
1 1642 GLY n 
1 1643 ASN n 
1 1644 SER n 
1 1645 LYS n 
1 1646 ASN n 
1 1647 VAL n 
1 1648 ALA n 
1 1649 LYS n 
1 1650 LEU n 
1 1651 GLN n 
1 1652 LYS n 
1 1653 HIS n 
1 1654 PHE n 
1 1655 LYS n 
1 1656 LYS n 
1 1657 MET n 
1 1658 PHE n 
1 1659 ALA n 
1 1660 GLY n 
1 1661 VAL n 
1 1662 SER n 
1 1663 SER n 
1 1664 ILE n 
1 1665 ILE n 
1 1666 LEU n 
1 1667 ASN n 
1 1668 GLU n 
1 1669 ASP n 
1 1670 ASN n 
1 1671 SER n 
1 1672 VAL n 
1 1673 VAL n 
1 1674 LEU n 
1 1675 GLY n 
1 1676 ILE n 
1 1677 SER n 
1 1678 SER n 
1 1679 ARG n 
1 1680 GLU n 
1 1681 GLY n 
1 1682 GLU n 
1 1683 GLU n 
1 1684 VAL n 
1 1685 MET n 
1 1686 PHE n 
1 1687 LYS n 
1 1688 THR n 
1 1689 PRO n 
1 1690 VAL n 
1 1691 SER n 
1 1692 ILE n 
1 1693 THR n 
1 1694 GLU n 
1 1695 HIS n 
1 1696 PRO n 
1 1697 LYS n 
1 1698 ILE n 
1 1699 ASN n 
1 1700 GLU n 
1 1701 TRP n 
1 1702 LEU n 
1 1703 THR n 
1 1704 LEU n 
1 1705 VAL n 
1 1706 GLU n 
1 1707 LYS n 
1 1708 GLU n 
1 1709 MET n 
1 1710 ARG n 
1 1711 VAL n 
1 1712 THR n 
1 1713 LEU n 
1 1714 ALA n 
1 1715 LYS n 
1 1716 LEU n 
1 1717 LEU n 
1 1718 ALA n 
1 1719 GLU n 
1 1720 SER n 
1 1721 VAL n 
1 1722 THR n 
1 1723 GLU n 
1 1724 VAL n 
1 1725 GLU n 
1 1726 ILE n 
1 1727 PHE n 
1 1728 GLY n 
1 1729 LYS n 
1 1730 ALA n 
1 1731 THR n 
1 1732 SER n 
1 1733 ILE n 
1 1734 ASP n 
1 1735 PRO n 
1 1736 ASN n 
1 1737 THR n 
1 1738 TYR n 
1 1739 ILE n 
1 1740 THR n 
1 1741 TRP n 
1 1742 ILE n 
1 1743 ASP n 
1 1744 LYS n 
1 1745 TYR n 
1 1746 GLN n 
1 1747 ALA n 
1 1748 GLN n 
1 1749 LEU n 
1 1750 VAL n 
1 1751 VAL n 
1 1752 LEU n 
1 1753 SER n 
1 1754 ALA n 
1 1755 GLN n 
1 1756 ILE n 
1 1757 ALA n 
1 1758 TRP n 
1 1759 SER n 
1 1760 GLU n 
1 1761 ASN n 
1 1762 VAL n 
1 1763 GLU n 
1 1764 THR n 
1 1765 ALA n 
1 1766 LEU n 
1 1767 SER n 
1 1768 SER n 
1 1769 MET n 
1 1770 GLY n 
1 1771 GLY n 
1 1772 GLY n 
1 1773 GLY n 
1 1774 ASP n 
1 1775 ALA n 
1 1776 ALA n 
1 1777 PRO n 
1 1778 LEU n 
1 1779 HIS n 
1 1780 SER n 
1 1781 VAL n 
1 1782 LEU n 
1 1783 SER n 
1 1784 ASN n 
1 1785 VAL n 
1 1786 GLU n 
1 1787 VAL n 
1 1788 THR n 
1 1789 LEU n 
1 1790 ASN n 
1 1791 VAL n 
1 1792 LEU n 
1 1793 ALA n 
1 1794 ASP n 
1 1795 SER n 
1 1796 VAL n 
1 1797 LEU n 
1 1798 MET n 
1 1799 GLU n 
1 1800 GLN n 
1 1801 PRO n 
1 1802 PRO n 
1 1803 LEU n 
1 1804 ARG n 
1 1805 ARG n 
1 1806 ARG n 
1 1807 LYS n 
1 1808 LEU n 
1 1809 GLU n 
1 1810 HIS n 
1 1811 LEU n 
1 1812 ILE n 
1 1813 THR n 
1 1814 GLU n 
1 1815 LEU n 
1 1816 VAL n 
1 1817 HIS n 
1 1818 GLN n 
1 1819 ARG n 
1 1820 ASP n 
1 1821 VAL n 
1 1822 THR n 
1 1823 ARG n 
1 1824 SER n 
1 1825 LEU n 
1 1826 ILE n 
1 1827 LYS n 
1 1828 SER n 
1 1829 LYS n 
1 1830 ILE n 
1 1831 ASP n 
1 1832 ASN n 
1 1833 ALA n 
1 1834 LYS n 
1 1835 SER n 
1 1836 PHE n 
1 1837 GLU n 
1 1838 TRP n 
1 1839 LEU n 
1 1840 SER n 
1 1841 GLN n 
1 1842 MET n 
1 1843 ARG n 
1 1844 PHE n 
1 1845 TYR n 
1 1846 PHE n 
1 1847 ASP n 
1 1848 PRO n 
1 1849 LYS n 
1 1850 GLN n 
1 1851 THR n 
1 1852 ASP n 
1 1853 VAL n 
1 1854 LEU n 
1 1855 GLN n 
1 1856 GLN n 
1 1857 LEU n 
1 1858 SER n 
1 1859 ILE n 
1 1860 GLN n 
1 1861 MET n 
1 1862 ALA n 
1 1863 ASN n 
1 1864 ALA n 
1 1865 LYS n 
1 1866 PHE n 
1 1867 ASN n 
1 1868 TYR n 
1 1869 GLY n 
1 1870 PHE n 
1 1871 GLU n 
1 1872 TYR n 
1 1873 LEU n 
1 1874 GLY n 
1 1875 VAL n 
1 1876 GLN n 
1 1877 ASP n 
1 1878 LYS n 
1 1879 LEU n 
1 1880 VAL n 
1 1881 GLN n 
1 1882 THR n 
1 1883 PRO n 
1 1884 LEU n 
1 1885 THR n 
1 1886 ASP n 
1 1887 ARG n 
1 1888 CYS n 
1 1889 TYR n 
1 1890 LEU n 
1 1891 THR n 
1 1892 MET n 
1 1893 THR n 
1 1894 GLN n 
1 1895 ALA n 
1 1896 LEU n 
1 1897 GLU n 
1 1898 ALA n 
1 1899 ARG n 
1 1900 LEU n 
1 1901 GLY n 
1 1902 GLY n 
1 1903 SER n 
1 1904 PRO n 
1 1905 PHE n 
1 1906 GLY n 
1 1907 PRO n 
1 1908 ALA n 
1 1909 GLY n 
1 1910 THR n 
1 1911 GLY n 
1 1912 LYS n 
1 1913 THR n 
1 1914 GLU n 
1 1915 SER n 
1 1916 VAL n 
1 1917 LYS n 
1 1918 ALA n 
1 1919 LEU n 
1 1920 GLY n 
1 1921 HIS n 
1 1922 GLN n 
1 1923 LEU n 
1 1924 GLY n 
1 1925 ARG n 
1 1926 PHE n 
1 1927 VAL n 
1 1928 LEU n 
1 1929 VAL n 
1 1930 PHE n 
1 1931 ASN n 
1 1932 CYS n 
1 1933 ASP n 
1 1934 GLU n 
1 1935 THR n 
1 1936 PHE n 
1 1937 ASP n 
1 1938 PHE n 
1 1939 GLN n 
1 1940 ALA n 
1 1941 MET n 
1 1942 GLY n 
1 1943 ARG n 
1 1944 ILE n 
1 1945 PHE n 
1 1946 VAL n 
1 1947 GLY n 
1 1948 LEU n 
1 1949 CYS n 
1 1950 GLN n 
1 1951 VAL n 
1 1952 GLY n 
1 1953 ALA n 
1 1954 TRP n 
1 1955 GLY n 
1 1956 CYS n 
1 1957 PHE n 
1 1958 ASP n 
1 1959 GLU n 
1 1960 PHE n 
1 1961 ASN n 
1 1962 ARG n 
1 1963 LEU n 
1 1964 GLU n 
1 1965 GLU n 
1 1966 ARG n 
1 1967 MET n 
1 1968 LEU n 
1 1969 SER n 
1 1970 ALA n 
1 1971 VAL n 
1 1972 SER n 
1 1973 GLN n 
1 1974 GLN n 
1 1975 VAL n 
1 1976 GLN n 
1 1977 CYS n 
1 1978 ILE n 
1 1979 GLN n 
1 1980 GLU n 
1 1981 ALA n 
1 1982 LEU n 
1 1983 ARG n 
1 1984 GLU n 
1 1985 HIS n 
1 1986 SER n 
1 1987 ASN n 
1 1988 PRO n 
1 1989 ASN n 
1 1990 TYR n 
1 1991 ASP n 
1 1992 LYS n 
1 1993 THR n 
1 1994 SER n 
1 1995 ALA n 
1 1996 PRO n 
1 1997 ILE n 
1 1998 THR n 
1 1999 CYS n 
1 2000 GLU n 
1 2001 LEU n 
1 2002 LEU n 
1 2003 ASN n 
1 2004 LYS n 
1 2005 GLN n 
1 2006 VAL n 
1 2007 LYS n 
1 2008 VAL n 
1 2009 SER n 
1 2010 PRO n 
1 2011 ASP n 
1 2012 MET n 
1 2013 ALA n 
1 2014 ILE n 
1 2015 PHE n 
1 2016 ILE n 
1 2017 THR n 
1 2018 MET n 
1 2019 ASN n 
1 2020 PRO n 
1 2021 GLY n 
1 2022 TYR n 
1 2023 ALA n 
1 2024 GLY n 
1 2025 ARG n 
1 2026 SER n 
1 2027 ASN n 
1 2028 LEU n 
1 2029 PRO n 
1 2030 ASP n 
1 2031 ASN n 
1 2032 LEU n 
1 2033 LYS n 
1 2034 LYS n 
1 2035 LEU n 
1 2036 PHE n 
1 2037 ARG n 
1 2038 SER n 
1 2039 LEU n 
1 2040 ALA n 
1 2041 MET n 
1 2042 THR n 
1 2043 LYS n 
1 2044 PRO n 
1 2045 ASP n 
1 2046 ARG n 
1 2047 GLN n 
1 2048 LEU n 
1 2049 ILE n 
1 2050 ALA n 
1 2051 GLN n 
1 2052 VAL n 
1 2053 MET n 
1 2054 LEU n 
1 2055 TYR n 
1 2056 SER n 
1 2057 GLN n 
1 2058 GLY n 
1 2059 PHE n 
1 2060 ARG n 
1 2061 THR n 
1 2062 ALA n 
1 2063 GLU n 
1 2064 VAL n 
1 2065 LEU n 
1 2066 ALA n 
1 2067 ASN n 
1 2068 LYS n 
1 2069 ILE n 
1 2070 VAL n 
1 2071 PRO n 
1 2072 PHE n 
1 2073 PHE n 
1 2074 LYS n 
1 2075 LEU n 
1 2076 CYS n 
1 2077 ASP n 
1 2078 GLU n 
1 2079 GLN n 
1 2080 LEU n 
1 2081 SER n 
1 2082 SER n 
1 2083 GLN n 
1 2084 SER n 
1 2085 HIS n 
1 2086 TYR n 
1 2087 ASP n 
1 2088 PHE n 
1 2089 GLY n 
1 2090 LEU n 
1 2091 ARG n 
1 2092 ALA n 
1 2093 LEU n 
1 2094 LYS n 
1 2095 SER n 
1 2096 VAL n 
1 2097 LEU n 
1 2098 VAL n 
1 2099 SER n 
1 2100 ALA n 
1 2101 GLY n 
1 2102 ASN n 
1 2103 VAL n 
1 2104 LYS n 
1 2105 ARG n 
1 2106 GLU n 
1 2107 ARG n 
1 2108 ILE n 
1 2109 GLN n 
1 2110 LYS n 
1 2111 ILE n 
1 2112 LYS n 
1 2113 ARG n 
1 2114 GLU n 
1 2115 LYS n 
1 2116 GLU n 
1 2117 GLU n 
1 2118 ARG n 
1 2119 GLY n 
1 2120 GLU n 
1 2121 ALA n 
1 2122 VAL n 
1 2123 ASP n 
1 2124 GLU n 
1 2125 GLY n 
1 2126 GLU n 
1 2127 ILE n 
1 2128 ALA n 
1 2129 GLU n 
1 2130 ASN n 
1 2131 LEU n 
1 2132 PRO n 
1 2133 GLU n 
1 2134 GLN n 
1 2135 GLU n 
1 2136 ILE n 
1 2137 LEU n 
1 2138 ILE n 
1 2139 GLN n 
1 2140 SER n 
1 2141 VAL n 
1 2142 CYS n 
1 2143 GLU n 
1 2144 THR n 
1 2145 MET n 
1 2146 VAL n 
1 2147 PRO n 
1 2148 LYS n 
1 2149 LEU n 
1 2150 VAL n 
1 2151 ALA n 
1 2152 GLU n 
1 2153 ASP n 
1 2154 ILE n 
1 2155 PRO n 
1 2156 LEU n 
1 2157 LEU n 
1 2158 PHE n 
1 2159 SER n 
1 2160 LEU n 
1 2161 LEU n 
1 2162 SER n 
1 2163 ASP n 
1 2164 VAL n 
1 2165 PHE n 
1 2166 PRO n 
1 2167 GLY n 
1 2168 VAL n 
1 2169 GLN n 
1 2170 TYR n 
1 2171 HIS n 
1 2172 ARG n 
1 2173 GLY n 
1 2174 GLU n 
1 2175 MET n 
1 2176 THR n 
1 2177 ALA n 
1 2178 LEU n 
1 2179 ARG n 
1 2180 GLU n 
1 2181 GLU n 
1 2182 LEU n 
1 2183 LYS n 
1 2184 LYS n 
1 2185 VAL n 
1 2186 CYS n 
1 2187 GLN n 
1 2188 GLU n 
1 2189 MET n 
1 2190 TYR n 
1 2191 LEU n 
1 2192 THR n 
1 2193 TYR n 
1 2194 GLY n 
1 2195 ASP n 
1 2196 GLY n 
1 2197 GLU n 
1 2198 GLU n 
1 2199 VAL n 
1 2200 GLY n 
1 2201 GLY n 
1 2202 MET n 
1 2203 TRP n 
1 2204 VAL n 
1 2205 GLU n 
1 2206 LYS n 
1 2207 VAL n 
1 2208 LEU n 
1 2209 GLN n 
1 2210 LEU n 
1 2211 TYR n 
1 2212 GLN n 
1 2213 ILE n 
1 2214 THR n 
1 2215 GLN n 
1 2216 ILE n 
1 2217 ASN n 
1 2218 HIS n 
1 2219 GLY n 
1 2220 LEU n 
1 2221 MET n 
1 2222 MET n 
1 2223 VAL n 
1 2224 GLY n 
1 2225 PRO n 
1 2226 SER n 
1 2227 GLY n 
1 2228 SER n 
1 2229 GLY n 
1 2230 LYS n 
1 2231 SER n 
1 2232 MET n 
1 2233 ALA n 
1 2234 TRP n 
1 2235 ARG n 
1 2236 VAL n 
1 2237 LEU n 
1 2238 LEU n 
1 2239 LYS n 
1 2240 ALA n 
1 2241 LEU n 
1 2242 GLU n 
1 2243 ARG n 
1 2244 LEU n 
1 2245 GLU n 
1 2246 GLY n 
1 2247 VAL n 
1 2248 GLU n 
1 2249 GLY n 
1 2250 VAL n 
1 2251 ALA n 
1 2252 HIS n 
1 2253 ILE n 
1 2254 ILE n 
1 2255 ASP n 
1 2256 PRO n 
1 2257 LYS n 
1 2258 ALA n 
1 2259 ILE n 
1 2260 SER n 
1 2261 LYS n 
1 2262 ASP n 
1 2263 HIS n 
1 2264 LEU n 
1 2265 TYR n 
1 2266 GLY n 
1 2267 THR n 
1 2268 LEU n 
1 2269 ASP n 
1 2270 PRO n 
1 2271 ASN n 
1 2272 THR n 
1 2273 ARG n 
1 2274 GLU n 
1 2275 TRP n 
1 2276 THR n 
1 2277 ASP n 
1 2278 GLY n 
1 2279 LEU n 
1 2280 PHE n 
1 2281 THR n 
1 2282 HIS n 
1 2283 VAL n 
1 2284 LEU n 
1 2285 ARG n 
1 2286 LYS n 
1 2287 ILE n 
1 2288 ILE n 
1 2289 ASP n 
1 2290 SER n 
1 2291 VAL n 
1 2292 ARG n 
1 2293 GLY n 
1 2294 GLU n 
1 2295 LEU n 
1 2296 GLN n 
1 2297 LYS n 
1 2298 ARG n 
1 2299 GLN n 
1 2300 TRP n 
1 2301 ILE n 
1 2302 VAL n 
1 2303 PHE n 
1 2304 ASP n 
1 2305 GLY n 
1 2306 ASP n 
1 2307 VAL n 
1 2308 ASP n 
1 2309 PRO n 
1 2310 GLU n 
1 2311 TRP n 
1 2312 VAL n 
1 2313 GLU n 
1 2314 ASN n 
1 2315 LEU n 
1 2316 ASN n 
1 2317 SER n 
1 2318 VAL n 
1 2319 LEU n 
1 2320 ASP n 
1 2321 ASP n 
1 2322 ASN n 
1 2323 LYS n 
1 2324 LEU n 
1 2325 LEU n 
1 2326 THR n 
1 2327 LEU n 
1 2328 PRO n 
1 2329 ASN n 
1 2330 GLY n 
1 2331 GLU n 
1 2332 ARG n 
1 2333 LEU n 
1 2334 SER n 
1 2335 LEU n 
1 2336 PRO n 
1 2337 PRO n 
1 2338 ASN n 
1 2339 VAL n 
1 2340 ARG n 
1 2341 ILE n 
1 2342 MET n 
1 2343 PHE n 
1 2344 GLU n 
1 2345 VAL n 
1 2346 GLN n 
1 2347 ASP n 
1 2348 LEU n 
1 2349 LYS n 
1 2350 TYR n 
1 2351 ALA n 
1 2352 THR n 
1 2353 LEU n 
1 2354 ALA n 
1 2355 THR n 
1 2356 VAL n 
1 2357 SER n 
1 2358 ARG n 
1 2359 CYS n 
1 2360 GLY n 
1 2361 MET n 
1 2362 VAL n 
1 2363 TRP n 
1 2364 PHE n 
1 2365 SER n 
1 2366 GLU n 
1 2367 ASP n 
1 2368 VAL n 
1 2369 LEU n 
1 2370 SER n 
1 2371 THR n 
1 2372 ASP n 
1 2373 MET n 
1 2374 ILE n 
1 2375 PHE n 
1 2376 ASN n 
1 2377 ASN n 
1 2378 PHE n 
1 2379 LEU n 
1 2380 ALA n 
1 2381 ARG n 
1 2382 LEU n 
1 2383 ARG n 
1 2384 SER n 
1 2385 ILE n 
1 2386 PRO n 
1 2387 LEU n 
1 2388 ASP n 
1 2389 GLU n 
1 2390 GLY n 
1 2391 GLU n 
1 2392 ASP n 
1 2393 GLU n 
1 2394 ALA n 
1 2395 GLN n 
1 2396 ARG n 
1 2397 ARG n 
1 2398 ARG n 
1 2399 LYS n 
1 2400 GLY n 
1 2401 LYS n 
1 2402 GLU n 
1 2403 ASP n 
1 2404 GLU n 
1 2405 GLY n 
1 2406 GLU n 
1 2407 GLU n 
1 2408 ALA n 
1 2409 ALA n 
1 2410 SER n 
1 2411 PRO n 
1 2412 MET n 
1 2413 LEU n 
1 2414 GLN n 
1 2415 ILE n 
1 2416 GLN n 
1 2417 ARG n 
1 2418 ASP n 
1 2419 ALA n 
1 2420 ALA n 
1 2421 THR n 
1 2422 ILE n 
1 2423 MET n 
1 2424 GLN n 
1 2425 PRO n 
1 2426 TYR n 
1 2427 PHE n 
1 2428 THR n 
1 2429 SER n 
1 2430 ASN n 
1 2431 GLY n 
1 2432 LEU n 
1 2433 VAL n 
1 2434 THR n 
1 2435 LYS n 
1 2436 ALA n 
1 2437 LEU n 
1 2438 GLU n 
1 2439 HIS n 
1 2440 ALA n 
1 2441 PHE n 
1 2442 GLN n 
1 2443 LEU n 
1 2444 GLU n 
1 2445 HIS n 
1 2446 ILE n 
1 2447 MET n 
1 2448 ASP n 
1 2449 LEU n 
1 2450 THR n 
1 2451 ARG n 
1 2452 LEU n 
1 2453 ARG n 
1 2454 CYS n 
1 2455 LEU n 
1 2456 GLY n 
1 2457 SER n 
1 2458 LEU n 
1 2459 PHE n 
1 2460 SER n 
1 2461 MET n 
1 2462 LEU n 
1 2463 HIS n 
1 2464 GLN n 
1 2465 ALA n 
1 2466 CYS n 
1 2467 ARG n 
1 2468 ASN n 
1 2469 VAL n 
1 2470 ALA n 
1 2471 GLN n 
1 2472 TYR n 
1 2473 ASN n 
1 2474 ALA n 
1 2475 ASN n 
1 2476 HIS n 
1 2477 PRO n 
1 2478 ASP n 
1 2479 PHE n 
1 2480 PRO n 
1 2481 MET n 
1 2482 GLN n 
1 2483 ILE n 
1 2484 GLU n 
1 2485 GLN n 
1 2486 LEU n 
1 2487 GLU n 
1 2488 ARG n 
1 2489 TYR n 
1 2490 ILE n 
1 2491 GLN n 
1 2492 ARG n 
1 2493 TYR n 
1 2494 LEU n 
1 2495 VAL n 
1 2496 TYR n 
1 2497 ALA n 
1 2498 ILE n 
1 2499 LEU n 
1 2500 TRP n 
1 2501 SER n 
1 2502 LEU n 
1 2503 SER n 
1 2504 GLY n 
1 2505 ASP n 
1 2506 SER n 
1 2507 ARG n 
1 2508 LEU n 
1 2509 LYS n 
1 2510 MET n 
1 2511 ARG n 
1 2512 ALA n 
1 2513 GLU n 
1 2514 LEU n 
1 2515 GLY n 
1 2516 GLU n 
1 2517 TYR n 
1 2518 ILE n 
1 2519 ARG n 
1 2520 ARG n 
1 2521 ILE n 
1 2522 THR n 
1 2523 THR n 
1 2524 VAL n 
1 2525 PRO n 
1 2526 LEU n 
1 2527 PRO n 
1 2528 THR n 
1 2529 ALA n 
1 2530 PRO n 
1 2531 ASN n 
1 2532 ILE n 
1 2533 PRO n 
1 2534 ILE n 
1 2535 ILE n 
1 2536 ASP n 
1 2537 TYR n 
1 2538 GLU n 
1 2539 VAL n 
1 2540 SER n 
1 2541 ILE n 
1 2542 SER n 
1 2543 GLY n 
1 2544 GLU n 
1 2545 TRP n 
1 2546 SER n 
1 2547 PRO n 
1 2548 TRP n 
1 2549 GLN n 
1 2550 ALA n 
1 2551 LYS n 
1 2552 VAL n 
1 2553 PRO n 
1 2554 GLN n 
1 2555 ILE n 
1 2556 GLU n 
1 2557 VAL n 
1 2558 GLU n 
1 2559 THR n 
1 2560 HIS n 
1 2561 LYS n 
1 2562 VAL n 
1 2563 ALA n 
1 2564 ALA n 
1 2565 PRO n 
1 2566 ASP n 
1 2567 VAL n 
1 2568 VAL n 
1 2569 VAL n 
1 2570 PRO n 
1 2571 THR n 
1 2572 LEU n 
1 2573 ASP n 
1 2574 THR n 
1 2575 VAL n 
1 2576 ARG n 
1 2577 HIS n 
1 2578 GLU n 
1 2579 ALA n 
1 2580 LEU n 
1 2581 LEU n 
1 2582 TYR n 
1 2583 THR n 
1 2584 TRP n 
1 2585 LEU n 
1 2586 ALA n 
1 2587 GLU n 
1 2588 HIS n 
1 2589 LYS n 
1 2590 PRO n 
1 2591 LEU n 
1 2592 VAL n 
1 2593 LEU n 
1 2594 CYS n 
1 2595 GLY n 
1 2596 PRO n 
1 2597 PRO n 
1 2598 GLY n 
1 2599 SER n 
1 2600 GLY n 
1 2601 LYS n 
1 2602 THR n 
1 2603 MET n 
1 2604 THR n 
1 2605 LEU n 
1 2606 PHE n 
1 2607 SER n 
1 2608 ALA n 
1 2609 LEU n 
1 2610 ARG n 
1 2611 ALA n 
1 2612 LEU n 
1 2613 PRO n 
1 2614 ASP n 
1 2615 MET n 
1 2616 GLU n 
1 2617 VAL n 
1 2618 VAL n 
1 2619 GLY n 
1 2620 LEU n 
1 2621 ASN n 
1 2622 PHE n 
1 2623 SER n 
1 2624 SER n 
1 2625 ALA n 
1 2626 THR n 
1 2627 THR n 
1 2628 PRO n 
1 2629 GLU n 
1 2630 LEU n 
1 2631 LEU n 
1 2632 LEU n 
1 2633 LYS n 
1 2634 THR n 
1 2635 PHE n 
1 2636 ASP n 
1 2637 HIS n 
1 2638 TYR n 
1 2639 CYS n 
1 2640 GLU n 
1 2641 TYR n 
1 2642 ARG n 
1 2643 ARG n 
1 2644 THR n 
1 2645 PRO n 
1 2646 ASN n 
1 2647 GLY n 
1 2648 VAL n 
1 2649 VAL n 
1 2650 LEU n 
1 2651 ALA n 
1 2652 PRO n 
1 2653 VAL n 
1 2654 GLN n 
1 2655 LEU n 
1 2656 GLY n 
1 2657 LYS n 
1 2658 TRP n 
1 2659 LEU n 
1 2660 VAL n 
1 2661 LEU n 
1 2662 PHE n 
1 2663 CYS n 
1 2664 ASP n 
1 2665 GLU n 
1 2666 ILE n 
1 2667 ASN n 
1 2668 LEU n 
1 2669 PRO n 
1 2670 ASP n 
1 2671 MET n 
1 2672 ASP n 
1 2673 LYS n 
1 2674 TYR n 
1 2675 GLY n 
1 2676 THR n 
1 2677 GLN n 
1 2678 ARG n 
1 2679 VAL n 
1 2680 ILE n 
1 2681 SER n 
1 2682 PHE n 
1 2683 ILE n 
1 2684 ARG n 
1 2685 GLN n 
1 2686 MET n 
1 2687 VAL n 
1 2688 GLU n 
1 2689 HIS n 
1 2690 GLY n 
1 2691 GLY n 
1 2692 PHE n 
1 2693 TYR n 
1 2694 ARG n 
1 2695 THR n 
1 2696 SER n 
1 2697 ASP n 
1 2698 GLN n 
1 2699 THR n 
1 2700 TRP n 
1 2701 VAL n 
1 2702 LYS n 
1 2703 LEU n 
1 2704 GLU n 
1 2705 ARG n 
1 2706 ILE n 
1 2707 GLN n 
1 2708 PHE n 
1 2709 VAL n 
1 2710 GLY n 
1 2711 ALA n 
1 2712 CYS n 
1 2713 ASN n 
1 2714 PRO n 
1 2715 PRO n 
1 2716 THR n 
1 2717 ASP n 
1 2718 PRO n 
1 2719 GLY n 
1 2720 ARG n 
1 2721 LYS n 
1 2722 PRO n 
1 2723 LEU n 
1 2724 SER n 
1 2725 HIS n 
1 2726 ARG n 
1 2727 PHE n 
1 2728 LEU n 
1 2729 ARG n 
1 2730 HIS n 
1 2731 VAL n 
1 2732 PRO n 
1 2733 VAL n 
1 2734 VAL n 
1 2735 TYR n 
1 2736 VAL n 
1 2737 ASP n 
1 2738 TYR n 
1 2739 PRO n 
1 2740 GLY n 
1 2741 PRO n 
1 2742 ALA n 
1 2743 SER n 
1 2744 LEU n 
1 2745 THR n 
1 2746 GLN n 
1 2747 ILE n 
1 2748 TYR n 
1 2749 GLY n 
1 2750 THR n 
1 2751 PHE n 
1 2752 ASN n 
1 2753 ARG n 
1 2754 ALA n 
1 2755 MET n 
1 2756 LEU n 
1 2757 ARG n 
1 2758 LEU n 
1 2759 ILE n 
1 2760 PRO n 
1 2761 SER n 
1 2762 LEU n 
1 2763 ARG n 
1 2764 THR n 
1 2765 TYR n 
1 2766 ALA n 
1 2767 GLU n 
1 2768 PRO n 
1 2769 LEU n 
1 2770 THR n 
1 2771 ALA n 
1 2772 ALA n 
1 2773 MET n 
1 2774 VAL n 
1 2775 GLU n 
1 2776 PHE n 
1 2777 TYR n 
1 2778 THR n 
1 2779 MET n 
1 2780 SER n 
1 2781 GLN n 
1 2782 GLU n 
1 2783 ARG n 
1 2784 PHE n 
1 2785 THR n 
1 2786 GLN n 
1 2787 ASP n 
1 2788 THR n 
1 2789 GLN n 
1 2790 PRO n 
1 2791 HIS n 
1 2792 TYR n 
1 2793 ILE n 
1 2794 TYR n 
1 2795 SER n 
1 2796 PRO n 
1 2797 ARG n 
1 2798 GLU n 
1 2799 MET n 
1 2800 THR n 
1 2801 ARG n 
1 2802 TRP n 
1 2803 VAL n 
1 2804 ARG n 
1 2805 GLY n 
1 2806 ILE n 
1 2807 PHE n 
1 2808 GLU n 
1 2809 ALA n 
1 2810 LEU n 
1 2811 ARG n 
1 2812 PRO n 
1 2813 LEU n 
1 2814 GLU n 
1 2815 THR n 
1 2816 LEU n 
1 2817 PRO n 
1 2818 VAL n 
1 2819 GLU n 
1 2820 GLY n 
1 2821 LEU n 
1 2822 ILE n 
1 2823 ARG n 
1 2824 ILE n 
1 2825 TRP n 
1 2826 ALA n 
1 2827 HIS n 
1 2828 GLU n 
1 2829 ALA n 
1 2830 LEU n 
1 2831 ARG n 
1 2832 LEU n 
1 2833 PHE n 
1 2834 GLN n 
1 2835 ASP n 
1 2836 ARG n 
1 2837 LEU n 
1 2838 VAL n 
1 2839 GLU n 
1 2840 ASP n 
1 2841 GLU n 
1 2842 GLU n 
1 2843 ARG n 
1 2844 ARG n 
1 2845 TRP n 
1 2846 THR n 
1 2847 ASP n 
1 2848 GLU n 
1 2849 ASN n 
1 2850 ILE n 
1 2851 ASP n 
1 2852 THR n 
1 2853 VAL n 
1 2854 ALA n 
1 2855 LEU n 
1 2856 LYS n 
1 2857 HIS n 
1 2858 PHE n 
1 2859 PRO n 
1 2860 ASN n 
1 2861 ILE n 
1 2862 ASP n 
1 2863 ARG n 
1 2864 GLU n 
1 2865 LYS n 
1 2866 ALA n 
1 2867 MET n 
1 2868 SER n 
1 2869 ARG n 
1 2870 PRO n 
1 2871 ILE n 
1 2872 LEU n 
1 2873 TYR n 
1 2874 SER n 
1 2875 ASN n 
1 2876 TRP n 
1 2877 LEU n 
1 2878 SER n 
1 2879 LYS n 
1 2880 ASP n 
1 2881 TYR n 
1 2882 ILE n 
1 2883 PRO n 
1 2884 VAL n 
1 2885 ASP n 
1 2886 GLN n 
1 2887 GLU n 
1 2888 GLU n 
1 2889 LEU n 
1 2890 ARG n 
1 2891 ASP n 
1 2892 TYR n 
1 2893 VAL n 
1 2894 LYS n 
1 2895 ALA n 
1 2896 ARG n 
1 2897 LEU n 
1 2898 LYS n 
1 2899 VAL n 
1 2900 PHE n 
1 2901 TYR n 
1 2902 GLU n 
1 2903 GLU n 
1 2904 GLU n 
1 2905 LEU n 
1 2906 ASP n 
1 2907 VAL n 
1 2908 PRO n 
1 2909 LEU n 
1 2910 VAL n 
1 2911 LEU n 
1 2912 PHE n 
1 2913 ASN n 
1 2914 GLU n 
1 2915 VAL n 
1 2916 LEU n 
1 2917 ASP n 
1 2918 HIS n 
1 2919 VAL n 
1 2920 LEU n 
1 2921 ARG n 
1 2922 ILE n 
1 2923 ASP n 
1 2924 ARG n 
1 2925 ILE n 
1 2926 PHE n 
1 2927 ARG n 
1 2928 GLN n 
1 2929 PRO n 
1 2930 GLN n 
1 2931 GLY n 
1 2932 HIS n 
1 2933 LEU n 
1 2934 LEU n 
1 2935 LEU n 
1 2936 ILE n 
1 2937 GLY n 
1 2938 VAL n 
1 2939 SER n 
1 2940 GLY n 
1 2941 ALA n 
1 2942 GLY n 
1 2943 LYS n 
1 2944 THR n 
1 2945 THR n 
1 2946 LEU n 
1 2947 SER n 
1 2948 ARG n 
1 2949 PHE n 
1 2950 VAL n 
1 2951 ALA n 
1 2952 TRP n 
1 2953 MET n 
1 2954 ASN n 
1 2955 GLY n 
1 2956 LEU n 
1 2957 SER n 
1 2958 VAL n 
1 2959 TYR n 
1 2960 GLN n 
1 2961 ILE n 
1 2962 LYS n 
1 2963 VAL n 
1 2964 HIS n 
1 2965 ARG n 
1 2966 LYS n 
1 2967 TYR n 
1 2968 THR n 
1 2969 GLY n 
1 2970 GLU n 
1 2971 ASP n 
1 2972 PHE n 
1 2973 ASP n 
1 2974 GLU n 
1 2975 ASP n 
1 2976 LEU n 
1 2977 ARG n 
1 2978 THR n 
1 2979 VAL n 
1 2980 LEU n 
1 2981 ARG n 
1 2982 ARG n 
1 2983 SER n 
1 2984 GLY n 
1 2985 CYS n 
1 2986 LYS n 
1 2987 ASN n 
1 2988 GLU n 
1 2989 LYS n 
1 2990 ILE n 
1 2991 ALA n 
1 2992 PHE n 
1 2993 ILE n 
1 2994 MET n 
1 2995 ASP n 
1 2996 GLU n 
1 2997 SER n 
1 2998 ASN n 
1 2999 VAL n 
1 3000 LEU n 
1 3001 ASP n 
1 3002 SER n 
1 3003 GLY n 
1 3004 PHE n 
1 3005 LEU n 
1 3006 GLU n 
1 3007 ARG n 
1 3008 MET n 
1 3009 ASN n 
1 3010 THR n 
1 3011 LEU n 
1 3012 LEU n 
1 3013 ALA n 
1 3014 ASN n 
1 3015 GLY n 
1 3016 GLU n 
1 3017 VAL n 
1 3018 PRO n 
1 3019 GLY n 
1 3020 LEU n 
1 3021 PHE n 
1 3022 GLU n 
1 3023 GLY n 
1 3024 ASP n 
1 3025 GLU n 
1 3026 TYR n 
1 3027 ALA n 
1 3028 THR n 
1 3029 LEU n 
1 3030 MET n 
1 3031 THR n 
1 3032 GLN n 
1 3033 CYS n 
1 3034 LYS n 
1 3035 GLU n 
1 3036 GLY n 
1 3037 ALA n 
1 3038 GLN n 
1 3039 LYS n 
1 3040 GLU n 
1 3041 GLY n 
1 3042 LEU n 
1 3043 MET n 
1 3044 LEU n 
1 3045 ASP n 
1 3046 SER n 
1 3047 HIS n 
1 3048 GLU n 
1 3049 GLU n 
1 3050 LEU n 
1 3051 TYR n 
1 3052 LYS n 
1 3053 TRP n 
1 3054 PHE n 
1 3055 THR n 
1 3056 SER n 
1 3057 GLN n 
1 3058 VAL n 
1 3059 ILE n 
1 3060 ARG n 
1 3061 ASN n 
1 3062 LEU n 
1 3063 HIS n 
1 3064 VAL n 
1 3065 VAL n 
1 3066 PHE n 
1 3067 THR n 
1 3068 MET n 
1 3069 ASN n 
1 3070 PRO n 
1 3071 SER n 
1 3072 SER n 
1 3073 GLU n 
1 3074 GLY n 
1 3075 LEU n 
1 3076 LYS n 
1 3077 ASP n 
1 3078 ARG n 
1 3079 ALA n 
1 3080 ALA n 
1 3081 THR n 
1 3082 SER n 
1 3083 PRO n 
1 3084 ALA n 
1 3085 LEU n 
1 3086 PHE n 
1 3087 ASN n 
1 3088 ARG n 
1 3089 CYS n 
1 3090 VAL n 
1 3091 LEU n 
1 3092 ASN n 
1 3093 TRP n 
1 3094 PHE n 
1 3095 GLY n 
1 3096 ASP n 
1 3097 TRP n 
1 3098 SER n 
1 3099 THR n 
1 3100 GLU n 
1 3101 ALA n 
1 3102 LEU n 
1 3103 TYR n 
1 3104 GLN n 
1 3105 VAL n 
1 3106 GLY n 
1 3107 LYS n 
1 3108 GLU n 
1 3109 PHE n 
1 3110 THR n 
1 3111 SER n 
1 3112 LYS n 
1 3113 MET n 
1 3114 ASP n 
1 3115 LEU n 
1 3116 GLU n 
1 3117 LYS n 
1 3118 PRO n 
1 3119 ASN n 
1 3120 TYR n 
1 3121 ILE n 
1 3122 VAL n 
1 3123 PRO n 
1 3124 ASP n 
1 3125 TYR n 
1 3126 MET n 
1 3127 PRO n 
1 3128 VAL n 
1 3129 VAL n 
1 3130 TYR n 
1 3131 ASP n 
1 3132 LYS n 
1 3133 LEU n 
1 3134 PRO n 
1 3135 GLN n 
1 3136 PRO n 
1 3137 PRO n 
1 3138 SER n 
1 3139 HIS n 
1 3140 ARG n 
1 3141 GLU n 
1 3142 ALA n 
1 3143 ILE n 
1 3144 VAL n 
1 3145 ASN n 
1 3146 SER n 
1 3147 CYS n 
1 3148 VAL n 
1 3149 PHE n 
1 3150 VAL n 
1 3151 HIS n 
1 3152 GLN n 
1 3153 THR n 
1 3154 LEU n 
1 3155 HIS n 
1 3156 GLN n 
1 3157 ALA n 
1 3158 ASN n 
1 3159 ALA n 
1 3160 ARG n 
1 3161 LEU n 
1 3162 ALA n 
1 3163 LYS n 
1 3164 ARG n 
1 3165 GLY n 
1 3166 GLY n 
1 3167 ARG n 
1 3168 THR n 
1 3169 MET n 
1 3170 ALA n 
1 3171 ILE n 
1 3172 THR n 
1 3173 PRO n 
1 3174 ARG n 
1 3175 HIS n 
1 3176 TYR n 
1 3177 LEU n 
1 3178 ASP n 
1 3179 PHE n 
1 3180 ILE n 
1 3181 ASN n 
1 3182 HIS n 
1 3183 TYR n 
1 3184 ALA n 
1 3185 ASN n 
1 3186 LEU n 
1 3187 PHE n 
1 3188 HIS n 
1 3189 GLU n 
1 3190 LYS n 
1 3191 ARG n 
1 3192 SER n 
1 3193 GLU n 
1 3194 LEU n 
1 3195 GLU n 
1 3196 GLU n 
1 3197 GLN n 
1 3198 GLN n 
1 3199 MET n 
1 3200 HIS n 
1 3201 LEU n 
1 3202 ASN n 
1 3203 VAL n 
1 3204 GLY n 
1 3205 LEU n 
1 3206 ARG n 
1 3207 LYS n 
1 3208 ILE n 
1 3209 LYS n 
1 3210 GLU n 
1 3211 THR n 
1 3212 VAL n 
1 3213 ASP n 
1 3214 GLN n 
1 3215 VAL n 
1 3216 GLU n 
1 3217 GLU n 
1 3218 LEU n 
1 3219 ARG n 
1 3220 ARG n 
1 3221 ASP n 
1 3222 LEU n 
1 3223 ARG n 
1 3224 ILE n 
1 3225 LYS n 
1 3226 SER n 
1 3227 GLN n 
1 3228 GLU n 
1 3229 LEU n 
1 3230 GLU n 
1 3231 VAL n 
1 3232 LYS n 
1 3233 ASN n 
1 3234 ALA n 
1 3235 ALA n 
1 3236 ALA n 
1 3237 ASN n 
1 3238 ASP n 
1 3239 LYS n 
1 3240 LEU n 
1 3241 LYS n 
1 3242 LYS n 
1 3243 MET n 
1 3244 VAL n 
1 3245 LYS n 
1 3246 ASP n 
1 3247 GLN n 
1 3248 GLN n 
1 3249 GLU n 
1 3250 ALA n 
1 3251 GLU n 
1 3252 LYS n 
1 3253 LYS n 
1 3254 LYS n 
1 3255 VAL n 
1 3256 MET n 
1 3257 SER n 
1 3258 GLN n 
1 3259 GLU n 
1 3260 ILE n 
1 3261 GLN n 
1 3262 GLU n 
1 3263 GLN n 
1 3264 LEU n 
1 3265 HIS n 
1 3266 LYS n 
1 3267 GLN n 
1 3268 GLN n 
1 3269 GLU n 
1 3270 VAL n 
1 3271 ILE n 
1 3272 ALA n 
1 3273 ASP n 
1 3274 LYS n 
1 3275 GLN n 
1 3276 MET n 
1 3277 SER n 
1 3278 VAL n 
1 3279 LYS n 
1 3280 GLU n 
1 3281 ASP n 
1 3282 LEU n 
1 3283 ASP n 
1 3284 LYS n 
1 3285 VAL n 
1 3286 GLU n 
1 3287 PRO n 
1 3288 ALA n 
1 3289 VAL n 
1 3290 ILE n 
1 3291 GLU n 
1 3292 ALA n 
1 3293 GLN n 
1 3294 ASN n 
1 3295 ALA n 
1 3296 VAL n 
1 3297 LYS n 
1 3298 SER n 
1 3299 ILE n 
1 3300 LYS n 
1 3301 LYS n 
1 3302 GLN n 
1 3303 HIS n 
1 3304 LEU n 
1 3305 VAL n 
1 3306 GLU n 
1 3307 VAL n 
1 3308 ARG n 
1 3309 SER n 
1 3310 MET n 
1 3311 ALA n 
1 3312 ASN n 
1 3313 PRO n 
1 3314 PRO n 
1 3315 ALA n 
1 3316 ALA n 
1 3317 VAL n 
1 3318 LYS n 
1 3319 LEU n 
1 3320 ALA n 
1 3321 LEU n 
1 3322 GLU n 
1 3323 SER n 
1 3324 ILE n 
1 3325 CYS n 
1 3326 LEU n 
1 3327 LEU n 
1 3328 LEU n 
1 3329 GLY n 
1 3330 GLU n 
1 3331 SER n 
1 3332 THR n 
1 3333 THR n 
1 3334 ASP n 
1 3335 TRP n 
1 3336 LYS n 
1 3337 GLN n 
1 3338 ILE n 
1 3339 ARG n 
1 3340 SER n 
1 3341 ILE n 
1 3342 ILE n 
1 3343 MET n 
1 3344 ARG n 
1 3345 GLU n 
1 3346 ASN n 
1 3347 PHE n 
1 3348 ILE n 
1 3349 PRO n 
1 3350 THR n 
1 3351 ILE n 
1 3352 VAL n 
1 3353 ASN n 
1 3354 PHE n 
1 3355 SER n 
1 3356 ALA n 
1 3357 GLU n 
1 3358 GLU n 
1 3359 ILE n 
1 3360 SER n 
1 3361 ASP n 
1 3362 ALA n 
1 3363 ILE n 
1 3364 ARG n 
1 3365 GLU n 
1 3366 LYS n 
1 3367 MET n 
1 3368 LYS n 
1 3369 LYS n 
1 3370 ASN n 
1 3371 TYR n 
1 3372 MET n 
1 3373 SER n 
1 3374 ASN n 
1 3375 PRO n 
1 3376 SER n 
1 3377 TYR n 
1 3378 ASN n 
1 3379 TYR n 
1 3380 GLU n 
1 3381 ILE n 
1 3382 VAL n 
1 3383 ASN n 
1 3384 ARG n 
1 3385 ALA n 
1 3386 SER n 
1 3387 LEU n 
1 3388 ALA n 
1 3389 CYS n 
1 3390 GLY n 
1 3391 PRO n 
1 3392 MET n 
1 3393 VAL n 
1 3394 LYS n 
1 3395 TRP n 
1 3396 ALA n 
1 3397 ILE n 
1 3398 ALA n 
1 3399 GLN n 
1 3400 LEU n 
1 3401 ASN n 
1 3402 TYR n 
1 3403 ALA n 
1 3404 ASP n 
1 3405 MET n 
1 3406 LEU n 
1 3407 LYS n 
1 3408 ARG n 
1 3409 VAL n 
1 3410 GLU n 
1 3411 PRO n 
1 3412 LEU n 
1 3413 ARG n 
1 3414 ASN n 
1 3415 GLU n 
1 3416 LEU n 
1 3417 GLN n 
1 3418 LYS n 
1 3419 LEU n 
1 3420 GLU n 
1 3421 ASP n 
1 3422 ASP n 
1 3423 ALA n 
1 3424 LYS n 
1 3425 ASP n 
1 3426 ASN n 
1 3427 GLN n 
1 3428 GLN n 
1 3429 LYS n 
1 3430 ALA n 
1 3431 ASN n 
1 3432 GLU n 
1 3433 VAL n 
1 3434 GLU n 
1 3435 GLN n 
1 3436 MET n 
1 3437 ILE n 
1 3438 ARG n 
1 3439 ASP n 
1 3440 LEU n 
1 3441 GLU n 
1 3442 ALA n 
1 3443 SER n 
1 3444 ILE n 
1 3445 ALA n 
1 3446 ARG n 
1 3447 TYR n 
1 3448 LYS n 
1 3449 GLU n 
1 3450 GLU n 
1 3451 TYR n 
1 3452 ALA n 
1 3453 VAL n 
1 3454 LEU n 
1 3455 ILE n 
1 3456 SER n 
1 3457 GLU n 
1 3458 ALA n 
1 3459 GLN n 
1 3460 ALA n 
1 3461 ILE n 
1 3462 LYS n 
1 3463 ALA n 
1 3464 ASP n 
1 3465 LEU n 
1 3466 ALA n 
1 3467 ALA n 
1 3468 VAL n 
1 3469 GLU n 
1 3470 ALA n 
1 3471 LYS n 
1 3472 VAL n 
1 3473 ASN n 
1 3474 ARG n 
1 3475 SER n 
1 3476 THR n 
1 3477 ALA n 
1 3478 LEU n 
1 3479 LEU n 
1 3480 LYS n 
1 3481 SER n 
1 3482 LEU n 
1 3483 SER n 
1 3484 ALA n 
1 3485 GLU n 
1 3486 ARG n 
1 3487 GLU n 
1 3488 ARG n 
1 3489 TRP n 
1 3490 GLU n 
1 3491 LYS n 
1 3492 THR n 
1 3493 SER n 
1 3494 GLU n 
1 3495 THR n 
1 3496 PHE n 
1 3497 LYS n 
1 3498 ASN n 
1 3499 GLN n 
1 3500 MET n 
1 3501 SER n 
1 3502 THR n 
1 3503 ILE n 
1 3504 ALA n 
1 3505 GLY n 
1 3506 ASP n 
1 3507 CYS n 
1 3508 LEU n 
1 3509 LEU n 
1 3510 SER n 
1 3511 ALA n 
1 3512 ALA n 
1 3513 PHE n 
1 3514 ILE n 
1 3515 ALA n 
1 3516 TYR n 
1 3517 ALA n 
1 3518 GLY n 
1 3519 TYR n 
1 3520 PHE n 
1 3521 ASP n 
1 3522 GLN n 
1 3523 GLN n 
1 3524 MET n 
1 3525 ARG n 
1 3526 GLN n 
1 3527 ASN n 
1 3528 LEU n 
1 3529 PHE n 
1 3530 THR n 
1 3531 THR n 
1 3532 TRP n 
1 3533 SER n 
1 3534 HIS n 
1 3535 HIS n 
1 3536 LEU n 
1 3537 GLN n 
1 3538 GLN n 
1 3539 ALA n 
1 3540 ASN n 
1 3541 ILE n 
1 3542 GLN n 
1 3543 PHE n 
1 3544 ARG n 
1 3545 THR n 
1 3546 ASP n 
1 3547 ILE n 
1 3548 ALA n 
1 3549 ARG n 
1 3550 THR n 
1 3551 GLU n 
1 3552 TYR n 
1 3553 LEU n 
1 3554 SER n 
1 3555 ASN n 
1 3556 ALA n 
1 3557 ASP n 
1 3558 GLU n 
1 3559 ARG n 
1 3560 LEU n 
1 3561 ARG n 
1 3562 TRP n 
1 3563 GLN n 
1 3564 ALA n 
1 3565 SER n 
1 3566 SER n 
1 3567 LEU n 
1 3568 PRO n 
1 3569 ALA n 
1 3570 ASP n 
1 3571 ASP n 
1 3572 LEU n 
1 3573 CYS n 
1 3574 THR n 
1 3575 GLU n 
1 3576 ASN n 
1 3577 ALA n 
1 3578 ILE n 
1 3579 MET n 
1 3580 LEU n 
1 3581 LYS n 
1 3582 ARG n 
1 3583 PHE n 
1 3584 ASN n 
1 3585 ARG n 
1 3586 TYR n 
1 3587 PRO n 
1 3588 LEU n 
1 3589 ILE n 
1 3590 ILE n 
1 3591 ASP n 
1 3592 PRO n 
1 3593 SER n 
1 3594 GLY n 
1 3595 GLN n 
1 3596 ALA n 
1 3597 THR n 
1 3598 GLU n 
1 3599 PHE n 
1 3600 ILE n 
1 3601 MET n 
1 3602 ASN n 
1 3603 GLU n 
1 3604 TYR n 
1 3605 LYS n 
1 3606 ASP n 
1 3607 ARG n 
1 3608 LYS n 
1 3609 ILE n 
1 3610 THR n 
1 3611 ARG n 
1 3612 THR n 
1 3613 SER n 
1 3614 PHE n 
1 3615 LEU n 
1 3616 ASP n 
1 3617 ASP n 
1 3618 ALA n 
1 3619 PHE n 
1 3620 ARG n 
1 3621 LYS n 
1 3622 ASN n 
1 3623 LEU n 
1 3624 GLU n 
1 3625 SER n 
1 3626 ALA n 
1 3627 LEU n 
1 3628 ARG n 
1 3629 PHE n 
1 3630 GLY n 
1 3631 ASN n 
1 3632 PRO n 
1 3633 LEU n 
1 3634 LEU n 
1 3635 VAL n 
1 3636 GLN n 
1 3637 ASP n 
1 3638 VAL n 
1 3639 GLU n 
1 3640 SER n 
1 3641 TYR n 
1 3642 ASP n 
1 3643 PRO n 
1 3644 VAL n 
1 3645 LEU n 
1 3646 ASN n 
1 3647 PRO n 
1 3648 VAL n 
1 3649 LEU n 
1 3650 ASN n 
1 3651 ARG n 
1 3652 GLU n 
1 3653 VAL n 
1 3654 ARG n 
1 3655 ARG n 
1 3656 THR n 
1 3657 GLY n 
1 3658 GLY n 
1 3659 ARG n 
1 3660 VAL n 
1 3661 LEU n 
1 3662 ILE n 
1 3663 THR n 
1 3664 LEU n 
1 3665 GLY n 
1 3666 ASP n 
1 3667 GLN n 
1 3668 ASP n 
1 3669 ILE n 
1 3670 ASP n 
1 3671 LEU n 
1 3672 SER n 
1 3673 PRO n 
1 3674 SER n 
1 3675 PHE n 
1 3676 VAL n 
1 3677 ILE n 
1 3678 PHE n 
1 3679 LEU n 
1 3680 SER n 
1 3681 THR n 
1 3682 ARG n 
1 3683 ASP n 
1 3684 PRO n 
1 3685 THR n 
1 3686 VAL n 
1 3687 GLU n 
1 3688 PHE n 
1 3689 PRO n 
1 3690 PRO n 
1 3691 ASP n 
1 3692 LEU n 
1 3693 CYS n 
1 3694 SER n 
1 3695 ARG n 
1 3696 VAL n 
1 3697 THR n 
1 3698 PHE n 
1 3699 VAL n 
1 3700 ASN n 
1 3701 PHE n 
1 3702 THR n 
1 3703 VAL n 
1 3704 THR n 
1 3705 ARG n 
1 3706 SER n 
1 3707 SER n 
1 3708 LEU n 
1 3709 GLN n 
1 3710 SER n 
1 3711 GLN n 
1 3712 CYS n 
1 3713 LEU n 
1 3714 ASN n 
1 3715 GLU n 
1 3716 VAL n 
1 3717 LEU n 
1 3718 LYS n 
1 3719 ALA n 
1 3720 GLU n 
1 3721 ARG n 
1 3722 PRO n 
1 3723 ASP n 
1 3724 VAL n 
1 3725 ASP n 
1 3726 GLU n 
1 3727 LYS n 
1 3728 ARG n 
1 3729 SER n 
1 3730 ASP n 
1 3731 LEU n 
1 3732 LEU n 
1 3733 LYS n 
1 3734 LEU n 
1 3735 GLN n 
1 3736 GLY n 
1 3737 GLU n 
1 3738 PHE n 
1 3739 GLN n 
1 3740 LEU n 
1 3741 ARG n 
1 3742 LEU n 
1 3743 ARG n 
1 3744 GLN n 
1 3745 LEU n 
1 3746 GLU n 
1 3747 LYS n 
1 3748 SER n 
1 3749 LEU n 
1 3750 LEU n 
1 3751 GLN n 
1 3752 ALA n 
1 3753 LEU n 
1 3754 ASN n 
1 3755 GLU n 
1 3756 VAL n 
1 3757 LYS n 
1 3758 GLY n 
1 3759 ARG n 
1 3760 ILE n 
1 3761 LEU n 
1 3762 ASP n 
1 3763 ASP n 
1 3764 ASP n 
1 3765 THR n 
1 3766 ILE n 
1 3767 ILE n 
1 3768 THR n 
1 3769 THR n 
1 3770 LEU n 
1 3771 GLU n 
1 3772 ASN n 
1 3773 LEU n 
1 3774 LYS n 
1 3775 ARG n 
1 3776 GLU n 
1 3777 ALA n 
1 3778 ALA n 
1 3779 GLU n 
1 3780 VAL n 
1 3781 THR n 
1 3782 ARG n 
1 3783 LYS n 
1 3784 VAL n 
1 3785 GLU n 
1 3786 GLU n 
1 3787 THR n 
1 3788 ASP n 
1 3789 ILE n 
1 3790 VAL n 
1 3791 MET n 
1 3792 GLN n 
1 3793 GLU n 
1 3794 VAL n 
1 3795 GLU n 
1 3796 THR n 
1 3797 VAL n 
1 3798 SER n 
1 3799 GLN n 
1 3800 GLN n 
1 3801 TYR n 
1 3802 LEU n 
1 3803 PRO n 
1 3804 LEU n 
1 3805 SER n 
1 3806 THR n 
1 3807 ALA n 
1 3808 CYS n 
1 3809 SER n 
1 3810 SER n 
1 3811 ILE n 
1 3812 TYR n 
1 3813 PHE n 
1 3814 THR n 
1 3815 MET n 
1 3816 GLU n 
1 3817 SER n 
1 3818 LEU n 
1 3819 LYS n 
1 3820 GLN n 
1 3821 ILE n 
1 3822 HIS n 
1 3823 PHE n 
1 3824 LEU n 
1 3825 TYR n 
1 3826 GLN n 
1 3827 TYR n 
1 3828 SER n 
1 3829 LEU n 
1 3830 GLN n 
1 3831 PHE n 
1 3832 PHE n 
1 3833 LEU n 
1 3834 ASP n 
1 3835 ILE n 
1 3836 TYR n 
1 3837 HIS n 
1 3838 ASN n 
1 3839 VAL n 
1 3840 LEU n 
1 3841 TYR n 
1 3842 GLU n 
1 3843 ASN n 
1 3844 PRO n 
1 3845 ASN n 
1 3846 LEU n 
1 3847 LYS n 
1 3848 GLY n 
1 3849 VAL n 
1 3850 THR n 
1 3851 ASP n 
1 3852 HIS n 
1 3853 THR n 
1 3854 GLN n 
1 3855 ARG n 
1 3856 LEU n 
1 3857 SER n 
1 3858 ILE n 
1 3859 ILE n 
1 3860 THR n 
1 3861 LYS n 
1 3862 ASP n 
1 3863 LEU n 
1 3864 PHE n 
1 3865 GLN n 
1 3866 VAL n 
1 3867 ALA n 
1 3868 PHE n 
1 3869 ASN n 
1 3870 ARG n 
1 3871 VAL n 
1 3872 ALA n 
1 3873 ARG n 
1 3874 GLY n 
1 3875 MET n 
1 3876 LEU n 
1 3877 HIS n 
1 3878 GLN n 
1 3879 ASP n 
1 3880 HIS n 
1 3881 ILE n 
1 3882 THR n 
1 3883 PHE n 
1 3884 ALA n 
1 3885 MET n 
1 3886 LEU n 
1 3887 LEU n 
1 3888 ALA n 
1 3889 ARG n 
1 3890 ILE n 
1 3891 LYS n 
1 3892 LEU n 
1 3893 LYS n 
1 3894 GLY n 
1 3895 THR n 
1 3896 VAL n 
1 3897 GLY n 
1 3898 GLU n 
1 3899 PRO n 
1 3900 THR n 
1 3901 TYR n 
1 3902 ASP n 
1 3903 ALA n 
1 3904 GLU n 
1 3905 PHE n 
1 3906 GLN n 
1 3907 HIS n 
1 3908 PHE n 
1 3909 LEU n 
1 3910 ARG n 
1 3911 GLY n 
1 3912 ASN n 
1 3913 GLU n 
1 3914 ILE n 
1 3915 VAL n 
1 3916 LEU n 
1 3917 SER n 
1 3918 ALA n 
1 3919 GLY n 
1 3920 SER n 
1 3921 THR n 
1 3922 PRO n 
1 3923 ARG n 
1 3924 ILE n 
1 3925 GLN n 
1 3926 GLY n 
1 3927 LEU n 
1 3928 THR n 
1 3929 VAL n 
1 3930 GLU n 
1 3931 GLN n 
1 3932 ALA n 
1 3933 GLU n 
1 3934 ALA n 
1 3935 VAL n 
1 3936 VAL n 
1 3937 ARG n 
1 3938 LEU n 
1 3939 SER n 
1 3940 CYS n 
1 3941 LEU n 
1 3942 PRO n 
1 3943 ALA n 
1 3944 PHE n 
1 3945 LYS n 
1 3946 ASP n 
1 3947 LEU n 
1 3948 ILE n 
1 3949 ALA n 
1 3950 LYS n 
1 3951 VAL n 
1 3952 GLN n 
1 3953 ALA n 
1 3954 ASP n 
1 3955 GLU n 
1 3956 GLN n 
1 3957 PHE n 
1 3958 GLY n 
1 3959 ILE n 
1 3960 TRP n 
1 3961 LEU n 
1 3962 ASP n 
1 3963 SER n 
1 3964 SER n 
1 3965 SER n 
1 3966 PRO n 
1 3967 GLU n 
1 3968 GLN n 
1 3969 THR n 
1 3970 VAL n 
1 3971 PRO n 
1 3972 TYR n 
1 3973 LEU n 
1 3974 TRP n 
1 3975 SER n 
1 3976 GLU n 
1 3977 GLU n 
1 3978 THR n 
1 3979 PRO n 
1 3980 ALA n 
1 3981 THR n 
1 3982 PRO n 
1 3983 ILE n 
1 3984 GLY n 
1 3985 GLN n 
1 3986 ALA n 
1 3987 ILE n 
1 3988 HIS n 
1 3989 ARG n 
1 3990 LEU n 
1 3991 LEU n 
1 3992 LEU n 
1 3993 ILE n 
1 3994 GLN n 
1 3995 ALA n 
1 3996 PHE n 
1 3997 ARG n 
1 3998 PRO n 
1 3999 ASP n 
1 4000 ARG n 
1 4001 LEU n 
1 4002 LEU n 
1 4003 ALA n 
1 4004 MET n 
1 4005 ALA n 
1 4006 HIS n 
1 4007 MET n 
1 4008 PHE n 
1 4009 VAL n 
1 4010 SER n 
1 4011 THR n 
1 4012 ASN n 
1 4013 LEU n 
1 4014 GLY n 
1 4015 GLU n 
1 4016 SER n 
1 4017 PHE n 
1 4018 MET n 
1 4019 SER n 
1 4020 ILE n 
1 4021 MET n 
1 4022 GLU n 
1 4023 GLN n 
1 4024 PRO n 
1 4025 LEU n 
1 4026 ASP n 
1 4027 LEU n 
1 4028 THR n 
1 4029 HIS n 
1 4030 ILE n 
1 4031 VAL n 
1 4032 GLY n 
1 4033 THR n 
1 4034 GLU n 
1 4035 VAL n 
1 4036 LYS n 
1 4037 PRO n 
1 4038 ASN n 
1 4039 THR n 
1 4040 PRO n 
1 4041 VAL n 
1 4042 LEU n 
1 4043 MET n 
1 4044 CYS n 
1 4045 SER n 
1 4046 VAL n 
1 4047 PRO n 
1 4048 GLY n 
1 4049 TYR n 
1 4050 ASP n 
1 4051 ALA n 
1 4052 SER n 
1 4053 GLY n 
1 4054 HIS n 
1 4055 VAL n 
1 4056 GLU n 
1 4057 ASP n 
1 4058 LEU n 
1 4059 ALA n 
1 4060 ALA n 
1 4061 GLU n 
1 4062 GLN n 
1 4063 ASN n 
1 4064 THR n 
1 4065 GLN n 
1 4066 ILE n 
1 4067 THR n 
1 4068 SER n 
1 4069 ILE n 
1 4070 ALA n 
1 4071 ILE n 
1 4072 GLY n 
1 4073 SER n 
1 4074 ALA n 
1 4075 GLU n 
1 4076 GLY n 
1 4077 PHE n 
1 4078 ASN n 
1 4079 GLN n 
1 4080 ALA n 
1 4081 ASP n 
1 4082 LYS n 
1 4083 ALA n 
1 4084 ILE n 
1 4085 ASN n 
1 4086 THR n 
1 4087 ALA n 
1 4088 VAL n 
1 4089 LYS n 
1 4090 SER n 
1 4091 GLY n 
1 4092 ARG n 
1 4093 TRP n 
1 4094 VAL n 
1 4095 MET n 
1 4096 LEU n 
1 4097 LYS n 
1 4098 ASN n 
1 4099 VAL n 
1 4100 HIS n 
1 4101 LEU n 
1 4102 ALA n 
1 4103 PRO n 
1 4104 GLY n 
1 4105 TRP n 
1 4106 LEU n 
1 4107 MET n 
1 4108 GLN n 
1 4109 LEU n 
1 4110 GLU n 
1 4111 LYS n 
1 4112 LYS n 
1 4113 LEU n 
1 4114 HIS n 
1 4115 SER n 
1 4116 LEU n 
1 4117 GLN n 
1 4118 PRO n 
1 4119 HIS n 
1 4120 ALA n 
1 4121 CYS n 
1 4122 PHE n 
1 4123 ARG n 
1 4124 LEU n 
1 4125 PHE n 
1 4126 LEU n 
1 4127 THR n 
1 4128 MET n 
1 4129 GLU n 
1 4130 ILE n 
1 4131 ASN n 
1 4132 PRO n 
1 4133 LYS n 
1 4134 VAL n 
1 4135 PRO n 
1 4136 VAL n 
1 4137 ASN n 
1 4138 LEU n 
1 4139 LEU n 
1 4140 ARG n 
1 4141 ALA n 
1 4142 GLY n 
1 4143 ARG n 
1 4144 ILE n 
1 4145 PHE n 
1 4146 VAL n 
1 4147 PHE n 
1 4148 GLU n 
1 4149 PRO n 
1 4150 PRO n 
1 4151 PRO n 
1 4152 GLY n 
1 4153 VAL n 
1 4154 LYS n 
1 4155 ALA n 
1 4156 ASN n 
1 4157 MET n 
1 4158 LEU n 
1 4159 ARG n 
1 4160 THR n 
1 4161 PHE n 
1 4162 SER n 
1 4163 SER n 
1 4164 ILE n 
1 4165 PRO n 
1 4166 VAL n 
1 4167 SER n 
1 4168 ARG n 
1 4169 ILE n 
1 4170 CYS n 
1 4171 LYS n 
1 4172 SER n 
1 4173 PRO n 
1 4174 ASN n 
1 4175 GLU n 
1 4176 ARG n 
1 4177 ALA n 
1 4178 ARG n 
1 4179 LEU n 
1 4180 TYR n 
1 4181 PHE n 
1 4182 LEU n 
1 4183 LEU n 
1 4184 ALA n 
1 4185 TRP n 
1 4186 PHE n 
1 4187 HIS n 
1 4188 ALA n 
1 4189 ILE n 
1 4190 ILE n 
1 4191 GLN n 
1 4192 GLU n 
1 4193 ARG n 
1 4194 LEU n 
1 4195 ARG n 
1 4196 TYR n 
1 4197 ALA n 
1 4198 PRO n 
1 4199 LEU n 
1 4200 GLY n 
1 4201 TRP n 
1 4202 SER n 
1 4203 LYS n 
1 4204 LYS n 
1 4205 TYR n 
1 4206 GLU n 
1 4207 PHE n 
1 4208 GLY n 
1 4209 GLU n 
1 4210 SER n 
1 4211 ASP n 
1 4212 LEU n 
1 4213 ARG n 
1 4214 SER n 
1 4215 ALA n 
1 4216 CYS n 
1 4217 ASP n 
1 4218 THR n 
1 4219 VAL n 
1 4220 ASP n 
1 4221 THR n 
1 4222 TRP n 
1 4223 LEU n 
1 4224 ASP n 
1 4225 ASP n 
1 4226 THR n 
1 4227 ALA n 
1 4228 LYS n 
1 4229 GLY n 
1 4230 ARG n 
1 4231 GLN n 
1 4232 ASN n 
1 4233 ILE n 
1 4234 SER n 
1 4235 PRO n 
1 4236 ASP n 
1 4237 LYS n 
1 4238 ILE n 
1 4239 PRO n 
1 4240 TRP n 
1 4241 SER n 
1 4242 ALA n 
1 4243 LEU n 
1 4244 LYS n 
1 4245 THR n 
1 4246 LEU n 
1 4247 MET n 
1 4248 ALA n 
1 4249 GLN n 
1 4250 SER n 
1 4251 ILE n 
1 4252 TYR n 
1 4253 GLY n 
1 4254 GLY n 
1 4255 ARG n 
1 4256 VAL n 
1 4257 ASP n 
1 4258 ASN n 
1 4259 GLU n 
1 4260 PHE n 
1 4261 ASP n 
1 4262 GLN n 
1 4263 ARG n 
1 4264 LEU n 
1 4265 LEU n 
1 4266 ASN n 
1 4267 THR n 
1 4268 PHE n 
1 4269 LEU n 
1 4270 GLU n 
1 4271 ARG n 
1 4272 LEU n 
1 4273 PHE n 
1 4274 THR n 
1 4275 THR n 
1 4276 ARG n 
1 4277 SER n 
1 4278 PHE n 
1 4279 ASP n 
1 4280 SER n 
1 4281 GLU n 
1 4282 PHE n 
1 4283 LYS n 
1 4284 LEU n 
1 4285 ALA n 
1 4286 CYS n 
1 4287 LYS n 
1 4288 VAL n 
1 4289 ASP n 
1 4290 GLY n 
1 4291 HIS n 
1 4292 LYS n 
1 4293 ASP n 
1 4294 ILE n 
1 4295 GLN n 
1 4296 MET n 
1 4297 PRO n 
1 4298 ASP n 
1 4299 GLY n 
1 4300 ILE n 
1 4301 ARG n 
1 4302 ARG n 
1 4303 GLU n 
1 4304 GLU n 
1 4305 PHE n 
1 4306 VAL n 
1 4307 GLN n 
1 4308 TRP n 
1 4309 VAL n 
1 4310 GLU n 
1 4311 LEU n 
1 4312 LEU n 
1 4313 PRO n 
1 4314 ASP n 
1 4315 THR n 
1 4316 GLN n 
1 4317 THR n 
1 4318 PRO n 
1 4319 SER n 
1 4320 TRP n 
1 4321 LEU n 
1 4322 GLY n 
1 4323 LEU n 
1 4324 PRO n 
1 4325 ASN n 
1 4326 ASN n 
1 4327 ALA n 
1 4328 GLU n 
1 4329 ARG n 
1 4330 VAL n 
1 4331 LEU n 
1 4332 LEU n 
1 4333 THR n 
1 4334 THR n 
1 4335 GLN n 
1 4336 GLY n 
1 4337 VAL n 
1 4338 ASP n 
1 4339 MET n 
1 4340 ILE n 
1 4341 SER n 
1 4342 LYS n 
1 4343 MET n 
1 4344 LEU n 
1 4345 LYS n 
1 4346 MET n 
1 4347 GLN n 
1 4348 MET n 
1 4349 LEU n 
1 4350 GLU n 
1 4351 ASP n 
1 4352 GLU n 
1 4353 ASP n 
1 4354 ASP n 
1 4355 LEU n 
1 4356 ALA n 
1 4357 TYR n 
1 4358 ALA n 
1 4359 GLU n 
1 4360 THR n 
1 4361 GLU n 
1 4362 LYS n 
1 4363 LYS n 
1 4364 THR n 
1 4365 ARG n 
1 4366 THR n 
1 4367 ASP n 
1 4368 SER n 
1 4369 THR n 
1 4370 SER n 
1 4371 ASP n 
1 4372 GLY n 
1 4373 ARG n 
1 4374 PRO n 
1 4375 ALA n 
1 4376 TRP n 
1 4377 MET n 
1 4378 ARG n 
1 4379 THR n 
1 4380 LEU n 
1 4381 HIS n 
1 4382 THR n 
1 4383 THR n 
1 4384 ALA n 
1 4385 SER n 
1 4386 ASN n 
1 4387 TRP n 
1 4388 LEU n 
1 4389 HIS n 
1 4390 LEU n 
1 4391 ILE n 
1 4392 PRO n 
1 4393 GLN n 
1 4394 THR n 
1 4395 LEU n 
1 4396 SER n 
1 4397 HIS n 
1 4398 LEU n 
1 4399 LYS n 
1 4400 ARG n 
1 4401 THR n 
1 4402 VAL n 
1 4403 GLU n 
1 4404 ASN n 
1 4405 ILE n 
1 4406 LYS n 
1 4407 ASP n 
1 4408 PRO n 
1 4409 LEU n 
1 4410 PHE n 
1 4411 ARG n 
1 4412 PHE n 
1 4413 PHE n 
1 4414 GLU n 
1 4415 ARG n 
1 4416 GLU n 
1 4417 VAL n 
1 4418 LYS n 
1 4419 MET n 
1 4420 GLY n 
1 4421 ALA n 
1 4422 LYS n 
1 4423 LEU n 
1 4424 LEU n 
1 4425 GLN n 
1 4426 ASP n 
1 4427 VAL n 
1 4428 ARG n 
1 4429 GLN n 
1 4430 ASP n 
1 4431 LEU n 
1 4432 ALA n 
1 4433 ASP n 
1 4434 VAL n 
1 4435 VAL n 
1 4436 GLN n 
1 4437 VAL n 
1 4438 CYS n 
1 4439 GLU n 
1 4440 GLY n 
1 4441 LYS n 
1 4442 LYS n 
1 4443 LYS n 
1 4444 GLN n 
1 4445 THR n 
1 4446 ASN n 
1 4447 TYR n 
1 4448 LEU n 
1 4449 ARG n 
1 4450 THR n 
1 4451 LEU n 
1 4452 ILE n 
1 4453 ASN n 
1 4454 GLU n 
1 4455 LEU n 
1 4456 VAL n 
1 4457 LYS n 
1 4458 GLY n 
1 4459 ILE n 
1 4460 LEU n 
1 4461 PRO n 
1 4462 ARG n 
1 4463 SER n 
1 4464 TRP n 
1 4465 SER n 
1 4466 HIS n 
1 4467 TYR n 
1 4468 THR n 
1 4469 VAL n 
1 4470 PRO n 
1 4471 ALA n 
1 4472 GLY n 
1 4473 MET n 
1 4474 THR n 
1 4475 VAL n 
1 4476 ILE n 
1 4477 GLN n 
1 4478 TRP n 
1 4479 VAL n 
1 4480 SER n 
1 4481 ASP n 
1 4482 PHE n 
1 4483 SER n 
1 4484 GLU n 
1 4485 ARG n 
1 4486 ILE n 
1 4487 LYS n 
1 4488 GLN n 
1 4489 LEU n 
1 4490 GLN n 
1 4491 ASN n 
1 4492 ILE n 
1 4493 SER n 
1 4494 LEU n 
1 4495 ALA n 
1 4496 ALA n 
1 4497 ALA n 
1 4498 SER n 
1 4499 GLY n 
1 4500 GLY n 
1 4501 ALA n 
1 4502 LYS n 
1 4503 GLU n 
1 4504 LEU n 
1 4505 LYS n 
1 4506 ASN n 
1 4507 ILE n 
1 4508 HIS n 
1 4509 VAL n 
1 4510 CYS n 
1 4511 LEU n 
1 4512 GLY n 
1 4513 GLY n 
1 4514 LEU n 
1 4515 PHE n 
1 4516 VAL n 
1 4517 PRO n 
1 4518 GLU n 
1 4519 ALA n 
1 4520 TYR n 
1 4521 ILE n 
1 4522 THR n 
1 4523 ALA n 
1 4524 THR n 
1 4525 ARG n 
1 4526 GLN n 
1 4527 TYR n 
1 4528 VAL n 
1 4529 ALA n 
1 4530 GLN n 
1 4531 ALA n 
1 4532 ASN n 
1 4533 SER n 
1 4534 TRP n 
1 4535 SER n 
1 4536 LEU n 
1 4537 GLU n 
1 4538 GLU n 
1 4539 LEU n 
1 4540 CYS n 
1 4541 LEU n 
1 4542 GLU n 
1 4543 VAL n 
1 4544 ASN n 
1 4545 VAL n 
1 4546 THR n 
1 4547 THR n 
1 4548 SER n 
1 4549 GLN n 
1 4550 GLY n 
1 4551 ALA n 
1 4552 THR n 
1 4553 LEU n 
1 4554 ASP n 
1 4555 ALA n 
1 4556 CYS n 
1 4557 SER n 
1 4558 PHE n 
1 4559 GLY n 
1 4560 VAL n 
1 4561 THR n 
1 4562 GLY n 
1 4563 LEU n 
1 4564 LYS n 
1 4565 LEU n 
1 4566 GLN n 
1 4567 GLY n 
1 4568 ALA n 
1 4569 THR n 
1 4570 CYS n 
1 4571 ASN n 
1 4572 ASN n 
1 4573 ASN n 
1 4574 LYS n 
1 4575 LEU n 
1 4576 SER n 
1 4577 LEU n 
1 4578 SER n 
1 4579 ASN n 
1 4580 ALA n 
1 4581 ILE n 
1 4582 SER n 
1 4583 THR n 
1 4584 ALA n 
1 4585 LEU n 
1 4586 PRO n 
1 4587 LEU n 
1 4588 THR n 
1 4589 GLN n 
1 4590 LEU n 
1 4591 ARG n 
1 4592 TRP n 
1 4593 VAL n 
1 4594 LYS n 
1 4595 GLN n 
1 4596 THR n 
1 4597 ASN n 
1 4598 THR n 
1 4599 GLU n 
1 4600 LYS n 
1 4601 LYS n 
1 4602 ALA n 
1 4603 SER n 
1 4604 VAL n 
1 4605 VAL n 
1 4606 THR n 
1 4607 LEU n 
1 4608 PRO n 
1 4609 VAL n 
1 4610 TYR n 
1 4611 LEU n 
1 4612 ASN n 
1 4613 PHE n 
1 4614 THR n 
1 4615 ARG n 
1 4616 ALA n 
1 4617 ASP n 
1 4618 LEU n 
1 4619 ILE n 
1 4620 PHE n 
1 4621 THR n 
1 4622 VAL n 
1 4623 ASP n 
1 4624 PHE n 
1 4625 GLU n 
1 4626 ILE n 
1 4627 ALA n 
1 4628 THR n 
1 4629 LYS n 
1 4630 GLU n 
1 4631 ASP n 
1 4632 PRO n 
1 4633 ARG n 
1 4634 SER n 
1 4635 PHE n 
1 4636 TYR n 
1 4637 GLU n 
1 4638 ARG n 
1 4639 GLY n 
1 4640 VAL n 
1 4641 ALA n 
1 4642 VAL n 
1 4643 LEU n 
1 4644 CYS n 
1 4645 THR n 
1 4646 GLU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   4646 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'DYNC1H1, DHC1, DNCH1, DNCL, DNECL, DYHC, KIAA0325' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Spodoptera frugiperda' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     7108 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ADP non-polymer         n "ADENOSINE-5'-DIPHOSPHATE"  ? 'C10 H15 N5 O10 P2'   427.201 
ALA 'L-peptide linking' y ALANINE                     ? 'C3 H7 N O2'          89.093  
AOV non-polymer         . 'ADP ORTHOVANADATE'         ? 'C10 H17 N5 O14 P2 V' 544.156 
ARG 'L-peptide linking' y ARGININE                    ? 'C6 H15 N4 O2 1'      175.209 
ASN 'L-peptide linking' y ASPARAGINE                  ? 'C4 H8 N2 O3'         132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'             ? 'C4 H7 N O4'          133.103 
ATP non-polymer         . "ADENOSINE-5'-TRIPHOSPHATE" ? 'C10 H16 N5 O13 P3'   507.181 
CYS 'L-peptide linking' y CYSTEINE                    ? 'C3 H7 N O2 S'        121.158 
GLN 'L-peptide linking' y GLUTAMINE                   ? 'C5 H10 N2 O3'        146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'             ? 'C5 H9 N O4'          147.129 
GLY 'peptide linking'   y GLYCINE                     ? 'C2 H5 N O2'          75.067  
HIS 'L-peptide linking' y HISTIDINE                   ? 'C6 H10 N3 O2 1'      156.162 
ILE 'L-peptide linking' y ISOLEUCINE                  ? 'C6 H13 N O2'         131.173 
LEU 'L-peptide linking' y LEUCINE                     ? 'C6 H13 N O2'         131.173 
LYS 'L-peptide linking' y LYSINE                      ? 'C6 H15 N2 O2 1'      147.195 
MET 'L-peptide linking' y METHIONINE                  ? 'C5 H11 N O2 S'       149.211 
MG  non-polymer         . 'MAGNESIUM ION'             ? 'Mg 2'                24.305  
PHE 'L-peptide linking' y PHENYLALANINE               ? 'C9 H11 N O2'         165.189 
PRO 'L-peptide linking' y PROLINE                     ? 'C5 H9 N O2'          115.130 
SER 'L-peptide linking' y SERINE                      ? 'C3 H7 N O3'          105.093 
THR 'L-peptide linking' y THREONINE                   ? 'C4 H9 N O3'          119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                  ? 'C11 H12 N2 O2'       204.225 
TYR 'L-peptide linking' y TYROSINE                    ? 'C9 H11 N O3'         181.189 
VAL 'L-peptide linking' y VALINE                      ? 'C5 H11 N O2'         117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1    MET 1    1    ?    ?   ?   A . n 
A 1 2    SER 2    2    ?    ?   ?   A . n 
A 1 3    GLU 3    3    ?    ?   ?   A . n 
A 1 4    PRO 4    4    ?    ?   ?   A . n 
A 1 5    GLY 5    5    ?    ?   ?   A . n 
A 1 6    GLY 6    6    ?    ?   ?   A . n 
A 1 7    GLY 7    7    ?    ?   ?   A . n 
A 1 8    GLY 8    8    ?    ?   ?   A . n 
A 1 9    GLY 9    9    ?    ?   ?   A . n 
A 1 10   GLU 10   10   ?    ?   ?   A . n 
A 1 11   ASP 11   11   ?    ?   ?   A . n 
A 1 12   GLY 12   12   ?    ?   ?   A . n 
A 1 13   SER 13   13   ?    ?   ?   A . n 
A 1 14   ALA 14   14   ?    ?   ?   A . n 
A 1 15   GLY 15   15   ?    ?   ?   A . n 
A 1 16   LEU 16   16   ?    ?   ?   A . n 
A 1 17   GLU 17   17   ?    ?   ?   A . n 
A 1 18   VAL 18   18   ?    ?   ?   A . n 
A 1 19   SER 19   19   ?    ?   ?   A . n 
A 1 20   ALA 20   20   ?    ?   ?   A . n 
A 1 21   VAL 21   21   ?    ?   ?   A . n 
A 1 22   GLN 22   22   ?    ?   ?   A . n 
A 1 23   ASN 23   23   ?    ?   ?   A . n 
A 1 24   VAL 24   24   ?    ?   ?   A . n 
A 1 25   ALA 25   25   ?    ?   ?   A . n 
A 1 26   ASP 26   26   ?    ?   ?   A . n 
A 1 27   VAL 27   27   ?    ?   ?   A . n 
A 1 28   SER 28   28   ?    ?   ?   A . n 
A 1 29   VAL 29   29   ?    ?   ?   A . n 
A 1 30   LEU 30   30   ?    ?   ?   A . n 
A 1 31   GLN 31   31   ?    ?   ?   A . n 
A 1 32   LYS 32   32   ?    ?   ?   A . n 
A 1 33   HIS 33   33   ?    ?   ?   A . n 
A 1 34   LEU 34   34   ?    ?   ?   A . n 
A 1 35   ARG 35   35   ?    ?   ?   A . n 
A 1 36   LYS 36   36   ?    ?   ?   A . n 
A 1 37   LEU 37   37   ?    ?   ?   A . n 
A 1 38   VAL 38   38   ?    ?   ?   A . n 
A 1 39   PRO 39   39   ?    ?   ?   A . n 
A 1 40   LEU 40   40   ?    ?   ?   A . n 
A 1 41   LEU 41   41   ?    ?   ?   A . n 
A 1 42   LEU 42   42   ?    ?   ?   A . n 
A 1 43   GLU 43   43   ?    ?   ?   A . n 
A 1 44   ASP 44   44   ?    ?   ?   A . n 
A 1 45   GLY 45   45   ?    ?   ?   A . n 
A 1 46   GLY 46   46   ?    ?   ?   A . n 
A 1 47   GLU 47   47   ?    ?   ?   A . n 
A 1 48   ALA 48   48   ?    ?   ?   A . n 
A 1 49   PRO 49   49   ?    ?   ?   A . n 
A 1 50   ALA 50   50   ?    ?   ?   A . n 
A 1 51   ALA 51   51   ?    ?   ?   A . n 
A 1 52   LEU 52   52   ?    ?   ?   A . n 
A 1 53   GLU 53   53   ?    ?   ?   A . n 
A 1 54   ALA 54   54   ?    ?   ?   A . n 
A 1 55   ALA 55   55   ?    ?   ?   A . n 
A 1 56   LEU 56   56   ?    ?   ?   A . n 
A 1 57   GLU 57   57   ?    ?   ?   A . n 
A 1 58   GLU 58   58   ?    ?   ?   A . n 
A 1 59   LYS 59   59   ?    ?   ?   A . n 
A 1 60   SER 60   60   ?    ?   ?   A . n 
A 1 61   ALA 61   61   ?    ?   ?   A . n 
A 1 62   LEU 62   62   ?    ?   ?   A . n 
A 1 63   GLU 63   63   ?    ?   ?   A . n 
A 1 64   GLN 64   64   ?    ?   ?   A . n 
A 1 65   MET 65   65   ?    ?   ?   A . n 
A 1 66   ARG 66   66   ?    ?   ?   A . n 
A 1 67   LYS 67   67   ?    ?   ?   A . n 
A 1 68   PHE 68   68   ?    ?   ?   A . n 
A 1 69   LEU 69   69   ?    ?   ?   A . n 
A 1 70   SER 70   70   ?    ?   ?   A . n 
A 1 71   ASP 71   71   ?    ?   ?   A . n 
A 1 72   PRO 72   72   ?    ?   ?   A . n 
A 1 73   GLN 73   73   ?    ?   ?   A . n 
A 1 74   VAL 74   74   ?    ?   ?   A . n 
A 1 75   HIS 75   75   ?    ?   ?   A . n 
A 1 76   THR 76   76   ?    ?   ?   A . n 
A 1 77   VAL 77   77   ?    ?   ?   A . n 
A 1 78   LEU 78   78   ?    ?   ?   A . n 
A 1 79   VAL 79   79   ?    ?   ?   A . n 
A 1 80   GLU 80   80   ?    ?   ?   A . n 
A 1 81   ARG 81   81   ?    ?   ?   A . n 
A 1 82   SER 82   82   ?    ?   ?   A . n 
A 1 83   THR 83   83   ?    ?   ?   A . n 
A 1 84   LEU 84   84   ?    ?   ?   A . n 
A 1 85   LYS 85   85   ?    ?   ?   A . n 
A 1 86   GLU 86   86   ?    ?   ?   A . n 
A 1 87   ASP 87   87   ?    ?   ?   A . n 
A 1 88   VAL 88   88   ?    ?   ?   A . n 
A 1 89   GLY 89   89   ?    ?   ?   A . n 
A 1 90   ASP 90   90   ?    ?   ?   A . n 
A 1 91   GLU 91   91   ?    ?   ?   A . n 
A 1 92   GLY 92   92   ?    ?   ?   A . n 
A 1 93   GLU 93   93   ?    ?   ?   A . n 
A 1 94   GLU 94   94   ?    ?   ?   A . n 
A 1 95   GLU 95   95   ?    ?   ?   A . n 
A 1 96   LYS 96   96   ?    ?   ?   A . n 
A 1 97   GLU 97   97   ?    ?   ?   A . n 
A 1 98   PHE 98   98   ?    ?   ?   A . n 
A 1 99   ILE 99   99   ?    ?   ?   A . n 
A 1 100  SER 100  100  ?    ?   ?   A . n 
A 1 101  TYR 101  101  ?    ?   ?   A . n 
A 1 102  ASN 102  102  ?    ?   ?   A . n 
A 1 103  ILE 103  103  ?    ?   ?   A . n 
A 1 104  ASN 104  104  ?    ?   ?   A . n 
A 1 105  ILE 105  105  ?    ?   ?   A . n 
A 1 106  ASP 106  106  ?    ?   ?   A . n 
A 1 107  ILE 107  107  ?    ?   ?   A . n 
A 1 108  HIS 108  108  ?    ?   ?   A . n 
A 1 109  TYR 109  109  ?    ?   ?   A . n 
A 1 110  GLY 110  110  ?    ?   ?   A . n 
A 1 111  VAL 111  111  ?    ?   ?   A . n 
A 1 112  LYS 112  112  ?    ?   ?   A . n 
A 1 113  SER 113  113  ?    ?   ?   A . n 
A 1 114  ASN 114  114  ?    ?   ?   A . n 
A 1 115  SER 115  115  ?    ?   ?   A . n 
A 1 116  LEU 116  116  ?    ?   ?   A . n 
A 1 117  ALA 117  117  ?    ?   ?   A . n 
A 1 118  PHE 118  118  ?    ?   ?   A . n 
A 1 119  ILE 119  119  ?    ?   ?   A . n 
A 1 120  LYS 120  120  ?    ?   ?   A . n 
A 1 121  ARG 121  121  ?    ?   ?   A . n 
A 1 122  THR 122  122  ?    ?   ?   A . n 
A 1 123  PRO 123  123  ?    ?   ?   A . n 
A 1 124  VAL 124  124  ?    ?   ?   A . n 
A 1 125  ILE 125  125  ?    ?   ?   A . n 
A 1 126  ASP 126  126  ?    ?   ?   A . n 
A 1 127  ALA 127  127  ?    ?   ?   A . n 
A 1 128  ASP 128  128  ?    ?   ?   A . n 
A 1 129  LYS 129  129  ?    ?   ?   A . n 
A 1 130  PRO 130  130  ?    ?   ?   A . n 
A 1 131  VAL 131  131  ?    ?   ?   A . n 
A 1 132  SER 132  132  ?    ?   ?   A . n 
A 1 133  SER 133  133  ?    ?   ?   A . n 
A 1 134  GLN 134  134  ?    ?   ?   A . n 
A 1 135  LEU 135  135  ?    ?   ?   A . n 
A 1 136  ARG 136  136  ?    ?   ?   A . n 
A 1 137  VAL 137  137  ?    ?   ?   A . n 
A 1 138  LEU 138  138  ?    ?   ?   A . n 
A 1 139  THR 139  139  ?    ?   ?   A . n 
A 1 140  LEU 140  140  ?    ?   ?   A . n 
A 1 141  SER 141  141  ?    ?   ?   A . n 
A 1 142  GLU 142  142  ?    ?   ?   A . n 
A 1 143  ASP 143  143  ?    ?   ?   A . n 
A 1 144  SER 144  144  ?    ?   ?   A . n 
A 1 145  PRO 145  145  ?    ?   ?   A . n 
A 1 146  TYR 146  146  ?    ?   ?   A . n 
A 1 147  GLU 147  147  ?    ?   ?   A . n 
A 1 148  THR 148  148  ?    ?   ?   A . n 
A 1 149  LEU 149  149  ?    ?   ?   A . n 
A 1 150  HIS 150  150  ?    ?   ?   A . n 
A 1 151  SER 151  151  ?    ?   ?   A . n 
A 1 152  PHE 152  152  ?    ?   ?   A . n 
A 1 153  ILE 153  153  ?    ?   ?   A . n 
A 1 154  SER 154  154  ?    ?   ?   A . n 
A 1 155  ASN 155  155  ?    ?   ?   A . n 
A 1 156  ALA 156  156  ?    ?   ?   A . n 
A 1 157  VAL 157  157  ?    ?   ?   A . n 
A 1 158  ALA 158  158  ?    ?   ?   A . n 
A 1 159  PRO 159  159  ?    ?   ?   A . n 
A 1 160  PHE 160  160  ?    ?   ?   A . n 
A 1 161  PHE 161  161  ?    ?   ?   A . n 
A 1 162  LYS 162  162  ?    ?   ?   A . n 
A 1 163  SER 163  163  ?    ?   ?   A . n 
A 1 164  TYR 164  164  ?    ?   ?   A . n 
A 1 165  ILE 165  165  ?    ?   ?   A . n 
A 1 166  ARG 166  166  ?    ?   ?   A . n 
A 1 167  GLU 167  167  ?    ?   ?   A . n 
A 1 168  SER 168  168  ?    ?   ?   A . n 
A 1 169  GLY 169  169  ?    ?   ?   A . n 
A 1 170  LYS 170  170  ?    ?   ?   A . n 
A 1 171  ALA 171  171  ?    ?   ?   A . n 
A 1 172  ASP 172  172  ?    ?   ?   A . n 
A 1 173  ARG 173  173  ?    ?   ?   A . n 
A 1 174  ASP 174  174  ?    ?   ?   A . n 
A 1 175  GLY 175  175  ?    ?   ?   A . n 
A 1 176  ASP 176  176  ?    ?   ?   A . n 
A 1 177  LYS 177  177  ?    ?   ?   A . n 
A 1 178  MET 178  178  ?    ?   ?   A . n 
A 1 179  ALA 179  179  ?    ?   ?   A . n 
A 1 180  PRO 180  180  ?    ?   ?   A . n 
A 1 181  SER 181  181  ?    ?   ?   A . n 
A 1 182  VAL 182  182  ?    ?   ?   A . n 
A 1 183  GLU 183  183  ?    ?   ?   A . n 
A 1 184  LYS 184  184  ?    ?   ?   A . n 
A 1 185  LYS 185  185  ?    ?   ?   A . n 
A 1 186  ILE 186  186  ?    ?   ?   A . n 
A 1 187  ALA 187  187  ?    ?   ?   A . n 
A 1 188  GLU 188  188  ?    ?   ?   A . n 
A 1 189  LEU 189  189  ?    ?   ?   A . n 
A 1 190  GLU 190  190  ?    ?   ?   A . n 
A 1 191  MET 191  191  ?    ?   ?   A . n 
A 1 192  GLY 192  192  ?    ?   ?   A . n 
A 1 193  LEU 193  193  ?    ?   ?   A . n 
A 1 194  LEU 194  194  ?    ?   ?   A . n 
A 1 195  HIS 195  195  ?    ?   ?   A . n 
A 1 196  LEU 196  196  ?    ?   ?   A . n 
A 1 197  GLN 197  197  ?    ?   ?   A . n 
A 1 198  GLN 198  198  ?    ?   ?   A . n 
A 1 199  ASN 199  199  ?    ?   ?   A . n 
A 1 200  ILE 200  200  ?    ?   ?   A . n 
A 1 201  GLU 201  201  ?    ?   ?   A . n 
A 1 202  ILE 202  202  ?    ?   ?   A . n 
A 1 203  PRO 203  203  ?    ?   ?   A . n 
A 1 204  GLU 204  204  ?    ?   ?   A . n 
A 1 205  ILE 205  205  ?    ?   ?   A . n 
A 1 206  SER 206  206  ?    ?   ?   A . n 
A 1 207  LEU 207  207  ?    ?   ?   A . n 
A 1 208  PRO 208  208  ?    ?   ?   A . n 
A 1 209  ILE 209  209  ?    ?   ?   A . n 
A 1 210  HIS 210  210  ?    ?   ?   A . n 
A 1 211  PRO 211  211  ?    ?   ?   A . n 
A 1 212  MET 212  212  ?    ?   ?   A . n 
A 1 213  ILE 213  213  ?    ?   ?   A . n 
A 1 214  THR 214  214  ?    ?   ?   A . n 
A 1 215  ASN 215  215  ?    ?   ?   A . n 
A 1 216  VAL 216  216  ?    ?   ?   A . n 
A 1 217  ALA 217  217  ?    ?   ?   A . n 
A 1 218  LYS 218  218  ?    ?   ?   A . n 
A 1 219  GLN 219  219  ?    ?   ?   A . n 
A 1 220  CYS 220  220  ?    ?   ?   A . n 
A 1 221  TYR 221  221  ?    ?   ?   A . n 
A 1 222  GLU 222  222  ?    ?   ?   A . n 
A 1 223  ARG 223  223  ?    ?   ?   A . n 
A 1 224  GLY 224  224  ?    ?   ?   A . n 
A 1 225  GLU 225  225  ?    ?   ?   A . n 
A 1 226  LYS 226  226  ?    ?   ?   A . n 
A 1 227  PRO 227  227  ?    ?   ?   A . n 
A 1 228  LYS 228  228  ?    ?   ?   A . n 
A 1 229  VAL 229  229  ?    ?   ?   A . n 
A 1 230  THR 230  230  ?    ?   ?   A . n 
A 1 231  ASP 231  231  ?    ?   ?   A . n 
A 1 232  PHE 232  232  ?    ?   ?   A . n 
A 1 233  GLY 233  233  ?    ?   ?   A . n 
A 1 234  ASP 234  234  ?    ?   ?   A . n 
A 1 235  LYS 235  235  ?    ?   ?   A . n 
A 1 236  VAL 236  236  ?    ?   ?   A . n 
A 1 237  GLU 237  237  ?    ?   ?   A . n 
A 1 238  ASP 238  238  ?    ?   ?   A . n 
A 1 239  PRO 239  239  ?    ?   ?   A . n 
A 1 240  THR 240  240  ?    ?   ?   A . n 
A 1 241  PHE 241  241  ?    ?   ?   A . n 
A 1 242  LEU 242  242  ?    ?   ?   A . n 
A 1 243  ASN 243  243  ?    ?   ?   A . n 
A 1 244  GLN 244  244  ?    ?   ?   A . n 
A 1 245  LEU 245  245  ?    ?   ?   A . n 
A 1 246  GLN 246  246  ?    ?   ?   A . n 
A 1 247  SER 247  247  ?    ?   ?   A . n 
A 1 248  GLY 248  248  ?    ?   ?   A . n 
A 1 249  VAL 249  249  ?    ?   ?   A . n 
A 1 250  ASN 250  250  ?    ?   ?   A . n 
A 1 251  ARG 251  251  ?    ?   ?   A . n 
A 1 252  TRP 252  252  ?    ?   ?   A . n 
A 1 253  ILE 253  253  ?    ?   ?   A . n 
A 1 254  ARG 254  254  ?    ?   ?   A . n 
A 1 255  GLU 255  255  ?    ?   ?   A . n 
A 1 256  ILE 256  256  ?    ?   ?   A . n 
A 1 257  GLN 257  257  ?    ?   ?   A . n 
A 1 258  LYS 258  258  ?    ?   ?   A . n 
A 1 259  VAL 259  259  ?    ?   ?   A . n 
A 1 260  THR 260  260  ?    ?   ?   A . n 
A 1 261  LYS 261  261  ?    ?   ?   A . n 
A 1 262  LEU 262  262  ?    ?   ?   A . n 
A 1 263  ASP 263  263  ?    ?   ?   A . n 
A 1 264  ARG 264  264  ?    ?   ?   A . n 
A 1 265  ASP 265  265  ?    ?   ?   A . n 
A 1 266  PRO 266  266  ?    ?   ?   A . n 
A 1 267  ALA 267  267  ?    ?   ?   A . n 
A 1 268  SER 268  268  ?    ?   ?   A . n 
A 1 269  GLY 269  269  ?    ?   ?   A . n 
A 1 270  THR 270  270  ?    ?   ?   A . n 
A 1 271  ALA 271  271  ?    ?   ?   A . n 
A 1 272  LEU 272  272  ?    ?   ?   A . n 
A 1 273  GLN 273  273  ?    ?   ?   A . n 
A 1 274  GLU 274  274  ?    ?   ?   A . n 
A 1 275  ILE 275  275  ?    ?   ?   A . n 
A 1 276  SER 276  276  ?    ?   ?   A . n 
A 1 277  PHE 277  277  ?    ?   ?   A . n 
A 1 278  TRP 278  278  ?    ?   ?   A . n 
A 1 279  LEU 279  279  ?    ?   ?   A . n 
A 1 280  ASN 280  280  ?    ?   ?   A . n 
A 1 281  LEU 281  281  ?    ?   ?   A . n 
A 1 282  GLU 282  282  ?    ?   ?   A . n 
A 1 283  ARG 283  283  ?    ?   ?   A . n 
A 1 284  ALA 284  284  ?    ?   ?   A . n 
A 1 285  LEU 285  285  ?    ?   ?   A . n 
A 1 286  TYR 286  286  ?    ?   ?   A . n 
A 1 287  ARG 287  287  ?    ?   ?   A . n 
A 1 288  ILE 288  288  ?    ?   ?   A . n 
A 1 289  GLN 289  289  ?    ?   ?   A . n 
A 1 290  GLU 290  290  ?    ?   ?   A . n 
A 1 291  LYS 291  291  ?    ?   ?   A . n 
A 1 292  ARG 292  292  ?    ?   ?   A . n 
A 1 293  GLU 293  293  ?    ?   ?   A . n 
A 1 294  SER 294  294  ?    ?   ?   A . n 
A 1 295  PRO 295  295  ?    ?   ?   A . n 
A 1 296  GLU 296  296  ?    ?   ?   A . n 
A 1 297  VAL 297  297  ?    ?   ?   A . n 
A 1 298  LEU 298  298  ?    ?   ?   A . n 
A 1 299  LEU 299  299  ?    ?   ?   A . n 
A 1 300  THR 300  300  ?    ?   ?   A . n 
A 1 301  LEU 301  301  ?    ?   ?   A . n 
A 1 302  ASP 302  302  ?    ?   ?   A . n 
A 1 303  ILE 303  303  ?    ?   ?   A . n 
A 1 304  LEU 304  304  ?    ?   ?   A . n 
A 1 305  LYS 305  305  ?    ?   ?   A . n 
A 1 306  HIS 306  306  ?    ?   ?   A . n 
A 1 307  GLY 307  307  ?    ?   ?   A . n 
A 1 308  LYS 308  308  ?    ?   ?   A . n 
A 1 309  ARG 309  309  ?    ?   ?   A . n 
A 1 310  PHE 310  310  ?    ?   ?   A . n 
A 1 311  HIS 311  311  ?    ?   ?   A . n 
A 1 312  ALA 312  312  ?    ?   ?   A . n 
A 1 313  THR 313  313  ?    ?   ?   A . n 
A 1 314  VAL 314  314  ?    ?   ?   A . n 
A 1 315  SER 315  315  ?    ?   ?   A . n 
A 1 316  PHE 316  316  ?    ?   ?   A . n 
A 1 317  ASP 317  317  ?    ?   ?   A . n 
A 1 318  THR 318  318  ?    ?   ?   A . n 
A 1 319  ASP 319  319  ?    ?   ?   A . n 
A 1 320  THR 320  320  ?    ?   ?   A . n 
A 1 321  GLY 321  321  ?    ?   ?   A . n 
A 1 322  LEU 322  322  ?    ?   ?   A . n 
A 1 323  LYS 323  323  ?    ?   ?   A . n 
A 1 324  GLN 324  324  ?    ?   ?   A . n 
A 1 325  ALA 325  325  ?    ?   ?   A . n 
A 1 326  LEU 326  326  ?    ?   ?   A . n 
A 1 327  GLU 327  327  ?    ?   ?   A . n 
A 1 328  THR 328  328  ?    ?   ?   A . n 
A 1 329  VAL 329  329  ?    ?   ?   A . n 
A 1 330  ASN 330  330  ?    ?   ?   A . n 
A 1 331  ASP 331  331  ?    ?   ?   A . n 
A 1 332  TYR 332  332  ?    ?   ?   A . n 
A 1 333  ASN 333  333  ?    ?   ?   A . n 
A 1 334  PRO 334  334  ?    ?   ?   A . n 
A 1 335  LEU 335  335  ?    ?   ?   A . n 
A 1 336  MET 336  336  ?    ?   ?   A . n 
A 1 337  LYS 337  337  ?    ?   ?   A . n 
A 1 338  ASP 338  338  ?    ?   ?   A . n 
A 1 339  PHE 339  339  ?    ?   ?   A . n 
A 1 340  PRO 340  340  ?    ?   ?   A . n 
A 1 341  LEU 341  341  ?    ?   ?   A . n 
A 1 342  ASN 342  342  ?    ?   ?   A . n 
A 1 343  ASP 343  343  ?    ?   ?   A . n 
A 1 344  LEU 344  344  ?    ?   ?   A . n 
A 1 345  LEU 345  345  ?    ?   ?   A . n 
A 1 346  SER 346  346  ?    ?   ?   A . n 
A 1 347  ALA 347  347  ?    ?   ?   A . n 
A 1 348  THR 348  348  ?    ?   ?   A . n 
A 1 349  GLU 349  349  ?    ?   ?   A . n 
A 1 350  LEU 350  350  ?    ?   ?   A . n 
A 1 351  ASP 351  351  ?    ?   ?   A . n 
A 1 352  LYS 352  352  ?    ?   ?   A . n 
A 1 353  ILE 353  353  ?    ?   ?   A . n 
A 1 354  ARG 354  354  ?    ?   ?   A . n 
A 1 355  GLN 355  355  ?    ?   ?   A . n 
A 1 356  ALA 356  356  ?    ?   ?   A . n 
A 1 357  LEU 357  357  ?    ?   ?   A . n 
A 1 358  VAL 358  358  ?    ?   ?   A . n 
A 1 359  ALA 359  359  ?    ?   ?   A . n 
A 1 360  ILE 360  360  ?    ?   ?   A . n 
A 1 361  PHE 361  361  ?    ?   ?   A . n 
A 1 362  THR 362  362  ?    ?   ?   A . n 
A 1 363  HIS 363  363  ?    ?   ?   A . n 
A 1 364  LEU 364  364  ?    ?   ?   A . n 
A 1 365  ARG 365  365  ?    ?   ?   A . n 
A 1 366  LYS 366  366  ?    ?   ?   A . n 
A 1 367  ILE 367  367  ?    ?   ?   A . n 
A 1 368  ARG 368  368  ?    ?   ?   A . n 
A 1 369  ASN 369  369  ?    ?   ?   A . n 
A 1 370  THR 370  370  ?    ?   ?   A . n 
A 1 371  LYS 371  371  ?    ?   ?   A . n 
A 1 372  TYR 372  372  ?    ?   ?   A . n 
A 1 373  PRO 373  373  ?    ?   ?   A . n 
A 1 374  ILE 374  374  ?    ?   ?   A . n 
A 1 375  GLN 375  375  ?    ?   ?   A . n 
A 1 376  ARG 376  376  ?    ?   ?   A . n 
A 1 377  ALA 377  377  ?    ?   ?   A . n 
A 1 378  LEU 378  378  ?    ?   ?   A . n 
A 1 379  ARG 379  379  ?    ?   ?   A . n 
A 1 380  LEU 380  380  ?    ?   ?   A . n 
A 1 381  VAL 381  381  ?    ?   ?   A . n 
A 1 382  GLU 382  382  ?    ?   ?   A . n 
A 1 383  ALA 383  383  ?    ?   ?   A . n 
A 1 384  ILE 384  384  ?    ?   ?   A . n 
A 1 385  SER 385  385  ?    ?   ?   A . n 
A 1 386  ARG 386  386  ?    ?   ?   A . n 
A 1 387  ASP 387  387  ?    ?   ?   A . n 
A 1 388  LEU 388  388  ?    ?   ?   A . n 
A 1 389  SER 389  389  ?    ?   ?   A . n 
A 1 390  SER 390  390  ?    ?   ?   A . n 
A 1 391  GLN 391  391  ?    ?   ?   A . n 
A 1 392  LEU 392  392  ?    ?   ?   A . n 
A 1 393  LEU 393  393  ?    ?   ?   A . n 
A 1 394  LYS 394  394  ?    ?   ?   A . n 
A 1 395  VAL 395  395  ?    ?   ?   A . n 
A 1 396  LEU 396  396  ?    ?   ?   A . n 
A 1 397  GLY 397  397  ?    ?   ?   A . n 
A 1 398  THR 398  398  ?    ?   ?   A . n 
A 1 399  ARG 399  399  ?    ?   ?   A . n 
A 1 400  LYS 400  400  ?    ?   ?   A . n 
A 1 401  LEU 401  401  ?    ?   ?   A . n 
A 1 402  MET 402  402  ?    ?   ?   A . n 
A 1 403  HIS 403  403  ?    ?   ?   A . n 
A 1 404  VAL 404  404  ?    ?   ?   A . n 
A 1 405  ALA 405  405  ?    ?   ?   A . n 
A 1 406  TYR 406  406  ?    ?   ?   A . n 
A 1 407  GLU 407  407  ?    ?   ?   A . n 
A 1 408  GLU 408  408  ?    ?   ?   A . n 
A 1 409  PHE 409  409  ?    ?   ?   A . n 
A 1 410  GLU 410  410  ?    ?   ?   A . n 
A 1 411  LYS 411  411  ?    ?   ?   A . n 
A 1 412  VAL 412  412  ?    ?   ?   A . n 
A 1 413  MET 413  413  ?    ?   ?   A . n 
A 1 414  VAL 414  414  ?    ?   ?   A . n 
A 1 415  ALA 415  415  ?    ?   ?   A . n 
A 1 416  CYS 416  416  ?    ?   ?   A . n 
A 1 417  PHE 417  417  ?    ?   ?   A . n 
A 1 418  GLU 418  418  ?    ?   ?   A . n 
A 1 419  VAL 419  419  ?    ?   ?   A . n 
A 1 420  PHE 420  420  ?    ?   ?   A . n 
A 1 421  GLN 421  421  ?    ?   ?   A . n 
A 1 422  THR 422  422  ?    ?   ?   A . n 
A 1 423  TRP 423  423  ?    ?   ?   A . n 
A 1 424  ASP 424  424  ?    ?   ?   A . n 
A 1 425  ASP 425  425  ?    ?   ?   A . n 
A 1 426  GLU 426  426  ?    ?   ?   A . n 
A 1 427  TYR 427  427  ?    ?   ?   A . n 
A 1 428  GLU 428  428  ?    ?   ?   A . n 
A 1 429  LYS 429  429  ?    ?   ?   A . n 
A 1 430  LEU 430  430  ?    ?   ?   A . n 
A 1 431  GLN 431  431  ?    ?   ?   A . n 
A 1 432  VAL 432  432  ?    ?   ?   A . n 
A 1 433  LEU 433  433  ?    ?   ?   A . n 
A 1 434  LEU 434  434  ?    ?   ?   A . n 
A 1 435  ARG 435  435  ?    ?   ?   A . n 
A 1 436  ASP 436  436  ?    ?   ?   A . n 
A 1 437  ILE 437  437  ?    ?   ?   A . n 
A 1 438  VAL 438  438  ?    ?   ?   A . n 
A 1 439  LYS 439  439  ?    ?   ?   A . n 
A 1 440  ARG 440  440  ?    ?   ?   A . n 
A 1 441  LYS 441  441  ?    ?   ?   A . n 
A 1 442  ARG 442  442  ?    ?   ?   A . n 
A 1 443  GLU 443  443  ?    ?   ?   A . n 
A 1 444  GLU 444  444  ?    ?   ?   A . n 
A 1 445  ASN 445  445  ?    ?   ?   A . n 
A 1 446  LEU 446  446  ?    ?   ?   A . n 
A 1 447  LYS 447  447  ?    ?   ?   A . n 
A 1 448  MET 448  448  ?    ?   ?   A . n 
A 1 449  VAL 449  449  ?    ?   ?   A . n 
A 1 450  TRP 450  450  ?    ?   ?   A . n 
A 1 451  ARG 451  451  ?    ?   ?   A . n 
A 1 452  ILE 452  452  ?    ?   ?   A . n 
A 1 453  ASN 453  453  ?    ?   ?   A . n 
A 1 454  PRO 454  454  ?    ?   ?   A . n 
A 1 455  ALA 455  455  ?    ?   ?   A . n 
A 1 456  HIS 456  456  ?    ?   ?   A . n 
A 1 457  ARG 457  457  ?    ?   ?   A . n 
A 1 458  LYS 458  458  ?    ?   ?   A . n 
A 1 459  LEU 459  459  ?    ?   ?   A . n 
A 1 460  GLN 460  460  ?    ?   ?   A . n 
A 1 461  ALA 461  461  ?    ?   ?   A . n 
A 1 462  ARG 462  462  ?    ?   ?   A . n 
A 1 463  LEU 463  463  ?    ?   ?   A . n 
A 1 464  ASP 464  464  ?    ?   ?   A . n 
A 1 465  GLN 465  465  ?    ?   ?   A . n 
A 1 466  MET 466  466  ?    ?   ?   A . n 
A 1 467  ARG 467  467  ?    ?   ?   A . n 
A 1 468  LYS 468  468  ?    ?   ?   A . n 
A 1 469  PHE 469  469  ?    ?   ?   A . n 
A 1 470  ARG 470  470  ?    ?   ?   A . n 
A 1 471  ARG 471  471  ?    ?   ?   A . n 
A 1 472  GLN 472  472  ?    ?   ?   A . n 
A 1 473  HIS 473  473  ?    ?   ?   A . n 
A 1 474  GLU 474  474  ?    ?   ?   A . n 
A 1 475  GLN 475  475  ?    ?   ?   A . n 
A 1 476  LEU 476  476  ?    ?   ?   A . n 
A 1 477  ARG 477  477  ?    ?   ?   A . n 
A 1 478  ALA 478  478  ?    ?   ?   A . n 
A 1 479  VAL 479  479  ?    ?   ?   A . n 
A 1 480  ILE 480  480  ?    ?   ?   A . n 
A 1 481  VAL 481  481  ?    ?   ?   A . n 
A 1 482  ARG 482  482  ?    ?   ?   A . n 
A 1 483  VAL 483  483  ?    ?   ?   A . n 
A 1 484  LEU 484  484  ?    ?   ?   A . n 
A 1 485  ARG 485  485  ?    ?   ?   A . n 
A 1 486  PRO 486  486  ?    ?   ?   A . n 
A 1 487  GLN 487  487  ?    ?   ?   A . n 
A 1 488  VAL 488  488  ?    ?   ?   A . n 
A 1 489  THR 489  489  ?    ?   ?   A . n 
A 1 490  ALA 490  490  ?    ?   ?   A . n 
A 1 491  VAL 491  491  ?    ?   ?   A . n 
A 1 492  ALA 492  492  ?    ?   ?   A . n 
A 1 493  GLN 493  493  ?    ?   ?   A . n 
A 1 494  GLN 494  494  ?    ?   ?   A . n 
A 1 495  ASN 495  495  ?    ?   ?   A . n 
A 1 496  GLN 496  496  ?    ?   ?   A . n 
A 1 497  GLY 497  497  ?    ?   ?   A . n 
A 1 498  GLU 498  498  ?    ?   ?   A . n 
A 1 499  VAL 499  499  ?    ?   ?   A . n 
A 1 500  PRO 500  500  ?    ?   ?   A . n 
A 1 501  GLU 501  501  ?    ?   ?   A . n 
A 1 502  PRO 502  502  ?    ?   ?   A . n 
A 1 503  GLN 503  503  ?    ?   ?   A . n 
A 1 504  ASP 504  504  ?    ?   ?   A . n 
A 1 505  MET 505  505  ?    ?   ?   A . n 
A 1 506  LYS 506  506  ?    ?   ?   A . n 
A 1 507  VAL 507  507  ?    ?   ?   A . n 
A 1 508  ALA 508  508  ?    ?   ?   A . n 
A 1 509  GLU 509  509  ?    ?   ?   A . n 
A 1 510  VAL 510  510  ?    ?   ?   A . n 
A 1 511  LEU 511  511  ?    ?   ?   A . n 
A 1 512  PHE 512  512  ?    ?   ?   A . n 
A 1 513  ASP 513  513  ?    ?   ?   A . n 
A 1 514  ALA 514  514  ?    ?   ?   A . n 
A 1 515  ALA 515  515  ?    ?   ?   A . n 
A 1 516  ASP 516  516  ?    ?   ?   A . n 
A 1 517  ALA 517  517  ?    ?   ?   A . n 
A 1 518  ASN 518  518  ?    ?   ?   A . n 
A 1 519  ALA 519  519  ?    ?   ?   A . n 
A 1 520  ILE 520  520  ?    ?   ?   A . n 
A 1 521  GLU 521  521  ?    ?   ?   A . n 
A 1 522  GLU 522  522  ?    ?   ?   A . n 
A 1 523  VAL 523  523  ?    ?   ?   A . n 
A 1 524  ASN 524  524  ?    ?   ?   A . n 
A 1 525  LEU 525  525  ?    ?   ?   A . n 
A 1 526  ALA 526  526  ?    ?   ?   A . n 
A 1 527  TYR 527  527  ?    ?   ?   A . n 
A 1 528  GLU 528  528  ?    ?   ?   A . n 
A 1 529  ASN 529  529  ?    ?   ?   A . n 
A 1 530  VAL 530  530  ?    ?   ?   A . n 
A 1 531  LYS 531  531  ?    ?   ?   A . n 
A 1 532  GLU 532  532  ?    ?   ?   A . n 
A 1 533  VAL 533  533  ?    ?   ?   A . n 
A 1 534  ASP 534  534  ?    ?   ?   A . n 
A 1 535  GLY 535  535  ?    ?   ?   A . n 
A 1 536  LEU 536  536  ?    ?   ?   A . n 
A 1 537  ASP 537  537  ?    ?   ?   A . n 
A 1 538  VAL 538  538  ?    ?   ?   A . n 
A 1 539  SER 539  539  ?    ?   ?   A . n 
A 1 540  LYS 540  540  ?    ?   ?   A . n 
A 1 541  GLU 541  541  ?    ?   ?   A . n 
A 1 542  GLY 542  542  ?    ?   ?   A . n 
A 1 543  THR 543  543  ?    ?   ?   A . n 
A 1 544  GLU 544  544  ?    ?   ?   A . n 
A 1 545  ALA 545  545  ?    ?   ?   A . n 
A 1 546  TRP 546  546  ?    ?   ?   A . n 
A 1 547  GLU 547  547  ?    ?   ?   A . n 
A 1 548  ALA 548  548  ?    ?   ?   A . n 
A 1 549  ALA 549  549  ?    ?   ?   A . n 
A 1 550  MET 550  550  ?    ?   ?   A . n 
A 1 551  LYS 551  551  ?    ?   ?   A . n 
A 1 552  ARG 552  552  ?    ?   ?   A . n 
A 1 553  TYR 553  553  ?    ?   ?   A . n 
A 1 554  ASP 554  554  ?    ?   ?   A . n 
A 1 555  GLU 555  555  ?    ?   ?   A . n 
A 1 556  ARG 556  556  ?    ?   ?   A . n 
A 1 557  ILE 557  557  ?    ?   ?   A . n 
A 1 558  ASP 558  558  ?    ?   ?   A . n 
A 1 559  ARG 559  559  ?    ?   ?   A . n 
A 1 560  VAL 560  560  ?    ?   ?   A . n 
A 1 561  GLU 561  561  ?    ?   ?   A . n 
A 1 562  THR 562  562  ?    ?   ?   A . n 
A 1 563  ARG 563  563  ?    ?   ?   A . n 
A 1 564  ILE 564  564  ?    ?   ?   A . n 
A 1 565  THR 565  565  ?    ?   ?   A . n 
A 1 566  ALA 566  566  ?    ?   ?   A . n 
A 1 567  ARG 567  567  ?    ?   ?   A . n 
A 1 568  LEU 568  568  ?    ?   ?   A . n 
A 1 569  ARG 569  569  ?    ?   ?   A . n 
A 1 570  ASP 570  570  ?    ?   ?   A . n 
A 1 571  GLN 571  571  ?    ?   ?   A . n 
A 1 572  LEU 572  572  ?    ?   ?   A . n 
A 1 573  GLY 573  573  ?    ?   ?   A . n 
A 1 574  THR 574  574  ?    ?   ?   A . n 
A 1 575  ALA 575  575  ?    ?   ?   A . n 
A 1 576  LYS 576  576  ?    ?   ?   A . n 
A 1 577  ASN 577  577  ?    ?   ?   A . n 
A 1 578  ALA 578  578  ?    ?   ?   A . n 
A 1 579  ASN 579  579  ?    ?   ?   A . n 
A 1 580  GLU 580  580  ?    ?   ?   A . n 
A 1 581  MET 581  581  ?    ?   ?   A . n 
A 1 582  PHE 582  582  ?    ?   ?   A . n 
A 1 583  ARG 583  583  ?    ?   ?   A . n 
A 1 584  ILE 584  584  ?    ?   ?   A . n 
A 1 585  PHE 585  585  ?    ?   ?   A . n 
A 1 586  SER 586  586  ?    ?   ?   A . n 
A 1 587  ARG 587  587  ?    ?   ?   A . n 
A 1 588  PHE 588  588  ?    ?   ?   A . n 
A 1 589  ASN 589  589  ?    ?   ?   A . n 
A 1 590  ALA 590  590  ?    ?   ?   A . n 
A 1 591  LEU 591  591  ?    ?   ?   A . n 
A 1 592  PHE 592  592  ?    ?   ?   A . n 
A 1 593  VAL 593  593  ?    ?   ?   A . n 
A 1 594  ARG 594  594  ?    ?   ?   A . n 
A 1 595  PRO 595  595  ?    ?   ?   A . n 
A 1 596  HIS 596  596  ?    ?   ?   A . n 
A 1 597  ILE 597  597  ?    ?   ?   A . n 
A 1 598  ARG 598  598  ?    ?   ?   A . n 
A 1 599  GLY 599  599  ?    ?   ?   A . n 
A 1 600  ALA 600  600  ?    ?   ?   A . n 
A 1 601  ILE 601  601  ?    ?   ?   A . n 
A 1 602  ARG 602  602  ?    ?   ?   A . n 
A 1 603  GLU 603  603  ?    ?   ?   A . n 
A 1 604  TYR 604  604  ?    ?   ?   A . n 
A 1 605  GLN 605  605  ?    ?   ?   A . n 
A 1 606  THR 606  606  ?    ?   ?   A . n 
A 1 607  GLN 607  607  ?    ?   ?   A . n 
A 1 608  LEU 608  608  ?    ?   ?   A . n 
A 1 609  ILE 609  609  ?    ?   ?   A . n 
A 1 610  GLN 610  610  ?    ?   ?   A . n 
A 1 611  ARG 611  611  ?    ?   ?   A . n 
A 1 612  VAL 612  612  ?    ?   ?   A . n 
A 1 613  LYS 613  613  ?    ?   ?   A . n 
A 1 614  ASP 614  614  ?    ?   ?   A . n 
A 1 615  ASP 615  615  ?    ?   ?   A . n 
A 1 616  ILE 616  616  ?    ?   ?   A . n 
A 1 617  GLU 617  617  ?    ?   ?   A . n 
A 1 618  SER 618  618  ?    ?   ?   A . n 
A 1 619  LEU 619  619  ?    ?   ?   A . n 
A 1 620  HIS 620  620  ?    ?   ?   A . n 
A 1 621  ASP 621  621  ?    ?   ?   A . n 
A 1 622  LYS 622  622  ?    ?   ?   A . n 
A 1 623  PHE 623  623  ?    ?   ?   A . n 
A 1 624  LYS 624  624  ?    ?   ?   A . n 
A 1 625  VAL 625  625  ?    ?   ?   A . n 
A 1 626  GLN 626  626  ?    ?   ?   A . n 
A 1 627  TYR 627  627  ?    ?   ?   A . n 
A 1 628  PRO 628  628  ?    ?   ?   A . n 
A 1 629  GLN 629  629  ?    ?   ?   A . n 
A 1 630  SER 630  630  ?    ?   ?   A . n 
A 1 631  GLN 631  631  ?    ?   ?   A . n 
A 1 632  ALA 632  632  ?    ?   ?   A . n 
A 1 633  CYS 633  633  ?    ?   ?   A . n 
A 1 634  LYS 634  634  ?    ?   ?   A . n 
A 1 635  MET 635  635  ?    ?   ?   A . n 
A 1 636  SER 636  636  ?    ?   ?   A . n 
A 1 637  HIS 637  637  ?    ?   ?   A . n 
A 1 638  VAL 638  638  ?    ?   ?   A . n 
A 1 639  ARG 639  639  ?    ?   ?   A . n 
A 1 640  ASP 640  640  ?    ?   ?   A . n 
A 1 641  LEU 641  641  ?    ?   ?   A . n 
A 1 642  PRO 642  642  ?    ?   ?   A . n 
A 1 643  PRO 643  643  ?    ?   ?   A . n 
A 1 644  VAL 644  644  ?    ?   ?   A . n 
A 1 645  SER 645  645  ?    ?   ?   A . n 
A 1 646  GLY 646  646  ?    ?   ?   A . n 
A 1 647  SER 647  647  ?    ?   ?   A . n 
A 1 648  ILE 648  648  ?    ?   ?   A . n 
A 1 649  ILE 649  649  ?    ?   ?   A . n 
A 1 650  TRP 650  650  ?    ?   ?   A . n 
A 1 651  ALA 651  651  ?    ?   ?   A . n 
A 1 652  LYS 652  652  ?    ?   ?   A . n 
A 1 653  GLN 653  653  ?    ?   ?   A . n 
A 1 654  ILE 654  654  ?    ?   ?   A . n 
A 1 655  ASP 655  655  ?    ?   ?   A . n 
A 1 656  ARG 656  656  ?    ?   ?   A . n 
A 1 657  GLN 657  657  ?    ?   ?   A . n 
A 1 658  LEU 658  658  ?    ?   ?   A . n 
A 1 659  THR 659  659  ?    ?   ?   A . n 
A 1 660  ALA 660  660  ?    ?   ?   A . n 
A 1 661  TYR 661  661  ?    ?   ?   A . n 
A 1 662  MET 662  662  ?    ?   ?   A . n 
A 1 663  LYS 663  663  ?    ?   ?   A . n 
A 1 664  ARG 664  664  ?    ?   ?   A . n 
A 1 665  VAL 665  665  ?    ?   ?   A . n 
A 1 666  GLU 666  666  ?    ?   ?   A . n 
A 1 667  ASP 667  667  ?    ?   ?   A . n 
A 1 668  VAL 668  668  ?    ?   ?   A . n 
A 1 669  LEU 669  669  ?    ?   ?   A . n 
A 1 670  GLY 670  670  ?    ?   ?   A . n 
A 1 671  LYS 671  671  ?    ?   ?   A . n 
A 1 672  GLY 672  672  ?    ?   ?   A . n 
A 1 673  TRP 673  673  ?    ?   ?   A . n 
A 1 674  GLU 674  674  ?    ?   ?   A . n 
A 1 675  ASN 675  675  ?    ?   ?   A . n 
A 1 676  HIS 676  676  ?    ?   ?   A . n 
A 1 677  VAL 677  677  ?    ?   ?   A . n 
A 1 678  GLU 678  678  ?    ?   ?   A . n 
A 1 679  GLY 679  679  ?    ?   ?   A . n 
A 1 680  GLN 680  680  ?    ?   ?   A . n 
A 1 681  LYS 681  681  ?    ?   ?   A . n 
A 1 682  LEU 682  682  ?    ?   ?   A . n 
A 1 683  LYS 683  683  ?    ?   ?   A . n 
A 1 684  GLN 684  684  ?    ?   ?   A . n 
A 1 685  ASP 685  685  ?    ?   ?   A . n 
A 1 686  GLY 686  686  ?    ?   ?   A . n 
A 1 687  ASP 687  687  ?    ?   ?   A . n 
A 1 688  SER 688  688  ?    ?   ?   A . n 
A 1 689  PHE 689  689  ?    ?   ?   A . n 
A 1 690  ARG 690  690  ?    ?   ?   A . n 
A 1 691  MET 691  691  ?    ?   ?   A . n 
A 1 692  LYS 692  692  ?    ?   ?   A . n 
A 1 693  LEU 693  693  ?    ?   ?   A . n 
A 1 694  ASN 694  694  ?    ?   ?   A . n 
A 1 695  THR 695  695  ?    ?   ?   A . n 
A 1 696  GLN 696  696  ?    ?   ?   A . n 
A 1 697  GLU 697  697  ?    ?   ?   A . n 
A 1 698  ILE 698  698  ?    ?   ?   A . n 
A 1 699  PHE 699  699  ?    ?   ?   A . n 
A 1 700  ASP 700  700  ?    ?   ?   A . n 
A 1 701  ASP 701  701  ?    ?   ?   A . n 
A 1 702  TRP 702  702  ?    ?   ?   A . n 
A 1 703  ALA 703  703  ?    ?   ?   A . n 
A 1 704  ARG 704  704  ?    ?   ?   A . n 
A 1 705  LYS 705  705  ?    ?   ?   A . n 
A 1 706  VAL 706  706  ?    ?   ?   A . n 
A 1 707  GLN 707  707  ?    ?   ?   A . n 
A 1 708  GLN 708  708  ?    ?   ?   A . n 
A 1 709  ARG 709  709  ?    ?   ?   A . n 
A 1 710  ASN 710  710  ?    ?   ?   A . n 
A 1 711  LEU 711  711  ?    ?   ?   A . n 
A 1 712  GLY 712  712  ?    ?   ?   A . n 
A 1 713  VAL 713  713  ?    ?   ?   A . n 
A 1 714  SER 714  714  ?    ?   ?   A . n 
A 1 715  GLY 715  715  ?    ?   ?   A . n 
A 1 716  ARG 716  716  ?    ?   ?   A . n 
A 1 717  ILE 717  717  ?    ?   ?   A . n 
A 1 718  PHE 718  718  ?    ?   ?   A . n 
A 1 719  THR 719  719  ?    ?   ?   A . n 
A 1 720  ILE 720  720  ?    ?   ?   A . n 
A 1 721  GLU 721  721  ?    ?   ?   A . n 
A 1 722  SER 722  722  ?    ?   ?   A . n 
A 1 723  THR 723  723  ?    ?   ?   A . n 
A 1 724  ARG 724  724  ?    ?   ?   A . n 
A 1 725  VAL 725  725  ?    ?   ?   A . n 
A 1 726  ARG 726  726  ?    ?   ?   A . n 
A 1 727  GLY 727  727  ?    ?   ?   A . n 
A 1 728  ARG 728  728  ?    ?   ?   A . n 
A 1 729  THR 729  729  ?    ?   ?   A . n 
A 1 730  GLY 730  730  ?    ?   ?   A . n 
A 1 731  ASN 731  731  ?    ?   ?   A . n 
A 1 732  VAL 732  732  ?    ?   ?   A . n 
A 1 733  LEU 733  733  ?    ?   ?   A . n 
A 1 734  LYS 734  734  ?    ?   ?   A . n 
A 1 735  LEU 735  735  ?    ?   ?   A . n 
A 1 736  LYS 736  736  ?    ?   ?   A . n 
A 1 737  VAL 737  737  ?    ?   ?   A . n 
A 1 738  ASN 738  738  ?    ?   ?   A . n 
A 1 739  PHE 739  739  ?    ?   ?   A . n 
A 1 740  LEU 740  740  ?    ?   ?   A . n 
A 1 741  PRO 741  741  ?    ?   ?   A . n 
A 1 742  GLU 742  742  ?    ?   ?   A . n 
A 1 743  ILE 743  743  ?    ?   ?   A . n 
A 1 744  ILE 744  744  ?    ?   ?   A . n 
A 1 745  THR 745  745  ?    ?   ?   A . n 
A 1 746  LEU 746  746  ?    ?   ?   A . n 
A 1 747  SER 747  747  ?    ?   ?   A . n 
A 1 748  LYS 748  748  ?    ?   ?   A . n 
A 1 749  GLU 749  749  ?    ?   ?   A . n 
A 1 750  VAL 750  750  ?    ?   ?   A . n 
A 1 751  ARG 751  751  ?    ?   ?   A . n 
A 1 752  ASN 752  752  ?    ?   ?   A . n 
A 1 753  LEU 753  753  ?    ?   ?   A . n 
A 1 754  LYS 754  754  ?    ?   ?   A . n 
A 1 755  TRP 755  755  ?    ?   ?   A . n 
A 1 756  LEU 756  756  ?    ?   ?   A . n 
A 1 757  GLY 757  757  ?    ?   ?   A . n 
A 1 758  PHE 758  758  ?    ?   ?   A . n 
A 1 759  ARG 759  759  ?    ?   ?   A . n 
A 1 760  VAL 760  760  ?    ?   ?   A . n 
A 1 761  PRO 761  761  ?    ?   ?   A . n 
A 1 762  LEU 762  762  ?    ?   ?   A . n 
A 1 763  ALA 763  763  ?    ?   ?   A . n 
A 1 764  ILE 764  764  ?    ?   ?   A . n 
A 1 765  VAL 765  765  ?    ?   ?   A . n 
A 1 766  ASN 766  766  ?    ?   ?   A . n 
A 1 767  LYS 767  767  ?    ?   ?   A . n 
A 1 768  ALA 768  768  ?    ?   ?   A . n 
A 1 769  HIS 769  769  ?    ?   ?   A . n 
A 1 770  GLN 770  770  ?    ?   ?   A . n 
A 1 771  ALA 771  771  ?    ?   ?   A . n 
A 1 772  ASN 772  772  ?    ?   ?   A . n 
A 1 773  GLN 773  773  ?    ?   ?   A . n 
A 1 774  LEU 774  774  ?    ?   ?   A . n 
A 1 775  TYR 775  775  ?    ?   ?   A . n 
A 1 776  PRO 776  776  ?    ?   ?   A . n 
A 1 777  PHE 777  777  ?    ?   ?   A . n 
A 1 778  ALA 778  778  ?    ?   ?   A . n 
A 1 779  ILE 779  779  ?    ?   ?   A . n 
A 1 780  SER 780  780  ?    ?   ?   A . n 
A 1 781  LEU 781  781  ?    ?   ?   A . n 
A 1 782  ILE 782  782  ?    ?   ?   A . n 
A 1 783  GLU 783  783  ?    ?   ?   A . n 
A 1 784  SER 784  784  ?    ?   ?   A . n 
A 1 785  VAL 785  785  ?    ?   ?   A . n 
A 1 786  ARG 786  786  ?    ?   ?   A . n 
A 1 787  THR 787  787  ?    ?   ?   A . n 
A 1 788  TYR 788  788  ?    ?   ?   A . n 
A 1 789  GLU 789  789  ?    ?   ?   A . n 
A 1 790  ARG 790  790  ?    ?   ?   A . n 
A 1 791  THR 791  791  ?    ?   ?   A . n 
A 1 792  CYS 792  792  ?    ?   ?   A . n 
A 1 793  GLU 793  793  ?    ?   ?   A . n 
A 1 794  LYS 794  794  ?    ?   ?   A . n 
A 1 795  VAL 795  795  ?    ?   ?   A . n 
A 1 796  GLU 796  796  ?    ?   ?   A . n 
A 1 797  GLU 797  797  ?    ?   ?   A . n 
A 1 798  ARG 798  798  ?    ?   ?   A . n 
A 1 799  ASN 799  799  ?    ?   ?   A . n 
A 1 800  THR 800  800  ?    ?   ?   A . n 
A 1 801  ILE 801  801  ?    ?   ?   A . n 
A 1 802  SER 802  802  ?    ?   ?   A . n 
A 1 803  LEU 803  803  ?    ?   ?   A . n 
A 1 804  LEU 804  804  ?    ?   ?   A . n 
A 1 805  VAL 805  805  ?    ?   ?   A . n 
A 1 806  ALA 806  806  ?    ?   ?   A . n 
A 1 807  GLY 807  807  ?    ?   ?   A . n 
A 1 808  LEU 808  808  ?    ?   ?   A . n 
A 1 809  LYS 809  809  ?    ?   ?   A . n 
A 1 810  LYS 810  810  ?    ?   ?   A . n 
A 1 811  GLU 811  811  ?    ?   ?   A . n 
A 1 812  VAL 812  812  ?    ?   ?   A . n 
A 1 813  GLN 813  813  ?    ?   ?   A . n 
A 1 814  ALA 814  814  ?    ?   ?   A . n 
A 1 815  LEU 815  815  ?    ?   ?   A . n 
A 1 816  ILE 816  816  ?    ?   ?   A . n 
A 1 817  ALA 817  817  ?    ?   ?   A . n 
A 1 818  GLU 818  818  ?    ?   ?   A . n 
A 1 819  GLY 819  819  ?    ?   ?   A . n 
A 1 820  ILE 820  820  ?    ?   ?   A . n 
A 1 821  ALA 821  821  ?    ?   ?   A . n 
A 1 822  LEU 822  822  ?    ?   ?   A . n 
A 1 823  VAL 823  823  ?    ?   ?   A . n 
A 1 824  TRP 824  824  ?    ?   ?   A . n 
A 1 825  GLU 825  825  ?    ?   ?   A . n 
A 1 826  SER 826  826  ?    ?   ?   A . n 
A 1 827  TYR 827  827  ?    ?   ?   A . n 
A 1 828  LYS 828  828  ?    ?   ?   A . n 
A 1 829  LEU 829  829  ?    ?   ?   A . n 
A 1 830  ASP 830  830  ?    ?   ?   A . n 
A 1 831  PRO 831  831  ?    ?   ?   A . n 
A 1 832  TYR 832  832  ?    ?   ?   A . n 
A 1 833  VAL 833  833  ?    ?   ?   A . n 
A 1 834  GLN 834  834  ?    ?   ?   A . n 
A 1 835  ARG 835  835  ?    ?   ?   A . n 
A 1 836  LEU 836  836  ?    ?   ?   A . n 
A 1 837  ALA 837  837  ?    ?   ?   A . n 
A 1 838  GLU 838  838  ?    ?   ?   A . n 
A 1 839  THR 839  839  ?    ?   ?   A . n 
A 1 840  VAL 840  840  ?    ?   ?   A . n 
A 1 841  PHE 841  841  ?    ?   ?   A . n 
A 1 842  ASN 842  842  ?    ?   ?   A . n 
A 1 843  PHE 843  843  ?    ?   ?   A . n 
A 1 844  GLN 844  844  ?    ?   ?   A . n 
A 1 845  GLU 845  845  ?    ?   ?   A . n 
A 1 846  LYS 846  846  ?    ?   ?   A . n 
A 1 847  VAL 847  847  ?    ?   ?   A . n 
A 1 848  ASP 848  848  ?    ?   ?   A . n 
A 1 849  ASP 849  849  ?    ?   ?   A . n 
A 1 850  LEU 850  850  ?    ?   ?   A . n 
A 1 851  LEU 851  851  ?    ?   ?   A . n 
A 1 852  ILE 852  852  ?    ?   ?   A . n 
A 1 853  ILE 853  853  ?    ?   ?   A . n 
A 1 854  GLU 854  854  ?    ?   ?   A . n 
A 1 855  GLU 855  855  ?    ?   ?   A . n 
A 1 856  LYS 856  856  ?    ?   ?   A . n 
A 1 857  ILE 857  857  ?    ?   ?   A . n 
A 1 858  ASP 858  858  ?    ?   ?   A . n 
A 1 859  LEU 859  859  ?    ?   ?   A . n 
A 1 860  GLU 860  860  ?    ?   ?   A . n 
A 1 861  VAL 861  861  ?    ?   ?   A . n 
A 1 862  ARG 862  862  ?    ?   ?   A . n 
A 1 863  SER 863  863  ?    ?   ?   A . n 
A 1 864  LEU 864  864  ?    ?   ?   A . n 
A 1 865  GLU 865  865  ?    ?   ?   A . n 
A 1 866  THR 866  866  ?    ?   ?   A . n 
A 1 867  CYS 867  867  ?    ?   ?   A . n 
A 1 868  MET 868  868  ?    ?   ?   A . n 
A 1 869  TYR 869  869  ?    ?   ?   A . n 
A 1 870  ASP 870  870  ?    ?   ?   A . n 
A 1 871  HIS 871  871  ?    ?   ?   A . n 
A 1 872  LYS 872  872  ?    ?   ?   A . n 
A 1 873  THR 873  873  ?    ?   ?   A . n 
A 1 874  PHE 874  874  ?    ?   ?   A . n 
A 1 875  SER 875  875  ?    ?   ?   A . n 
A 1 876  GLU 876  876  ?    ?   ?   A . n 
A 1 877  ILE 877  877  ?    ?   ?   A . n 
A 1 878  LEU 878  878  ?    ?   ?   A . n 
A 1 879  ASN 879  879  ?    ?   ?   A . n 
A 1 880  ARG 880  880  ?    ?   ?   A . n 
A 1 881  VAL 881  881  ?    ?   ?   A . n 
A 1 882  GLN 882  882  ?    ?   ?   A . n 
A 1 883  LYS 883  883  ?    ?   ?   A . n 
A 1 884  ALA 884  884  ?    ?   ?   A . n 
A 1 885  VAL 885  885  ?    ?   ?   A . n 
A 1 886  ASP 886  886  ?    ?   ?   A . n 
A 1 887  ASP 887  887  ?    ?   ?   A . n 
A 1 888  LEU 888  888  ?    ?   ?   A . n 
A 1 889  ASN 889  889  ?    ?   ?   A . n 
A 1 890  LEU 890  890  ?    ?   ?   A . n 
A 1 891  HIS 891  891  ?    ?   ?   A . n 
A 1 892  SER 892  892  ?    ?   ?   A . n 
A 1 893  TYR 893  893  ?    ?   ?   A . n 
A 1 894  SER 894  894  ?    ?   ?   A . n 
A 1 895  ASN 895  895  ?    ?   ?   A . n 
A 1 896  LEU 896  896  ?    ?   ?   A . n 
A 1 897  PRO 897  897  ?    ?   ?   A . n 
A 1 898  ILE 898  898  ?    ?   ?   A . n 
A 1 899  TRP 899  899  ?    ?   ?   A . n 
A 1 900  VAL 900  900  ?    ?   ?   A . n 
A 1 901  ASN 901  901  ?    ?   ?   A . n 
A 1 902  LYS 902  902  ?    ?   ?   A . n 
A 1 903  LEU 903  903  ?    ?   ?   A . n 
A 1 904  ASP 904  904  ?    ?   ?   A . n 
A 1 905  MET 905  905  ?    ?   ?   A . n 
A 1 906  GLU 906  906  ?    ?   ?   A . n 
A 1 907  ILE 907  907  ?    ?   ?   A . n 
A 1 908  GLU 908  908  ?    ?   ?   A . n 
A 1 909  ARG 909  909  ?    ?   ?   A . n 
A 1 910  ILE 910  910  ?    ?   ?   A . n 
A 1 911  LEU 911  911  ?    ?   ?   A . n 
A 1 912  GLY 912  912  ?    ?   ?   A . n 
A 1 913  VAL 913  913  ?    ?   ?   A . n 
A 1 914  ARG 914  914  ?    ?   ?   A . n 
A 1 915  LEU 915  915  ?    ?   ?   A . n 
A 1 916  GLN 916  916  ?    ?   ?   A . n 
A 1 917  ALA 917  917  ?    ?   ?   A . n 
A 1 918  GLY 918  918  ?    ?   ?   A . n 
A 1 919  LEU 919  919  ?    ?   ?   A . n 
A 1 920  ARG 920  920  ?    ?   ?   A . n 
A 1 921  ALA 921  921  ?    ?   ?   A . n 
A 1 922  TRP 922  922  ?    ?   ?   A . n 
A 1 923  THR 923  923  ?    ?   ?   A . n 
A 1 924  GLN 924  924  ?    ?   ?   A . n 
A 1 925  VAL 925  925  ?    ?   ?   A . n 
A 1 926  LEU 926  926  ?    ?   ?   A . n 
A 1 927  LEU 927  927  ?    ?   ?   A . n 
A 1 928  GLY 928  928  ?    ?   ?   A . n 
A 1 929  GLN 929  929  ?    ?   ?   A . n 
A 1 930  ALA 930  930  ?    ?   ?   A . n 
A 1 931  GLU 931  931  ?    ?   ?   A . n 
A 1 932  ASP 932  932  ?    ?   ?   A . n 
A 1 933  LYS 933  933  ?    ?   ?   A . n 
A 1 934  ALA 934  934  ?    ?   ?   A . n 
A 1 935  GLU 935  935  ?    ?   ?   A . n 
A 1 936  VAL 936  936  ?    ?   ?   A . n 
A 1 937  ASP 937  937  ?    ?   ?   A . n 
A 1 938  MET 938  938  ?    ?   ?   A . n 
A 1 939  ASP 939  939  ?    ?   ?   A . n 
A 1 940  THR 940  940  ?    ?   ?   A . n 
A 1 941  ASP 941  941  ?    ?   ?   A . n 
A 1 942  ALA 942  942  ?    ?   ?   A . n 
A 1 943  PRO 943  943  ?    ?   ?   A . n 
A 1 944  GLN 944  944  ?    ?   ?   A . n 
A 1 945  VAL 945  945  ?    ?   ?   A . n 
A 1 946  SER 946  946  ?    ?   ?   A . n 
A 1 947  HIS 947  947  ?    ?   ?   A . n 
A 1 948  LYS 948  948  ?    ?   ?   A . n 
A 1 949  PRO 949  949  ?    ?   ?   A . n 
A 1 950  GLY 950  950  ?    ?   ?   A . n 
A 1 951  GLY 951  951  ?    ?   ?   A . n 
A 1 952  GLU 952  952  ?    ?   ?   A . n 
A 1 953  PRO 953  953  ?    ?   ?   A . n 
A 1 954  LYS 954  954  ?    ?   ?   A . n 
A 1 955  ILE 955  955  ?    ?   ?   A . n 
A 1 956  LYS 956  956  ?    ?   ?   A . n 
A 1 957  ASN 957  957  ?    ?   ?   A . n 
A 1 958  VAL 958  958  ?    ?   ?   A . n 
A 1 959  VAL 959  959  ?    ?   ?   A . n 
A 1 960  HIS 960  960  ?    ?   ?   A . n 
A 1 961  GLU 961  961  ?    ?   ?   A . n 
A 1 962  LEU 962  962  ?    ?   ?   A . n 
A 1 963  ARG 963  963  ?    ?   ?   A . n 
A 1 964  ILE 964  964  ?    ?   ?   A . n 
A 1 965  THR 965  965  ?    ?   ?   A . n 
A 1 966  ASN 966  966  ?    ?   ?   A . n 
A 1 967  GLN 967  967  ?    ?   ?   A . n 
A 1 968  VAL 968  968  ?    ?   ?   A . n 
A 1 969  ILE 969  969  ?    ?   ?   A . n 
A 1 970  TYR 970  970  ?    ?   ?   A . n 
A 1 971  LEU 971  971  ?    ?   ?   A . n 
A 1 972  ASN 972  972  ?    ?   ?   A . n 
A 1 973  PRO 973  973  ?    ?   ?   A . n 
A 1 974  PRO 974  974  ?    ?   ?   A . n 
A 1 975  ILE 975  975  ?    ?   ?   A . n 
A 1 976  GLU 976  976  ?    ?   ?   A . n 
A 1 977  GLU 977  977  ?    ?   ?   A . n 
A 1 978  CYS 978  978  ?    ?   ?   A . n 
A 1 979  ARG 979  979  ?    ?   ?   A . n 
A 1 980  TYR 980  980  ?    ?   ?   A . n 
A 1 981  LYS 981  981  ?    ?   ?   A . n 
A 1 982  LEU 982  982  ?    ?   ?   A . n 
A 1 983  TYR 983  983  ?    ?   ?   A . n 
A 1 984  GLN 984  984  ?    ?   ?   A . n 
A 1 985  GLU 985  985  ?    ?   ?   A . n 
A 1 986  MET 986  986  ?    ?   ?   A . n 
A 1 987  PHE 987  987  ?    ?   ?   A . n 
A 1 988  ALA 988  988  ?    ?   ?   A . n 
A 1 989  TRP 989  989  ?    ?   ?   A . n 
A 1 990  LYS 990  990  ?    ?   ?   A . n 
A 1 991  MET 991  991  ?    ?   ?   A . n 
A 1 992  VAL 992  992  ?    ?   ?   A . n 
A 1 993  VAL 993  993  ?    ?   ?   A . n 
A 1 994  LEU 994  994  ?    ?   ?   A . n 
A 1 995  SER 995  995  ?    ?   ?   A . n 
A 1 996  LEU 996  996  ?    ?   ?   A . n 
A 1 997  PRO 997  997  ?    ?   ?   A . n 
A 1 998  ARG 998  998  ?    ?   ?   A . n 
A 1 999  ILE 999  999  ?    ?   ?   A . n 
A 1 1000 GLN 1000 1000 ?    ?   ?   A . n 
A 1 1001 SER 1001 1001 ?    ?   ?   A . n 
A 1 1002 GLN 1002 1002 ?    ?   ?   A . n 
A 1 1003 ARG 1003 1003 ?    ?   ?   A . n 
A 1 1004 TYR 1004 1004 ?    ?   ?   A . n 
A 1 1005 GLN 1005 1005 ?    ?   ?   A . n 
A 1 1006 VAL 1006 1006 ?    ?   ?   A . n 
A 1 1007 GLY 1007 1007 ?    ?   ?   A . n 
A 1 1008 VAL 1008 1008 ?    ?   ?   A . n 
A 1 1009 HIS 1009 1009 ?    ?   ?   A . n 
A 1 1010 TYR 1010 1010 ?    ?   ?   A . n 
A 1 1011 GLU 1011 1011 ?    ?   ?   A . n 
A 1 1012 LEU 1012 1012 ?    ?   ?   A . n 
A 1 1013 THR 1013 1013 ?    ?   ?   A . n 
A 1 1014 GLU 1014 1014 ?    ?   ?   A . n 
A 1 1015 GLU 1015 1015 ?    ?   ?   A . n 
A 1 1016 GLU 1016 1016 ?    ?   ?   A . n 
A 1 1017 LYS 1017 1017 ?    ?   ?   A . n 
A 1 1018 PHE 1018 1018 ?    ?   ?   A . n 
A 1 1019 TYR 1019 1019 ?    ?   ?   A . n 
A 1 1020 ARG 1020 1020 ?    ?   ?   A . n 
A 1 1021 ASN 1021 1021 ?    ?   ?   A . n 
A 1 1022 ALA 1022 1022 ?    ?   ?   A . n 
A 1 1023 LEU 1023 1023 ?    ?   ?   A . n 
A 1 1024 THR 1024 1024 ?    ?   ?   A . n 
A 1 1025 ARG 1025 1025 ?    ?   ?   A . n 
A 1 1026 MET 1026 1026 ?    ?   ?   A . n 
A 1 1027 PRO 1027 1027 ?    ?   ?   A . n 
A 1 1028 ASP 1028 1028 ?    ?   ?   A . n 
A 1 1029 GLY 1029 1029 ?    ?   ?   A . n 
A 1 1030 PRO 1030 1030 ?    ?   ?   A . n 
A 1 1031 VAL 1031 1031 ?    ?   ?   A . n 
A 1 1032 ALA 1032 1032 ?    ?   ?   A . n 
A 1 1033 LEU 1033 1033 ?    ?   ?   A . n 
A 1 1034 GLU 1034 1034 ?    ?   ?   A . n 
A 1 1035 GLU 1035 1035 ?    ?   ?   A . n 
A 1 1036 SER 1036 1036 ?    ?   ?   A . n 
A 1 1037 TYR 1037 1037 ?    ?   ?   A . n 
A 1 1038 SER 1038 1038 ?    ?   ?   A . n 
A 1 1039 ALA 1039 1039 ?    ?   ?   A . n 
A 1 1040 VAL 1040 1040 ?    ?   ?   A . n 
A 1 1041 MET 1041 1041 ?    ?   ?   A . n 
A 1 1042 GLY 1042 1042 ?    ?   ?   A . n 
A 1 1043 ILE 1043 1043 ?    ?   ?   A . n 
A 1 1044 VAL 1044 1044 ?    ?   ?   A . n 
A 1 1045 SER 1045 1045 ?    ?   ?   A . n 
A 1 1046 GLU 1046 1046 ?    ?   ?   A . n 
A 1 1047 VAL 1047 1047 ?    ?   ?   A . n 
A 1 1048 GLU 1048 1048 ?    ?   ?   A . n 
A 1 1049 GLN 1049 1049 ?    ?   ?   A . n 
A 1 1050 TYR 1050 1050 ?    ?   ?   A . n 
A 1 1051 VAL 1051 1051 ?    ?   ?   A . n 
A 1 1052 LYS 1052 1052 ?    ?   ?   A . n 
A 1 1053 VAL 1053 1053 ?    ?   ?   A . n 
A 1 1054 TRP 1054 1054 ?    ?   ?   A . n 
A 1 1055 LEU 1055 1055 ?    ?   ?   A . n 
A 1 1056 GLN 1056 1056 ?    ?   ?   A . n 
A 1 1057 TYR 1057 1057 ?    ?   ?   A . n 
A 1 1058 GLN 1058 1058 ?    ?   ?   A . n 
A 1 1059 CYS 1059 1059 ?    ?   ?   A . n 
A 1 1060 LEU 1060 1060 ?    ?   ?   A . n 
A 1 1061 TRP 1061 1061 ?    ?   ?   A . n 
A 1 1062 ASP 1062 1062 ?    ?   ?   A . n 
A 1 1063 MET 1063 1063 ?    ?   ?   A . n 
A 1 1064 GLN 1064 1064 ?    ?   ?   A . n 
A 1 1065 ALA 1065 1065 ?    ?   ?   A . n 
A 1 1066 GLU 1066 1066 ?    ?   ?   A . n 
A 1 1067 ASN 1067 1067 ?    ?   ?   A . n 
A 1 1068 ILE 1068 1068 ?    ?   ?   A . n 
A 1 1069 TYR 1069 1069 ?    ?   ?   A . n 
A 1 1070 ASN 1070 1070 ?    ?   ?   A . n 
A 1 1071 ARG 1071 1071 ?    ?   ?   A . n 
A 1 1072 LEU 1072 1072 ?    ?   ?   A . n 
A 1 1073 GLY 1073 1073 ?    ?   ?   A . n 
A 1 1074 GLU 1074 1074 ?    ?   ?   A . n 
A 1 1075 ASP 1075 1075 ?    ?   ?   A . n 
A 1 1076 LEU 1076 1076 ?    ?   ?   A . n 
A 1 1077 ASN 1077 1077 ?    ?   ?   A . n 
A 1 1078 LYS 1078 1078 ?    ?   ?   A . n 
A 1 1079 TRP 1079 1079 ?    ?   ?   A . n 
A 1 1080 GLN 1080 1080 ?    ?   ?   A . n 
A 1 1081 ALA 1081 1081 ?    ?   ?   A . n 
A 1 1082 LEU 1082 1082 ?    ?   ?   A . n 
A 1 1083 LEU 1083 1083 ?    ?   ?   A . n 
A 1 1084 VAL 1084 1084 ?    ?   ?   A . n 
A 1 1085 GLN 1085 1085 ?    ?   ?   A . n 
A 1 1086 ILE 1086 1086 ?    ?   ?   A . n 
A 1 1087 ARG 1087 1087 ?    ?   ?   A . n 
A 1 1088 LYS 1088 1088 ?    ?   ?   A . n 
A 1 1089 ALA 1089 1089 ?    ?   ?   A . n 
A 1 1090 ARG 1090 1090 ?    ?   ?   A . n 
A 1 1091 GLY 1091 1091 ?    ?   ?   A . n 
A 1 1092 THR 1092 1092 ?    ?   ?   A . n 
A 1 1093 PHE 1093 1093 ?    ?   ?   A . n 
A 1 1094 ASP 1094 1094 ?    ?   ?   A . n 
A 1 1095 ASN 1095 1095 ?    ?   ?   A . n 
A 1 1096 ALA 1096 1096 ?    ?   ?   A . n 
A 1 1097 GLU 1097 1097 ?    ?   ?   A . n 
A 1 1098 THR 1098 1098 ?    ?   ?   A . n 
A 1 1099 LYS 1099 1099 ?    ?   ?   A . n 
A 1 1100 LYS 1100 1100 ?    ?   ?   A . n 
A 1 1101 GLU 1101 1101 ?    ?   ?   A . n 
A 1 1102 PHE 1102 1102 ?    ?   ?   A . n 
A 1 1103 GLY 1103 1103 ?    ?   ?   A . n 
A 1 1104 PRO 1104 1104 ?    ?   ?   A . n 
A 1 1105 VAL 1105 1105 ?    ?   ?   A . n 
A 1 1106 VAL 1106 1106 ?    ?   ?   A . n 
A 1 1107 ILE 1107 1107 ?    ?   ?   A . n 
A 1 1108 ASP 1108 1108 ?    ?   ?   A . n 
A 1 1109 TYR 1109 1109 ?    ?   ?   A . n 
A 1 1110 GLY 1110 1110 ?    ?   ?   A . n 
A 1 1111 LYS 1111 1111 ?    ?   ?   A . n 
A 1 1112 VAL 1112 1112 ?    ?   ?   A . n 
A 1 1113 GLN 1113 1113 ?    ?   ?   A . n 
A 1 1114 SER 1114 1114 ?    ?   ?   A . n 
A 1 1115 LYS 1115 1115 ?    ?   ?   A . n 
A 1 1116 VAL 1116 1116 ?    ?   ?   A . n 
A 1 1117 ASN 1117 1117 ?    ?   ?   A . n 
A 1 1118 LEU 1118 1118 ?    ?   ?   A . n 
A 1 1119 LYS 1119 1119 ?    ?   ?   A . n 
A 1 1120 TYR 1120 1120 ?    ?   ?   A . n 
A 1 1121 ASP 1121 1121 ?    ?   ?   A . n 
A 1 1122 SER 1122 1122 ?    ?   ?   A . n 
A 1 1123 TRP 1123 1123 ?    ?   ?   A . n 
A 1 1124 HIS 1124 1124 ?    ?   ?   A . n 
A 1 1125 LYS 1125 1125 ?    ?   ?   A . n 
A 1 1126 GLU 1126 1126 ?    ?   ?   A . n 
A 1 1127 VAL 1127 1127 ?    ?   ?   A . n 
A 1 1128 LEU 1128 1128 ?    ?   ?   A . n 
A 1 1129 SER 1129 1129 ?    ?   ?   A . n 
A 1 1130 LYS 1130 1130 ?    ?   ?   A . n 
A 1 1131 PHE 1131 1131 ?    ?   ?   A . n 
A 1 1132 GLY 1132 1132 ?    ?   ?   A . n 
A 1 1133 GLN 1133 1133 ?    ?   ?   A . n 
A 1 1134 MET 1134 1134 ?    ?   ?   A . n 
A 1 1135 LEU 1135 1135 ?    ?   ?   A . n 
A 1 1136 GLY 1136 1136 ?    ?   ?   A . n 
A 1 1137 SER 1137 1137 ?    ?   ?   A . n 
A 1 1138 ASN 1138 1138 ?    ?   ?   A . n 
A 1 1139 MET 1139 1139 ?    ?   ?   A . n 
A 1 1140 THR 1140 1140 ?    ?   ?   A . n 
A 1 1141 GLU 1141 1141 ?    ?   ?   A . n 
A 1 1142 PHE 1142 1142 ?    ?   ?   A . n 
A 1 1143 HIS 1143 1143 ?    ?   ?   A . n 
A 1 1144 SER 1144 1144 ?    ?   ?   A . n 
A 1 1145 GLN 1145 1145 ?    ?   ?   A . n 
A 1 1146 ILE 1146 1146 ?    ?   ?   A . n 
A 1 1147 SER 1147 1147 ?    ?   ?   A . n 
A 1 1148 LYS 1148 1148 ?    ?   ?   A . n 
A 1 1149 SER 1149 1149 ?    ?   ?   A . n 
A 1 1150 ARG 1150 1150 ?    ?   ?   A . n 
A 1 1151 GLN 1151 1151 ?    ?   ?   A . n 
A 1 1152 GLU 1152 1152 ?    ?   ?   A . n 
A 1 1153 LEU 1153 1153 ?    ?   ?   A . n 
A 1 1154 GLU 1154 1154 ?    ?   ?   A . n 
A 1 1155 GLN 1155 1155 ?    ?   ?   A . n 
A 1 1156 HIS 1156 1156 ?    ?   ?   A . n 
A 1 1157 SER 1157 1157 ?    ?   ?   A . n 
A 1 1158 VAL 1158 1158 ?    ?   ?   A . n 
A 1 1159 ASP 1159 1159 ?    ?   ?   A . n 
A 1 1160 THR 1160 1160 ?    ?   ?   A . n 
A 1 1161 ALA 1161 1161 ?    ?   ?   A . n 
A 1 1162 SER 1162 1162 ?    ?   ?   A . n 
A 1 1163 THR 1163 1163 ?    ?   ?   A . n 
A 1 1164 SER 1164 1164 ?    ?   ?   A . n 
A 1 1165 ASP 1165 1165 ?    ?   ?   A . n 
A 1 1166 ALA 1166 1166 ?    ?   ?   A . n 
A 1 1167 VAL 1167 1167 ?    ?   ?   A . n 
A 1 1168 THR 1168 1168 ?    ?   ?   A . n 
A 1 1169 PHE 1169 1169 ?    ?   ?   A . n 
A 1 1170 ILE 1170 1170 ?    ?   ?   A . n 
A 1 1171 THR 1171 1171 ?    ?   ?   A . n 
A 1 1172 TYR 1172 1172 ?    ?   ?   A . n 
A 1 1173 VAL 1173 1173 ?    ?   ?   A . n 
A 1 1174 GLN 1174 1174 ?    ?   ?   A . n 
A 1 1175 SER 1175 1175 ?    ?   ?   A . n 
A 1 1176 LEU 1176 1176 ?    ?   ?   A . n 
A 1 1177 LYS 1177 1177 ?    ?   ?   A . n 
A 1 1178 ARG 1178 1178 ?    ?   ?   A . n 
A 1 1179 LYS 1179 1179 ?    ?   ?   A . n 
A 1 1180 ILE 1180 1180 ?    ?   ?   A . n 
A 1 1181 LYS 1181 1181 ?    ?   ?   A . n 
A 1 1182 GLN 1182 1182 ?    ?   ?   A . n 
A 1 1183 PHE 1183 1183 ?    ?   ?   A . n 
A 1 1184 GLU 1184 1184 ?    ?   ?   A . n 
A 1 1185 LYS 1185 1185 ?    ?   ?   A . n 
A 1 1186 GLN 1186 1186 ?    ?   ?   A . n 
A 1 1187 VAL 1187 1187 ?    ?   ?   A . n 
A 1 1188 GLU 1188 1188 ?    ?   ?   A . n 
A 1 1189 LEU 1189 1189 ?    ?   ?   A . n 
A 1 1190 TYR 1190 1190 ?    ?   ?   A . n 
A 1 1191 ARG 1191 1191 ?    ?   ?   A . n 
A 1 1192 ASN 1192 1192 ?    ?   ?   A . n 
A 1 1193 GLY 1193 1193 ?    ?   ?   A . n 
A 1 1194 GLN 1194 1194 ?    ?   ?   A . n 
A 1 1195 ARG 1195 1195 ?    ?   ?   A . n 
A 1 1196 LEU 1196 1196 ?    ?   ?   A . n 
A 1 1197 LEU 1197 1197 ?    ?   ?   A . n 
A 1 1198 GLU 1198 1198 ?    ?   ?   A . n 
A 1 1199 LYS 1199 1199 ?    ?   ?   A . n 
A 1 1200 GLN 1200 1200 ?    ?   ?   A . n 
A 1 1201 ARG 1201 1201 ?    ?   ?   A . n 
A 1 1202 PHE 1202 1202 ?    ?   ?   A . n 
A 1 1203 GLN 1203 1203 ?    ?   ?   A . n 
A 1 1204 PHE 1204 1204 ?    ?   ?   A . n 
A 1 1205 PRO 1205 1205 ?    ?   ?   A . n 
A 1 1206 PRO 1206 1206 ?    ?   ?   A . n 
A 1 1207 SER 1207 1207 ?    ?   ?   A . n 
A 1 1208 TRP 1208 1208 ?    ?   ?   A . n 
A 1 1209 LEU 1209 1209 ?    ?   ?   A . n 
A 1 1210 TYR 1210 1210 ?    ?   ?   A . n 
A 1 1211 ILE 1211 1211 ?    ?   ?   A . n 
A 1 1212 ASP 1212 1212 ?    ?   ?   A . n 
A 1 1213 ASN 1213 1213 ?    ?   ?   A . n 
A 1 1214 ILE 1214 1214 ?    ?   ?   A . n 
A 1 1215 GLU 1215 1215 ?    ?   ?   A . n 
A 1 1216 GLY 1216 1216 ?    ?   ?   A . n 
A 1 1217 GLU 1217 1217 ?    ?   ?   A . n 
A 1 1218 TRP 1218 1218 ?    ?   ?   A . n 
A 1 1219 GLY 1219 1219 ?    ?   ?   A . n 
A 1 1220 ALA 1220 1220 ?    ?   ?   A . n 
A 1 1221 PHE 1221 1221 ?    ?   ?   A . n 
A 1 1222 ASN 1222 1222 ?    ?   ?   A . n 
A 1 1223 ASP 1223 1223 ?    ?   ?   A . n 
A 1 1224 ILE 1224 1224 ?    ?   ?   A . n 
A 1 1225 MET 1225 1225 ?    ?   ?   A . n 
A 1 1226 ARG 1226 1226 ?    ?   ?   A . n 
A 1 1227 ARG 1227 1227 ?    ?   ?   A . n 
A 1 1228 LYS 1228 1228 ?    ?   ?   A . n 
A 1 1229 ASP 1229 1229 ?    ?   ?   A . n 
A 1 1230 SER 1230 1230 ?    ?   ?   A . n 
A 1 1231 ALA 1231 1231 ?    ?   ?   A . n 
A 1 1232 ILE 1232 1232 ?    ?   ?   A . n 
A 1 1233 GLN 1233 1233 ?    ?   ?   A . n 
A 1 1234 GLN 1234 1234 ?    ?   ?   A . n 
A 1 1235 GLN 1235 1235 ?    ?   ?   A . n 
A 1 1236 VAL 1236 1236 ?    ?   ?   A . n 
A 1 1237 ALA 1237 1237 ?    ?   ?   A . n 
A 1 1238 ASN 1238 1238 ?    ?   ?   A . n 
A 1 1239 LEU 1239 1239 ?    ?   ?   A . n 
A 1 1240 GLN 1240 1240 ?    ?   ?   A . n 
A 1 1241 MET 1241 1241 ?    ?   ?   A . n 
A 1 1242 LYS 1242 1242 ?    ?   ?   A . n 
A 1 1243 ILE 1243 1243 ?    ?   ?   A . n 
A 1 1244 VAL 1244 1244 ?    ?   ?   A . n 
A 1 1245 GLN 1245 1245 ?    ?   ?   A . n 
A 1 1246 GLU 1246 1246 ?    ?   ?   A . n 
A 1 1247 ASP 1247 1247 ?    ?   ?   A . n 
A 1 1248 ARG 1248 1248 ?    ?   ?   A . n 
A 1 1249 ALA 1249 1249 ?    ?   ?   A . n 
A 1 1250 VAL 1250 1250 ?    ?   ?   A . n 
A 1 1251 GLU 1251 1251 ?    ?   ?   A . n 
A 1 1252 SER 1252 1252 ?    ?   ?   A . n 
A 1 1253 ARG 1253 1253 ?    ?   ?   A . n 
A 1 1254 THR 1254 1254 ?    ?   ?   A . n 
A 1 1255 THR 1255 1255 ?    ?   ?   A . n 
A 1 1256 ASP 1256 1256 ?    ?   ?   A . n 
A 1 1257 LEU 1257 1257 ?    ?   ?   A . n 
A 1 1258 LEU 1258 1258 ?    ?   ?   A . n 
A 1 1259 THR 1259 1259 ?    ?   ?   A . n 
A 1 1260 ASP 1260 1260 ?    ?   ?   A . n 
A 1 1261 TRP 1261 1261 ?    ?   ?   A . n 
A 1 1262 GLU 1262 1262 ?    ?   ?   A . n 
A 1 1263 LYS 1263 1263 ?    ?   ?   A . n 
A 1 1264 THR 1264 1264 ?    ?   ?   A . n 
A 1 1265 LYS 1265 1265 ?    ?   ?   A . n 
A 1 1266 PRO 1266 1266 ?    ?   ?   A . n 
A 1 1267 VAL 1267 1267 ?    ?   ?   A . n 
A 1 1268 THR 1268 1268 ?    ?   ?   A . n 
A 1 1269 GLY 1269 1269 ?    ?   ?   A . n 
A 1 1270 ASN 1270 1270 ?    ?   ?   A . n 
A 1 1271 LEU 1271 1271 ?    ?   ?   A . n 
A 1 1272 ARG 1272 1272 ?    ?   ?   A . n 
A 1 1273 PRO 1273 1273 ?    ?   ?   A . n 
A 1 1274 GLU 1274 1274 ?    ?   ?   A . n 
A 1 1275 GLU 1275 1275 ?    ?   ?   A . n 
A 1 1276 ALA 1276 1276 ?    ?   ?   A . n 
A 1 1277 LEU 1277 1277 ?    ?   ?   A . n 
A 1 1278 GLN 1278 1278 ?    ?   ?   A . n 
A 1 1279 ALA 1279 1279 ?    ?   ?   A . n 
A 1 1280 LEU 1280 1280 ?    ?   ?   A . n 
A 1 1281 THR 1281 1281 ?    ?   ?   A . n 
A 1 1282 ILE 1282 1282 ?    ?   ?   A . n 
A 1 1283 TYR 1283 1283 ?    ?   ?   A . n 
A 1 1284 GLU 1284 1284 ?    ?   ?   A . n 
A 1 1285 GLY 1285 1285 ?    ?   ?   A . n 
A 1 1286 LYS 1286 1286 ?    ?   ?   A . n 
A 1 1287 PHE 1287 1287 ?    ?   ?   A . n 
A 1 1288 GLY 1288 1288 ?    ?   ?   A . n 
A 1 1289 ARG 1289 1289 ?    ?   ?   A . n 
A 1 1290 LEU 1290 1290 ?    ?   ?   A . n 
A 1 1291 LYS 1291 1291 ?    ?   ?   A . n 
A 1 1292 ASP 1292 1292 ?    ?   ?   A . n 
A 1 1293 ASP 1293 1293 ?    ?   ?   A . n 
A 1 1294 ARG 1294 1294 ?    ?   ?   A . n 
A 1 1295 GLU 1295 1295 ?    ?   ?   A . n 
A 1 1296 LYS 1296 1296 ?    ?   ?   A . n 
A 1 1297 CYS 1297 1297 ?    ?   ?   A . n 
A 1 1298 ALA 1298 1298 ?    ?   ?   A . n 
A 1 1299 LYS 1299 1299 ?    ?   ?   A . n 
A 1 1300 ALA 1300 1300 ?    ?   ?   A . n 
A 1 1301 LYS 1301 1301 ?    ?   ?   A . n 
A 1 1302 GLU 1302 1302 ?    ?   ?   A . n 
A 1 1303 ALA 1303 1303 ?    ?   ?   A . n 
A 1 1304 LEU 1304 1304 ?    ?   ?   A . n 
A 1 1305 GLU 1305 1305 ?    ?   ?   A . n 
A 1 1306 LEU 1306 1306 ?    ?   ?   A . n 
A 1 1307 THR 1307 1307 ?    ?   ?   A . n 
A 1 1308 ASP 1308 1308 ?    ?   ?   A . n 
A 1 1309 THR 1309 1309 ?    ?   ?   A . n 
A 1 1310 GLY 1310 1310 ?    ?   ?   A . n 
A 1 1311 LEU 1311 1311 ?    ?   ?   A . n 
A 1 1312 LEU 1312 1312 ?    ?   ?   A . n 
A 1 1313 SER 1313 1313 ?    ?   ?   A . n 
A 1 1314 GLY 1314 1314 ?    ?   ?   A . n 
A 1 1315 SER 1315 1315 ?    ?   ?   A . n 
A 1 1316 GLU 1316 1316 ?    ?   ?   A . n 
A 1 1317 GLU 1317 1317 ?    ?   ?   A . n 
A 1 1318 ARG 1318 1318 ?    ?   ?   A . n 
A 1 1319 VAL 1319 1319 ?    ?   ?   A . n 
A 1 1320 GLN 1320 1320 ?    ?   ?   A . n 
A 1 1321 VAL 1321 1321 ?    ?   ?   A . n 
A 1 1322 ALA 1322 1322 ?    ?   ?   A . n 
A 1 1323 LEU 1323 1323 ?    ?   ?   A . n 
A 1 1324 GLU 1324 1324 ?    ?   ?   A . n 
A 1 1325 GLU 1325 1325 ?    ?   ?   A . n 
A 1 1326 LEU 1326 1326 ?    ?   ?   A . n 
A 1 1327 GLN 1327 1327 ?    ?   ?   A . n 
A 1 1328 ASP 1328 1328 ?    ?   ?   A . n 
A 1 1329 LEU 1329 1329 ?    ?   ?   A . n 
A 1 1330 LYS 1330 1330 ?    ?   ?   A . n 
A 1 1331 GLY 1331 1331 ?    ?   ?   A . n 
A 1 1332 VAL 1332 1332 ?    ?   ?   A . n 
A 1 1333 TRP 1333 1333 ?    ?   ?   A . n 
A 1 1334 SER 1334 1334 ?    ?   ?   A . n 
A 1 1335 GLU 1335 1335 ?    ?   ?   A . n 
A 1 1336 LEU 1336 1336 ?    ?   ?   A . n 
A 1 1337 SER 1337 1337 ?    ?   ?   A . n 
A 1 1338 LYS 1338 1338 ?    ?   ?   A . n 
A 1 1339 VAL 1339 1339 ?    ?   ?   A . n 
A 1 1340 TRP 1340 1340 ?    ?   ?   A . n 
A 1 1341 GLU 1341 1341 ?    ?   ?   A . n 
A 1 1342 GLN 1342 1342 ?    ?   ?   A . n 
A 1 1343 ILE 1343 1343 ?    ?   ?   A . n 
A 1 1344 ASP 1344 1344 ?    ?   ?   A . n 
A 1 1345 GLN 1345 1345 ?    ?   ?   A . n 
A 1 1346 MET 1346 1346 ?    ?   ?   A . n 
A 1 1347 LYS 1347 1347 ?    ?   ?   A . n 
A 1 1348 GLU 1348 1348 ?    ?   ?   A . n 
A 1 1349 GLN 1349 1349 ?    ?   ?   A . n 
A 1 1350 PRO 1350 1350 ?    ?   ?   A . n 
A 1 1351 TRP 1351 1351 ?    ?   ?   A . n 
A 1 1352 VAL 1352 1352 ?    ?   ?   A . n 
A 1 1353 SER 1353 1353 ?    ?   ?   A . n 
A 1 1354 VAL 1354 1354 ?    ?   ?   A . n 
A 1 1355 GLN 1355 1355 ?    ?   ?   A . n 
A 1 1356 PRO 1356 1356 ?    ?   ?   A . n 
A 1 1357 ARG 1357 1357 ?    ?   ?   A . n 
A 1 1358 LYS 1358 1358 ?    ?   ?   A . n 
A 1 1359 LEU 1359 1359 ?    ?   ?   A . n 
A 1 1360 ARG 1360 1360 ?    ?   ?   A . n 
A 1 1361 GLN 1361 1361 ?    ?   ?   A . n 
A 1 1362 ASN 1362 1362 ?    ?   ?   A . n 
A 1 1363 LEU 1363 1363 ?    ?   ?   A . n 
A 1 1364 ASP 1364 1364 ?    ?   ?   A . n 
A 1 1365 ALA 1365 1365 ?    ?   ?   A . n 
A 1 1366 LEU 1366 1366 ?    ?   ?   A . n 
A 1 1367 LEU 1367 1367 ?    ?   ?   A . n 
A 1 1368 ASN 1368 1368 ?    ?   ?   A . n 
A 1 1369 GLN 1369 1369 ?    ?   ?   A . n 
A 1 1370 LEU 1370 1370 ?    ?   ?   A . n 
A 1 1371 LYS 1371 1371 ?    ?   ?   A . n 
A 1 1372 SER 1372 1372 ?    ?   ?   A . n 
A 1 1373 PHE 1373 1373 ?    ?   ?   A . n 
A 1 1374 PRO 1374 1374 ?    ?   ?   A . n 
A 1 1375 ALA 1375 1375 ?    ?   ?   A . n 
A 1 1376 ARG 1376 1376 ?    ?   ?   A . n 
A 1 1377 LEU 1377 1377 ?    ?   ?   A . n 
A 1 1378 ARG 1378 1378 ?    ?   ?   A . n 
A 1 1379 GLN 1379 1379 ?    ?   ?   A . n 
A 1 1380 TYR 1380 1380 ?    ?   ?   A . n 
A 1 1381 ALA 1381 1381 ?    ?   ?   A . n 
A 1 1382 SER 1382 1382 ?    ?   ?   A . n 
A 1 1383 TYR 1383 1383 ?    ?   ?   A . n 
A 1 1384 GLU 1384 1384 ?    ?   ?   A . n 
A 1 1385 PHE 1385 1385 ?    ?   ?   A . n 
A 1 1386 VAL 1386 1386 ?    ?   ?   A . n 
A 1 1387 GLN 1387 1387 ?    ?   ?   A . n 
A 1 1388 ARG 1388 1388 ?    ?   ?   A . n 
A 1 1389 LEU 1389 1389 ?    ?   ?   A . n 
A 1 1390 LEU 1390 1390 ?    ?   ?   A . n 
A 1 1391 LYS 1391 1391 ?    ?   ?   A . n 
A 1 1392 GLY 1392 1392 ?    ?   ?   A . n 
A 1 1393 TYR 1393 1393 ?    ?   ?   A . n 
A 1 1394 MET 1394 1394 ?    ?   ?   A . n 
A 1 1395 LYS 1395 1395 ?    ?   ?   A . n 
A 1 1396 ILE 1396 1396 ?    ?   ?   A . n 
A 1 1397 ASN 1397 1397 ?    ?   ?   A . n 
A 1 1398 MET 1398 1398 ?    ?   ?   A . n 
A 1 1399 LEU 1399 1399 ?    ?   ?   A . n 
A 1 1400 VAL 1400 1400 ?    ?   ?   A . n 
A 1 1401 ILE 1401 1401 ?    ?   ?   A . n 
A 1 1402 GLU 1402 1402 ?    ?   ?   A . n 
A 1 1403 LEU 1403 1403 ?    ?   ?   A . n 
A 1 1404 LYS 1404 1404 ?    ?   ?   A . n 
A 1 1405 SER 1405 1405 ?    ?   ?   A . n 
A 1 1406 GLU 1406 1406 ?    ?   ?   A . n 
A 1 1407 ALA 1407 1407 ?    ?   ?   A . n 
A 1 1408 LEU 1408 1408 ?    ?   ?   A . n 
A 1 1409 LYS 1409 1409 ?    ?   ?   A . n 
A 1 1410 ASP 1410 1410 ?    ?   ?   A . n 
A 1 1411 ARG 1411 1411 ?    ?   ?   A . n 
A 1 1412 HIS 1412 1412 ?    ?   ?   A . n 
A 1 1413 TRP 1413 1413 ?    ?   ?   A . n 
A 1 1414 LYS 1414 1414 ?    ?   ?   A . n 
A 1 1415 GLN 1415 1415 ?    ?   ?   A . n 
A 1 1416 LEU 1416 1416 ?    ?   ?   A . n 
A 1 1417 MET 1417 1417 ?    ?   ?   A . n 
A 1 1418 LYS 1418 1418 ?    ?   ?   A . n 
A 1 1419 ARG 1419 1419 ?    ?   ?   A . n 
A 1 1420 LEU 1420 1420 ?    ?   ?   A . n 
A 1 1421 HIS 1421 1421 ?    ?   ?   A . n 
A 1 1422 VAL 1422 1422 ?    ?   ?   A . n 
A 1 1423 ASN 1423 1423 ?    ?   ?   A . n 
A 1 1424 TRP 1424 1424 ?    ?   ?   A . n 
A 1 1425 VAL 1425 1425 ?    ?   ?   A . n 
A 1 1426 VAL 1426 1426 ?    ?   ?   A . n 
A 1 1427 SER 1427 1427 ?    ?   ?   A . n 
A 1 1428 GLU 1428 1428 ?    ?   ?   A . n 
A 1 1429 LEU 1429 1429 ?    ?   ?   A . n 
A 1 1430 THR 1430 1430 ?    ?   ?   A . n 
A 1 1431 LEU 1431 1431 ?    ?   ?   A . n 
A 1 1432 GLY 1432 1432 ?    ?   ?   A . n 
A 1 1433 GLN 1433 1433 ?    ?   ?   A . n 
A 1 1434 ILE 1434 1434 ?    ?   ?   A . n 
A 1 1435 TRP 1435 1435 ?    ?   ?   A . n 
A 1 1436 ASP 1436 1436 ?    ?   ?   A . n 
A 1 1437 VAL 1437 1437 ?    ?   ?   A . n 
A 1 1438 ASP 1438 1438 ?    ?   ?   A . n 
A 1 1439 LEU 1439 1439 ?    ?   ?   A . n 
A 1 1440 GLN 1440 1440 ?    ?   ?   A . n 
A 1 1441 LYS 1441 1441 ?    ?   ?   A . n 
A 1 1442 ASN 1442 1442 ?    ?   ?   A . n 
A 1 1443 GLU 1443 1443 ?    ?   ?   A . n 
A 1 1444 ALA 1444 1444 ?    ?   ?   A . n 
A 1 1445 ILE 1445 1445 ?    ?   ?   A . n 
A 1 1446 VAL 1446 1446 ?    ?   ?   A . n 
A 1 1447 LYS 1447 1447 ?    ?   ?   A . n 
A 1 1448 ASP 1448 1448 ?    ?   ?   A . n 
A 1 1449 VAL 1449 1449 ?    ?   ?   A . n 
A 1 1450 LEU 1450 1450 ?    ?   ?   A . n 
A 1 1451 LEU 1451 1451 ?    ?   ?   A . n 
A 1 1452 VAL 1452 1452 ?    ?   ?   A . n 
A 1 1453 ALA 1453 1453 ?    ?   ?   A . n 
A 1 1454 GLN 1454 1454 ?    ?   ?   A . n 
A 1 1455 GLY 1455 1455 ?    ?   ?   A . n 
A 1 1456 GLU 1456 1456 ?    ?   ?   A . n 
A 1 1457 MET 1457 1457 ?    ?   ?   A . n 
A 1 1458 ALA 1458 1458 ?    ?   ?   A . n 
A 1 1459 LEU 1459 1459 ?    ?   ?   A . n 
A 1 1460 GLU 1460 1460 ?    ?   ?   A . n 
A 1 1461 GLU 1461 1461 ?    ?   ?   A . n 
A 1 1462 PHE 1462 1462 ?    ?   ?   A . n 
A 1 1463 LEU 1463 1463 ?    ?   ?   A . n 
A 1 1464 LYS 1464 1464 ?    ?   ?   A . n 
A 1 1465 GLN 1465 1465 ?    ?   ?   A . n 
A 1 1466 ILE 1466 1466 ?    ?   ?   A . n 
A 1 1467 ARG 1467 1467 ?    ?   ?   A . n 
A 1 1468 GLU 1468 1468 ?    ?   ?   A . n 
A 1 1469 VAL 1469 1469 ?    ?   ?   A . n 
A 1 1470 TRP 1470 1470 ?    ?   ?   A . n 
A 1 1471 ASN 1471 1471 ?    ?   ?   A . n 
A 1 1472 THR 1472 1472 ?    ?   ?   A . n 
A 1 1473 TYR 1473 1473 ?    ?   ?   A . n 
A 1 1474 GLU 1474 1474 ?    ?   ?   A . n 
A 1 1475 LEU 1475 1475 ?    ?   ?   A . n 
A 1 1476 ASP 1476 1476 ?    ?   ?   A . n 
A 1 1477 LEU 1477 1477 ?    ?   ?   A . n 
A 1 1478 VAL 1478 1478 ?    ?   ?   A . n 
A 1 1479 ASN 1479 1479 ?    ?   ?   A . n 
A 1 1480 TYR 1480 1480 ?    ?   ?   A . n 
A 1 1481 GLN 1481 1481 ?    ?   ?   A . n 
A 1 1482 ASN 1482 1482 ?    ?   ?   A . n 
A 1 1483 LYS 1483 1483 ?    ?   ?   A . n 
A 1 1484 CYS 1484 1484 ?    ?   ?   A . n 
A 1 1485 ARG 1485 1485 ?    ?   ?   A . n 
A 1 1486 LEU 1486 1486 ?    ?   ?   A . n 
A 1 1487 ILE 1487 1487 ?    ?   ?   A . n 
A 1 1488 ARG 1488 1488 ?    ?   ?   A . n 
A 1 1489 GLY 1489 1489 ?    ?   ?   A . n 
A 1 1490 TRP 1490 1490 ?    ?   ?   A . n 
A 1 1491 ASP 1491 1491 ?    ?   ?   A . n 
A 1 1492 ASP 1492 1492 ?    ?   ?   A . n 
A 1 1493 LEU 1493 1493 ?    ?   ?   A . n 
A 1 1494 PHE 1494 1494 ?    ?   ?   A . n 
A 1 1495 ASN 1495 1495 ?    ?   ?   A . n 
A 1 1496 LYS 1496 1496 ?    ?   ?   A . n 
A 1 1497 VAL 1497 1497 ?    ?   ?   A . n 
A 1 1498 LYS 1498 1498 ?    ?   ?   A . n 
A 1 1499 GLU 1499 1499 ?    ?   ?   A . n 
A 1 1500 HIS 1500 1500 ?    ?   ?   A . n 
A 1 1501 ILE 1501 1501 ?    ?   ?   A . n 
A 1 1502 ASN 1502 1502 ?    ?   ?   A . n 
A 1 1503 SER 1503 1503 ?    ?   ?   A . n 
A 1 1504 VAL 1504 1504 ?    ?   ?   A . n 
A 1 1505 SER 1505 1505 ?    ?   ?   A . n 
A 1 1506 ALA 1506 1506 ?    ?   ?   A . n 
A 1 1507 MET 1507 1507 ?    ?   ?   A . n 
A 1 1508 LYS 1508 1508 ?    ?   ?   A . n 
A 1 1509 LEU 1509 1509 ?    ?   ?   A . n 
A 1 1510 SER 1510 1510 ?    ?   ?   A . n 
A 1 1511 PRO 1511 1511 ?    ?   ?   A . n 
A 1 1512 TYR 1512 1512 ?    ?   ?   A . n 
A 1 1513 TYR 1513 1513 ?    ?   ?   A . n 
A 1 1514 LYS 1514 1514 ?    ?   ?   A . n 
A 1 1515 VAL 1515 1515 ?    ?   ?   A . n 
A 1 1516 PHE 1516 1516 ?    ?   ?   A . n 
A 1 1517 GLU 1517 1517 ?    ?   ?   A . n 
A 1 1518 GLU 1518 1518 ?    ?   ?   A . n 
A 1 1519 ASP 1519 1519 ?    ?   ?   A . n 
A 1 1520 ALA 1520 1520 ?    ?   ?   A . n 
A 1 1521 LEU 1521 1521 ?    ?   ?   A . n 
A 1 1522 SER 1522 1522 ?    ?   ?   A . n 
A 1 1523 TRP 1523 1523 ?    ?   ?   A . n 
A 1 1524 GLU 1524 1524 ?    ?   ?   A . n 
A 1 1525 ASP 1525 1525 ?    ?   ?   A . n 
A 1 1526 LYS 1526 1526 ?    ?   ?   A . n 
A 1 1527 LEU 1527 1527 ?    ?   ?   A . n 
A 1 1528 ASN 1528 1528 ?    ?   ?   A . n 
A 1 1529 ARG 1529 1529 ?    ?   ?   A . n 
A 1 1530 ILE 1530 1530 ?    ?   ?   A . n 
A 1 1531 MET 1531 1531 ?    ?   ?   A . n 
A 1 1532 ALA 1532 1532 ?    ?   ?   A . n 
A 1 1533 LEU 1533 1533 ?    ?   ?   A . n 
A 1 1534 PHE 1534 1534 ?    ?   ?   A . n 
A 1 1535 ASP 1535 1535 1535 ASP ASP A . n 
A 1 1536 VAL 1536 1536 1536 VAL VAL A . n 
A 1 1537 TRP 1537 1537 1537 TRP TRP A . n 
A 1 1538 ILE 1538 1538 1538 ILE ILE A . n 
A 1 1539 ASP 1539 1539 1539 ASP ASP A . n 
A 1 1540 VAL 1540 1540 1540 VAL VAL A . n 
A 1 1541 GLN 1541 1541 1541 GLN GLN A . n 
A 1 1542 ARG 1542 1542 1542 ARG ARG A . n 
A 1 1543 ARG 1543 1543 1543 ARG ARG A . n 
A 1 1544 TRP 1544 1544 1544 TRP TRP A . n 
A 1 1545 VAL 1545 1545 1545 VAL VAL A . n 
A 1 1546 TYR 1546 1546 1546 TYR TYR A . n 
A 1 1547 LEU 1547 1547 1547 LEU LEU A . n 
A 1 1548 GLU 1548 1548 1548 GLU GLU A . n 
A 1 1549 GLY 1549 1549 1549 GLY GLY A . n 
A 1 1550 ILE 1550 1550 1550 ILE ILE A . n 
A 1 1551 PHE 1551 1551 1551 PHE PHE A . n 
A 1 1552 THR 1552 1552 1552 THR THR A . n 
A 1 1553 GLY 1553 1553 1553 GLY GLY A . n 
A 1 1554 SER 1554 1554 1554 SER SER A . n 
A 1 1555 ALA 1555 1555 1555 ALA ALA A . n 
A 1 1556 ASP 1556 1556 1556 ASP ASP A . n 
A 1 1557 ILE 1557 1557 1557 ILE ILE A . n 
A 1 1558 LYS 1558 1558 1558 LYS LYS A . n 
A 1 1559 HIS 1559 1559 1559 HIS HIS A . n 
A 1 1560 LEU 1560 1560 1560 LEU LEU A . n 
A 1 1561 LEU 1561 1561 1561 LEU LEU A . n 
A 1 1562 PRO 1562 1562 1562 PRO PRO A . n 
A 1 1563 VAL 1563 1563 1563 VAL VAL A . n 
A 1 1564 GLU 1564 1564 1564 GLU GLU A . n 
A 1 1565 THR 1565 1565 1565 THR THR A . n 
A 1 1566 GLN 1566 1566 1566 GLN GLN A . n 
A 1 1567 ARG 1567 1567 1567 ARG ARG A . n 
A 1 1568 PHE 1568 1568 1568 PHE PHE A . n 
A 1 1569 GLN 1569 1569 1569 GLN GLN A . n 
A 1 1570 SER 1570 1570 1570 SER SER A . n 
A 1 1571 ILE 1571 1571 1571 ILE ILE A . n 
A 1 1572 SER 1572 1572 1572 SER SER A . n 
A 1 1573 THR 1573 1573 1573 THR THR A . n 
A 1 1574 GLU 1574 1574 1574 GLU GLU A . n 
A 1 1575 PHE 1575 1575 1575 PHE PHE A . n 
A 1 1576 LEU 1576 1576 1576 LEU LEU A . n 
A 1 1577 ALA 1577 1577 1577 ALA ALA A . n 
A 1 1578 LEU 1578 1578 1578 LEU LEU A . n 
A 1 1579 MET 1579 1579 1579 MET MET A . n 
A 1 1580 LYS 1580 1580 1580 LYS LYS A . n 
A 1 1581 LYS 1581 1581 1581 LYS LYS A . n 
A 1 1582 VAL 1582 1582 1582 VAL VAL A . n 
A 1 1583 SER 1583 1583 1583 SER SER A . n 
A 1 1584 LYS 1584 1584 1584 LYS LYS A . n 
A 1 1585 SER 1585 1585 1585 SER SER A . n 
A 1 1586 PRO 1586 1586 1586 PRO PRO A . n 
A 1 1587 LEU 1587 1587 1587 LEU LEU A . n 
A 1 1588 VAL 1588 1588 1588 VAL VAL A . n 
A 1 1589 MET 1589 1589 1589 MET MET A . n 
A 1 1590 ASP 1590 1590 1590 ASP ASP A . n 
A 1 1591 VAL 1591 1591 1591 VAL VAL A . n 
A 1 1592 LEU 1592 1592 1592 LEU LEU A . n 
A 1 1593 ASN 1593 1593 1593 ASN ASN A . n 
A 1 1594 ILE 1594 1594 1594 ILE ILE A . n 
A 1 1595 GLN 1595 1595 1595 GLN GLN A . n 
A 1 1596 GLY 1596 1596 1596 GLY GLY A . n 
A 1 1597 VAL 1597 1597 1597 VAL VAL A . n 
A 1 1598 GLN 1598 1598 1598 GLN GLN A . n 
A 1 1599 ARG 1599 1599 1599 ARG ARG A . n 
A 1 1600 SER 1600 1600 1600 SER SER A . n 
A 1 1601 LEU 1601 1601 1601 LEU LEU A . n 
A 1 1602 GLU 1602 1602 1602 GLU GLU A . n 
A 1 1603 ARG 1603 1603 1603 ARG ARG A . n 
A 1 1604 LEU 1604 1604 1604 LEU LEU A . n 
A 1 1605 ALA 1605 1605 1605 ALA ALA A . n 
A 1 1606 ASP 1606 1606 1606 ASP ASP A . n 
A 1 1607 LEU 1607 1607 1607 LEU LEU A . n 
A 1 1608 LEU 1608 1608 1608 LEU LEU A . n 
A 1 1609 GLY 1609 1609 1609 GLY GLY A . n 
A 1 1610 LYS 1610 1610 1610 LYS LYS A . n 
A 1 1611 ILE 1611 1611 1611 ILE ILE A . n 
A 1 1612 GLN 1612 1612 1612 GLN GLN A . n 
A 1 1613 LYS 1613 1613 1613 LYS LYS A . n 
A 1 1614 ALA 1614 1614 1614 ALA ALA A . n 
A 1 1615 LEU 1615 1615 1615 LEU LEU A . n 
A 1 1616 GLY 1616 1616 1616 GLY GLY A . n 
A 1 1617 GLU 1617 1617 1617 GLU GLU A . n 
A 1 1618 TYR 1618 1618 1618 TYR TYR A . n 
A 1 1619 LEU 1619 1619 1619 LEU LEU A . n 
A 1 1620 GLU 1620 1620 1620 GLU GLU A . n 
A 1 1621 ARG 1621 1621 1621 ARG ARG A . n 
A 1 1622 GLU 1622 1622 1622 GLU GLU A . n 
A 1 1623 ARG 1623 1623 1623 ARG ARG A . n 
A 1 1624 SER 1624 1624 1624 SER SER A . n 
A 1 1625 SER 1625 1625 1625 SER SER A . n 
A 1 1626 PHE 1626 1626 1626 PHE PHE A . n 
A 1 1627 PRO 1627 1627 1627 PRO PRO A . n 
A 1 1628 ARG 1628 1628 1628 ARG ARG A . n 
A 1 1629 PHE 1629 1629 1629 PHE PHE A . n 
A 1 1630 TYR 1630 1630 1630 TYR TYR A . n 
A 1 1631 PHE 1631 1631 1631 PHE PHE A . n 
A 1 1632 VAL 1632 1632 1632 VAL VAL A . n 
A 1 1633 GLY 1633 1633 1633 GLY GLY A . n 
A 1 1634 ASP 1634 1634 1634 ASP ASP A . n 
A 1 1635 GLU 1635 1635 1635 GLU GLU A . n 
A 1 1636 ASP 1636 1636 1636 ASP ASP A . n 
A 1 1637 LEU 1637 1637 1637 LEU LEU A . n 
A 1 1638 LEU 1638 1638 1638 LEU LEU A . n 
A 1 1639 GLU 1639 1639 1639 GLU GLU A . n 
A 1 1640 ILE 1640 1640 1640 ILE ILE A . n 
A 1 1641 ILE 1641 1641 1641 ILE ILE A . n 
A 1 1642 GLY 1642 1642 1642 GLY GLY A . n 
A 1 1643 ASN 1643 1643 1643 ASN ASN A . n 
A 1 1644 SER 1644 1644 1644 SER SER A . n 
A 1 1645 LYS 1645 1645 1645 LYS LYS A . n 
A 1 1646 ASN 1646 1646 1646 ASN ASN A . n 
A 1 1647 VAL 1647 1647 1647 VAL VAL A . n 
A 1 1648 ALA 1648 1648 1648 ALA ALA A . n 
A 1 1649 LYS 1649 1649 1649 LYS LYS A . n 
A 1 1650 LEU 1650 1650 1650 LEU LEU A . n 
A 1 1651 GLN 1651 1651 1651 GLN GLN A . n 
A 1 1652 LYS 1652 1652 1652 LYS LYS A . n 
A 1 1653 HIS 1653 1653 1653 HIS HIS A . n 
A 1 1654 PHE 1654 1654 1654 PHE PHE A . n 
A 1 1655 LYS 1655 1655 1655 LYS LYS A . n 
A 1 1656 LYS 1656 1656 1656 LYS LYS A . n 
A 1 1657 MET 1657 1657 1657 MET MET A . n 
A 1 1658 PHE 1658 1658 1658 PHE PHE A . n 
A 1 1659 ALA 1659 1659 1659 ALA ALA A . n 
A 1 1660 GLY 1660 1660 1660 GLY GLY A . n 
A 1 1661 VAL 1661 1661 1661 VAL VAL A . n 
A 1 1662 SER 1662 1662 1662 SER SER A . n 
A 1 1663 SER 1663 1663 1663 SER SER A . n 
A 1 1664 ILE 1664 1664 1664 ILE ILE A . n 
A 1 1665 ILE 1665 1665 1665 ILE ILE A . n 
A 1 1666 LEU 1666 1666 1666 LEU LEU A . n 
A 1 1667 ASN 1667 1667 1667 ASN ASN A . n 
A 1 1668 GLU 1668 1668 1668 GLU GLU A . n 
A 1 1669 ASP 1669 1669 1669 ASP ASP A . n 
A 1 1670 ASN 1670 1670 1670 ASN ASN A . n 
A 1 1671 SER 1671 1671 1671 SER SER A . n 
A 1 1672 VAL 1672 1672 1672 VAL VAL A . n 
A 1 1673 VAL 1673 1673 1673 VAL VAL A . n 
A 1 1674 LEU 1674 1674 1674 LEU LEU A . n 
A 1 1675 GLY 1675 1675 1675 GLY GLY A . n 
A 1 1676 ILE 1676 1676 1676 ILE ILE A . n 
A 1 1677 SER 1677 1677 1677 SER SER A . n 
A 1 1678 SER 1678 1678 1678 SER SER A . n 
A 1 1679 ARG 1679 1679 1679 ARG ARG A . n 
A 1 1680 GLU 1680 1680 1680 GLU GLU A . n 
A 1 1681 GLY 1681 1681 1681 GLY GLY A . n 
A 1 1682 GLU 1682 1682 1682 GLU GLU A . n 
A 1 1683 GLU 1683 1683 1683 GLU GLU A . n 
A 1 1684 VAL 1684 1684 1684 VAL VAL A . n 
A 1 1685 MET 1685 1685 1685 MET MET A . n 
A 1 1686 PHE 1686 1686 1686 PHE PHE A . n 
A 1 1687 LYS 1687 1687 1687 LYS LYS A . n 
A 1 1688 THR 1688 1688 1688 THR THR A . n 
A 1 1689 PRO 1689 1689 1689 PRO PRO A . n 
A 1 1690 VAL 1690 1690 1690 VAL VAL A . n 
A 1 1691 SER 1691 1691 1691 SER SER A . n 
A 1 1692 ILE 1692 1692 1692 ILE ILE A . n 
A 1 1693 THR 1693 1693 1693 THR THR A . n 
A 1 1694 GLU 1694 1694 1694 GLU GLU A . n 
A 1 1695 HIS 1695 1695 1695 HIS HIS A . n 
A 1 1696 PRO 1696 1696 1696 PRO PRO A . n 
A 1 1697 LYS 1697 1697 1697 LYS LYS A . n 
A 1 1698 ILE 1698 1698 1698 ILE ILE A . n 
A 1 1699 ASN 1699 1699 1699 ASN ASN A . n 
A 1 1700 GLU 1700 1700 1700 GLU GLU A . n 
A 1 1701 TRP 1701 1701 1701 TRP TRP A . n 
A 1 1702 LEU 1702 1702 1702 LEU LEU A . n 
A 1 1703 THR 1703 1703 1703 THR THR A . n 
A 1 1704 LEU 1704 1704 1704 LEU LEU A . n 
A 1 1705 VAL 1705 1705 1705 VAL VAL A . n 
A 1 1706 GLU 1706 1706 1706 GLU GLU A . n 
A 1 1707 LYS 1707 1707 1707 LYS LYS A . n 
A 1 1708 GLU 1708 1708 1708 GLU GLU A . n 
A 1 1709 MET 1709 1709 1709 MET MET A . n 
A 1 1710 ARG 1710 1710 1710 ARG ARG A . n 
A 1 1711 VAL 1711 1711 1711 VAL VAL A . n 
A 1 1712 THR 1712 1712 1712 THR THR A . n 
A 1 1713 LEU 1713 1713 1713 LEU LEU A . n 
A 1 1714 ALA 1714 1714 1714 ALA ALA A . n 
A 1 1715 LYS 1715 1715 1715 LYS LYS A . n 
A 1 1716 LEU 1716 1716 1716 LEU LEU A . n 
A 1 1717 LEU 1717 1717 1717 LEU LEU A . n 
A 1 1718 ALA 1718 1718 1718 ALA ALA A . n 
A 1 1719 GLU 1719 1719 1719 GLU GLU A . n 
A 1 1720 SER 1720 1720 1720 SER SER A . n 
A 1 1721 VAL 1721 1721 1721 VAL VAL A . n 
A 1 1722 THR 1722 1722 1722 THR THR A . n 
A 1 1723 GLU 1723 1723 1723 GLU GLU A . n 
A 1 1724 VAL 1724 1724 1724 VAL VAL A . n 
A 1 1725 GLU 1725 1725 1725 GLU GLU A . n 
A 1 1726 ILE 1726 1726 1726 ILE ILE A . n 
A 1 1727 PHE 1727 1727 1727 PHE PHE A . n 
A 1 1728 GLY 1728 1728 1728 GLY GLY A . n 
A 1 1729 LYS 1729 1729 1729 LYS LYS A . n 
A 1 1730 ALA 1730 1730 1730 ALA ALA A . n 
A 1 1731 THR 1731 1731 1731 THR THR A . n 
A 1 1732 SER 1732 1732 1732 SER SER A . n 
A 1 1733 ILE 1733 1733 1733 ILE ILE A . n 
A 1 1734 ASP 1734 1734 1734 ASP ASP A . n 
A 1 1735 PRO 1735 1735 1735 PRO PRO A . n 
A 1 1736 ASN 1736 1736 1736 ASN ASN A . n 
A 1 1737 THR 1737 1737 1737 THR THR A . n 
A 1 1738 TYR 1738 1738 1738 TYR TYR A . n 
A 1 1739 ILE 1739 1739 1739 ILE ILE A . n 
A 1 1740 THR 1740 1740 1740 THR THR A . n 
A 1 1741 TRP 1741 1741 1741 TRP TRP A . n 
A 1 1742 ILE 1742 1742 1742 ILE ILE A . n 
A 1 1743 ASP 1743 1743 1743 ASP ASP A . n 
A 1 1744 LYS 1744 1744 1744 LYS LYS A . n 
A 1 1745 TYR 1745 1745 1745 TYR TYR A . n 
A 1 1746 GLN 1746 1746 1746 GLN GLN A . n 
A 1 1747 ALA 1747 1747 1747 ALA ALA A . n 
A 1 1748 GLN 1748 1748 1748 GLN GLN A . n 
A 1 1749 LEU 1749 1749 1749 LEU LEU A . n 
A 1 1750 VAL 1750 1750 1750 VAL VAL A . n 
A 1 1751 VAL 1751 1751 1751 VAL VAL A . n 
A 1 1752 LEU 1752 1752 1752 LEU LEU A . n 
A 1 1753 SER 1753 1753 1753 SER SER A . n 
A 1 1754 ALA 1754 1754 1754 ALA ALA A . n 
A 1 1755 GLN 1755 1755 1755 GLN GLN A . n 
A 1 1756 ILE 1756 1756 1756 ILE ILE A . n 
A 1 1757 ALA 1757 1757 1757 ALA ALA A . n 
A 1 1758 TRP 1758 1758 1758 TRP TRP A . n 
A 1 1759 SER 1759 1759 1759 SER SER A . n 
A 1 1760 GLU 1760 1760 1760 GLU GLU A . n 
A 1 1761 ASN 1761 1761 1761 ASN ASN A . n 
A 1 1762 VAL 1762 1762 1762 VAL VAL A . n 
A 1 1763 GLU 1763 1763 1763 GLU GLU A . n 
A 1 1764 THR 1764 1764 1764 THR THR A . n 
A 1 1765 ALA 1765 1765 1765 ALA ALA A . n 
A 1 1766 LEU 1766 1766 1766 LEU LEU A . n 
A 1 1767 SER 1767 1767 1767 SER SER A . n 
A 1 1768 SER 1768 1768 1768 SER SER A . n 
A 1 1769 MET 1769 1769 1769 MET MET A . n 
A 1 1770 GLY 1770 1770 1770 GLY GLY A . n 
A 1 1771 GLY 1771 1771 1771 GLY GLY A . n 
A 1 1772 GLY 1772 1772 1772 GLY GLY A . n 
A 1 1773 GLY 1773 1773 1773 GLY GLY A . n 
A 1 1774 ASP 1774 1774 1774 ASP ASP A . n 
A 1 1775 ALA 1775 1775 1775 ALA ALA A . n 
A 1 1776 ALA 1776 1776 1776 ALA ALA A . n 
A 1 1777 PRO 1777 1777 1777 PRO PRO A . n 
A 1 1778 LEU 1778 1778 1778 LEU LEU A . n 
A 1 1779 HIS 1779 1779 1779 HIS HIS A . n 
A 1 1780 SER 1780 1780 1780 SER SER A . n 
A 1 1781 VAL 1781 1781 1781 VAL VAL A . n 
A 1 1782 LEU 1782 1782 1782 LEU LEU A . n 
A 1 1783 SER 1783 1783 1783 SER SER A . n 
A 1 1784 ASN 1784 1784 1784 ASN ASN A . n 
A 1 1785 VAL 1785 1785 1785 VAL VAL A . n 
A 1 1786 GLU 1786 1786 1786 GLU GLU A . n 
A 1 1787 VAL 1787 1787 1787 VAL VAL A . n 
A 1 1788 THR 1788 1788 1788 THR THR A . n 
A 1 1789 LEU 1789 1789 1789 LEU LEU A . n 
A 1 1790 ASN 1790 1790 1790 ASN ASN A . n 
A 1 1791 VAL 1791 1791 1791 VAL VAL A . n 
A 1 1792 LEU 1792 1792 1792 LEU LEU A . n 
A 1 1793 ALA 1793 1793 1793 ALA ALA A . n 
A 1 1794 ASP 1794 1794 1794 ASP ASP A . n 
A 1 1795 SER 1795 1795 1795 SER SER A . n 
A 1 1796 VAL 1796 1796 1796 VAL VAL A . n 
A 1 1797 LEU 1797 1797 1797 LEU LEU A . n 
A 1 1798 MET 1798 1798 1798 MET MET A . n 
A 1 1799 GLU 1799 1799 1799 GLU GLU A . n 
A 1 1800 GLN 1800 1800 1800 GLN GLN A . n 
A 1 1801 PRO 1801 1801 1801 PRO PRO A . n 
A 1 1802 PRO 1802 1802 1802 PRO PRO A . n 
A 1 1803 LEU 1803 1803 1803 LEU LEU A . n 
A 1 1804 ARG 1804 1804 1804 ARG ARG A . n 
A 1 1805 ARG 1805 1805 1805 ARG ARG A . n 
A 1 1806 ARG 1806 1806 1806 ARG ARG A . n 
A 1 1807 LYS 1807 1807 1807 LYS LYS A . n 
A 1 1808 LEU 1808 1808 1808 LEU LEU A . n 
A 1 1809 GLU 1809 1809 1809 GLU GLU A . n 
A 1 1810 HIS 1810 1810 1810 HIS HIS A . n 
A 1 1811 LEU 1811 1811 1811 LEU LEU A . n 
A 1 1812 ILE 1812 1812 1812 ILE ILE A . n 
A 1 1813 THR 1813 1813 1813 THR THR A . n 
A 1 1814 GLU 1814 1814 1814 GLU GLU A . n 
A 1 1815 LEU 1815 1815 1815 LEU LEU A . n 
A 1 1816 VAL 1816 1816 1816 VAL VAL A . n 
A 1 1817 HIS 1817 1817 1817 HIS HIS A . n 
A 1 1818 GLN 1818 1818 1818 GLN GLN A . n 
A 1 1819 ARG 1819 1819 1819 ARG ARG A . n 
A 1 1820 ASP 1820 1820 1820 ASP ASP A . n 
A 1 1821 VAL 1821 1821 1821 VAL VAL A . n 
A 1 1822 THR 1822 1822 1822 THR THR A . n 
A 1 1823 ARG 1823 1823 1823 ARG ARG A . n 
A 1 1824 SER 1824 1824 1824 SER SER A . n 
A 1 1825 LEU 1825 1825 1825 LEU LEU A . n 
A 1 1826 ILE 1826 1826 1826 ILE ILE A . n 
A 1 1827 LYS 1827 1827 1827 LYS LYS A . n 
A 1 1828 SER 1828 1828 1828 SER SER A . n 
A 1 1829 LYS 1829 1829 1829 LYS LYS A . n 
A 1 1830 ILE 1830 1830 1830 ILE ILE A . n 
A 1 1831 ASP 1831 1831 1831 ASP ASP A . n 
A 1 1832 ASN 1832 1832 1832 ASN ASN A . n 
A 1 1833 ALA 1833 1833 1833 ALA ALA A . n 
A 1 1834 LYS 1834 1834 1834 LYS LYS A . n 
A 1 1835 SER 1835 1835 1835 SER SER A . n 
A 1 1836 PHE 1836 1836 1836 PHE PHE A . n 
A 1 1837 GLU 1837 1837 1837 GLU GLU A . n 
A 1 1838 TRP 1838 1838 1838 TRP TRP A . n 
A 1 1839 LEU 1839 1839 1839 LEU LEU A . n 
A 1 1840 SER 1840 1840 1840 SER SER A . n 
A 1 1841 GLN 1841 1841 1841 GLN GLN A . n 
A 1 1842 MET 1842 1842 1842 MET MET A . n 
A 1 1843 ARG 1843 1843 1843 ARG ARG A . n 
A 1 1844 PHE 1844 1844 1844 PHE PHE A . n 
A 1 1845 TYR 1845 1845 1845 TYR TYR A . n 
A 1 1846 PHE 1846 1846 1846 PHE PHE A . n 
A 1 1847 ASP 1847 1847 1847 ASP ASP A . n 
A 1 1848 PRO 1848 1848 1848 PRO PRO A . n 
A 1 1849 LYS 1849 1849 1849 LYS LYS A . n 
A 1 1850 GLN 1850 1850 1850 GLN GLN A . n 
A 1 1851 THR 1851 1851 1851 THR THR A . n 
A 1 1852 ASP 1852 1852 1852 ASP ASP A . n 
A 1 1853 VAL 1853 1853 1853 VAL VAL A . n 
A 1 1854 LEU 1854 1854 1854 LEU LEU A . n 
A 1 1855 GLN 1855 1855 1855 GLN GLN A . n 
A 1 1856 GLN 1856 1856 1856 GLN GLN A . n 
A 1 1857 LEU 1857 1857 1857 LEU LEU A . n 
A 1 1858 SER 1858 1858 1858 SER SER A . n 
A 1 1859 ILE 1859 1859 1859 ILE ILE A . n 
A 1 1860 GLN 1860 1860 1860 GLN GLN A . n 
A 1 1861 MET 1861 1861 1861 MET MET A . n 
A 1 1862 ALA 1862 1862 1862 ALA ALA A . n 
A 1 1863 ASN 1863 1863 1863 ASN ASN A . n 
A 1 1864 ALA 1864 1864 1864 ALA ALA A . n 
A 1 1865 LYS 1865 1865 1865 LYS LYS A . n 
A 1 1866 PHE 1866 1866 1866 PHE PHE A . n 
A 1 1867 ASN 1867 1867 1867 ASN ASN A . n 
A 1 1868 TYR 1868 1868 1868 TYR TYR A . n 
A 1 1869 GLY 1869 1869 1869 GLY GLY A . n 
A 1 1870 PHE 1870 1870 1870 PHE PHE A . n 
A 1 1871 GLU 1871 1871 1871 GLU GLU A . n 
A 1 1872 TYR 1872 1872 1872 TYR TYR A . n 
A 1 1873 LEU 1873 1873 1873 LEU LEU A . n 
A 1 1874 GLY 1874 1874 1874 GLY GLY A . n 
A 1 1875 VAL 1875 1875 1875 VAL VAL A . n 
A 1 1876 GLN 1876 1876 1876 GLN GLN A . n 
A 1 1877 ASP 1877 1877 1877 ASP ASP A . n 
A 1 1878 LYS 1878 1878 1878 LYS LYS A . n 
A 1 1879 LEU 1879 1879 1879 LEU LEU A . n 
A 1 1880 VAL 1880 1880 1880 VAL VAL A . n 
A 1 1881 GLN 1881 1881 1881 GLN GLN A . n 
A 1 1882 THR 1882 1882 1882 THR THR A . n 
A 1 1883 PRO 1883 1883 1883 PRO PRO A . n 
A 1 1884 LEU 1884 1884 1884 LEU LEU A . n 
A 1 1885 THR 1885 1885 1885 THR THR A . n 
A 1 1886 ASP 1886 1886 1886 ASP ASP A . n 
A 1 1887 ARG 1887 1887 1887 ARG ARG A . n 
A 1 1888 CYS 1888 1888 1888 CYS CYS A . n 
A 1 1889 TYR 1889 1889 1889 TYR TYR A . n 
A 1 1890 LEU 1890 1890 1890 LEU LEU A . n 
A 1 1891 THR 1891 1891 1891 THR THR A . n 
A 1 1892 MET 1892 1892 1892 MET MET A . n 
A 1 1893 THR 1893 1893 1893 THR THR A . n 
A 1 1894 GLN 1894 1894 1894 GLN GLN A . n 
A 1 1895 ALA 1895 1895 1895 ALA ALA A . n 
A 1 1896 LEU 1896 1896 1896 LEU LEU A . n 
A 1 1897 GLU 1897 1897 1897 GLU GLU A . n 
A 1 1898 ALA 1898 1898 1898 ALA ALA A . n 
A 1 1899 ARG 1899 1899 1899 ARG ARG A . n 
A 1 1900 LEU 1900 1900 1900 LEU LEU A . n 
A 1 1901 GLY 1901 1901 1901 GLY GLY A . n 
A 1 1902 GLY 1902 1902 1902 GLY GLY A . n 
A 1 1903 SER 1903 1903 1903 SER SER A . n 
A 1 1904 PRO 1904 1904 1904 PRO PRO A . n 
A 1 1905 PHE 1905 1905 1905 PHE PHE A . n 
A 1 1906 GLY 1906 1906 1906 GLY GLY A . n 
A 1 1907 PRO 1907 1907 1907 PRO PRO A . n 
A 1 1908 ALA 1908 1908 1908 ALA ALA A . n 
A 1 1909 GLY 1909 1909 1909 GLY GLY A . n 
A 1 1910 THR 1910 1910 1910 THR THR A . n 
A 1 1911 GLY 1911 1911 1911 GLY GLY A . n 
A 1 1912 LYS 1912 1912 1912 LYS LYS A . n 
A 1 1913 THR 1913 1913 1913 THR THR A . n 
A 1 1914 GLU 1914 1914 1914 GLU GLU A . n 
A 1 1915 SER 1915 1915 1915 SER SER A . n 
A 1 1916 VAL 1916 1916 1916 VAL VAL A . n 
A 1 1917 LYS 1917 1917 1917 LYS LYS A . n 
A 1 1918 ALA 1918 1918 1918 ALA ALA A . n 
A 1 1919 LEU 1919 1919 1919 LEU LEU A . n 
A 1 1920 GLY 1920 1920 1920 GLY GLY A . n 
A 1 1921 HIS 1921 1921 1921 HIS HIS A . n 
A 1 1922 GLN 1922 1922 1922 GLN GLN A . n 
A 1 1923 LEU 1923 1923 1923 LEU LEU A . n 
A 1 1924 GLY 1924 1924 1924 GLY GLY A . n 
A 1 1925 ARG 1925 1925 1925 ARG ARG A . n 
A 1 1926 PHE 1926 1926 1926 PHE PHE A . n 
A 1 1927 VAL 1927 1927 1927 VAL VAL A . n 
A 1 1928 LEU 1928 1928 1928 LEU LEU A . n 
A 1 1929 VAL 1929 1929 1929 VAL VAL A . n 
A 1 1930 PHE 1930 1930 1930 PHE PHE A . n 
A 1 1931 ASN 1931 1931 1931 ASN ASN A . n 
A 1 1932 CYS 1932 1932 1932 CYS CYS A . n 
A 1 1933 ASP 1933 1933 1933 ASP ASP A . n 
A 1 1934 GLU 1934 1934 1934 GLU GLU A . n 
A 1 1935 THR 1935 1935 1935 THR THR A . n 
A 1 1936 PHE 1936 1936 1936 PHE PHE A . n 
A 1 1937 ASP 1937 1937 1937 ASP ASP A . n 
A 1 1938 PHE 1938 1938 1938 PHE PHE A . n 
A 1 1939 GLN 1939 1939 1939 GLN GLN A . n 
A 1 1940 ALA 1940 1940 1940 ALA ALA A . n 
A 1 1941 MET 1941 1941 1941 MET MET A . n 
A 1 1942 GLY 1942 1942 1942 GLY GLY A . n 
A 1 1943 ARG 1943 1943 1943 ARG ARG A . n 
A 1 1944 ILE 1944 1944 1944 ILE ILE A . n 
A 1 1945 PHE 1945 1945 1945 PHE PHE A . n 
A 1 1946 VAL 1946 1946 1946 VAL VAL A . n 
A 1 1947 GLY 1947 1947 1947 GLY GLY A . n 
A 1 1948 LEU 1948 1948 1948 LEU LEU A . n 
A 1 1949 CYS 1949 1949 1949 CYS CYS A . n 
A 1 1950 GLN 1950 1950 1950 GLN GLN A . n 
A 1 1951 VAL 1951 1951 1951 VAL VAL A . n 
A 1 1952 GLY 1952 1952 1952 GLY GLY A . n 
A 1 1953 ALA 1953 1953 1953 ALA ALA A . n 
A 1 1954 TRP 1954 1954 1954 TRP TRP A . n 
A 1 1955 GLY 1955 1955 1955 GLY GLY A . n 
A 1 1956 CYS 1956 1956 1956 CYS CYS A . n 
A 1 1957 PHE 1957 1957 1957 PHE PHE A . n 
A 1 1958 ASP 1958 1958 1958 ASP ASP A . n 
A 1 1959 GLU 1959 1959 1959 GLU GLU A . n 
A 1 1960 PHE 1960 1960 1960 PHE PHE A . n 
A 1 1961 ASN 1961 1961 1961 ASN ASN A . n 
A 1 1962 ARG 1962 1962 1962 ARG ARG A . n 
A 1 1963 LEU 1963 1963 1963 LEU LEU A . n 
A 1 1964 GLU 1964 1964 1964 GLU GLU A . n 
A 1 1965 GLU 1965 1965 1965 GLU GLU A . n 
A 1 1966 ARG 1966 1966 1966 ARG ARG A . n 
A 1 1967 MET 1967 1967 1967 MET MET A . n 
A 1 1968 LEU 1968 1968 1968 LEU LEU A . n 
A 1 1969 SER 1969 1969 1969 SER SER A . n 
A 1 1970 ALA 1970 1970 1970 ALA ALA A . n 
A 1 1971 VAL 1971 1971 1971 VAL VAL A . n 
A 1 1972 SER 1972 1972 1972 SER SER A . n 
A 1 1973 GLN 1973 1973 1973 GLN GLN A . n 
A 1 1974 GLN 1974 1974 1974 GLN GLN A . n 
A 1 1975 VAL 1975 1975 1975 VAL VAL A . n 
A 1 1976 GLN 1976 1976 1976 GLN GLN A . n 
A 1 1977 CYS 1977 1977 1977 CYS CYS A . n 
A 1 1978 ILE 1978 1978 1978 ILE ILE A . n 
A 1 1979 GLN 1979 1979 1979 GLN GLN A . n 
A 1 1980 GLU 1980 1980 1980 GLU GLU A . n 
A 1 1981 ALA 1981 1981 1981 ALA ALA A . n 
A 1 1982 LEU 1982 1982 1982 LEU LEU A . n 
A 1 1983 ARG 1983 1983 1983 ARG ARG A . n 
A 1 1984 GLU 1984 1984 1984 GLU GLU A . n 
A 1 1985 HIS 1985 1985 1985 HIS HIS A . n 
A 1 1986 SER 1986 1986 1986 SER SER A . n 
A 1 1987 ASN 1987 1987 1987 ASN ASN A . n 
A 1 1988 PRO 1988 1988 1988 PRO PRO A . n 
A 1 1989 ASN 1989 1989 1989 ASN ASN A . n 
A 1 1990 TYR 1990 1990 1990 TYR TYR A . n 
A 1 1991 ASP 1991 1991 1991 ASP ASP A . n 
A 1 1992 LYS 1992 1992 1992 LYS LYS A . n 
A 1 1993 THR 1993 1993 1993 THR THR A . n 
A 1 1994 SER 1994 1994 1994 SER SER A . n 
A 1 1995 ALA 1995 1995 1995 ALA ALA A . n 
A 1 1996 PRO 1996 1996 1996 PRO PRO A . n 
A 1 1997 ILE 1997 1997 1997 ILE ILE A . n 
A 1 1998 THR 1998 1998 1998 THR THR A . n 
A 1 1999 CYS 1999 1999 1999 CYS CYS A . n 
A 1 2000 GLU 2000 2000 2000 GLU GLU A . n 
A 1 2001 LEU 2001 2001 2001 LEU LEU A . n 
A 1 2002 LEU 2002 2002 2002 LEU LEU A . n 
A 1 2003 ASN 2003 2003 2003 ASN ASN A . n 
A 1 2004 LYS 2004 2004 2004 LYS LYS A . n 
A 1 2005 GLN 2005 2005 2005 GLN GLN A . n 
A 1 2006 VAL 2006 2006 2006 VAL VAL A . n 
A 1 2007 LYS 2007 2007 2007 LYS LYS A . n 
A 1 2008 VAL 2008 2008 2008 VAL VAL A . n 
A 1 2009 SER 2009 2009 2009 SER SER A . n 
A 1 2010 PRO 2010 2010 2010 PRO PRO A . n 
A 1 2011 ASP 2011 2011 2011 ASP ASP A . n 
A 1 2012 MET 2012 2012 2012 MET MET A . n 
A 1 2013 ALA 2013 2013 2013 ALA ALA A . n 
A 1 2014 ILE 2014 2014 2014 ILE ILE A . n 
A 1 2015 PHE 2015 2015 2015 PHE PHE A . n 
A 1 2016 ILE 2016 2016 2016 ILE ILE A . n 
A 1 2017 THR 2017 2017 2017 THR THR A . n 
A 1 2018 MET 2018 2018 2018 MET MET A . n 
A 1 2019 ASN 2019 2019 2019 ASN ASN A . n 
A 1 2020 PRO 2020 2020 2020 PRO PRO A . n 
A 1 2021 GLY 2021 2021 2021 GLY GLY A . n 
A 1 2022 TYR 2022 2022 2022 TYR TYR A . n 
A 1 2023 ALA 2023 2023 2023 ALA ALA A . n 
A 1 2024 GLY 2024 2024 2024 GLY GLY A . n 
A 1 2025 ARG 2025 2025 2025 ARG ARG A . n 
A 1 2026 SER 2026 2026 2026 SER SER A . n 
A 1 2027 ASN 2027 2027 2027 ASN ASN A . n 
A 1 2028 LEU 2028 2028 2028 LEU LEU A . n 
A 1 2029 PRO 2029 2029 2029 PRO PRO A . n 
A 1 2030 ASP 2030 2030 2030 ASP ASP A . n 
A 1 2031 ASN 2031 2031 2031 ASN ASN A . n 
A 1 2032 LEU 2032 2032 2032 LEU LEU A . n 
A 1 2033 LYS 2033 2033 2033 LYS LYS A . n 
A 1 2034 LYS 2034 2034 2034 LYS LYS A . n 
A 1 2035 LEU 2035 2035 2035 LEU LEU A . n 
A 1 2036 PHE 2036 2036 2036 PHE PHE A . n 
A 1 2037 ARG 2037 2037 2037 ARG ARG A . n 
A 1 2038 SER 2038 2038 2038 SER SER A . n 
A 1 2039 LEU 2039 2039 2039 LEU LEU A . n 
A 1 2040 ALA 2040 2040 2040 ALA ALA A . n 
A 1 2041 MET 2041 2041 2041 MET MET A . n 
A 1 2042 THR 2042 2042 2042 THR THR A . n 
A 1 2043 LYS 2043 2043 2043 LYS LYS A . n 
A 1 2044 PRO 2044 2044 2044 PRO PRO A . n 
A 1 2045 ASP 2045 2045 2045 ASP ASP A . n 
A 1 2046 ARG 2046 2046 2046 ARG ARG A . n 
A 1 2047 GLN 2047 2047 2047 GLN GLN A . n 
A 1 2048 LEU 2048 2048 2048 LEU LEU A . n 
A 1 2049 ILE 2049 2049 2049 ILE ILE A . n 
A 1 2050 ALA 2050 2050 2050 ALA ALA A . n 
A 1 2051 GLN 2051 2051 2051 GLN GLN A . n 
A 1 2052 VAL 2052 2052 2052 VAL VAL A . n 
A 1 2053 MET 2053 2053 2053 MET MET A . n 
A 1 2054 LEU 2054 2054 2054 LEU LEU A . n 
A 1 2055 TYR 2055 2055 2055 TYR TYR A . n 
A 1 2056 SER 2056 2056 2056 SER SER A . n 
A 1 2057 GLN 2057 2057 2057 GLN GLN A . n 
A 1 2058 GLY 2058 2058 2058 GLY GLY A . n 
A 1 2059 PHE 2059 2059 2059 PHE PHE A . n 
A 1 2060 ARG 2060 2060 2060 ARG ARG A . n 
A 1 2061 THR 2061 2061 2061 THR THR A . n 
A 1 2062 ALA 2062 2062 2062 ALA ALA A . n 
A 1 2063 GLU 2063 2063 2063 GLU GLU A . n 
A 1 2064 VAL 2064 2064 2064 VAL VAL A . n 
A 1 2065 LEU 2065 2065 2065 LEU LEU A . n 
A 1 2066 ALA 2066 2066 2066 ALA ALA A . n 
A 1 2067 ASN 2067 2067 2067 ASN ASN A . n 
A 1 2068 LYS 2068 2068 2068 LYS LYS A . n 
A 1 2069 ILE 2069 2069 2069 ILE ILE A . n 
A 1 2070 VAL 2070 2070 2070 VAL VAL A . n 
A 1 2071 PRO 2071 2071 2071 PRO PRO A . n 
A 1 2072 PHE 2072 2072 2072 PHE PHE A . n 
A 1 2073 PHE 2073 2073 2073 PHE PHE A . n 
A 1 2074 LYS 2074 2074 2074 LYS LYS A . n 
A 1 2075 LEU 2075 2075 2075 LEU LEU A . n 
A 1 2076 CYS 2076 2076 2076 CYS CYS A . n 
A 1 2077 ASP 2077 2077 2077 ASP ASP A . n 
A 1 2078 GLU 2078 2078 2078 GLU GLU A . n 
A 1 2079 GLN 2079 2079 2079 GLN GLN A . n 
A 1 2080 LEU 2080 2080 2080 LEU LEU A . n 
A 1 2081 SER 2081 2081 2081 SER SER A . n 
A 1 2082 SER 2082 2082 2082 SER SER A . n 
A 1 2083 GLN 2083 2083 2083 GLN GLN A . n 
A 1 2084 SER 2084 2084 2084 SER SER A . n 
A 1 2085 HIS 2085 2085 2085 HIS HIS A . n 
A 1 2086 TYR 2086 2086 2086 TYR TYR A . n 
A 1 2087 ASP 2087 2087 2087 ASP ASP A . n 
A 1 2088 PHE 2088 2088 2088 PHE PHE A . n 
A 1 2089 GLY 2089 2089 2089 GLY GLY A . n 
A 1 2090 LEU 2090 2090 2090 LEU LEU A . n 
A 1 2091 ARG 2091 2091 2091 ARG ARG A . n 
A 1 2092 ALA 2092 2092 2092 ALA ALA A . n 
A 1 2093 LEU 2093 2093 2093 LEU LEU A . n 
A 1 2094 LYS 2094 2094 2094 LYS LYS A . n 
A 1 2095 SER 2095 2095 2095 SER SER A . n 
A 1 2096 VAL 2096 2096 2096 VAL VAL A . n 
A 1 2097 LEU 2097 2097 2097 LEU LEU A . n 
A 1 2098 VAL 2098 2098 2098 VAL VAL A . n 
A 1 2099 SER 2099 2099 2099 SER SER A . n 
A 1 2100 ALA 2100 2100 2100 ALA ALA A . n 
A 1 2101 GLY 2101 2101 2101 GLY GLY A . n 
A 1 2102 ASN 2102 2102 2102 ASN ASN A . n 
A 1 2103 VAL 2103 2103 2103 VAL VAL A . n 
A 1 2104 LYS 2104 2104 2104 LYS LYS A . n 
A 1 2105 ARG 2105 2105 2105 ARG ARG A . n 
A 1 2106 GLU 2106 2106 2106 GLU GLU A . n 
A 1 2107 ARG 2107 2107 2107 ARG ARG A . n 
A 1 2108 ILE 2108 2108 2108 ILE ILE A . n 
A 1 2109 GLN 2109 2109 2109 GLN GLN A . n 
A 1 2110 LYS 2110 2110 2110 LYS LYS A . n 
A 1 2111 ILE 2111 2111 2111 ILE ILE A . n 
A 1 2112 LYS 2112 2112 2112 LYS LYS A . n 
A 1 2113 ARG 2113 2113 2113 ARG ARG A . n 
A 1 2114 GLU 2114 2114 2114 GLU GLU A . n 
A 1 2115 LYS 2115 2115 2115 LYS LYS A . n 
A 1 2116 GLU 2116 2116 2116 GLU GLU A . n 
A 1 2117 GLU 2117 2117 2117 GLU GLU A . n 
A 1 2118 ARG 2118 2118 2118 ARG ARG A . n 
A 1 2119 GLY 2119 2119 2119 GLY GLY A . n 
A 1 2120 GLU 2120 2120 2120 GLU GLU A . n 
A 1 2121 ALA 2121 2121 2121 ALA ALA A . n 
A 1 2122 VAL 2122 2122 2122 VAL VAL A . n 
A 1 2123 ASP 2123 2123 2123 ASP ASP A . n 
A 1 2124 GLU 2124 2124 2124 GLU GLU A . n 
A 1 2125 GLY 2125 2125 2125 GLY GLY A . n 
A 1 2126 GLU 2126 2126 2126 GLU GLU A . n 
A 1 2127 ILE 2127 2127 2127 ILE ILE A . n 
A 1 2128 ALA 2128 2128 2128 ALA ALA A . n 
A 1 2129 GLU 2129 2129 2129 GLU GLU A . n 
A 1 2130 ASN 2130 2130 2130 ASN ASN A . n 
A 1 2131 LEU 2131 2131 2131 LEU LEU A . n 
A 1 2132 PRO 2132 2132 2132 PRO PRO A . n 
A 1 2133 GLU 2133 2133 2133 GLU GLU A . n 
A 1 2134 GLN 2134 2134 2134 GLN GLN A . n 
A 1 2135 GLU 2135 2135 2135 GLU GLU A . n 
A 1 2136 ILE 2136 2136 2136 ILE ILE A . n 
A 1 2137 LEU 2137 2137 2137 LEU LEU A . n 
A 1 2138 ILE 2138 2138 2138 ILE ILE A . n 
A 1 2139 GLN 2139 2139 2139 GLN GLN A . n 
A 1 2140 SER 2140 2140 2140 SER SER A . n 
A 1 2141 VAL 2141 2141 2141 VAL VAL A . n 
A 1 2142 CYS 2142 2142 2142 CYS CYS A . n 
A 1 2143 GLU 2143 2143 2143 GLU GLU A . n 
A 1 2144 THR 2144 2144 2144 THR THR A . n 
A 1 2145 MET 2145 2145 2145 MET MET A . n 
A 1 2146 VAL 2146 2146 2146 VAL VAL A . n 
A 1 2147 PRO 2147 2147 2147 PRO PRO A . n 
A 1 2148 LYS 2148 2148 2148 LYS LYS A . n 
A 1 2149 LEU 2149 2149 2149 LEU LEU A . n 
A 1 2150 VAL 2150 2150 2150 VAL VAL A . n 
A 1 2151 ALA 2151 2151 2151 ALA ALA A . n 
A 1 2152 GLU 2152 2152 2152 GLU GLU A . n 
A 1 2153 ASP 2153 2153 2153 ASP ASP A . n 
A 1 2154 ILE 2154 2154 2154 ILE ILE A . n 
A 1 2155 PRO 2155 2155 2155 PRO PRO A . n 
A 1 2156 LEU 2156 2156 2156 LEU LEU A . n 
A 1 2157 LEU 2157 2157 2157 LEU LEU A . n 
A 1 2158 PHE 2158 2158 2158 PHE PHE A . n 
A 1 2159 SER 2159 2159 2159 SER SER A . n 
A 1 2160 LEU 2160 2160 2160 LEU LEU A . n 
A 1 2161 LEU 2161 2161 2161 LEU LEU A . n 
A 1 2162 SER 2162 2162 2162 SER SER A . n 
A 1 2163 ASP 2163 2163 2163 ASP ASP A . n 
A 1 2164 VAL 2164 2164 2164 VAL VAL A . n 
A 1 2165 PHE 2165 2165 2165 PHE PHE A . n 
A 1 2166 PRO 2166 2166 2166 PRO PRO A . n 
A 1 2167 GLY 2167 2167 2167 GLY GLY A . n 
A 1 2168 VAL 2168 2168 2168 VAL VAL A . n 
A 1 2169 GLN 2169 2169 2169 GLN GLN A . n 
A 1 2170 TYR 2170 2170 2170 TYR TYR A . n 
A 1 2171 HIS 2171 2171 2171 HIS HIS A . n 
A 1 2172 ARG 2172 2172 2172 ARG ARG A . n 
A 1 2173 GLY 2173 2173 2173 GLY GLY A . n 
A 1 2174 GLU 2174 2174 2174 GLU GLU A . n 
A 1 2175 MET 2175 2175 2175 MET MET A . n 
A 1 2176 THR 2176 2176 2176 THR THR A . n 
A 1 2177 ALA 2177 2177 2177 ALA ALA A . n 
A 1 2178 LEU 2178 2178 2178 LEU LEU A . n 
A 1 2179 ARG 2179 2179 2179 ARG ARG A . n 
A 1 2180 GLU 2180 2180 2180 GLU GLU A . n 
A 1 2181 GLU 2181 2181 2181 GLU GLU A . n 
A 1 2182 LEU 2182 2182 2182 LEU LEU A . n 
A 1 2183 LYS 2183 2183 2183 LYS LYS A . n 
A 1 2184 LYS 2184 2184 2184 LYS LYS A . n 
A 1 2185 VAL 2185 2185 2185 VAL VAL A . n 
A 1 2186 CYS 2186 2186 2186 CYS CYS A . n 
A 1 2187 GLN 2187 2187 2187 GLN GLN A . n 
A 1 2188 GLU 2188 2188 2188 GLU GLU A . n 
A 1 2189 MET 2189 2189 2189 MET MET A . n 
A 1 2190 TYR 2190 2190 2190 TYR TYR A . n 
A 1 2191 LEU 2191 2191 2191 LEU LEU A . n 
A 1 2192 THR 2192 2192 2192 THR THR A . n 
A 1 2193 TYR 2193 2193 2193 TYR TYR A . n 
A 1 2194 GLY 2194 2194 2194 GLY GLY A . n 
A 1 2195 ASP 2195 2195 2195 ASP ASP A . n 
A 1 2196 GLY 2196 2196 2196 GLY GLY A . n 
A 1 2197 GLU 2197 2197 2197 GLU GLU A . n 
A 1 2198 GLU 2198 2198 2198 GLU GLU A . n 
A 1 2199 VAL 2199 2199 2199 VAL VAL A . n 
A 1 2200 GLY 2200 2200 2200 GLY GLY A . n 
A 1 2201 GLY 2201 2201 2201 GLY GLY A . n 
A 1 2202 MET 2202 2202 2202 MET MET A . n 
A 1 2203 TRP 2203 2203 2203 TRP TRP A . n 
A 1 2204 VAL 2204 2204 2204 VAL VAL A . n 
A 1 2205 GLU 2205 2205 2205 GLU GLU A . n 
A 1 2206 LYS 2206 2206 2206 LYS LYS A . n 
A 1 2207 VAL 2207 2207 2207 VAL VAL A . n 
A 1 2208 LEU 2208 2208 2208 LEU LEU A . n 
A 1 2209 GLN 2209 2209 2209 GLN GLN A . n 
A 1 2210 LEU 2210 2210 2210 LEU LEU A . n 
A 1 2211 TYR 2211 2211 2211 TYR TYR A . n 
A 1 2212 GLN 2212 2212 2212 GLN GLN A . n 
A 1 2213 ILE 2213 2213 2213 ILE ILE A . n 
A 1 2214 THR 2214 2214 2214 THR THR A . n 
A 1 2215 GLN 2215 2215 2215 GLN GLN A . n 
A 1 2216 ILE 2216 2216 2216 ILE ILE A . n 
A 1 2217 ASN 2217 2217 2217 ASN ASN A . n 
A 1 2218 HIS 2218 2218 2218 HIS HIS A . n 
A 1 2219 GLY 2219 2219 2219 GLY GLY A . n 
A 1 2220 LEU 2220 2220 2220 LEU LEU A . n 
A 1 2221 MET 2221 2221 2221 MET MET A . n 
A 1 2222 MET 2222 2222 2222 MET MET A . n 
A 1 2223 VAL 2223 2223 2223 VAL VAL A . n 
A 1 2224 GLY 2224 2224 2224 GLY GLY A . n 
A 1 2225 PRO 2225 2225 2225 PRO PRO A . n 
A 1 2226 SER 2226 2226 2226 SER SER A . n 
A 1 2227 GLY 2227 2227 2227 GLY GLY A . n 
A 1 2228 SER 2228 2228 2228 SER SER A . n 
A 1 2229 GLY 2229 2229 2229 GLY GLY A . n 
A 1 2230 LYS 2230 2230 2230 LYS LYS A . n 
A 1 2231 SER 2231 2231 2231 SER SER A . n 
A 1 2232 MET 2232 2232 2232 MET MET A . n 
A 1 2233 ALA 2233 2233 2233 ALA ALA A . n 
A 1 2234 TRP 2234 2234 2234 TRP TRP A . n 
A 1 2235 ARG 2235 2235 2235 ARG ARG A . n 
A 1 2236 VAL 2236 2236 2236 VAL VAL A . n 
A 1 2237 LEU 2237 2237 2237 LEU LEU A . n 
A 1 2238 LEU 2238 2238 2238 LEU LEU A . n 
A 1 2239 LYS 2239 2239 2239 LYS LYS A . n 
A 1 2240 ALA 2240 2240 2240 ALA ALA A . n 
A 1 2241 LEU 2241 2241 2241 LEU LEU A . n 
A 1 2242 GLU 2242 2242 2242 GLU GLU A . n 
A 1 2243 ARG 2243 2243 2243 ARG ARG A . n 
A 1 2244 LEU 2244 2244 2244 LEU LEU A . n 
A 1 2245 GLU 2245 2245 2245 GLU GLU A . n 
A 1 2246 GLY 2246 2246 2246 GLY GLY A . n 
A 1 2247 VAL 2247 2247 2247 VAL VAL A . n 
A 1 2248 GLU 2248 2248 2248 GLU GLU A . n 
A 1 2249 GLY 2249 2249 2249 GLY GLY A . n 
A 1 2250 VAL 2250 2250 2250 VAL VAL A . n 
A 1 2251 ALA 2251 2251 2251 ALA ALA A . n 
A 1 2252 HIS 2252 2252 2252 HIS HIS A . n 
A 1 2253 ILE 2253 2253 2253 ILE ILE A . n 
A 1 2254 ILE 2254 2254 2254 ILE ILE A . n 
A 1 2255 ASP 2255 2255 2255 ASP ASP A . n 
A 1 2256 PRO 2256 2256 2256 PRO PRO A . n 
A 1 2257 LYS 2257 2257 2257 LYS LYS A . n 
A 1 2258 ALA 2258 2258 2258 ALA ALA A . n 
A 1 2259 ILE 2259 2259 2259 ILE ILE A . n 
A 1 2260 SER 2260 2260 2260 SER SER A . n 
A 1 2261 LYS 2261 2261 2261 LYS LYS A . n 
A 1 2262 ASP 2262 2262 2262 ASP ASP A . n 
A 1 2263 HIS 2263 2263 2263 HIS HIS A . n 
A 1 2264 LEU 2264 2264 2264 LEU LEU A . n 
A 1 2265 TYR 2265 2265 2265 TYR TYR A . n 
A 1 2266 GLY 2266 2266 2266 GLY GLY A . n 
A 1 2267 THR 2267 2267 2267 THR THR A . n 
A 1 2268 LEU 2268 2268 2268 LEU LEU A . n 
A 1 2269 ASP 2269 2269 2269 ASP ASP A . n 
A 1 2270 PRO 2270 2270 2270 PRO PRO A . n 
A 1 2271 ASN 2271 2271 2271 ASN ASN A . n 
A 1 2272 THR 2272 2272 2272 THR THR A . n 
A 1 2273 ARG 2273 2273 2273 ARG ARG A . n 
A 1 2274 GLU 2274 2274 2274 GLU GLU A . n 
A 1 2275 TRP 2275 2275 2275 TRP TRP A . n 
A 1 2276 THR 2276 2276 2276 THR THR A . n 
A 1 2277 ASP 2277 2277 2277 ASP ASP A . n 
A 1 2278 GLY 2278 2278 2278 GLY GLY A . n 
A 1 2279 LEU 2279 2279 2279 LEU LEU A . n 
A 1 2280 PHE 2280 2280 2280 PHE PHE A . n 
A 1 2281 THR 2281 2281 2281 THR THR A . n 
A 1 2282 HIS 2282 2282 2282 HIS HIS A . n 
A 1 2283 VAL 2283 2283 2283 VAL VAL A . n 
A 1 2284 LEU 2284 2284 2284 LEU LEU A . n 
A 1 2285 ARG 2285 2285 2285 ARG ARG A . n 
A 1 2286 LYS 2286 2286 2286 LYS LYS A . n 
A 1 2287 ILE 2287 2287 2287 ILE ILE A . n 
A 1 2288 ILE 2288 2288 2288 ILE ILE A . n 
A 1 2289 ASP 2289 2289 2289 ASP ASP A . n 
A 1 2290 SER 2290 2290 2290 SER SER A . n 
A 1 2291 VAL 2291 2291 2291 VAL VAL A . n 
A 1 2292 ARG 2292 2292 2292 ARG ARG A . n 
A 1 2293 GLY 2293 2293 2293 GLY GLY A . n 
A 1 2294 GLU 2294 2294 2294 GLU GLU A . n 
A 1 2295 LEU 2295 2295 2295 LEU LEU A . n 
A 1 2296 GLN 2296 2296 2296 GLN GLN A . n 
A 1 2297 LYS 2297 2297 2297 LYS LYS A . n 
A 1 2298 ARG 2298 2298 2298 ARG ARG A . n 
A 1 2299 GLN 2299 2299 2299 GLN GLN A . n 
A 1 2300 TRP 2300 2300 2300 TRP TRP A . n 
A 1 2301 ILE 2301 2301 2301 ILE ILE A . n 
A 1 2302 VAL 2302 2302 2302 VAL VAL A . n 
A 1 2303 PHE 2303 2303 2303 PHE PHE A . n 
A 1 2304 ASP 2304 2304 2304 ASP ASP A . n 
A 1 2305 GLY 2305 2305 2305 GLY GLY A . n 
A 1 2306 ASP 2306 2306 2306 ASP ASP A . n 
A 1 2307 VAL 2307 2307 2307 VAL VAL A . n 
A 1 2308 ASP 2308 2308 2308 ASP ASP A . n 
A 1 2309 PRO 2309 2309 2309 PRO PRO A . n 
A 1 2310 GLU 2310 2310 2310 GLU GLU A . n 
A 1 2311 TRP 2311 2311 2311 TRP TRP A . n 
A 1 2312 VAL 2312 2312 2312 VAL VAL A . n 
A 1 2313 GLU 2313 2313 2313 GLU GLU A . n 
A 1 2314 ASN 2314 2314 2314 ASN ASN A . n 
A 1 2315 LEU 2315 2315 2315 LEU LEU A . n 
A 1 2316 ASN 2316 2316 2316 ASN ASN A . n 
A 1 2317 SER 2317 2317 2317 SER SER A . n 
A 1 2318 VAL 2318 2318 2318 VAL VAL A . n 
A 1 2319 LEU 2319 2319 2319 LEU LEU A . n 
A 1 2320 ASP 2320 2320 2320 ASP ASP A . n 
A 1 2321 ASP 2321 2321 2321 ASP ASP A . n 
A 1 2322 ASN 2322 2322 2322 ASN ASN A . n 
A 1 2323 LYS 2323 2323 2323 LYS LYS A . n 
A 1 2324 LEU 2324 2324 2324 LEU LEU A . n 
A 1 2325 LEU 2325 2325 2325 LEU LEU A . n 
A 1 2326 THR 2326 2326 2326 THR THR A . n 
A 1 2327 LEU 2327 2327 2327 LEU LEU A . n 
A 1 2328 PRO 2328 2328 2328 PRO PRO A . n 
A 1 2329 ASN 2329 2329 2329 ASN ASN A . n 
A 1 2330 GLY 2330 2330 2330 GLY GLY A . n 
A 1 2331 GLU 2331 2331 2331 GLU GLU A . n 
A 1 2332 ARG 2332 2332 2332 ARG ARG A . n 
A 1 2333 LEU 2333 2333 2333 LEU LEU A . n 
A 1 2334 SER 2334 2334 2334 SER SER A . n 
A 1 2335 LEU 2335 2335 2335 LEU LEU A . n 
A 1 2336 PRO 2336 2336 2336 PRO PRO A . n 
A 1 2337 PRO 2337 2337 2337 PRO PRO A . n 
A 1 2338 ASN 2338 2338 2338 ASN ASN A . n 
A 1 2339 VAL 2339 2339 2339 VAL VAL A . n 
A 1 2340 ARG 2340 2340 2340 ARG ARG A . n 
A 1 2341 ILE 2341 2341 2341 ILE ILE A . n 
A 1 2342 MET 2342 2342 2342 MET MET A . n 
A 1 2343 PHE 2343 2343 2343 PHE PHE A . n 
A 1 2344 GLU 2344 2344 2344 GLU GLU A . n 
A 1 2345 VAL 2345 2345 2345 VAL VAL A . n 
A 1 2346 GLN 2346 2346 2346 GLN GLN A . n 
A 1 2347 ASP 2347 2347 2347 ASP ASP A . n 
A 1 2348 LEU 2348 2348 2348 LEU LEU A . n 
A 1 2349 LYS 2349 2349 2349 LYS LYS A . n 
A 1 2350 TYR 2350 2350 2350 TYR TYR A . n 
A 1 2351 ALA 2351 2351 2351 ALA ALA A . n 
A 1 2352 THR 2352 2352 2352 THR THR A . n 
A 1 2353 LEU 2353 2353 2353 LEU LEU A . n 
A 1 2354 ALA 2354 2354 2354 ALA ALA A . n 
A 1 2355 THR 2355 2355 2355 THR THR A . n 
A 1 2356 VAL 2356 2356 2356 VAL VAL A . n 
A 1 2357 SER 2357 2357 2357 SER SER A . n 
A 1 2358 ARG 2358 2358 2358 ARG ARG A . n 
A 1 2359 CYS 2359 2359 2359 CYS CYS A . n 
A 1 2360 GLY 2360 2360 2360 GLY GLY A . n 
A 1 2361 MET 2361 2361 2361 MET MET A . n 
A 1 2362 VAL 2362 2362 2362 VAL VAL A . n 
A 1 2363 TRP 2363 2363 2363 TRP TRP A . n 
A 1 2364 PHE 2364 2364 2364 PHE PHE A . n 
A 1 2365 SER 2365 2365 2365 SER SER A . n 
A 1 2366 GLU 2366 2366 2366 GLU GLU A . n 
A 1 2367 ASP 2367 2367 2367 ASP ASP A . n 
A 1 2368 VAL 2368 2368 2368 VAL VAL A . n 
A 1 2369 LEU 2369 2369 2369 LEU LEU A . n 
A 1 2370 SER 2370 2370 2370 SER SER A . n 
A 1 2371 THR 2371 2371 2371 THR THR A . n 
A 1 2372 ASP 2372 2372 2372 ASP ASP A . n 
A 1 2373 MET 2373 2373 2373 MET MET A . n 
A 1 2374 ILE 2374 2374 2374 ILE ILE A . n 
A 1 2375 PHE 2375 2375 2375 PHE PHE A . n 
A 1 2376 ASN 2376 2376 2376 ASN ASN A . n 
A 1 2377 ASN 2377 2377 2377 ASN ASN A . n 
A 1 2378 PHE 2378 2378 2378 PHE PHE A . n 
A 1 2379 LEU 2379 2379 2379 LEU LEU A . n 
A 1 2380 ALA 2380 2380 2380 ALA ALA A . n 
A 1 2381 ARG 2381 2381 2381 ARG ARG A . n 
A 1 2382 LEU 2382 2382 2382 LEU LEU A . n 
A 1 2383 ARG 2383 2383 2383 ARG ARG A . n 
A 1 2384 SER 2384 2384 2384 SER SER A . n 
A 1 2385 ILE 2385 2385 2385 ILE ILE A . n 
A 1 2386 PRO 2386 2386 2386 PRO PRO A . n 
A 1 2387 LEU 2387 2387 2387 LEU LEU A . n 
A 1 2388 ASP 2388 2388 2388 ASP ASP A . n 
A 1 2389 GLU 2389 2389 2389 GLU GLU A . n 
A 1 2390 GLY 2390 2390 ?    ?   ?   A . n 
A 1 2391 GLU 2391 2391 ?    ?   ?   A . n 
A 1 2392 ASP 2392 2392 ?    ?   ?   A . n 
A 1 2393 GLU 2393 2393 ?    ?   ?   A . n 
A 1 2394 ALA 2394 2394 ?    ?   ?   A . n 
A 1 2395 GLN 2395 2395 ?    ?   ?   A . n 
A 1 2396 ARG 2396 2396 ?    ?   ?   A . n 
A 1 2397 ARG 2397 2397 ?    ?   ?   A . n 
A 1 2398 ARG 2398 2398 ?    ?   ?   A . n 
A 1 2399 LYS 2399 2399 ?    ?   ?   A . n 
A 1 2400 GLY 2400 2400 ?    ?   ?   A . n 
A 1 2401 LYS 2401 2401 ?    ?   ?   A . n 
A 1 2402 GLU 2402 2402 ?    ?   ?   A . n 
A 1 2403 ASP 2403 2403 ?    ?   ?   A . n 
A 1 2404 GLU 2404 2404 ?    ?   ?   A . n 
A 1 2405 GLY 2405 2405 ?    ?   ?   A . n 
A 1 2406 GLU 2406 2406 ?    ?   ?   A . n 
A 1 2407 GLU 2407 2407 ?    ?   ?   A . n 
A 1 2408 ALA 2408 2408 ?    ?   ?   A . n 
A 1 2409 ALA 2409 2409 ?    ?   ?   A . n 
A 1 2410 SER 2410 2410 2410 SER SER A . n 
A 1 2411 PRO 2411 2411 2411 PRO PRO A . n 
A 1 2412 MET 2412 2412 2412 MET MET A . n 
A 1 2413 LEU 2413 2413 2413 LEU LEU A . n 
A 1 2414 GLN 2414 2414 2414 GLN GLN A . n 
A 1 2415 ILE 2415 2415 2415 ILE ILE A . n 
A 1 2416 GLN 2416 2416 2416 GLN GLN A . n 
A 1 2417 ARG 2417 2417 2417 ARG ARG A . n 
A 1 2418 ASP 2418 2418 2418 ASP ASP A . n 
A 1 2419 ALA 2419 2419 2419 ALA ALA A . n 
A 1 2420 ALA 2420 2420 2420 ALA ALA A . n 
A 1 2421 THR 2421 2421 2421 THR THR A . n 
A 1 2422 ILE 2422 2422 2422 ILE ILE A . n 
A 1 2423 MET 2423 2423 2423 MET MET A . n 
A 1 2424 GLN 2424 2424 2424 GLN GLN A . n 
A 1 2425 PRO 2425 2425 2425 PRO PRO A . n 
A 1 2426 TYR 2426 2426 2426 TYR TYR A . n 
A 1 2427 PHE 2427 2427 2427 PHE PHE A . n 
A 1 2428 THR 2428 2428 2428 THR THR A . n 
A 1 2429 SER 2429 2429 2429 SER SER A . n 
A 1 2430 ASN 2430 2430 2430 ASN ASN A . n 
A 1 2431 GLY 2431 2431 2431 GLY GLY A . n 
A 1 2432 LEU 2432 2432 2432 LEU LEU A . n 
A 1 2433 VAL 2433 2433 2433 VAL VAL A . n 
A 1 2434 THR 2434 2434 2434 THR THR A . n 
A 1 2435 LYS 2435 2435 2435 LYS LYS A . n 
A 1 2436 ALA 2436 2436 2436 ALA ALA A . n 
A 1 2437 LEU 2437 2437 2437 LEU LEU A . n 
A 1 2438 GLU 2438 2438 2438 GLU GLU A . n 
A 1 2439 HIS 2439 2439 2439 HIS HIS A . n 
A 1 2440 ALA 2440 2440 2440 ALA ALA A . n 
A 1 2441 PHE 2441 2441 2441 PHE PHE A . n 
A 1 2442 GLN 2442 2442 2442 GLN GLN A . n 
A 1 2443 LEU 2443 2443 2443 LEU LEU A . n 
A 1 2444 GLU 2444 2444 2444 GLU GLU A . n 
A 1 2445 HIS 2445 2445 2445 HIS HIS A . n 
A 1 2446 ILE 2446 2446 2446 ILE ILE A . n 
A 1 2447 MET 2447 2447 2447 MET MET A . n 
A 1 2448 ASP 2448 2448 2448 ASP ASP A . n 
A 1 2449 LEU 2449 2449 2449 LEU LEU A . n 
A 1 2450 THR 2450 2450 2450 THR THR A . n 
A 1 2451 ARG 2451 2451 2451 ARG ARG A . n 
A 1 2452 LEU 2452 2452 2452 LEU LEU A . n 
A 1 2453 ARG 2453 2453 2453 ARG ARG A . n 
A 1 2454 CYS 2454 2454 2454 CYS CYS A . n 
A 1 2455 LEU 2455 2455 2455 LEU LEU A . n 
A 1 2456 GLY 2456 2456 2456 GLY GLY A . n 
A 1 2457 SER 2457 2457 2457 SER SER A . n 
A 1 2458 LEU 2458 2458 2458 LEU LEU A . n 
A 1 2459 PHE 2459 2459 2459 PHE PHE A . n 
A 1 2460 SER 2460 2460 2460 SER SER A . n 
A 1 2461 MET 2461 2461 2461 MET MET A . n 
A 1 2462 LEU 2462 2462 2462 LEU LEU A . n 
A 1 2463 HIS 2463 2463 2463 HIS HIS A . n 
A 1 2464 GLN 2464 2464 2464 GLN GLN A . n 
A 1 2465 ALA 2465 2465 2465 ALA ALA A . n 
A 1 2466 CYS 2466 2466 2466 CYS CYS A . n 
A 1 2467 ARG 2467 2467 2467 ARG ARG A . n 
A 1 2468 ASN 2468 2468 2468 ASN ASN A . n 
A 1 2469 VAL 2469 2469 2469 VAL VAL A . n 
A 1 2470 ALA 2470 2470 2470 ALA ALA A . n 
A 1 2471 GLN 2471 2471 2471 GLN GLN A . n 
A 1 2472 TYR 2472 2472 2472 TYR TYR A . n 
A 1 2473 ASN 2473 2473 2473 ASN ASN A . n 
A 1 2474 ALA 2474 2474 2474 ALA ALA A . n 
A 1 2475 ASN 2475 2475 2475 ASN ASN A . n 
A 1 2476 HIS 2476 2476 2476 HIS HIS A . n 
A 1 2477 PRO 2477 2477 2477 PRO PRO A . n 
A 1 2478 ASP 2478 2478 2478 ASP ASP A . n 
A 1 2479 PHE 2479 2479 2479 PHE PHE A . n 
A 1 2480 PRO 2480 2480 2480 PRO PRO A . n 
A 1 2481 MET 2481 2481 2481 MET MET A . n 
A 1 2482 GLN 2482 2482 2482 GLN GLN A . n 
A 1 2483 ILE 2483 2483 2483 ILE ILE A . n 
A 1 2484 GLU 2484 2484 2484 GLU GLU A . n 
A 1 2485 GLN 2485 2485 2485 GLN GLN A . n 
A 1 2486 LEU 2486 2486 2486 LEU LEU A . n 
A 1 2487 GLU 2487 2487 2487 GLU GLU A . n 
A 1 2488 ARG 2488 2488 2488 ARG ARG A . n 
A 1 2489 TYR 2489 2489 2489 TYR TYR A . n 
A 1 2490 ILE 2490 2490 2490 ILE ILE A . n 
A 1 2491 GLN 2491 2491 2491 GLN GLN A . n 
A 1 2492 ARG 2492 2492 2492 ARG ARG A . n 
A 1 2493 TYR 2493 2493 2493 TYR TYR A . n 
A 1 2494 LEU 2494 2494 2494 LEU LEU A . n 
A 1 2495 VAL 2495 2495 2495 VAL VAL A . n 
A 1 2496 TYR 2496 2496 2496 TYR TYR A . n 
A 1 2497 ALA 2497 2497 2497 ALA ALA A . n 
A 1 2498 ILE 2498 2498 2498 ILE ILE A . n 
A 1 2499 LEU 2499 2499 2499 LEU LEU A . n 
A 1 2500 TRP 2500 2500 2500 TRP TRP A . n 
A 1 2501 SER 2501 2501 2501 SER SER A . n 
A 1 2502 LEU 2502 2502 2502 LEU LEU A . n 
A 1 2503 SER 2503 2503 2503 SER SER A . n 
A 1 2504 GLY 2504 2504 2504 GLY GLY A . n 
A 1 2505 ASP 2505 2505 2505 ASP ASP A . n 
A 1 2506 SER 2506 2506 2506 SER SER A . n 
A 1 2507 ARG 2507 2507 2507 ARG ARG A . n 
A 1 2508 LEU 2508 2508 2508 LEU LEU A . n 
A 1 2509 LYS 2509 2509 2509 LYS LYS A . n 
A 1 2510 MET 2510 2510 2510 MET MET A . n 
A 1 2511 ARG 2511 2511 2511 ARG ARG A . n 
A 1 2512 ALA 2512 2512 2512 ALA ALA A . n 
A 1 2513 GLU 2513 2513 2513 GLU GLU A . n 
A 1 2514 LEU 2514 2514 2514 LEU LEU A . n 
A 1 2515 GLY 2515 2515 2515 GLY GLY A . n 
A 1 2516 GLU 2516 2516 2516 GLU GLU A . n 
A 1 2517 TYR 2517 2517 2517 TYR TYR A . n 
A 1 2518 ILE 2518 2518 2518 ILE ILE A . n 
A 1 2519 ARG 2519 2519 2519 ARG ARG A . n 
A 1 2520 ARG 2520 2520 2520 ARG ARG A . n 
A 1 2521 ILE 2521 2521 2521 ILE ILE A . n 
A 1 2522 THR 2522 2522 2522 THR THR A . n 
A 1 2523 THR 2523 2523 2523 THR THR A . n 
A 1 2524 VAL 2524 2524 2524 VAL VAL A . n 
A 1 2525 PRO 2525 2525 2525 PRO PRO A . n 
A 1 2526 LEU 2526 2526 2526 LEU LEU A . n 
A 1 2527 PRO 2527 2527 2527 PRO PRO A . n 
A 1 2528 THR 2528 2528 2528 THR THR A . n 
A 1 2529 ALA 2529 2529 2529 ALA ALA A . n 
A 1 2530 PRO 2530 2530 2530 PRO PRO A . n 
A 1 2531 ASN 2531 2531 2531 ASN ASN A . n 
A 1 2532 ILE 2532 2532 2532 ILE ILE A . n 
A 1 2533 PRO 2533 2533 2533 PRO PRO A . n 
A 1 2534 ILE 2534 2534 2534 ILE ILE A . n 
A 1 2535 ILE 2535 2535 2535 ILE ILE A . n 
A 1 2536 ASP 2536 2536 2536 ASP ASP A . n 
A 1 2537 TYR 2537 2537 2537 TYR TYR A . n 
A 1 2538 GLU 2538 2538 2538 GLU GLU A . n 
A 1 2539 VAL 2539 2539 2539 VAL VAL A . n 
A 1 2540 SER 2540 2540 2540 SER SER A . n 
A 1 2541 ILE 2541 2541 2541 ILE ILE A . n 
A 1 2542 SER 2542 2542 2542 SER SER A . n 
A 1 2543 GLY 2543 2543 2543 GLY GLY A . n 
A 1 2544 GLU 2544 2544 2544 GLU GLU A . n 
A 1 2545 TRP 2545 2545 2545 TRP TRP A . n 
A 1 2546 SER 2546 2546 2546 SER SER A . n 
A 1 2547 PRO 2547 2547 2547 PRO PRO A . n 
A 1 2548 TRP 2548 2548 2548 TRP TRP A . n 
A 1 2549 GLN 2549 2549 2549 GLN GLN A . n 
A 1 2550 ALA 2550 2550 2550 ALA ALA A . n 
A 1 2551 LYS 2551 2551 2551 LYS LYS A . n 
A 1 2552 VAL 2552 2552 2552 VAL VAL A . n 
A 1 2553 PRO 2553 2553 2553 PRO PRO A . n 
A 1 2554 GLN 2554 2554 2554 GLN GLN A . n 
A 1 2555 ILE 2555 2555 2555 ILE ILE A . n 
A 1 2556 GLU 2556 2556 2556 GLU GLU A . n 
A 1 2557 VAL 2557 2557 2557 VAL VAL A . n 
A 1 2558 GLU 2558 2558 2558 GLU GLU A . n 
A 1 2559 THR 2559 2559 2559 THR THR A . n 
A 1 2560 HIS 2560 2560 2560 HIS HIS A . n 
A 1 2561 LYS 2561 2561 2561 LYS LYS A . n 
A 1 2562 VAL 2562 2562 2562 VAL VAL A . n 
A 1 2563 ALA 2563 2563 2563 ALA ALA A . n 
A 1 2564 ALA 2564 2564 2564 ALA ALA A . n 
A 1 2565 PRO 2565 2565 2565 PRO PRO A . n 
A 1 2566 ASP 2566 2566 2566 ASP ASP A . n 
A 1 2567 VAL 2567 2567 2567 VAL VAL A . n 
A 1 2568 VAL 2568 2568 2568 VAL VAL A . n 
A 1 2569 VAL 2569 2569 2569 VAL VAL A . n 
A 1 2570 PRO 2570 2570 2570 PRO PRO A . n 
A 1 2571 THR 2571 2571 2571 THR THR A . n 
A 1 2572 LEU 2572 2572 2572 LEU LEU A . n 
A 1 2573 ASP 2573 2573 2573 ASP ASP A . n 
A 1 2574 THR 2574 2574 2574 THR THR A . n 
A 1 2575 VAL 2575 2575 2575 VAL VAL A . n 
A 1 2576 ARG 2576 2576 2576 ARG ARG A . n 
A 1 2577 HIS 2577 2577 2577 HIS HIS A . n 
A 1 2578 GLU 2578 2578 2578 GLU GLU A . n 
A 1 2579 ALA 2579 2579 2579 ALA ALA A . n 
A 1 2580 LEU 2580 2580 2580 LEU LEU A . n 
A 1 2581 LEU 2581 2581 2581 LEU LEU A . n 
A 1 2582 TYR 2582 2582 2582 TYR TYR A . n 
A 1 2583 THR 2583 2583 2583 THR THR A . n 
A 1 2584 TRP 2584 2584 2584 TRP TRP A . n 
A 1 2585 LEU 2585 2585 2585 LEU LEU A . n 
A 1 2586 ALA 2586 2586 2586 ALA ALA A . n 
A 1 2587 GLU 2587 2587 2587 GLU GLU A . n 
A 1 2588 HIS 2588 2588 2588 HIS HIS A . n 
A 1 2589 LYS 2589 2589 2589 LYS LYS A . n 
A 1 2590 PRO 2590 2590 2590 PRO PRO A . n 
A 1 2591 LEU 2591 2591 2591 LEU LEU A . n 
A 1 2592 VAL 2592 2592 2592 VAL VAL A . n 
A 1 2593 LEU 2593 2593 2593 LEU LEU A . n 
A 1 2594 CYS 2594 2594 2594 CYS CYS A . n 
A 1 2595 GLY 2595 2595 2595 GLY GLY A . n 
A 1 2596 PRO 2596 2596 2596 PRO PRO A . n 
A 1 2597 PRO 2597 2597 2597 PRO PRO A . n 
A 1 2598 GLY 2598 2598 2598 GLY GLY A . n 
A 1 2599 SER 2599 2599 2599 SER SER A . n 
A 1 2600 GLY 2600 2600 2600 GLY GLY A . n 
A 1 2601 LYS 2601 2601 2601 LYS LYS A . n 
A 1 2602 THR 2602 2602 2602 THR THR A . n 
A 1 2603 MET 2603 2603 2603 MET MET A . n 
A 1 2604 THR 2604 2604 2604 THR THR A . n 
A 1 2605 LEU 2605 2605 2605 LEU LEU A . n 
A 1 2606 PHE 2606 2606 2606 PHE PHE A . n 
A 1 2607 SER 2607 2607 2607 SER SER A . n 
A 1 2608 ALA 2608 2608 2608 ALA ALA A . n 
A 1 2609 LEU 2609 2609 2609 LEU LEU A . n 
A 1 2610 ARG 2610 2610 2610 ARG ARG A . n 
A 1 2611 ALA 2611 2611 2611 ALA ALA A . n 
A 1 2612 LEU 2612 2612 2612 LEU LEU A . n 
A 1 2613 PRO 2613 2613 2613 PRO PRO A . n 
A 1 2614 ASP 2614 2614 2614 ASP ASP A . n 
A 1 2615 MET 2615 2615 2615 MET MET A . n 
A 1 2616 GLU 2616 2616 2616 GLU GLU A . n 
A 1 2617 VAL 2617 2617 2617 VAL VAL A . n 
A 1 2618 VAL 2618 2618 2618 VAL VAL A . n 
A 1 2619 GLY 2619 2619 2619 GLY GLY A . n 
A 1 2620 LEU 2620 2620 2620 LEU LEU A . n 
A 1 2621 ASN 2621 2621 2621 ASN ASN A . n 
A 1 2622 PHE 2622 2622 2622 PHE PHE A . n 
A 1 2623 SER 2623 2623 2623 SER SER A . n 
A 1 2624 SER 2624 2624 2624 SER SER A . n 
A 1 2625 ALA 2625 2625 2625 ALA ALA A . n 
A 1 2626 THR 2626 2626 2626 THR THR A . n 
A 1 2627 THR 2627 2627 2627 THR THR A . n 
A 1 2628 PRO 2628 2628 2628 PRO PRO A . n 
A 1 2629 GLU 2629 2629 2629 GLU GLU A . n 
A 1 2630 LEU 2630 2630 2630 LEU LEU A . n 
A 1 2631 LEU 2631 2631 2631 LEU LEU A . n 
A 1 2632 LEU 2632 2632 2632 LEU LEU A . n 
A 1 2633 LYS 2633 2633 2633 LYS LYS A . n 
A 1 2634 THR 2634 2634 2634 THR THR A . n 
A 1 2635 PHE 2635 2635 2635 PHE PHE A . n 
A 1 2636 ASP 2636 2636 2636 ASP ASP A . n 
A 1 2637 HIS 2637 2637 2637 HIS HIS A . n 
A 1 2638 TYR 2638 2638 2638 TYR TYR A . n 
A 1 2639 CYS 2639 2639 2639 CYS CYS A . n 
A 1 2640 GLU 2640 2640 2640 GLU GLU A . n 
A 1 2641 TYR 2641 2641 2641 TYR TYR A . n 
A 1 2642 ARG 2642 2642 2642 ARG ARG A . n 
A 1 2643 ARG 2643 2643 2643 ARG ARG A . n 
A 1 2644 THR 2644 2644 2644 THR THR A . n 
A 1 2645 PRO 2645 2645 2645 PRO PRO A . n 
A 1 2646 ASN 2646 2646 2646 ASN ASN A . n 
A 1 2647 GLY 2647 2647 2647 GLY GLY A . n 
A 1 2648 VAL 2648 2648 2648 VAL VAL A . n 
A 1 2649 VAL 2649 2649 2649 VAL VAL A . n 
A 1 2650 LEU 2650 2650 2650 LEU LEU A . n 
A 1 2651 ALA 2651 2651 2651 ALA ALA A . n 
A 1 2652 PRO 2652 2652 2652 PRO PRO A . n 
A 1 2653 VAL 2653 2653 2653 VAL VAL A . n 
A 1 2654 GLN 2654 2654 2654 GLN GLN A . n 
A 1 2655 LEU 2655 2655 2655 LEU LEU A . n 
A 1 2656 GLY 2656 2656 2656 GLY GLY A . n 
A 1 2657 LYS 2657 2657 2657 LYS LYS A . n 
A 1 2658 TRP 2658 2658 2658 TRP TRP A . n 
A 1 2659 LEU 2659 2659 2659 LEU LEU A . n 
A 1 2660 VAL 2660 2660 2660 VAL VAL A . n 
A 1 2661 LEU 2661 2661 2661 LEU LEU A . n 
A 1 2662 PHE 2662 2662 2662 PHE PHE A . n 
A 1 2663 CYS 2663 2663 2663 CYS CYS A . n 
A 1 2664 ASP 2664 2664 2664 ASP ASP A . n 
A 1 2665 GLU 2665 2665 2665 GLU GLU A . n 
A 1 2666 ILE 2666 2666 2666 ILE ILE A . n 
A 1 2667 ASN 2667 2667 2667 ASN ASN A . n 
A 1 2668 LEU 2668 2668 2668 LEU LEU A . n 
A 1 2669 PRO 2669 2669 2669 PRO PRO A . n 
A 1 2670 ASP 2670 2670 2670 ASP ASP A . n 
A 1 2671 MET 2671 2671 2671 MET MET A . n 
A 1 2672 ASP 2672 2672 2672 ASP ASP A . n 
A 1 2673 LYS 2673 2673 2673 LYS LYS A . n 
A 1 2674 TYR 2674 2674 2674 TYR TYR A . n 
A 1 2675 GLY 2675 2675 2675 GLY GLY A . n 
A 1 2676 THR 2676 2676 2676 THR THR A . n 
A 1 2677 GLN 2677 2677 2677 GLN GLN A . n 
A 1 2678 ARG 2678 2678 2678 ARG ARG A . n 
A 1 2679 VAL 2679 2679 2679 VAL VAL A . n 
A 1 2680 ILE 2680 2680 2680 ILE ILE A . n 
A 1 2681 SER 2681 2681 2681 SER SER A . n 
A 1 2682 PHE 2682 2682 2682 PHE PHE A . n 
A 1 2683 ILE 2683 2683 2683 ILE ILE A . n 
A 1 2684 ARG 2684 2684 2684 ARG ARG A . n 
A 1 2685 GLN 2685 2685 2685 GLN GLN A . n 
A 1 2686 MET 2686 2686 2686 MET MET A . n 
A 1 2687 VAL 2687 2687 2687 VAL VAL A . n 
A 1 2688 GLU 2688 2688 2688 GLU GLU A . n 
A 1 2689 HIS 2689 2689 2689 HIS HIS A . n 
A 1 2690 GLY 2690 2690 2690 GLY GLY A . n 
A 1 2691 GLY 2691 2691 2691 GLY GLY A . n 
A 1 2692 PHE 2692 2692 2692 PHE PHE A . n 
A 1 2693 TYR 2693 2693 2693 TYR TYR A . n 
A 1 2694 ARG 2694 2694 2694 ARG ARG A . n 
A 1 2695 THR 2695 2695 2695 THR THR A . n 
A 1 2696 SER 2696 2696 2696 SER SER A . n 
A 1 2697 ASP 2697 2697 2697 ASP ASP A . n 
A 1 2698 GLN 2698 2698 2698 GLN GLN A . n 
A 1 2699 THR 2699 2699 2699 THR THR A . n 
A 1 2700 TRP 2700 2700 2700 TRP TRP A . n 
A 1 2701 VAL 2701 2701 2701 VAL VAL A . n 
A 1 2702 LYS 2702 2702 2702 LYS LYS A . n 
A 1 2703 LEU 2703 2703 2703 LEU LEU A . n 
A 1 2704 GLU 2704 2704 2704 GLU GLU A . n 
A 1 2705 ARG 2705 2705 2705 ARG ARG A . n 
A 1 2706 ILE 2706 2706 2706 ILE ILE A . n 
A 1 2707 GLN 2707 2707 2707 GLN GLN A . n 
A 1 2708 PHE 2708 2708 2708 PHE PHE A . n 
A 1 2709 VAL 2709 2709 2709 VAL VAL A . n 
A 1 2710 GLY 2710 2710 2710 GLY GLY A . n 
A 1 2711 ALA 2711 2711 2711 ALA ALA A . n 
A 1 2712 CYS 2712 2712 2712 CYS CYS A . n 
A 1 2713 ASN 2713 2713 2713 ASN ASN A . n 
A 1 2714 PRO 2714 2714 2714 PRO PRO A . n 
A 1 2715 PRO 2715 2715 2715 PRO PRO A . n 
A 1 2716 THR 2716 2716 2716 THR THR A . n 
A 1 2717 ASP 2717 2717 2717 ASP ASP A . n 
A 1 2718 PRO 2718 2718 2718 PRO PRO A . n 
A 1 2719 GLY 2719 2719 2719 GLY GLY A . n 
A 1 2720 ARG 2720 2720 2720 ARG ARG A . n 
A 1 2721 LYS 2721 2721 2721 LYS LYS A . n 
A 1 2722 PRO 2722 2722 2722 PRO PRO A . n 
A 1 2723 LEU 2723 2723 2723 LEU LEU A . n 
A 1 2724 SER 2724 2724 2724 SER SER A . n 
A 1 2725 HIS 2725 2725 2725 HIS HIS A . n 
A 1 2726 ARG 2726 2726 2726 ARG ARG A . n 
A 1 2727 PHE 2727 2727 2727 PHE PHE A . n 
A 1 2728 LEU 2728 2728 2728 LEU LEU A . n 
A 1 2729 ARG 2729 2729 2729 ARG ARG A . n 
A 1 2730 HIS 2730 2730 2730 HIS HIS A . n 
A 1 2731 VAL 2731 2731 2731 VAL VAL A . n 
A 1 2732 PRO 2732 2732 2732 PRO PRO A . n 
A 1 2733 VAL 2733 2733 2733 VAL VAL A . n 
A 1 2734 VAL 2734 2734 2734 VAL VAL A . n 
A 1 2735 TYR 2735 2735 2735 TYR TYR A . n 
A 1 2736 VAL 2736 2736 2736 VAL VAL A . n 
A 1 2737 ASP 2737 2737 2737 ASP ASP A . n 
A 1 2738 TYR 2738 2738 2738 TYR TYR A . n 
A 1 2739 PRO 2739 2739 2739 PRO PRO A . n 
A 1 2740 GLY 2740 2740 2740 GLY GLY A . n 
A 1 2741 PRO 2741 2741 2741 PRO PRO A . n 
A 1 2742 ALA 2742 2742 2742 ALA ALA A . n 
A 1 2743 SER 2743 2743 2743 SER SER A . n 
A 1 2744 LEU 2744 2744 2744 LEU LEU A . n 
A 1 2745 THR 2745 2745 2745 THR THR A . n 
A 1 2746 GLN 2746 2746 2746 GLN GLN A . n 
A 1 2747 ILE 2747 2747 2747 ILE ILE A . n 
A 1 2748 TYR 2748 2748 2748 TYR TYR A . n 
A 1 2749 GLY 2749 2749 2749 GLY GLY A . n 
A 1 2750 THR 2750 2750 2750 THR THR A . n 
A 1 2751 PHE 2751 2751 2751 PHE PHE A . n 
A 1 2752 ASN 2752 2752 2752 ASN ASN A . n 
A 1 2753 ARG 2753 2753 2753 ARG ARG A . n 
A 1 2754 ALA 2754 2754 2754 ALA ALA A . n 
A 1 2755 MET 2755 2755 2755 MET MET A . n 
A 1 2756 LEU 2756 2756 2756 LEU LEU A . n 
A 1 2757 ARG 2757 2757 2757 ARG ARG A . n 
A 1 2758 LEU 2758 2758 2758 LEU LEU A . n 
A 1 2759 ILE 2759 2759 2759 ILE ILE A . n 
A 1 2760 PRO 2760 2760 2760 PRO PRO A . n 
A 1 2761 SER 2761 2761 2761 SER SER A . n 
A 1 2762 LEU 2762 2762 2762 LEU LEU A . n 
A 1 2763 ARG 2763 2763 2763 ARG ARG A . n 
A 1 2764 THR 2764 2764 2764 THR THR A . n 
A 1 2765 TYR 2765 2765 2765 TYR TYR A . n 
A 1 2766 ALA 2766 2766 2766 ALA ALA A . n 
A 1 2767 GLU 2767 2767 2767 GLU GLU A . n 
A 1 2768 PRO 2768 2768 2768 PRO PRO A . n 
A 1 2769 LEU 2769 2769 2769 LEU LEU A . n 
A 1 2770 THR 2770 2770 2770 THR THR A . n 
A 1 2771 ALA 2771 2771 2771 ALA ALA A . n 
A 1 2772 ALA 2772 2772 2772 ALA ALA A . n 
A 1 2773 MET 2773 2773 2773 MET MET A . n 
A 1 2774 VAL 2774 2774 2774 VAL VAL A . n 
A 1 2775 GLU 2775 2775 2775 GLU GLU A . n 
A 1 2776 PHE 2776 2776 2776 PHE PHE A . n 
A 1 2777 TYR 2777 2777 2777 TYR TYR A . n 
A 1 2778 THR 2778 2778 2778 THR THR A . n 
A 1 2779 MET 2779 2779 2779 MET MET A . n 
A 1 2780 SER 2780 2780 2780 SER SER A . n 
A 1 2781 GLN 2781 2781 2781 GLN GLN A . n 
A 1 2782 GLU 2782 2782 2782 GLU GLU A . n 
A 1 2783 ARG 2783 2783 2783 ARG ARG A . n 
A 1 2784 PHE 2784 2784 2784 PHE PHE A . n 
A 1 2785 THR 2785 2785 2785 THR THR A . n 
A 1 2786 GLN 2786 2786 2786 GLN GLN A . n 
A 1 2787 ASP 2787 2787 2787 ASP ASP A . n 
A 1 2788 THR 2788 2788 2788 THR THR A . n 
A 1 2789 GLN 2789 2789 2789 GLN GLN A . n 
A 1 2790 PRO 2790 2790 2790 PRO PRO A . n 
A 1 2791 HIS 2791 2791 2791 HIS HIS A . n 
A 1 2792 TYR 2792 2792 2792 TYR TYR A . n 
A 1 2793 ILE 2793 2793 2793 ILE ILE A . n 
A 1 2794 TYR 2794 2794 2794 TYR TYR A . n 
A 1 2795 SER 2795 2795 2795 SER SER A . n 
A 1 2796 PRO 2796 2796 2796 PRO PRO A . n 
A 1 2797 ARG 2797 2797 2797 ARG ARG A . n 
A 1 2798 GLU 2798 2798 2798 GLU GLU A . n 
A 1 2799 MET 2799 2799 2799 MET MET A . n 
A 1 2800 THR 2800 2800 2800 THR THR A . n 
A 1 2801 ARG 2801 2801 2801 ARG ARG A . n 
A 1 2802 TRP 2802 2802 2802 TRP TRP A . n 
A 1 2803 VAL 2803 2803 2803 VAL VAL A . n 
A 1 2804 ARG 2804 2804 2804 ARG ARG A . n 
A 1 2805 GLY 2805 2805 2805 GLY GLY A . n 
A 1 2806 ILE 2806 2806 2806 ILE ILE A . n 
A 1 2807 PHE 2807 2807 2807 PHE PHE A . n 
A 1 2808 GLU 2808 2808 2808 GLU GLU A . n 
A 1 2809 ALA 2809 2809 2809 ALA ALA A . n 
A 1 2810 LEU 2810 2810 2810 LEU LEU A . n 
A 1 2811 ARG 2811 2811 2811 ARG ARG A . n 
A 1 2812 PRO 2812 2812 2812 PRO PRO A . n 
A 1 2813 LEU 2813 2813 2813 LEU LEU A . n 
A 1 2814 GLU 2814 2814 2814 GLU GLU A . n 
A 1 2815 THR 2815 2815 2815 THR THR A . n 
A 1 2816 LEU 2816 2816 2816 LEU LEU A . n 
A 1 2817 PRO 2817 2817 2817 PRO PRO A . n 
A 1 2818 VAL 2818 2818 2818 VAL VAL A . n 
A 1 2819 GLU 2819 2819 2819 GLU GLU A . n 
A 1 2820 GLY 2820 2820 2820 GLY GLY A . n 
A 1 2821 LEU 2821 2821 2821 LEU LEU A . n 
A 1 2822 ILE 2822 2822 2822 ILE ILE A . n 
A 1 2823 ARG 2823 2823 2823 ARG ARG A . n 
A 1 2824 ILE 2824 2824 2824 ILE ILE A . n 
A 1 2825 TRP 2825 2825 2825 TRP TRP A . n 
A 1 2826 ALA 2826 2826 2826 ALA ALA A . n 
A 1 2827 HIS 2827 2827 2827 HIS HIS A . n 
A 1 2828 GLU 2828 2828 2828 GLU GLU A . n 
A 1 2829 ALA 2829 2829 2829 ALA ALA A . n 
A 1 2830 LEU 2830 2830 2830 LEU LEU A . n 
A 1 2831 ARG 2831 2831 2831 ARG ARG A . n 
A 1 2832 LEU 2832 2832 2832 LEU LEU A . n 
A 1 2833 PHE 2833 2833 2833 PHE PHE A . n 
A 1 2834 GLN 2834 2834 2834 GLN GLN A . n 
A 1 2835 ASP 2835 2835 2835 ASP ASP A . n 
A 1 2836 ARG 2836 2836 2836 ARG ARG A . n 
A 1 2837 LEU 2837 2837 2837 LEU LEU A . n 
A 1 2838 VAL 2838 2838 2838 VAL VAL A . n 
A 1 2839 GLU 2839 2839 2839 GLU GLU A . n 
A 1 2840 ASP 2840 2840 2840 ASP ASP A . n 
A 1 2841 GLU 2841 2841 2841 GLU GLU A . n 
A 1 2842 GLU 2842 2842 2842 GLU GLU A . n 
A 1 2843 ARG 2843 2843 2843 ARG ARG A . n 
A 1 2844 ARG 2844 2844 2844 ARG ARG A . n 
A 1 2845 TRP 2845 2845 2845 TRP TRP A . n 
A 1 2846 THR 2846 2846 2846 THR THR A . n 
A 1 2847 ASP 2847 2847 2847 ASP ASP A . n 
A 1 2848 GLU 2848 2848 2848 GLU GLU A . n 
A 1 2849 ASN 2849 2849 2849 ASN ASN A . n 
A 1 2850 ILE 2850 2850 2850 ILE ILE A . n 
A 1 2851 ASP 2851 2851 2851 ASP ASP A . n 
A 1 2852 THR 2852 2852 2852 THR THR A . n 
A 1 2853 VAL 2853 2853 2853 VAL VAL A . n 
A 1 2854 ALA 2854 2854 2854 ALA ALA A . n 
A 1 2855 LEU 2855 2855 2855 LEU LEU A . n 
A 1 2856 LYS 2856 2856 2856 LYS LYS A . n 
A 1 2857 HIS 2857 2857 2857 HIS HIS A . n 
A 1 2858 PHE 2858 2858 2858 PHE PHE A . n 
A 1 2859 PRO 2859 2859 2859 PRO PRO A . n 
A 1 2860 ASN 2860 2860 2860 ASN ASN A . n 
A 1 2861 ILE 2861 2861 2861 ILE ILE A . n 
A 1 2862 ASP 2862 2862 2862 ASP ASP A . n 
A 1 2863 ARG 2863 2863 2863 ARG ARG A . n 
A 1 2864 GLU 2864 2864 2864 GLU GLU A . n 
A 1 2865 LYS 2865 2865 2865 LYS LYS A . n 
A 1 2866 ALA 2866 2866 2866 ALA ALA A . n 
A 1 2867 MET 2867 2867 2867 MET MET A . n 
A 1 2868 SER 2868 2868 2868 SER SER A . n 
A 1 2869 ARG 2869 2869 2869 ARG ARG A . n 
A 1 2870 PRO 2870 2870 2870 PRO PRO A . n 
A 1 2871 ILE 2871 2871 2871 ILE ILE A . n 
A 1 2872 LEU 2872 2872 2872 LEU LEU A . n 
A 1 2873 TYR 2873 2873 2873 TYR TYR A . n 
A 1 2874 SER 2874 2874 2874 SER SER A . n 
A 1 2875 ASN 2875 2875 2875 ASN ASN A . n 
A 1 2876 TRP 2876 2876 2876 TRP TRP A . n 
A 1 2877 LEU 2877 2877 2877 LEU LEU A . n 
A 1 2878 SER 2878 2878 2878 SER SER A . n 
A 1 2879 LYS 2879 2879 2879 LYS LYS A . n 
A 1 2880 ASP 2880 2880 2880 ASP ASP A . n 
A 1 2881 TYR 2881 2881 2881 TYR TYR A . n 
A 1 2882 ILE 2882 2882 2882 ILE ILE A . n 
A 1 2883 PRO 2883 2883 2883 PRO PRO A . n 
A 1 2884 VAL 2884 2884 2884 VAL VAL A . n 
A 1 2885 ASP 2885 2885 2885 ASP ASP A . n 
A 1 2886 GLN 2886 2886 2886 GLN GLN A . n 
A 1 2887 GLU 2887 2887 2887 GLU GLU A . n 
A 1 2888 GLU 2888 2888 2888 GLU GLU A . n 
A 1 2889 LEU 2889 2889 2889 LEU LEU A . n 
A 1 2890 ARG 2890 2890 2890 ARG ARG A . n 
A 1 2891 ASP 2891 2891 2891 ASP ASP A . n 
A 1 2892 TYR 2892 2892 2892 TYR TYR A . n 
A 1 2893 VAL 2893 2893 2893 VAL VAL A . n 
A 1 2894 LYS 2894 2894 2894 LYS LYS A . n 
A 1 2895 ALA 2895 2895 2895 ALA ALA A . n 
A 1 2896 ARG 2896 2896 2896 ARG ARG A . n 
A 1 2897 LEU 2897 2897 2897 LEU LEU A . n 
A 1 2898 LYS 2898 2898 2898 LYS LYS A . n 
A 1 2899 VAL 2899 2899 2899 VAL VAL A . n 
A 1 2900 PHE 2900 2900 2900 PHE PHE A . n 
A 1 2901 TYR 2901 2901 2901 TYR TYR A . n 
A 1 2902 GLU 2902 2902 2902 GLU GLU A . n 
A 1 2903 GLU 2903 2903 2903 GLU GLU A . n 
A 1 2904 GLU 2904 2904 2904 GLU GLU A . n 
A 1 2905 LEU 2905 2905 2905 LEU LEU A . n 
A 1 2906 ASP 2906 2906 2906 ASP ASP A . n 
A 1 2907 VAL 2907 2907 2907 VAL VAL A . n 
A 1 2908 PRO 2908 2908 2908 PRO PRO A . n 
A 1 2909 LEU 2909 2909 2909 LEU LEU A . n 
A 1 2910 VAL 2910 2910 2910 VAL VAL A . n 
A 1 2911 LEU 2911 2911 2911 LEU LEU A . n 
A 1 2912 PHE 2912 2912 2912 PHE PHE A . n 
A 1 2913 ASN 2913 2913 2913 ASN ASN A . n 
A 1 2914 GLU 2914 2914 2914 GLU GLU A . n 
A 1 2915 VAL 2915 2915 2915 VAL VAL A . n 
A 1 2916 LEU 2916 2916 2916 LEU LEU A . n 
A 1 2917 ASP 2917 2917 2917 ASP ASP A . n 
A 1 2918 HIS 2918 2918 2918 HIS HIS A . n 
A 1 2919 VAL 2919 2919 2919 VAL VAL A . n 
A 1 2920 LEU 2920 2920 2920 LEU LEU A . n 
A 1 2921 ARG 2921 2921 2921 ARG ARG A . n 
A 1 2922 ILE 2922 2922 2922 ILE ILE A . n 
A 1 2923 ASP 2923 2923 2923 ASP ASP A . n 
A 1 2924 ARG 2924 2924 2924 ARG ARG A . n 
A 1 2925 ILE 2925 2925 2925 ILE ILE A . n 
A 1 2926 PHE 2926 2926 2926 PHE PHE A . n 
A 1 2927 ARG 2927 2927 2927 ARG ARG A . n 
A 1 2928 GLN 2928 2928 2928 GLN GLN A . n 
A 1 2929 PRO 2929 2929 2929 PRO PRO A . n 
A 1 2930 GLN 2930 2930 2930 GLN GLN A . n 
A 1 2931 GLY 2931 2931 2931 GLY GLY A . n 
A 1 2932 HIS 2932 2932 2932 HIS HIS A . n 
A 1 2933 LEU 2933 2933 2933 LEU LEU A . n 
A 1 2934 LEU 2934 2934 2934 LEU LEU A . n 
A 1 2935 LEU 2935 2935 2935 LEU LEU A . n 
A 1 2936 ILE 2936 2936 2936 ILE ILE A . n 
A 1 2937 GLY 2937 2937 2937 GLY GLY A . n 
A 1 2938 VAL 2938 2938 2938 VAL VAL A . n 
A 1 2939 SER 2939 2939 2939 SER SER A . n 
A 1 2940 GLY 2940 2940 2940 GLY GLY A . n 
A 1 2941 ALA 2941 2941 2941 ALA ALA A . n 
A 1 2942 GLY 2942 2942 2942 GLY GLY A . n 
A 1 2943 LYS 2943 2943 2943 LYS LYS A . n 
A 1 2944 THR 2944 2944 2944 THR THR A . n 
A 1 2945 THR 2945 2945 2945 THR THR A . n 
A 1 2946 LEU 2946 2946 2946 LEU LEU A . n 
A 1 2947 SER 2947 2947 2947 SER SER A . n 
A 1 2948 ARG 2948 2948 2948 ARG ARG A . n 
A 1 2949 PHE 2949 2949 2949 PHE PHE A . n 
A 1 2950 VAL 2950 2950 2950 VAL VAL A . n 
A 1 2951 ALA 2951 2951 2951 ALA ALA A . n 
A 1 2952 TRP 2952 2952 2952 TRP TRP A . n 
A 1 2953 MET 2953 2953 2953 MET MET A . n 
A 1 2954 ASN 2954 2954 2954 ASN ASN A . n 
A 1 2955 GLY 2955 2955 2955 GLY GLY A . n 
A 1 2956 LEU 2956 2956 2956 LEU LEU A . n 
A 1 2957 SER 2957 2957 2957 SER SER A . n 
A 1 2958 VAL 2958 2958 2958 VAL VAL A . n 
A 1 2959 TYR 2959 2959 2959 TYR TYR A . n 
A 1 2960 GLN 2960 2960 2960 GLN GLN A . n 
A 1 2961 ILE 2961 2961 2961 ILE ILE A . n 
A 1 2962 LYS 2962 2962 2962 LYS LYS A . n 
A 1 2963 VAL 2963 2963 2963 VAL VAL A . n 
A 1 2964 HIS 2964 2964 2964 HIS HIS A . n 
A 1 2965 ARG 2965 2965 2965 ARG ARG A . n 
A 1 2966 LYS 2966 2966 2966 LYS LYS A . n 
A 1 2967 TYR 2967 2967 2967 TYR TYR A . n 
A 1 2968 THR 2968 2968 2968 THR THR A . n 
A 1 2969 GLY 2969 2969 2969 GLY GLY A . n 
A 1 2970 GLU 2970 2970 2970 GLU GLU A . n 
A 1 2971 ASP 2971 2971 2971 ASP ASP A . n 
A 1 2972 PHE 2972 2972 2972 PHE PHE A . n 
A 1 2973 ASP 2973 2973 2973 ASP ASP A . n 
A 1 2974 GLU 2974 2974 2974 GLU GLU A . n 
A 1 2975 ASP 2975 2975 2975 ASP ASP A . n 
A 1 2976 LEU 2976 2976 2976 LEU LEU A . n 
A 1 2977 ARG 2977 2977 2977 ARG ARG A . n 
A 1 2978 THR 2978 2978 2978 THR THR A . n 
A 1 2979 VAL 2979 2979 2979 VAL VAL A . n 
A 1 2980 LEU 2980 2980 2980 LEU LEU A . n 
A 1 2981 ARG 2981 2981 2981 ARG ARG A . n 
A 1 2982 ARG 2982 2982 2982 ARG ARG A . n 
A 1 2983 SER 2983 2983 2983 SER SER A . n 
A 1 2984 GLY 2984 2984 2984 GLY GLY A . n 
A 1 2985 CYS 2985 2985 2985 CYS CYS A . n 
A 1 2986 LYS 2986 2986 2986 LYS LYS A . n 
A 1 2987 ASN 2987 2987 2987 ASN ASN A . n 
A 1 2988 GLU 2988 2988 2988 GLU GLU A . n 
A 1 2989 LYS 2989 2989 2989 LYS LYS A . n 
A 1 2990 ILE 2990 2990 2990 ILE ILE A . n 
A 1 2991 ALA 2991 2991 2991 ALA ALA A . n 
A 1 2992 PHE 2992 2992 2992 PHE PHE A . n 
A 1 2993 ILE 2993 2993 2993 ILE ILE A . n 
A 1 2994 MET 2994 2994 2994 MET MET A . n 
A 1 2995 ASP 2995 2995 2995 ASP ASP A . n 
A 1 2996 GLU 2996 2996 2996 GLU GLU A . n 
A 1 2997 SER 2997 2997 2997 SER SER A . n 
A 1 2998 ASN 2998 2998 2998 ASN ASN A . n 
A 1 2999 VAL 2999 2999 2999 VAL VAL A . n 
A 1 3000 LEU 3000 3000 3000 LEU LEU A . n 
A 1 3001 ASP 3001 3001 3001 ASP ASP A . n 
A 1 3002 SER 3002 3002 3002 SER SER A . n 
A 1 3003 GLY 3003 3003 3003 GLY GLY A . n 
A 1 3004 PHE 3004 3004 3004 PHE PHE A . n 
A 1 3005 LEU 3005 3005 3005 LEU LEU A . n 
A 1 3006 GLU 3006 3006 3006 GLU GLU A . n 
A 1 3007 ARG 3007 3007 3007 ARG ARG A . n 
A 1 3008 MET 3008 3008 3008 MET MET A . n 
A 1 3009 ASN 3009 3009 3009 ASN ASN A . n 
A 1 3010 THR 3010 3010 3010 THR THR A . n 
A 1 3011 LEU 3011 3011 3011 LEU LEU A . n 
A 1 3012 LEU 3012 3012 3012 LEU LEU A . n 
A 1 3013 ALA 3013 3013 3013 ALA ALA A . n 
A 1 3014 ASN 3014 3014 3014 ASN ASN A . n 
A 1 3015 GLY 3015 3015 3015 GLY GLY A . n 
A 1 3016 GLU 3016 3016 3016 GLU GLU A . n 
A 1 3017 VAL 3017 3017 3017 VAL VAL A . n 
A 1 3018 PRO 3018 3018 3018 PRO PRO A . n 
A 1 3019 GLY 3019 3019 3019 GLY GLY A . n 
A 1 3020 LEU 3020 3020 3020 LEU LEU A . n 
A 1 3021 PHE 3021 3021 3021 PHE PHE A . n 
A 1 3022 GLU 3022 3022 3022 GLU GLU A . n 
A 1 3023 GLY 3023 3023 3023 GLY GLY A . n 
A 1 3024 ASP 3024 3024 3024 ASP ASP A . n 
A 1 3025 GLU 3025 3025 3025 GLU GLU A . n 
A 1 3026 TYR 3026 3026 3026 TYR TYR A . n 
A 1 3027 ALA 3027 3027 3027 ALA ALA A . n 
A 1 3028 THR 3028 3028 3028 THR THR A . n 
A 1 3029 LEU 3029 3029 3029 LEU LEU A . n 
A 1 3030 MET 3030 3030 3030 MET MET A . n 
A 1 3031 THR 3031 3031 3031 THR THR A . n 
A 1 3032 GLN 3032 3032 3032 GLN GLN A . n 
A 1 3033 CYS 3033 3033 3033 CYS CYS A . n 
A 1 3034 LYS 3034 3034 3034 LYS LYS A . n 
A 1 3035 GLU 3035 3035 3035 GLU GLU A . n 
A 1 3036 GLY 3036 3036 3036 GLY GLY A . n 
A 1 3037 ALA 3037 3037 3037 ALA ALA A . n 
A 1 3038 GLN 3038 3038 3038 GLN GLN A . n 
A 1 3039 LYS 3039 3039 3039 LYS LYS A . n 
A 1 3040 GLU 3040 3040 3040 GLU GLU A . n 
A 1 3041 GLY 3041 3041 3041 GLY GLY A . n 
A 1 3042 LEU 3042 3042 3042 LEU LEU A . n 
A 1 3043 MET 3043 3043 3043 MET MET A . n 
A 1 3044 LEU 3044 3044 3044 LEU LEU A . n 
A 1 3045 ASP 3045 3045 3045 ASP ASP A . n 
A 1 3046 SER 3046 3046 3046 SER SER A . n 
A 1 3047 HIS 3047 3047 3047 HIS HIS A . n 
A 1 3048 GLU 3048 3048 3048 GLU GLU A . n 
A 1 3049 GLU 3049 3049 3049 GLU GLU A . n 
A 1 3050 LEU 3050 3050 3050 LEU LEU A . n 
A 1 3051 TYR 3051 3051 3051 TYR TYR A . n 
A 1 3052 LYS 3052 3052 3052 LYS LYS A . n 
A 1 3053 TRP 3053 3053 3053 TRP TRP A . n 
A 1 3054 PHE 3054 3054 3054 PHE PHE A . n 
A 1 3055 THR 3055 3055 3055 THR THR A . n 
A 1 3056 SER 3056 3056 3056 SER SER A . n 
A 1 3057 GLN 3057 3057 3057 GLN GLN A . n 
A 1 3058 VAL 3058 3058 3058 VAL VAL A . n 
A 1 3059 ILE 3059 3059 3059 ILE ILE A . n 
A 1 3060 ARG 3060 3060 3060 ARG ARG A . n 
A 1 3061 ASN 3061 3061 3061 ASN ASN A . n 
A 1 3062 LEU 3062 3062 3062 LEU LEU A . n 
A 1 3063 HIS 3063 3063 3063 HIS HIS A . n 
A 1 3064 VAL 3064 3064 3064 VAL VAL A . n 
A 1 3065 VAL 3065 3065 3065 VAL VAL A . n 
A 1 3066 PHE 3066 3066 3066 PHE PHE A . n 
A 1 3067 THR 3067 3067 3067 THR THR A . n 
A 1 3068 MET 3068 3068 3068 MET MET A . n 
A 1 3069 ASN 3069 3069 3069 ASN ASN A . n 
A 1 3070 PRO 3070 3070 3070 PRO PRO A . n 
A 1 3071 SER 3071 3071 3071 SER SER A . n 
A 1 3072 SER 3072 3072 3072 SER SER A . n 
A 1 3073 GLU 3073 3073 3073 GLU GLU A . n 
A 1 3074 GLY 3074 3074 3074 GLY GLY A . n 
A 1 3075 LEU 3075 3075 3075 LEU LEU A . n 
A 1 3076 LYS 3076 3076 3076 LYS LYS A . n 
A 1 3077 ASP 3077 3077 3077 ASP ASP A . n 
A 1 3078 ARG 3078 3078 3078 ARG ARG A . n 
A 1 3079 ALA 3079 3079 3079 ALA ALA A . n 
A 1 3080 ALA 3080 3080 3080 ALA ALA A . n 
A 1 3081 THR 3081 3081 3081 THR THR A . n 
A 1 3082 SER 3082 3082 3082 SER SER A . n 
A 1 3083 PRO 3083 3083 3083 PRO PRO A . n 
A 1 3084 ALA 3084 3084 3084 ALA ALA A . n 
A 1 3085 LEU 3085 3085 3085 LEU LEU A . n 
A 1 3086 PHE 3086 3086 3086 PHE PHE A . n 
A 1 3087 ASN 3087 3087 3087 ASN ASN A . n 
A 1 3088 ARG 3088 3088 3088 ARG ARG A . n 
A 1 3089 CYS 3089 3089 3089 CYS CYS A . n 
A 1 3090 VAL 3090 3090 3090 VAL VAL A . n 
A 1 3091 LEU 3091 3091 3091 LEU LEU A . n 
A 1 3092 ASN 3092 3092 3092 ASN ASN A . n 
A 1 3093 TRP 3093 3093 3093 TRP TRP A . n 
A 1 3094 PHE 3094 3094 3094 PHE PHE A . n 
A 1 3095 GLY 3095 3095 3095 GLY GLY A . n 
A 1 3096 ASP 3096 3096 3096 ASP ASP A . n 
A 1 3097 TRP 3097 3097 3097 TRP TRP A . n 
A 1 3098 SER 3098 3098 3098 SER SER A . n 
A 1 3099 THR 3099 3099 3099 THR THR A . n 
A 1 3100 GLU 3100 3100 3100 GLU GLU A . n 
A 1 3101 ALA 3101 3101 3101 ALA ALA A . n 
A 1 3102 LEU 3102 3102 3102 LEU LEU A . n 
A 1 3103 TYR 3103 3103 3103 TYR TYR A . n 
A 1 3104 GLN 3104 3104 3104 GLN GLN A . n 
A 1 3105 VAL 3105 3105 3105 VAL VAL A . n 
A 1 3106 GLY 3106 3106 3106 GLY GLY A . n 
A 1 3107 LYS 3107 3107 3107 LYS LYS A . n 
A 1 3108 GLU 3108 3108 3108 GLU GLU A . n 
A 1 3109 PHE 3109 3109 3109 PHE PHE A . n 
A 1 3110 THR 3110 3110 3110 THR THR A . n 
A 1 3111 SER 3111 3111 3111 SER SER A . n 
A 1 3112 LYS 3112 3112 3112 LYS LYS A . n 
A 1 3113 MET 3113 3113 3113 MET MET A . n 
A 1 3114 ASP 3114 3114 3114 ASP ASP A . n 
A 1 3115 LEU 3115 3115 3115 LEU LEU A . n 
A 1 3116 GLU 3116 3116 3116 GLU GLU A . n 
A 1 3117 LYS 3117 3117 3117 LYS LYS A . n 
A 1 3118 PRO 3118 3118 3118 PRO PRO A . n 
A 1 3119 ASN 3119 3119 3119 ASN ASN A . n 
A 1 3120 TYR 3120 3120 3120 TYR TYR A . n 
A 1 3121 ILE 3121 3121 3121 ILE ILE A . n 
A 1 3122 VAL 3122 3122 3122 VAL VAL A . n 
A 1 3123 PRO 3123 3123 3123 PRO PRO A . n 
A 1 3124 ASP 3124 3124 3124 ASP ASP A . n 
A 1 3125 TYR 3125 3125 3125 TYR TYR A . n 
A 1 3126 MET 3126 3126 3126 MET MET A . n 
A 1 3127 PRO 3127 3127 3127 PRO PRO A . n 
A 1 3128 VAL 3128 3128 3128 VAL VAL A . n 
A 1 3129 VAL 3129 3129 3129 VAL VAL A . n 
A 1 3130 TYR 3130 3130 3130 TYR TYR A . n 
A 1 3131 ASP 3131 3131 3131 ASP ASP A . n 
A 1 3132 LYS 3132 3132 3132 LYS LYS A . n 
A 1 3133 LEU 3133 3133 3133 LEU LEU A . n 
A 1 3134 PRO 3134 3134 3134 PRO PRO A . n 
A 1 3135 GLN 3135 3135 3135 GLN GLN A . n 
A 1 3136 PRO 3136 3136 3136 PRO PRO A . n 
A 1 3137 PRO 3137 3137 3137 PRO PRO A . n 
A 1 3138 SER 3138 3138 3138 SER SER A . n 
A 1 3139 HIS 3139 3139 3139 HIS HIS A . n 
A 1 3140 ARG 3140 3140 3140 ARG ARG A . n 
A 1 3141 GLU 3141 3141 3141 GLU GLU A . n 
A 1 3142 ALA 3142 3142 3142 ALA ALA A . n 
A 1 3143 ILE 3143 3143 3143 ILE ILE A . n 
A 1 3144 VAL 3144 3144 3144 VAL VAL A . n 
A 1 3145 ASN 3145 3145 3145 ASN ASN A . n 
A 1 3146 SER 3146 3146 3146 SER SER A . n 
A 1 3147 CYS 3147 3147 3147 CYS CYS A . n 
A 1 3148 VAL 3148 3148 3148 VAL VAL A . n 
A 1 3149 PHE 3149 3149 3149 PHE PHE A . n 
A 1 3150 VAL 3150 3150 3150 VAL VAL A . n 
A 1 3151 HIS 3151 3151 3151 HIS HIS A . n 
A 1 3152 GLN 3152 3152 3152 GLN GLN A . n 
A 1 3153 THR 3153 3153 3153 THR THR A . n 
A 1 3154 LEU 3154 3154 3154 LEU LEU A . n 
A 1 3155 HIS 3155 3155 3155 HIS HIS A . n 
A 1 3156 GLN 3156 3156 3156 GLN GLN A . n 
A 1 3157 ALA 3157 3157 3157 ALA ALA A . n 
A 1 3158 ASN 3158 3158 3158 ASN ASN A . n 
A 1 3159 ALA 3159 3159 3159 ALA ALA A . n 
A 1 3160 ARG 3160 3160 3160 ARG ARG A . n 
A 1 3161 LEU 3161 3161 3161 LEU LEU A . n 
A 1 3162 ALA 3162 3162 3162 ALA ALA A . n 
A 1 3163 LYS 3163 3163 3163 LYS LYS A . n 
A 1 3164 ARG 3164 3164 3164 ARG ARG A . n 
A 1 3165 GLY 3165 3165 3165 GLY GLY A . n 
A 1 3166 GLY 3166 3166 3166 GLY GLY A . n 
A 1 3167 ARG 3167 3167 3167 ARG ARG A . n 
A 1 3168 THR 3168 3168 3168 THR THR A . n 
A 1 3169 MET 3169 3169 3169 MET MET A . n 
A 1 3170 ALA 3170 3170 3170 ALA ALA A . n 
A 1 3171 ILE 3171 3171 3171 ILE ILE A . n 
A 1 3172 THR 3172 3172 3172 THR THR A . n 
A 1 3173 PRO 3173 3173 3173 PRO PRO A . n 
A 1 3174 ARG 3174 3174 3174 ARG ARG A . n 
A 1 3175 HIS 3175 3175 3175 HIS HIS A . n 
A 1 3176 TYR 3176 3176 3176 TYR TYR A . n 
A 1 3177 LEU 3177 3177 3177 LEU LEU A . n 
A 1 3178 ASP 3178 3178 3178 ASP ASP A . n 
A 1 3179 PHE 3179 3179 3179 PHE PHE A . n 
A 1 3180 ILE 3180 3180 3180 ILE ILE A . n 
A 1 3181 ASN 3181 3181 3181 ASN ASN A . n 
A 1 3182 HIS 3182 3182 3182 HIS HIS A . n 
A 1 3183 TYR 3183 3183 3183 TYR TYR A . n 
A 1 3184 ALA 3184 3184 3184 ALA ALA A . n 
A 1 3185 ASN 3185 3185 3185 ASN ASN A . n 
A 1 3186 LEU 3186 3186 3186 LEU LEU A . n 
A 1 3187 PHE 3187 3187 3187 PHE PHE A . n 
A 1 3188 HIS 3188 3188 3188 HIS HIS A . n 
A 1 3189 GLU 3189 3189 3189 GLU GLU A . n 
A 1 3190 LYS 3190 3190 3190 LYS LYS A . n 
A 1 3191 ARG 3191 3191 3191 ARG ARG A . n 
A 1 3192 SER 3192 3192 3192 SER SER A . n 
A 1 3193 GLU 3193 3193 3193 GLU GLU A . n 
A 1 3194 LEU 3194 3194 3194 LEU LEU A . n 
A 1 3195 GLU 3195 3195 3195 GLU GLU A . n 
A 1 3196 GLU 3196 3196 3196 GLU GLU A . n 
A 1 3197 GLN 3197 3197 3197 GLN GLN A . n 
A 1 3198 GLN 3198 3198 3198 GLN GLN A . n 
A 1 3199 MET 3199 3199 3199 MET MET A . n 
A 1 3200 HIS 3200 3200 3200 HIS HIS A . n 
A 1 3201 LEU 3201 3201 3201 LEU LEU A . n 
A 1 3202 ASN 3202 3202 3202 ASN ASN A . n 
A 1 3203 VAL 3203 3203 3203 VAL VAL A . n 
A 1 3204 GLY 3204 3204 3204 GLY GLY A . n 
A 1 3205 LEU 3205 3205 3205 LEU LEU A . n 
A 1 3206 ARG 3206 3206 3206 ARG ARG A . n 
A 1 3207 LYS 3207 3207 3207 LYS LYS A . n 
A 1 3208 ILE 3208 3208 3208 ILE ILE A . n 
A 1 3209 LYS 3209 3209 3209 LYS LYS A . n 
A 1 3210 GLU 3210 3210 3210 GLU GLU A . n 
A 1 3211 THR 3211 3211 3211 THR THR A . n 
A 1 3212 VAL 3212 3212 3212 VAL VAL A . n 
A 1 3213 ASP 3213 3213 3213 ASP ASP A . n 
A 1 3214 GLN 3214 3214 3214 GLN GLN A . n 
A 1 3215 VAL 3215 3215 3215 VAL VAL A . n 
A 1 3216 GLU 3216 3216 3216 GLU GLU A . n 
A 1 3217 GLU 3217 3217 3217 GLU GLU A . n 
A 1 3218 LEU 3218 3218 3218 LEU LEU A . n 
A 1 3219 ARG 3219 3219 3219 ARG ARG A . n 
A 1 3220 ARG 3220 3220 3220 ARG ARG A . n 
A 1 3221 ASP 3221 3221 3221 ASP ASP A . n 
A 1 3222 LEU 3222 3222 3222 LEU LEU A . n 
A 1 3223 ARG 3223 3223 3223 ARG ARG A . n 
A 1 3224 ILE 3224 3224 3224 ILE ILE A . n 
A 1 3225 LYS 3225 3225 3225 LYS LYS A . n 
A 1 3226 SER 3226 3226 3226 SER SER A . n 
A 1 3227 GLN 3227 3227 3227 GLN GLN A . n 
A 1 3228 GLU 3228 3228 3228 GLU GLU A . n 
A 1 3229 LEU 3229 3229 3229 LEU LEU A . n 
A 1 3230 GLU 3230 3230 3230 GLU GLU A . n 
A 1 3231 VAL 3231 3231 3231 VAL VAL A . n 
A 1 3232 LYS 3232 3232 3232 LYS LYS A . n 
A 1 3233 ASN 3233 3233 3233 ASN ASN A . n 
A 1 3234 ALA 3234 3234 3234 ALA ALA A . n 
A 1 3235 ALA 3235 3235 3235 ALA ALA A . n 
A 1 3236 ALA 3236 3236 3236 ALA ALA A . n 
A 1 3237 ASN 3237 3237 3237 ASN ASN A . n 
A 1 3238 ASP 3238 3238 3238 ASP ASP A . n 
A 1 3239 LYS 3239 3239 3239 LYS LYS A . n 
A 1 3240 LEU 3240 3240 3240 LEU LEU A . n 
A 1 3241 LYS 3241 3241 3241 LYS LYS A . n 
A 1 3242 LYS 3242 3242 3242 LYS LYS A . n 
A 1 3243 MET 3243 3243 ?    ?   ?   A . n 
A 1 3244 VAL 3244 3244 ?    ?   ?   A . n 
A 1 3245 LYS 3245 3245 ?    ?   ?   A . n 
A 1 3246 ASP 3246 3246 ?    ?   ?   A . n 
A 1 3247 GLN 3247 3247 ?    ?   ?   A . n 
A 1 3248 GLN 3248 3248 ?    ?   ?   A . n 
A 1 3249 GLU 3249 3249 ?    ?   ?   A . n 
A 1 3250 ALA 3250 3250 ?    ?   ?   A . n 
A 1 3251 GLU 3251 3251 ?    ?   ?   A . n 
A 1 3252 LYS 3252 3252 ?    ?   ?   A . n 
A 1 3253 LYS 3253 3253 ?    ?   ?   A . n 
A 1 3254 LYS 3254 3254 ?    ?   ?   A . n 
A 1 3255 VAL 3255 3255 ?    ?   ?   A . n 
A 1 3256 MET 3256 3256 ?    ?   ?   A . n 
A 1 3257 SER 3257 3257 ?    ?   ?   A . n 
A 1 3258 GLN 3258 3258 ?    ?   ?   A . n 
A 1 3259 GLU 3259 3259 ?    ?   ?   A . n 
A 1 3260 ILE 3260 3260 ?    ?   ?   A . n 
A 1 3261 GLN 3261 3261 ?    ?   ?   A . n 
A 1 3262 GLU 3262 3262 ?    ?   ?   A . n 
A 1 3263 GLN 3263 3263 ?    ?   ?   A . n 
A 1 3264 LEU 3264 3264 ?    ?   ?   A . n 
A 1 3265 HIS 3265 3265 ?    ?   ?   A . n 
A 1 3266 LYS 3266 3266 ?    ?   ?   A . n 
A 1 3267 GLN 3267 3267 ?    ?   ?   A . n 
A 1 3268 GLN 3268 3268 ?    ?   ?   A . n 
A 1 3269 GLU 3269 3269 ?    ?   ?   A . n 
A 1 3270 VAL 3270 3270 ?    ?   ?   A . n 
A 1 3271 ILE 3271 3271 ?    ?   ?   A . n 
A 1 3272 ALA 3272 3272 ?    ?   ?   A . n 
A 1 3273 ASP 3273 3273 ?    ?   ?   A . n 
A 1 3274 LYS 3274 3274 ?    ?   ?   A . n 
A 1 3275 GLN 3275 3275 ?    ?   ?   A . n 
A 1 3276 MET 3276 3276 ?    ?   ?   A . n 
A 1 3277 SER 3277 3277 ?    ?   ?   A . n 
A 1 3278 VAL 3278 3278 ?    ?   ?   A . n 
A 1 3279 LYS 3279 3279 ?    ?   ?   A . n 
A 1 3280 GLU 3280 3280 ?    ?   ?   A . n 
A 1 3281 ASP 3281 3281 ?    ?   ?   A . n 
A 1 3282 LEU 3282 3282 ?    ?   ?   A . n 
A 1 3283 ASP 3283 3283 ?    ?   ?   A . n 
A 1 3284 LYS 3284 3284 ?    ?   ?   A . n 
A 1 3285 VAL 3285 3285 ?    ?   ?   A . n 
A 1 3286 GLU 3286 3286 ?    ?   ?   A . n 
A 1 3287 PRO 3287 3287 ?    ?   ?   A . n 
A 1 3288 ALA 3288 3288 ?    ?   ?   A . n 
A 1 3289 VAL 3289 3289 ?    ?   ?   A . n 
A 1 3290 ILE 3290 3290 ?    ?   ?   A . n 
A 1 3291 GLU 3291 3291 ?    ?   ?   A . n 
A 1 3292 ALA 3292 3292 ?    ?   ?   A . n 
A 1 3293 GLN 3293 3293 ?    ?   ?   A . n 
A 1 3294 ASN 3294 3294 ?    ?   ?   A . n 
A 1 3295 ALA 3295 3295 ?    ?   ?   A . n 
A 1 3296 VAL 3296 3296 ?    ?   ?   A . n 
A 1 3297 LYS 3297 3297 ?    ?   ?   A . n 
A 1 3298 SER 3298 3298 ?    ?   ?   A . n 
A 1 3299 ILE 3299 3299 ?    ?   ?   A . n 
A 1 3300 LYS 3300 3300 ?    ?   ?   A . n 
A 1 3301 LYS 3301 3301 ?    ?   ?   A . n 
A 1 3302 GLN 3302 3302 ?    ?   ?   A . n 
A 1 3303 HIS 3303 3303 ?    ?   ?   A . n 
A 1 3304 LEU 3304 3304 ?    ?   ?   A . n 
A 1 3305 VAL 3305 3305 ?    ?   ?   A . n 
A 1 3306 GLU 3306 3306 ?    ?   ?   A . n 
A 1 3307 VAL 3307 3307 ?    ?   ?   A . n 
A 1 3308 ARG 3308 3308 ?    ?   ?   A . n 
A 1 3309 SER 3309 3309 ?    ?   ?   A . n 
A 1 3310 MET 3310 3310 ?    ?   ?   A . n 
A 1 3311 ALA 3311 3311 ?    ?   ?   A . n 
A 1 3312 ASN 3312 3312 ?    ?   ?   A . n 
A 1 3313 PRO 3313 3313 ?    ?   ?   A . n 
A 1 3314 PRO 3314 3314 ?    ?   ?   A . n 
A 1 3315 ALA 3315 3315 ?    ?   ?   A . n 
A 1 3316 ALA 3316 3316 ?    ?   ?   A . n 
A 1 3317 VAL 3317 3317 ?    ?   ?   A . n 
A 1 3318 LYS 3318 3318 ?    ?   ?   A . n 
A 1 3319 LEU 3319 3319 ?    ?   ?   A . n 
A 1 3320 ALA 3320 3320 ?    ?   ?   A . n 
A 1 3321 LEU 3321 3321 ?    ?   ?   A . n 
A 1 3322 GLU 3322 3322 ?    ?   ?   A . n 
A 1 3323 SER 3323 3323 ?    ?   ?   A . n 
A 1 3324 ILE 3324 3324 ?    ?   ?   A . n 
A 1 3325 CYS 3325 3325 ?    ?   ?   A . n 
A 1 3326 LEU 3326 3326 ?    ?   ?   A . n 
A 1 3327 LEU 3327 3327 ?    ?   ?   A . n 
A 1 3328 LEU 3328 3328 ?    ?   ?   A . n 
A 1 3329 GLY 3329 3329 ?    ?   ?   A . n 
A 1 3330 GLU 3330 3330 ?    ?   ?   A . n 
A 1 3331 SER 3331 3331 ?    ?   ?   A . n 
A 1 3332 THR 3332 3332 ?    ?   ?   A . n 
A 1 3333 THR 3333 3333 ?    ?   ?   A . n 
A 1 3334 ASP 3334 3334 ?    ?   ?   A . n 
A 1 3335 TRP 3335 3335 ?    ?   ?   A . n 
A 1 3336 LYS 3336 3336 ?    ?   ?   A . n 
A 1 3337 GLN 3337 3337 ?    ?   ?   A . n 
A 1 3338 ILE 3338 3338 ?    ?   ?   A . n 
A 1 3339 ARG 3339 3339 ?    ?   ?   A . n 
A 1 3340 SER 3340 3340 ?    ?   ?   A . n 
A 1 3341 ILE 3341 3341 ?    ?   ?   A . n 
A 1 3342 ILE 3342 3342 ?    ?   ?   A . n 
A 1 3343 MET 3343 3343 ?    ?   ?   A . n 
A 1 3344 ARG 3344 3344 ?    ?   ?   A . n 
A 1 3345 GLU 3345 3345 ?    ?   ?   A . n 
A 1 3346 ASN 3346 3346 ?    ?   ?   A . n 
A 1 3347 PHE 3347 3347 ?    ?   ?   A . n 
A 1 3348 ILE 3348 3348 ?    ?   ?   A . n 
A 1 3349 PRO 3349 3349 ?    ?   ?   A . n 
A 1 3350 THR 3350 3350 ?    ?   ?   A . n 
A 1 3351 ILE 3351 3351 ?    ?   ?   A . n 
A 1 3352 VAL 3352 3352 ?    ?   ?   A . n 
A 1 3353 ASN 3353 3353 ?    ?   ?   A . n 
A 1 3354 PHE 3354 3354 ?    ?   ?   A . n 
A 1 3355 SER 3355 3355 ?    ?   ?   A . n 
A 1 3356 ALA 3356 3356 ?    ?   ?   A . n 
A 1 3357 GLU 3357 3357 ?    ?   ?   A . n 
A 1 3358 GLU 3358 3358 ?    ?   ?   A . n 
A 1 3359 ILE 3359 3359 ?    ?   ?   A . n 
A 1 3360 SER 3360 3360 ?    ?   ?   A . n 
A 1 3361 ASP 3361 3361 ?    ?   ?   A . n 
A 1 3362 ALA 3362 3362 ?    ?   ?   A . n 
A 1 3363 ILE 3363 3363 ?    ?   ?   A . n 
A 1 3364 ARG 3364 3364 ?    ?   ?   A . n 
A 1 3365 GLU 3365 3365 ?    ?   ?   A . n 
A 1 3366 LYS 3366 3366 ?    ?   ?   A . n 
A 1 3367 MET 3367 3367 ?    ?   ?   A . n 
A 1 3368 LYS 3368 3368 ?    ?   ?   A . n 
A 1 3369 LYS 3369 3369 ?    ?   ?   A . n 
A 1 3370 ASN 3370 3370 ?    ?   ?   A . n 
A 1 3371 TYR 3371 3371 ?    ?   ?   A . n 
A 1 3372 MET 3372 3372 ?    ?   ?   A . n 
A 1 3373 SER 3373 3373 ?    ?   ?   A . n 
A 1 3374 ASN 3374 3374 ?    ?   ?   A . n 
A 1 3375 PRO 3375 3375 ?    ?   ?   A . n 
A 1 3376 SER 3376 3376 ?    ?   ?   A . n 
A 1 3377 TYR 3377 3377 ?    ?   ?   A . n 
A 1 3378 ASN 3378 3378 ?    ?   ?   A . n 
A 1 3379 TYR 3379 3379 ?    ?   ?   A . n 
A 1 3380 GLU 3380 3380 ?    ?   ?   A . n 
A 1 3381 ILE 3381 3381 ?    ?   ?   A . n 
A 1 3382 VAL 3382 3382 ?    ?   ?   A . n 
A 1 3383 ASN 3383 3383 ?    ?   ?   A . n 
A 1 3384 ARG 3384 3384 ?    ?   ?   A . n 
A 1 3385 ALA 3385 3385 ?    ?   ?   A . n 
A 1 3386 SER 3386 3386 ?    ?   ?   A . n 
A 1 3387 LEU 3387 3387 ?    ?   ?   A . n 
A 1 3388 ALA 3388 3388 ?    ?   ?   A . n 
A 1 3389 CYS 3389 3389 ?    ?   ?   A . n 
A 1 3390 GLY 3390 3390 ?    ?   ?   A . n 
A 1 3391 PRO 3391 3391 ?    ?   ?   A . n 
A 1 3392 MET 3392 3392 ?    ?   ?   A . n 
A 1 3393 VAL 3393 3393 ?    ?   ?   A . n 
A 1 3394 LYS 3394 3394 ?    ?   ?   A . n 
A 1 3395 TRP 3395 3395 ?    ?   ?   A . n 
A 1 3396 ALA 3396 3396 ?    ?   ?   A . n 
A 1 3397 ILE 3397 3397 ?    ?   ?   A . n 
A 1 3398 ALA 3398 3398 ?    ?   ?   A . n 
A 1 3399 GLN 3399 3399 ?    ?   ?   A . n 
A 1 3400 LEU 3400 3400 ?    ?   ?   A . n 
A 1 3401 ASN 3401 3401 ?    ?   ?   A . n 
A 1 3402 TYR 3402 3402 ?    ?   ?   A . n 
A 1 3403 ALA 3403 3403 ?    ?   ?   A . n 
A 1 3404 ASP 3404 3404 ?    ?   ?   A . n 
A 1 3405 MET 3405 3405 ?    ?   ?   A . n 
A 1 3406 LEU 3406 3406 ?    ?   ?   A . n 
A 1 3407 LYS 3407 3407 ?    ?   ?   A . n 
A 1 3408 ARG 3408 3408 ?    ?   ?   A . n 
A 1 3409 VAL 3409 3409 ?    ?   ?   A . n 
A 1 3410 GLU 3410 3410 ?    ?   ?   A . n 
A 1 3411 PRO 3411 3411 ?    ?   ?   A . n 
A 1 3412 LEU 3412 3412 ?    ?   ?   A . n 
A 1 3413 ARG 3413 3413 ?    ?   ?   A . n 
A 1 3414 ASN 3414 3414 ?    ?   ?   A . n 
A 1 3415 GLU 3415 3415 ?    ?   ?   A . n 
A 1 3416 LEU 3416 3416 ?    ?   ?   A . n 
A 1 3417 GLN 3417 3417 ?    ?   ?   A . n 
A 1 3418 LYS 3418 3418 ?    ?   ?   A . n 
A 1 3419 LEU 3419 3419 ?    ?   ?   A . n 
A 1 3420 GLU 3420 3420 ?    ?   ?   A . n 
A 1 3421 ASP 3421 3421 ?    ?   ?   A . n 
A 1 3422 ASP 3422 3422 ?    ?   ?   A . n 
A 1 3423 ALA 3423 3423 ?    ?   ?   A . n 
A 1 3424 LYS 3424 3424 ?    ?   ?   A . n 
A 1 3425 ASP 3425 3425 ?    ?   ?   A . n 
A 1 3426 ASN 3426 3426 ?    ?   ?   A . n 
A 1 3427 GLN 3427 3427 ?    ?   ?   A . n 
A 1 3428 GLN 3428 3428 ?    ?   ?   A . n 
A 1 3429 LYS 3429 3429 ?    ?   ?   A . n 
A 1 3430 ALA 3430 3430 ?    ?   ?   A . n 
A 1 3431 ASN 3431 3431 ?    ?   ?   A . n 
A 1 3432 GLU 3432 3432 ?    ?   ?   A . n 
A 1 3433 VAL 3433 3433 ?    ?   ?   A . n 
A 1 3434 GLU 3434 3434 ?    ?   ?   A . n 
A 1 3435 GLN 3435 3435 ?    ?   ?   A . n 
A 1 3436 MET 3436 3436 ?    ?   ?   A . n 
A 1 3437 ILE 3437 3437 ?    ?   ?   A . n 
A 1 3438 ARG 3438 3438 ?    ?   ?   A . n 
A 1 3439 ASP 3439 3439 ?    ?   ?   A . n 
A 1 3440 LEU 3440 3440 ?    ?   ?   A . n 
A 1 3441 GLU 3441 3441 ?    ?   ?   A . n 
A 1 3442 ALA 3442 3442 ?    ?   ?   A . n 
A 1 3443 SER 3443 3443 ?    ?   ?   A . n 
A 1 3444 ILE 3444 3444 ?    ?   ?   A . n 
A 1 3445 ALA 3445 3445 ?    ?   ?   A . n 
A 1 3446 ARG 3446 3446 ?    ?   ?   A . n 
A 1 3447 TYR 3447 3447 ?    ?   ?   A . n 
A 1 3448 LYS 3448 3448 ?    ?   ?   A . n 
A 1 3449 GLU 3449 3449 3449 GLU GLU A . n 
A 1 3450 GLU 3450 3450 3450 GLU GLU A . n 
A 1 3451 TYR 3451 3451 3451 TYR TYR A . n 
A 1 3452 ALA 3452 3452 3452 ALA ALA A . n 
A 1 3453 VAL 3453 3453 3453 VAL VAL A . n 
A 1 3454 LEU 3454 3454 3454 LEU LEU A . n 
A 1 3455 ILE 3455 3455 3455 ILE ILE A . n 
A 1 3456 SER 3456 3456 3456 SER SER A . n 
A 1 3457 GLU 3457 3457 3457 GLU GLU A . n 
A 1 3458 ALA 3458 3458 3458 ALA ALA A . n 
A 1 3459 GLN 3459 3459 3459 GLN GLN A . n 
A 1 3460 ALA 3460 3460 3460 ALA ALA A . n 
A 1 3461 ILE 3461 3461 3461 ILE ILE A . n 
A 1 3462 LYS 3462 3462 3462 LYS LYS A . n 
A 1 3463 ALA 3463 3463 3463 ALA ALA A . n 
A 1 3464 ASP 3464 3464 3464 ASP ASP A . n 
A 1 3465 LEU 3465 3465 3465 LEU LEU A . n 
A 1 3466 ALA 3466 3466 3466 ALA ALA A . n 
A 1 3467 ALA 3467 3467 3467 ALA ALA A . n 
A 1 3468 VAL 3468 3468 3468 VAL VAL A . n 
A 1 3469 GLU 3469 3469 3469 GLU GLU A . n 
A 1 3470 ALA 3470 3470 3470 ALA ALA A . n 
A 1 3471 LYS 3471 3471 3471 LYS LYS A . n 
A 1 3472 VAL 3472 3472 3472 VAL VAL A . n 
A 1 3473 ASN 3473 3473 3473 ASN ASN A . n 
A 1 3474 ARG 3474 3474 3474 ARG ARG A . n 
A 1 3475 SER 3475 3475 3475 SER SER A . n 
A 1 3476 THR 3476 3476 3476 THR THR A . n 
A 1 3477 ALA 3477 3477 3477 ALA ALA A . n 
A 1 3478 LEU 3478 3478 3478 LEU LEU A . n 
A 1 3479 LEU 3479 3479 3479 LEU LEU A . n 
A 1 3480 LYS 3480 3480 3480 LYS LYS A . n 
A 1 3481 SER 3481 3481 3481 SER SER A . n 
A 1 3482 LEU 3482 3482 3482 LEU LEU A . n 
A 1 3483 SER 3483 3483 3483 SER SER A . n 
A 1 3484 ALA 3484 3484 3484 ALA ALA A . n 
A 1 3485 GLU 3485 3485 3485 GLU GLU A . n 
A 1 3486 ARG 3486 3486 3486 ARG ARG A . n 
A 1 3487 GLU 3487 3487 3487 GLU GLU A . n 
A 1 3488 ARG 3488 3488 3488 ARG ARG A . n 
A 1 3489 TRP 3489 3489 3489 TRP TRP A . n 
A 1 3490 GLU 3490 3490 3490 GLU GLU A . n 
A 1 3491 LYS 3491 3491 3491 LYS LYS A . n 
A 1 3492 THR 3492 3492 3492 THR THR A . n 
A 1 3493 SER 3493 3493 3493 SER SER A . n 
A 1 3494 GLU 3494 3494 3494 GLU GLU A . n 
A 1 3495 THR 3495 3495 3495 THR THR A . n 
A 1 3496 PHE 3496 3496 3496 PHE PHE A . n 
A 1 3497 LYS 3497 3497 3497 LYS LYS A . n 
A 1 3498 ASN 3498 3498 3498 ASN ASN A . n 
A 1 3499 GLN 3499 3499 3499 GLN GLN A . n 
A 1 3500 MET 3500 3500 3500 MET MET A . n 
A 1 3501 SER 3501 3501 3501 SER SER A . n 
A 1 3502 THR 3502 3502 3502 THR THR A . n 
A 1 3503 ILE 3503 3503 3503 ILE ILE A . n 
A 1 3504 ALA 3504 3504 3504 ALA ALA A . n 
A 1 3505 GLY 3505 3505 3505 GLY GLY A . n 
A 1 3506 ASP 3506 3506 3506 ASP ASP A . n 
A 1 3507 CYS 3507 3507 3507 CYS CYS A . n 
A 1 3508 LEU 3508 3508 3508 LEU LEU A . n 
A 1 3509 LEU 3509 3509 3509 LEU LEU A . n 
A 1 3510 SER 3510 3510 3510 SER SER A . n 
A 1 3511 ALA 3511 3511 3511 ALA ALA A . n 
A 1 3512 ALA 3512 3512 3512 ALA ALA A . n 
A 1 3513 PHE 3513 3513 3513 PHE PHE A . n 
A 1 3514 ILE 3514 3514 3514 ILE ILE A . n 
A 1 3515 ALA 3515 3515 3515 ALA ALA A . n 
A 1 3516 TYR 3516 3516 3516 TYR TYR A . n 
A 1 3517 ALA 3517 3517 3517 ALA ALA A . n 
A 1 3518 GLY 3518 3518 3518 GLY GLY A . n 
A 1 3519 TYR 3519 3519 3519 TYR TYR A . n 
A 1 3520 PHE 3520 3520 3520 PHE PHE A . n 
A 1 3521 ASP 3521 3521 3521 ASP ASP A . n 
A 1 3522 GLN 3522 3522 3522 GLN GLN A . n 
A 1 3523 GLN 3523 3523 3523 GLN GLN A . n 
A 1 3524 MET 3524 3524 3524 MET MET A . n 
A 1 3525 ARG 3525 3525 3525 ARG ARG A . n 
A 1 3526 GLN 3526 3526 3526 GLN GLN A . n 
A 1 3527 ASN 3527 3527 3527 ASN ASN A . n 
A 1 3528 LEU 3528 3528 3528 LEU LEU A . n 
A 1 3529 PHE 3529 3529 3529 PHE PHE A . n 
A 1 3530 THR 3530 3530 3530 THR THR A . n 
A 1 3531 THR 3531 3531 3531 THR THR A . n 
A 1 3532 TRP 3532 3532 3532 TRP TRP A . n 
A 1 3533 SER 3533 3533 3533 SER SER A . n 
A 1 3534 HIS 3534 3534 3534 HIS HIS A . n 
A 1 3535 HIS 3535 3535 3535 HIS HIS A . n 
A 1 3536 LEU 3536 3536 3536 LEU LEU A . n 
A 1 3537 GLN 3537 3537 3537 GLN GLN A . n 
A 1 3538 GLN 3538 3538 3538 GLN GLN A . n 
A 1 3539 ALA 3539 3539 3539 ALA ALA A . n 
A 1 3540 ASN 3540 3540 3540 ASN ASN A . n 
A 1 3541 ILE 3541 3541 3541 ILE ILE A . n 
A 1 3542 GLN 3542 3542 3542 GLN GLN A . n 
A 1 3543 PHE 3543 3543 3543 PHE PHE A . n 
A 1 3544 ARG 3544 3544 3544 ARG ARG A . n 
A 1 3545 THR 3545 3545 3545 THR THR A . n 
A 1 3546 ASP 3546 3546 3546 ASP ASP A . n 
A 1 3547 ILE 3547 3547 3547 ILE ILE A . n 
A 1 3548 ALA 3548 3548 3548 ALA ALA A . n 
A 1 3549 ARG 3549 3549 3549 ARG ARG A . n 
A 1 3550 THR 3550 3550 3550 THR THR A . n 
A 1 3551 GLU 3551 3551 3551 GLU GLU A . n 
A 1 3552 TYR 3552 3552 3552 TYR TYR A . n 
A 1 3553 LEU 3553 3553 3553 LEU LEU A . n 
A 1 3554 SER 3554 3554 3554 SER SER A . n 
A 1 3555 ASN 3555 3555 3555 ASN ASN A . n 
A 1 3556 ALA 3556 3556 3556 ALA ALA A . n 
A 1 3557 ASP 3557 3557 3557 ASP ASP A . n 
A 1 3558 GLU 3558 3558 3558 GLU GLU A . n 
A 1 3559 ARG 3559 3559 3559 ARG ARG A . n 
A 1 3560 LEU 3560 3560 3560 LEU LEU A . n 
A 1 3561 ARG 3561 3561 3561 ARG ARG A . n 
A 1 3562 TRP 3562 3562 3562 TRP TRP A . n 
A 1 3563 GLN 3563 3563 3563 GLN GLN A . n 
A 1 3564 ALA 3564 3564 3564 ALA ALA A . n 
A 1 3565 SER 3565 3565 3565 SER SER A . n 
A 1 3566 SER 3566 3566 3566 SER SER A . n 
A 1 3567 LEU 3567 3567 3567 LEU LEU A . n 
A 1 3568 PRO 3568 3568 3568 PRO PRO A . n 
A 1 3569 ALA 3569 3569 3569 ALA ALA A . n 
A 1 3570 ASP 3570 3570 3570 ASP ASP A . n 
A 1 3571 ASP 3571 3571 3571 ASP ASP A . n 
A 1 3572 LEU 3572 3572 3572 LEU LEU A . n 
A 1 3573 CYS 3573 3573 3573 CYS CYS A . n 
A 1 3574 THR 3574 3574 3574 THR THR A . n 
A 1 3575 GLU 3575 3575 3575 GLU GLU A . n 
A 1 3576 ASN 3576 3576 3576 ASN ASN A . n 
A 1 3577 ALA 3577 3577 3577 ALA ALA A . n 
A 1 3578 ILE 3578 3578 3578 ILE ILE A . n 
A 1 3579 MET 3579 3579 3579 MET MET A . n 
A 1 3580 LEU 3580 3580 3580 LEU LEU A . n 
A 1 3581 LYS 3581 3581 3581 LYS LYS A . n 
A 1 3582 ARG 3582 3582 3582 ARG ARG A . n 
A 1 3583 PHE 3583 3583 3583 PHE PHE A . n 
A 1 3584 ASN 3584 3584 3584 ASN ASN A . n 
A 1 3585 ARG 3585 3585 3585 ARG ARG A . n 
A 1 3586 TYR 3586 3586 3586 TYR TYR A . n 
A 1 3587 PRO 3587 3587 3587 PRO PRO A . n 
A 1 3588 LEU 3588 3588 3588 LEU LEU A . n 
A 1 3589 ILE 3589 3589 3589 ILE ILE A . n 
A 1 3590 ILE 3590 3590 3590 ILE ILE A . n 
A 1 3591 ASP 3591 3591 3591 ASP ASP A . n 
A 1 3592 PRO 3592 3592 3592 PRO PRO A . n 
A 1 3593 SER 3593 3593 3593 SER SER A . n 
A 1 3594 GLY 3594 3594 3594 GLY GLY A . n 
A 1 3595 GLN 3595 3595 3595 GLN GLN A . n 
A 1 3596 ALA 3596 3596 3596 ALA ALA A . n 
A 1 3597 THR 3597 3597 3597 THR THR A . n 
A 1 3598 GLU 3598 3598 3598 GLU GLU A . n 
A 1 3599 PHE 3599 3599 3599 PHE PHE A . n 
A 1 3600 ILE 3600 3600 3600 ILE ILE A . n 
A 1 3601 MET 3601 3601 3601 MET MET A . n 
A 1 3602 ASN 3602 3602 3602 ASN ASN A . n 
A 1 3603 GLU 3603 3603 3603 GLU GLU A . n 
A 1 3604 TYR 3604 3604 3604 TYR TYR A . n 
A 1 3605 LYS 3605 3605 3605 LYS LYS A . n 
A 1 3606 ASP 3606 3606 3606 ASP ASP A . n 
A 1 3607 ARG 3607 3607 3607 ARG ARG A . n 
A 1 3608 LYS 3608 3608 3608 LYS LYS A . n 
A 1 3609 ILE 3609 3609 3609 ILE ILE A . n 
A 1 3610 THR 3610 3610 3610 THR THR A . n 
A 1 3611 ARG 3611 3611 3611 ARG ARG A . n 
A 1 3612 THR 3612 3612 3612 THR THR A . n 
A 1 3613 SER 3613 3613 3613 SER SER A . n 
A 1 3614 PHE 3614 3614 3614 PHE PHE A . n 
A 1 3615 LEU 3615 3615 3615 LEU LEU A . n 
A 1 3616 ASP 3616 3616 3616 ASP ASP A . n 
A 1 3617 ASP 3617 3617 3617 ASP ASP A . n 
A 1 3618 ALA 3618 3618 3618 ALA ALA A . n 
A 1 3619 PHE 3619 3619 3619 PHE PHE A . n 
A 1 3620 ARG 3620 3620 3620 ARG ARG A . n 
A 1 3621 LYS 3621 3621 3621 LYS LYS A . n 
A 1 3622 ASN 3622 3622 3622 ASN ASN A . n 
A 1 3623 LEU 3623 3623 3623 LEU LEU A . n 
A 1 3624 GLU 3624 3624 3624 GLU GLU A . n 
A 1 3625 SER 3625 3625 3625 SER SER A . n 
A 1 3626 ALA 3626 3626 3626 ALA ALA A . n 
A 1 3627 LEU 3627 3627 3627 LEU LEU A . n 
A 1 3628 ARG 3628 3628 3628 ARG ARG A . n 
A 1 3629 PHE 3629 3629 3629 PHE PHE A . n 
A 1 3630 GLY 3630 3630 3630 GLY GLY A . n 
A 1 3631 ASN 3631 3631 3631 ASN ASN A . n 
A 1 3632 PRO 3632 3632 3632 PRO PRO A . n 
A 1 3633 LEU 3633 3633 3633 LEU LEU A . n 
A 1 3634 LEU 3634 3634 3634 LEU LEU A . n 
A 1 3635 VAL 3635 3635 3635 VAL VAL A . n 
A 1 3636 GLN 3636 3636 3636 GLN GLN A . n 
A 1 3637 ASP 3637 3637 3637 ASP ASP A . n 
A 1 3638 VAL 3638 3638 3638 VAL VAL A . n 
A 1 3639 GLU 3639 3639 3639 GLU GLU A . n 
A 1 3640 SER 3640 3640 3640 SER SER A . n 
A 1 3641 TYR 3641 3641 3641 TYR TYR A . n 
A 1 3642 ASP 3642 3642 3642 ASP ASP A . n 
A 1 3643 PRO 3643 3643 3643 PRO PRO A . n 
A 1 3644 VAL 3644 3644 3644 VAL VAL A . n 
A 1 3645 LEU 3645 3645 3645 LEU LEU A . n 
A 1 3646 ASN 3646 3646 3646 ASN ASN A . n 
A 1 3647 PRO 3647 3647 3647 PRO PRO A . n 
A 1 3648 VAL 3648 3648 3648 VAL VAL A . n 
A 1 3649 LEU 3649 3649 3649 LEU LEU A . n 
A 1 3650 ASN 3650 3650 3650 ASN ASN A . n 
A 1 3651 ARG 3651 3651 3651 ARG ARG A . n 
A 1 3652 GLU 3652 3652 3652 GLU GLU A . n 
A 1 3653 VAL 3653 3653 3653 VAL VAL A . n 
A 1 3654 ARG 3654 3654 3654 ARG ARG A . n 
A 1 3655 ARG 3655 3655 3655 ARG ARG A . n 
A 1 3656 THR 3656 3656 3656 THR THR A . n 
A 1 3657 GLY 3657 3657 3657 GLY GLY A . n 
A 1 3658 GLY 3658 3658 3658 GLY GLY A . n 
A 1 3659 ARG 3659 3659 3659 ARG ARG A . n 
A 1 3660 VAL 3660 3660 3660 VAL VAL A . n 
A 1 3661 LEU 3661 3661 3661 LEU LEU A . n 
A 1 3662 ILE 3662 3662 3662 ILE ILE A . n 
A 1 3663 THR 3663 3663 3663 THR THR A . n 
A 1 3664 LEU 3664 3664 3664 LEU LEU A . n 
A 1 3665 GLY 3665 3665 3665 GLY GLY A . n 
A 1 3666 ASP 3666 3666 3666 ASP ASP A . n 
A 1 3667 GLN 3667 3667 3667 GLN GLN A . n 
A 1 3668 ASP 3668 3668 3668 ASP ASP A . n 
A 1 3669 ILE 3669 3669 3669 ILE ILE A . n 
A 1 3670 ASP 3670 3670 3670 ASP ASP A . n 
A 1 3671 LEU 3671 3671 3671 LEU LEU A . n 
A 1 3672 SER 3672 3672 3672 SER SER A . n 
A 1 3673 PRO 3673 3673 3673 PRO PRO A . n 
A 1 3674 SER 3674 3674 3674 SER SER A . n 
A 1 3675 PHE 3675 3675 3675 PHE PHE A . n 
A 1 3676 VAL 3676 3676 3676 VAL VAL A . n 
A 1 3677 ILE 3677 3677 3677 ILE ILE A . n 
A 1 3678 PHE 3678 3678 3678 PHE PHE A . n 
A 1 3679 LEU 3679 3679 3679 LEU LEU A . n 
A 1 3680 SER 3680 3680 3680 SER SER A . n 
A 1 3681 THR 3681 3681 3681 THR THR A . n 
A 1 3682 ARG 3682 3682 3682 ARG ARG A . n 
A 1 3683 ASP 3683 3683 3683 ASP ASP A . n 
A 1 3684 PRO 3684 3684 3684 PRO PRO A . n 
A 1 3685 THR 3685 3685 3685 THR THR A . n 
A 1 3686 VAL 3686 3686 3686 VAL VAL A . n 
A 1 3687 GLU 3687 3687 3687 GLU GLU A . n 
A 1 3688 PHE 3688 3688 3688 PHE PHE A . n 
A 1 3689 PRO 3689 3689 3689 PRO PRO A . n 
A 1 3690 PRO 3690 3690 3690 PRO PRO A . n 
A 1 3691 ASP 3691 3691 3691 ASP ASP A . n 
A 1 3692 LEU 3692 3692 3692 LEU LEU A . n 
A 1 3693 CYS 3693 3693 3693 CYS CYS A . n 
A 1 3694 SER 3694 3694 3694 SER SER A . n 
A 1 3695 ARG 3695 3695 3695 ARG ARG A . n 
A 1 3696 VAL 3696 3696 3696 VAL VAL A . n 
A 1 3697 THR 3697 3697 3697 THR THR A . n 
A 1 3698 PHE 3698 3698 3698 PHE PHE A . n 
A 1 3699 VAL 3699 3699 3699 VAL VAL A . n 
A 1 3700 ASN 3700 3700 3700 ASN ASN A . n 
A 1 3701 PHE 3701 3701 3701 PHE PHE A . n 
A 1 3702 THR 3702 3702 3702 THR THR A . n 
A 1 3703 VAL 3703 3703 3703 VAL VAL A . n 
A 1 3704 THR 3704 3704 3704 THR THR A . n 
A 1 3705 ARG 3705 3705 3705 ARG ARG A . n 
A 1 3706 SER 3706 3706 3706 SER SER A . n 
A 1 3707 SER 3707 3707 3707 SER SER A . n 
A 1 3708 LEU 3708 3708 3708 LEU LEU A . n 
A 1 3709 GLN 3709 3709 3709 GLN GLN A . n 
A 1 3710 SER 3710 3710 3710 SER SER A . n 
A 1 3711 GLN 3711 3711 3711 GLN GLN A . n 
A 1 3712 CYS 3712 3712 3712 CYS CYS A . n 
A 1 3713 LEU 3713 3713 3713 LEU LEU A . n 
A 1 3714 ASN 3714 3714 3714 ASN ASN A . n 
A 1 3715 GLU 3715 3715 3715 GLU GLU A . n 
A 1 3716 VAL 3716 3716 3716 VAL VAL A . n 
A 1 3717 LEU 3717 3717 3717 LEU LEU A . n 
A 1 3718 LYS 3718 3718 3718 LYS LYS A . n 
A 1 3719 ALA 3719 3719 3719 ALA ALA A . n 
A 1 3720 GLU 3720 3720 3720 GLU GLU A . n 
A 1 3721 ARG 3721 3721 3721 ARG ARG A . n 
A 1 3722 PRO 3722 3722 3722 PRO PRO A . n 
A 1 3723 ASP 3723 3723 3723 ASP ASP A . n 
A 1 3724 VAL 3724 3724 3724 VAL VAL A . n 
A 1 3725 ASP 3725 3725 3725 ASP ASP A . n 
A 1 3726 GLU 3726 3726 3726 GLU GLU A . n 
A 1 3727 LYS 3727 3727 3727 LYS LYS A . n 
A 1 3728 ARG 3728 3728 3728 ARG ARG A . n 
A 1 3729 SER 3729 3729 3729 SER SER A . n 
A 1 3730 ASP 3730 3730 3730 ASP ASP A . n 
A 1 3731 LEU 3731 3731 3731 LEU LEU A . n 
A 1 3732 LEU 3732 3732 3732 LEU LEU A . n 
A 1 3733 LYS 3733 3733 3733 LYS LYS A . n 
A 1 3734 LEU 3734 3734 3734 LEU LEU A . n 
A 1 3735 GLN 3735 3735 3735 GLN GLN A . n 
A 1 3736 GLY 3736 3736 3736 GLY GLY A . n 
A 1 3737 GLU 3737 3737 3737 GLU GLU A . n 
A 1 3738 PHE 3738 3738 3738 PHE PHE A . n 
A 1 3739 GLN 3739 3739 3739 GLN GLN A . n 
A 1 3740 LEU 3740 3740 3740 LEU LEU A . n 
A 1 3741 ARG 3741 3741 3741 ARG ARG A . n 
A 1 3742 LEU 3742 3742 3742 LEU LEU A . n 
A 1 3743 ARG 3743 3743 3743 ARG ARG A . n 
A 1 3744 GLN 3744 3744 3744 GLN GLN A . n 
A 1 3745 LEU 3745 3745 3745 LEU LEU A . n 
A 1 3746 GLU 3746 3746 3746 GLU GLU A . n 
A 1 3747 LYS 3747 3747 3747 LYS LYS A . n 
A 1 3748 SER 3748 3748 3748 SER SER A . n 
A 1 3749 LEU 3749 3749 3749 LEU LEU A . n 
A 1 3750 LEU 3750 3750 3750 LEU LEU A . n 
A 1 3751 GLN 3751 3751 3751 GLN GLN A . n 
A 1 3752 ALA 3752 3752 3752 ALA ALA A . n 
A 1 3753 LEU 3753 3753 3753 LEU LEU A . n 
A 1 3754 ASN 3754 3754 3754 ASN ASN A . n 
A 1 3755 GLU 3755 3755 3755 GLU GLU A . n 
A 1 3756 VAL 3756 3756 3756 VAL VAL A . n 
A 1 3757 LYS 3757 3757 3757 LYS LYS A . n 
A 1 3758 GLY 3758 3758 3758 GLY GLY A . n 
A 1 3759 ARG 3759 3759 3759 ARG ARG A . n 
A 1 3760 ILE 3760 3760 3760 ILE ILE A . n 
A 1 3761 LEU 3761 3761 3761 LEU LEU A . n 
A 1 3762 ASP 3762 3762 3762 ASP ASP A . n 
A 1 3763 ASP 3763 3763 3763 ASP ASP A . n 
A 1 3764 ASP 3764 3764 3764 ASP ASP A . n 
A 1 3765 THR 3765 3765 3765 THR THR A . n 
A 1 3766 ILE 3766 3766 3766 ILE ILE A . n 
A 1 3767 ILE 3767 3767 3767 ILE ILE A . n 
A 1 3768 THR 3768 3768 3768 THR THR A . n 
A 1 3769 THR 3769 3769 3769 THR THR A . n 
A 1 3770 LEU 3770 3770 3770 LEU LEU A . n 
A 1 3771 GLU 3771 3771 3771 GLU GLU A . n 
A 1 3772 ASN 3772 3772 3772 ASN ASN A . n 
A 1 3773 LEU 3773 3773 3773 LEU LEU A . n 
A 1 3774 LYS 3774 3774 3774 LYS LYS A . n 
A 1 3775 ARG 3775 3775 3775 ARG ARG A . n 
A 1 3776 GLU 3776 3776 3776 GLU GLU A . n 
A 1 3777 ALA 3777 3777 3777 ALA ALA A . n 
A 1 3778 ALA 3778 3778 3778 ALA ALA A . n 
A 1 3779 GLU 3779 3779 3779 GLU GLU A . n 
A 1 3780 VAL 3780 3780 3780 VAL VAL A . n 
A 1 3781 THR 3781 3781 3781 THR THR A . n 
A 1 3782 ARG 3782 3782 3782 ARG ARG A . n 
A 1 3783 LYS 3783 3783 3783 LYS LYS A . n 
A 1 3784 VAL 3784 3784 3784 VAL VAL A . n 
A 1 3785 GLU 3785 3785 3785 GLU GLU A . n 
A 1 3786 GLU 3786 3786 3786 GLU GLU A . n 
A 1 3787 THR 3787 3787 3787 THR THR A . n 
A 1 3788 ASP 3788 3788 3788 ASP ASP A . n 
A 1 3789 ILE 3789 3789 3789 ILE ILE A . n 
A 1 3790 VAL 3790 3790 3790 VAL VAL A . n 
A 1 3791 MET 3791 3791 3791 MET MET A . n 
A 1 3792 GLN 3792 3792 3792 GLN GLN A . n 
A 1 3793 GLU 3793 3793 3793 GLU GLU A . n 
A 1 3794 VAL 3794 3794 3794 VAL VAL A . n 
A 1 3795 GLU 3795 3795 3795 GLU GLU A . n 
A 1 3796 THR 3796 3796 3796 THR THR A . n 
A 1 3797 VAL 3797 3797 3797 VAL VAL A . n 
A 1 3798 SER 3798 3798 3798 SER SER A . n 
A 1 3799 GLN 3799 3799 3799 GLN GLN A . n 
A 1 3800 GLN 3800 3800 3800 GLN GLN A . n 
A 1 3801 TYR 3801 3801 3801 TYR TYR A . n 
A 1 3802 LEU 3802 3802 3802 LEU LEU A . n 
A 1 3803 PRO 3803 3803 3803 PRO PRO A . n 
A 1 3804 LEU 3804 3804 3804 LEU LEU A . n 
A 1 3805 SER 3805 3805 3805 SER SER A . n 
A 1 3806 THR 3806 3806 3806 THR THR A . n 
A 1 3807 ALA 3807 3807 3807 ALA ALA A . n 
A 1 3808 CYS 3808 3808 3808 CYS CYS A . n 
A 1 3809 SER 3809 3809 3809 SER SER A . n 
A 1 3810 SER 3810 3810 3810 SER SER A . n 
A 1 3811 ILE 3811 3811 3811 ILE ILE A . n 
A 1 3812 TYR 3812 3812 3812 TYR TYR A . n 
A 1 3813 PHE 3813 3813 3813 PHE PHE A . n 
A 1 3814 THR 3814 3814 3814 THR THR A . n 
A 1 3815 MET 3815 3815 3815 MET MET A . n 
A 1 3816 GLU 3816 3816 3816 GLU GLU A . n 
A 1 3817 SER 3817 3817 3817 SER SER A . n 
A 1 3818 LEU 3818 3818 3818 LEU LEU A . n 
A 1 3819 LYS 3819 3819 3819 LYS LYS A . n 
A 1 3820 GLN 3820 3820 3820 GLN GLN A . n 
A 1 3821 ILE 3821 3821 3821 ILE ILE A . n 
A 1 3822 HIS 3822 3822 3822 HIS HIS A . n 
A 1 3823 PHE 3823 3823 3823 PHE PHE A . n 
A 1 3824 LEU 3824 3824 3824 LEU LEU A . n 
A 1 3825 TYR 3825 3825 3825 TYR TYR A . n 
A 1 3826 GLN 3826 3826 3826 GLN GLN A . n 
A 1 3827 TYR 3827 3827 3827 TYR TYR A . n 
A 1 3828 SER 3828 3828 3828 SER SER A . n 
A 1 3829 LEU 3829 3829 3829 LEU LEU A . n 
A 1 3830 GLN 3830 3830 3830 GLN GLN A . n 
A 1 3831 PHE 3831 3831 3831 PHE PHE A . n 
A 1 3832 PHE 3832 3832 3832 PHE PHE A . n 
A 1 3833 LEU 3833 3833 3833 LEU LEU A . n 
A 1 3834 ASP 3834 3834 3834 ASP ASP A . n 
A 1 3835 ILE 3835 3835 3835 ILE ILE A . n 
A 1 3836 TYR 3836 3836 3836 TYR TYR A . n 
A 1 3837 HIS 3837 3837 3837 HIS HIS A . n 
A 1 3838 ASN 3838 3838 3838 ASN ASN A . n 
A 1 3839 VAL 3839 3839 3839 VAL VAL A . n 
A 1 3840 LEU 3840 3840 3840 LEU LEU A . n 
A 1 3841 TYR 3841 3841 3841 TYR TYR A . n 
A 1 3842 GLU 3842 3842 3842 GLU GLU A . n 
A 1 3843 ASN 3843 3843 3843 ASN ASN A . n 
A 1 3844 PRO 3844 3844 3844 PRO PRO A . n 
A 1 3845 ASN 3845 3845 3845 ASN ASN A . n 
A 1 3846 LEU 3846 3846 3846 LEU LEU A . n 
A 1 3847 LYS 3847 3847 3847 LYS LYS A . n 
A 1 3848 GLY 3848 3848 3848 GLY GLY A . n 
A 1 3849 VAL 3849 3849 3849 VAL VAL A . n 
A 1 3850 THR 3850 3850 3850 THR THR A . n 
A 1 3851 ASP 3851 3851 3851 ASP ASP A . n 
A 1 3852 HIS 3852 3852 3852 HIS HIS A . n 
A 1 3853 THR 3853 3853 3853 THR THR A . n 
A 1 3854 GLN 3854 3854 3854 GLN GLN A . n 
A 1 3855 ARG 3855 3855 3855 ARG ARG A . n 
A 1 3856 LEU 3856 3856 3856 LEU LEU A . n 
A 1 3857 SER 3857 3857 3857 SER SER A . n 
A 1 3858 ILE 3858 3858 3858 ILE ILE A . n 
A 1 3859 ILE 3859 3859 3859 ILE ILE A . n 
A 1 3860 THR 3860 3860 3860 THR THR A . n 
A 1 3861 LYS 3861 3861 3861 LYS LYS A . n 
A 1 3862 ASP 3862 3862 3862 ASP ASP A . n 
A 1 3863 LEU 3863 3863 3863 LEU LEU A . n 
A 1 3864 PHE 3864 3864 3864 PHE PHE A . n 
A 1 3865 GLN 3865 3865 3865 GLN GLN A . n 
A 1 3866 VAL 3866 3866 3866 VAL VAL A . n 
A 1 3867 ALA 3867 3867 3867 ALA ALA A . n 
A 1 3868 PHE 3868 3868 3868 PHE PHE A . n 
A 1 3869 ASN 3869 3869 3869 ASN ASN A . n 
A 1 3870 ARG 3870 3870 3870 ARG ARG A . n 
A 1 3871 VAL 3871 3871 3871 VAL VAL A . n 
A 1 3872 ALA 3872 3872 3872 ALA ALA A . n 
A 1 3873 ARG 3873 3873 3873 ARG ARG A . n 
A 1 3874 GLY 3874 3874 3874 GLY GLY A . n 
A 1 3875 MET 3875 3875 3875 MET MET A . n 
A 1 3876 LEU 3876 3876 3876 LEU LEU A . n 
A 1 3877 HIS 3877 3877 3877 HIS HIS A . n 
A 1 3878 GLN 3878 3878 3878 GLN GLN A . n 
A 1 3879 ASP 3879 3879 3879 ASP ASP A . n 
A 1 3880 HIS 3880 3880 3880 HIS HIS A . n 
A 1 3881 ILE 3881 3881 3881 ILE ILE A . n 
A 1 3882 THR 3882 3882 3882 THR THR A . n 
A 1 3883 PHE 3883 3883 3883 PHE PHE A . n 
A 1 3884 ALA 3884 3884 3884 ALA ALA A . n 
A 1 3885 MET 3885 3885 3885 MET MET A . n 
A 1 3886 LEU 3886 3886 3886 LEU LEU A . n 
A 1 3887 LEU 3887 3887 3887 LEU LEU A . n 
A 1 3888 ALA 3888 3888 3888 ALA ALA A . n 
A 1 3889 ARG 3889 3889 3889 ARG ARG A . n 
A 1 3890 ILE 3890 3890 3890 ILE ILE A . n 
A 1 3891 LYS 3891 3891 3891 LYS LYS A . n 
A 1 3892 LEU 3892 3892 3892 LEU LEU A . n 
A 1 3893 LYS 3893 3893 3893 LYS LYS A . n 
A 1 3894 GLY 3894 3894 3894 GLY GLY A . n 
A 1 3895 THR 3895 3895 3895 THR THR A . n 
A 1 3896 VAL 3896 3896 3896 VAL VAL A . n 
A 1 3897 GLY 3897 3897 3897 GLY GLY A . n 
A 1 3898 GLU 3898 3898 3898 GLU GLU A . n 
A 1 3899 PRO 3899 3899 3899 PRO PRO A . n 
A 1 3900 THR 3900 3900 3900 THR THR A . n 
A 1 3901 TYR 3901 3901 3901 TYR TYR A . n 
A 1 3902 ASP 3902 3902 3902 ASP ASP A . n 
A 1 3903 ALA 3903 3903 3903 ALA ALA A . n 
A 1 3904 GLU 3904 3904 3904 GLU GLU A . n 
A 1 3905 PHE 3905 3905 3905 PHE PHE A . n 
A 1 3906 GLN 3906 3906 3906 GLN GLN A . n 
A 1 3907 HIS 3907 3907 3907 HIS HIS A . n 
A 1 3908 PHE 3908 3908 3908 PHE PHE A . n 
A 1 3909 LEU 3909 3909 3909 LEU LEU A . n 
A 1 3910 ARG 3910 3910 3910 ARG ARG A . n 
A 1 3911 GLY 3911 3911 3911 GLY GLY A . n 
A 1 3912 ASN 3912 3912 3912 ASN ASN A . n 
A 1 3913 GLU 3913 3913 3913 GLU GLU A . n 
A 1 3914 ILE 3914 3914 3914 ILE ILE A . n 
A 1 3915 VAL 3915 3915 3915 VAL VAL A . n 
A 1 3916 LEU 3916 3916 3916 LEU LEU A . n 
A 1 3917 SER 3917 3917 3917 SER SER A . n 
A 1 3918 ALA 3918 3918 3918 ALA ALA A . n 
A 1 3919 GLY 3919 3919 3919 GLY GLY A . n 
A 1 3920 SER 3920 3920 3920 SER SER A . n 
A 1 3921 THR 3921 3921 3921 THR THR A . n 
A 1 3922 PRO 3922 3922 3922 PRO PRO A . n 
A 1 3923 ARG 3923 3923 3923 ARG ARG A . n 
A 1 3924 ILE 3924 3924 3924 ILE ILE A . n 
A 1 3925 GLN 3925 3925 3925 GLN GLN A . n 
A 1 3926 GLY 3926 3926 3926 GLY GLY A . n 
A 1 3927 LEU 3927 3927 3927 LEU LEU A . n 
A 1 3928 THR 3928 3928 3928 THR THR A . n 
A 1 3929 VAL 3929 3929 3929 VAL VAL A . n 
A 1 3930 GLU 3930 3930 3930 GLU GLU A . n 
A 1 3931 GLN 3931 3931 3931 GLN GLN A . n 
A 1 3932 ALA 3932 3932 3932 ALA ALA A . n 
A 1 3933 GLU 3933 3933 3933 GLU GLU A . n 
A 1 3934 ALA 3934 3934 3934 ALA ALA A . n 
A 1 3935 VAL 3935 3935 3935 VAL VAL A . n 
A 1 3936 VAL 3936 3936 3936 VAL VAL A . n 
A 1 3937 ARG 3937 3937 3937 ARG ARG A . n 
A 1 3938 LEU 3938 3938 3938 LEU LEU A . n 
A 1 3939 SER 3939 3939 3939 SER SER A . n 
A 1 3940 CYS 3940 3940 3940 CYS CYS A . n 
A 1 3941 LEU 3941 3941 3941 LEU LEU A . n 
A 1 3942 PRO 3942 3942 3942 PRO PRO A . n 
A 1 3943 ALA 3943 3943 3943 ALA ALA A . n 
A 1 3944 PHE 3944 3944 3944 PHE PHE A . n 
A 1 3945 LYS 3945 3945 3945 LYS LYS A . n 
A 1 3946 ASP 3946 3946 3946 ASP ASP A . n 
A 1 3947 LEU 3947 3947 3947 LEU LEU A . n 
A 1 3948 ILE 3948 3948 3948 ILE ILE A . n 
A 1 3949 ALA 3949 3949 3949 ALA ALA A . n 
A 1 3950 LYS 3950 3950 3950 LYS LYS A . n 
A 1 3951 VAL 3951 3951 3951 VAL VAL A . n 
A 1 3952 GLN 3952 3952 3952 GLN GLN A . n 
A 1 3953 ALA 3953 3953 3953 ALA ALA A . n 
A 1 3954 ASP 3954 3954 3954 ASP ASP A . n 
A 1 3955 GLU 3955 3955 3955 GLU GLU A . n 
A 1 3956 GLN 3956 3956 3956 GLN GLN A . n 
A 1 3957 PHE 3957 3957 3957 PHE PHE A . n 
A 1 3958 GLY 3958 3958 3958 GLY GLY A . n 
A 1 3959 ILE 3959 3959 3959 ILE ILE A . n 
A 1 3960 TRP 3960 3960 3960 TRP TRP A . n 
A 1 3961 LEU 3961 3961 3961 LEU LEU A . n 
A 1 3962 ASP 3962 3962 3962 ASP ASP A . n 
A 1 3963 SER 3963 3963 3963 SER SER A . n 
A 1 3964 SER 3964 3964 3964 SER SER A . n 
A 1 3965 SER 3965 3965 3965 SER SER A . n 
A 1 3966 PRO 3966 3966 3966 PRO PRO A . n 
A 1 3967 GLU 3967 3967 3967 GLU GLU A . n 
A 1 3968 GLN 3968 3968 3968 GLN GLN A . n 
A 1 3969 THR 3969 3969 3969 THR THR A . n 
A 1 3970 VAL 3970 3970 3970 VAL VAL A . n 
A 1 3971 PRO 3971 3971 3971 PRO PRO A . n 
A 1 3972 TYR 3972 3972 3972 TYR TYR A . n 
A 1 3973 LEU 3973 3973 3973 LEU LEU A . n 
A 1 3974 TRP 3974 3974 3974 TRP TRP A . n 
A 1 3975 SER 3975 3975 3975 SER SER A . n 
A 1 3976 GLU 3976 3976 3976 GLU GLU A . n 
A 1 3977 GLU 3977 3977 3977 GLU GLU A . n 
A 1 3978 THR 3978 3978 3978 THR THR A . n 
A 1 3979 PRO 3979 3979 3979 PRO PRO A . n 
A 1 3980 ALA 3980 3980 3980 ALA ALA A . n 
A 1 3981 THR 3981 3981 3981 THR THR A . n 
A 1 3982 PRO 3982 3982 3982 PRO PRO A . n 
A 1 3983 ILE 3983 3983 3983 ILE ILE A . n 
A 1 3984 GLY 3984 3984 3984 GLY GLY A . n 
A 1 3985 GLN 3985 3985 3985 GLN GLN A . n 
A 1 3986 ALA 3986 3986 3986 ALA ALA A . n 
A 1 3987 ILE 3987 3987 3987 ILE ILE A . n 
A 1 3988 HIS 3988 3988 3988 HIS HIS A . n 
A 1 3989 ARG 3989 3989 3989 ARG ARG A . n 
A 1 3990 LEU 3990 3990 3990 LEU LEU A . n 
A 1 3991 LEU 3991 3991 3991 LEU LEU A . n 
A 1 3992 LEU 3992 3992 3992 LEU LEU A . n 
A 1 3993 ILE 3993 3993 3993 ILE ILE A . n 
A 1 3994 GLN 3994 3994 3994 GLN GLN A . n 
A 1 3995 ALA 3995 3995 3995 ALA ALA A . n 
A 1 3996 PHE 3996 3996 3996 PHE PHE A . n 
A 1 3997 ARG 3997 3997 3997 ARG ARG A . n 
A 1 3998 PRO 3998 3998 3998 PRO PRO A . n 
A 1 3999 ASP 3999 3999 3999 ASP ASP A . n 
A 1 4000 ARG 4000 4000 4000 ARG ARG A . n 
A 1 4001 LEU 4001 4001 4001 LEU LEU A . n 
A 1 4002 LEU 4002 4002 4002 LEU LEU A . n 
A 1 4003 ALA 4003 4003 4003 ALA ALA A . n 
A 1 4004 MET 4004 4004 4004 MET MET A . n 
A 1 4005 ALA 4005 4005 4005 ALA ALA A . n 
A 1 4006 HIS 4006 4006 4006 HIS HIS A . n 
A 1 4007 MET 4007 4007 4007 MET MET A . n 
A 1 4008 PHE 4008 4008 4008 PHE PHE A . n 
A 1 4009 VAL 4009 4009 4009 VAL VAL A . n 
A 1 4010 SER 4010 4010 4010 SER SER A . n 
A 1 4011 THR 4011 4011 4011 THR THR A . n 
A 1 4012 ASN 4012 4012 4012 ASN ASN A . n 
A 1 4013 LEU 4013 4013 4013 LEU LEU A . n 
A 1 4014 GLY 4014 4014 4014 GLY GLY A . n 
A 1 4015 GLU 4015 4015 4015 GLU GLU A . n 
A 1 4016 SER 4016 4016 4016 SER SER A . n 
A 1 4017 PHE 4017 4017 4017 PHE PHE A . n 
A 1 4018 MET 4018 4018 4018 MET MET A . n 
A 1 4019 SER 4019 4019 4019 SER SER A . n 
A 1 4020 ILE 4020 4020 4020 ILE ILE A . n 
A 1 4021 MET 4021 4021 4021 MET MET A . n 
A 1 4022 GLU 4022 4022 4022 GLU GLU A . n 
A 1 4023 GLN 4023 4023 4023 GLN GLN A . n 
A 1 4024 PRO 4024 4024 4024 PRO PRO A . n 
A 1 4025 LEU 4025 4025 4025 LEU LEU A . n 
A 1 4026 ASP 4026 4026 4026 ASP ASP A . n 
A 1 4027 LEU 4027 4027 4027 LEU LEU A . n 
A 1 4028 THR 4028 4028 4028 THR THR A . n 
A 1 4029 HIS 4029 4029 4029 HIS HIS A . n 
A 1 4030 ILE 4030 4030 4030 ILE ILE A . n 
A 1 4031 VAL 4031 4031 4031 VAL VAL A . n 
A 1 4032 GLY 4032 4032 4032 GLY GLY A . n 
A 1 4033 THR 4033 4033 4033 THR THR A . n 
A 1 4034 GLU 4034 4034 4034 GLU GLU A . n 
A 1 4035 VAL 4035 4035 4035 VAL VAL A . n 
A 1 4036 LYS 4036 4036 4036 LYS LYS A . n 
A 1 4037 PRO 4037 4037 4037 PRO PRO A . n 
A 1 4038 ASN 4038 4038 4038 ASN ASN A . n 
A 1 4039 THR 4039 4039 4039 THR THR A . n 
A 1 4040 PRO 4040 4040 4040 PRO PRO A . n 
A 1 4041 VAL 4041 4041 4041 VAL VAL A . n 
A 1 4042 LEU 4042 4042 4042 LEU LEU A . n 
A 1 4043 MET 4043 4043 4043 MET MET A . n 
A 1 4044 CYS 4044 4044 4044 CYS CYS A . n 
A 1 4045 SER 4045 4045 4045 SER SER A . n 
A 1 4046 VAL 4046 4046 4046 VAL VAL A . n 
A 1 4047 PRO 4047 4047 4047 PRO PRO A . n 
A 1 4048 GLY 4048 4048 4048 GLY GLY A . n 
A 1 4049 TYR 4049 4049 4049 TYR TYR A . n 
A 1 4050 ASP 4050 4050 4050 ASP ASP A . n 
A 1 4051 ALA 4051 4051 4051 ALA ALA A . n 
A 1 4052 SER 4052 4052 4052 SER SER A . n 
A 1 4053 GLY 4053 4053 4053 GLY GLY A . n 
A 1 4054 HIS 4054 4054 4054 HIS HIS A . n 
A 1 4055 VAL 4055 4055 4055 VAL VAL A . n 
A 1 4056 GLU 4056 4056 4056 GLU GLU A . n 
A 1 4057 ASP 4057 4057 4057 ASP ASP A . n 
A 1 4058 LEU 4058 4058 4058 LEU LEU A . n 
A 1 4059 ALA 4059 4059 4059 ALA ALA A . n 
A 1 4060 ALA 4060 4060 4060 ALA ALA A . n 
A 1 4061 GLU 4061 4061 4061 GLU GLU A . n 
A 1 4062 GLN 4062 4062 4062 GLN GLN A . n 
A 1 4063 ASN 4063 4063 4063 ASN ASN A . n 
A 1 4064 THR 4064 4064 4064 THR THR A . n 
A 1 4065 GLN 4065 4065 4065 GLN GLN A . n 
A 1 4066 ILE 4066 4066 4066 ILE ILE A . n 
A 1 4067 THR 4067 4067 4067 THR THR A . n 
A 1 4068 SER 4068 4068 4068 SER SER A . n 
A 1 4069 ILE 4069 4069 4069 ILE ILE A . n 
A 1 4070 ALA 4070 4070 4070 ALA ALA A . n 
A 1 4071 ILE 4071 4071 4071 ILE ILE A . n 
A 1 4072 GLY 4072 4072 4072 GLY GLY A . n 
A 1 4073 SER 4073 4073 4073 SER SER A . n 
A 1 4074 ALA 4074 4074 4074 ALA ALA A . n 
A 1 4075 GLU 4075 4075 4075 GLU GLU A . n 
A 1 4076 GLY 4076 4076 4076 GLY GLY A . n 
A 1 4077 PHE 4077 4077 4077 PHE PHE A . n 
A 1 4078 ASN 4078 4078 4078 ASN ASN A . n 
A 1 4079 GLN 4079 4079 4079 GLN GLN A . n 
A 1 4080 ALA 4080 4080 4080 ALA ALA A . n 
A 1 4081 ASP 4081 4081 4081 ASP ASP A . n 
A 1 4082 LYS 4082 4082 4082 LYS LYS A . n 
A 1 4083 ALA 4083 4083 4083 ALA ALA A . n 
A 1 4084 ILE 4084 4084 4084 ILE ILE A . n 
A 1 4085 ASN 4085 4085 4085 ASN ASN A . n 
A 1 4086 THR 4086 4086 4086 THR THR A . n 
A 1 4087 ALA 4087 4087 4087 ALA ALA A . n 
A 1 4088 VAL 4088 4088 4088 VAL VAL A . n 
A 1 4089 LYS 4089 4089 4089 LYS LYS A . n 
A 1 4090 SER 4090 4090 4090 SER SER A . n 
A 1 4091 GLY 4091 4091 4091 GLY GLY A . n 
A 1 4092 ARG 4092 4092 4092 ARG ARG A . n 
A 1 4093 TRP 4093 4093 4093 TRP TRP A . n 
A 1 4094 VAL 4094 4094 4094 VAL VAL A . n 
A 1 4095 MET 4095 4095 4095 MET MET A . n 
A 1 4096 LEU 4096 4096 4096 LEU LEU A . n 
A 1 4097 LYS 4097 4097 4097 LYS LYS A . n 
A 1 4098 ASN 4098 4098 4098 ASN ASN A . n 
A 1 4099 VAL 4099 4099 4099 VAL VAL A . n 
A 1 4100 HIS 4100 4100 4100 HIS HIS A . n 
A 1 4101 LEU 4101 4101 4101 LEU LEU A . n 
A 1 4102 ALA 4102 4102 4102 ALA ALA A . n 
A 1 4103 PRO 4103 4103 4103 PRO PRO A . n 
A 1 4104 GLY 4104 4104 4104 GLY GLY A . n 
A 1 4105 TRP 4105 4105 4105 TRP TRP A . n 
A 1 4106 LEU 4106 4106 4106 LEU LEU A . n 
A 1 4107 MET 4107 4107 4107 MET MET A . n 
A 1 4108 GLN 4108 4108 4108 GLN GLN A . n 
A 1 4109 LEU 4109 4109 4109 LEU LEU A . n 
A 1 4110 GLU 4110 4110 4110 GLU GLU A . n 
A 1 4111 LYS 4111 4111 4111 LYS LYS A . n 
A 1 4112 LYS 4112 4112 4112 LYS LYS A . n 
A 1 4113 LEU 4113 4113 4113 LEU LEU A . n 
A 1 4114 HIS 4114 4114 4114 HIS HIS A . n 
A 1 4115 SER 4115 4115 4115 SER SER A . n 
A 1 4116 LEU 4116 4116 4116 LEU LEU A . n 
A 1 4117 GLN 4117 4117 4117 GLN GLN A . n 
A 1 4118 PRO 4118 4118 4118 PRO PRO A . n 
A 1 4119 HIS 4119 4119 4119 HIS HIS A . n 
A 1 4120 ALA 4120 4120 4120 ALA ALA A . n 
A 1 4121 CYS 4121 4121 4121 CYS CYS A . n 
A 1 4122 PHE 4122 4122 4122 PHE PHE A . n 
A 1 4123 ARG 4123 4123 4123 ARG ARG A . n 
A 1 4124 LEU 4124 4124 4124 LEU LEU A . n 
A 1 4125 PHE 4125 4125 4125 PHE PHE A . n 
A 1 4126 LEU 4126 4126 4126 LEU LEU A . n 
A 1 4127 THR 4127 4127 4127 THR THR A . n 
A 1 4128 MET 4128 4128 4128 MET MET A . n 
A 1 4129 GLU 4129 4129 4129 GLU GLU A . n 
A 1 4130 ILE 4130 4130 4130 ILE ILE A . n 
A 1 4131 ASN 4131 4131 4131 ASN ASN A . n 
A 1 4132 PRO 4132 4132 4132 PRO PRO A . n 
A 1 4133 LYS 4133 4133 4133 LYS LYS A . n 
A 1 4134 VAL 4134 4134 4134 VAL VAL A . n 
A 1 4135 PRO 4135 4135 4135 PRO PRO A . n 
A 1 4136 VAL 4136 4136 4136 VAL VAL A . n 
A 1 4137 ASN 4137 4137 4137 ASN ASN A . n 
A 1 4138 LEU 4138 4138 4138 LEU LEU A . n 
A 1 4139 LEU 4139 4139 4139 LEU LEU A . n 
A 1 4140 ARG 4140 4140 4140 ARG ARG A . n 
A 1 4141 ALA 4141 4141 4141 ALA ALA A . n 
A 1 4142 GLY 4142 4142 4142 GLY GLY A . n 
A 1 4143 ARG 4143 4143 4143 ARG ARG A . n 
A 1 4144 ILE 4144 4144 4144 ILE ILE A . n 
A 1 4145 PHE 4145 4145 4145 PHE PHE A . n 
A 1 4146 VAL 4146 4146 4146 VAL VAL A . n 
A 1 4147 PHE 4147 4147 4147 PHE PHE A . n 
A 1 4148 GLU 4148 4148 4148 GLU GLU A . n 
A 1 4149 PRO 4149 4149 4149 PRO PRO A . n 
A 1 4150 PRO 4150 4150 4150 PRO PRO A . n 
A 1 4151 PRO 4151 4151 4151 PRO PRO A . n 
A 1 4152 GLY 4152 4152 4152 GLY GLY A . n 
A 1 4153 VAL 4153 4153 4153 VAL VAL A . n 
A 1 4154 LYS 4154 4154 4154 LYS LYS A . n 
A 1 4155 ALA 4155 4155 4155 ALA ALA A . n 
A 1 4156 ASN 4156 4156 4156 ASN ASN A . n 
A 1 4157 MET 4157 4157 4157 MET MET A . n 
A 1 4158 LEU 4158 4158 4158 LEU LEU A . n 
A 1 4159 ARG 4159 4159 4159 ARG ARG A . n 
A 1 4160 THR 4160 4160 4160 THR THR A . n 
A 1 4161 PHE 4161 4161 4161 PHE PHE A . n 
A 1 4162 SER 4162 4162 4162 SER SER A . n 
A 1 4163 SER 4163 4163 4163 SER SER A . n 
A 1 4164 ILE 4164 4164 4164 ILE ILE A . n 
A 1 4165 PRO 4165 4165 4165 PRO PRO A . n 
A 1 4166 VAL 4166 4166 4166 VAL VAL A . n 
A 1 4167 SER 4167 4167 4167 SER SER A . n 
A 1 4168 ARG 4168 4168 4168 ARG ARG A . n 
A 1 4169 ILE 4169 4169 4169 ILE ILE A . n 
A 1 4170 CYS 4170 4170 4170 CYS CYS A . n 
A 1 4171 LYS 4171 4171 4171 LYS LYS A . n 
A 1 4172 SER 4172 4172 4172 SER SER A . n 
A 1 4173 PRO 4173 4173 4173 PRO PRO A . n 
A 1 4174 ASN 4174 4174 4174 ASN ASN A . n 
A 1 4175 GLU 4175 4175 4175 GLU GLU A . n 
A 1 4176 ARG 4176 4176 4176 ARG ARG A . n 
A 1 4177 ALA 4177 4177 4177 ALA ALA A . n 
A 1 4178 ARG 4178 4178 4178 ARG ARG A . n 
A 1 4179 LEU 4179 4179 4179 LEU LEU A . n 
A 1 4180 TYR 4180 4180 4180 TYR TYR A . n 
A 1 4181 PHE 4181 4181 4181 PHE PHE A . n 
A 1 4182 LEU 4182 4182 4182 LEU LEU A . n 
A 1 4183 LEU 4183 4183 4183 LEU LEU A . n 
A 1 4184 ALA 4184 4184 4184 ALA ALA A . n 
A 1 4185 TRP 4185 4185 4185 TRP TRP A . n 
A 1 4186 PHE 4186 4186 4186 PHE PHE A . n 
A 1 4187 HIS 4187 4187 4187 HIS HIS A . n 
A 1 4188 ALA 4188 4188 4188 ALA ALA A . n 
A 1 4189 ILE 4189 4189 4189 ILE ILE A . n 
A 1 4190 ILE 4190 4190 4190 ILE ILE A . n 
A 1 4191 GLN 4191 4191 4191 GLN GLN A . n 
A 1 4192 GLU 4192 4192 4192 GLU GLU A . n 
A 1 4193 ARG 4193 4193 4193 ARG ARG A . n 
A 1 4194 LEU 4194 4194 4194 LEU LEU A . n 
A 1 4195 ARG 4195 4195 4195 ARG ARG A . n 
A 1 4196 TYR 4196 4196 4196 TYR TYR A . n 
A 1 4197 ALA 4197 4197 4197 ALA ALA A . n 
A 1 4198 PRO 4198 4198 4198 PRO PRO A . n 
A 1 4199 LEU 4199 4199 4199 LEU LEU A . n 
A 1 4200 GLY 4200 4200 4200 GLY GLY A . n 
A 1 4201 TRP 4201 4201 4201 TRP TRP A . n 
A 1 4202 SER 4202 4202 4202 SER SER A . n 
A 1 4203 LYS 4203 4203 4203 LYS LYS A . n 
A 1 4204 LYS 4204 4204 4204 LYS LYS A . n 
A 1 4205 TYR 4205 4205 4205 TYR TYR A . n 
A 1 4206 GLU 4206 4206 4206 GLU GLU A . n 
A 1 4207 PHE 4207 4207 4207 PHE PHE A . n 
A 1 4208 GLY 4208 4208 4208 GLY GLY A . n 
A 1 4209 GLU 4209 4209 4209 GLU GLU A . n 
A 1 4210 SER 4210 4210 4210 SER SER A . n 
A 1 4211 ASP 4211 4211 4211 ASP ASP A . n 
A 1 4212 LEU 4212 4212 4212 LEU LEU A . n 
A 1 4213 ARG 4213 4213 4213 ARG ARG A . n 
A 1 4214 SER 4214 4214 4214 SER SER A . n 
A 1 4215 ALA 4215 4215 4215 ALA ALA A . n 
A 1 4216 CYS 4216 4216 4216 CYS CYS A . n 
A 1 4217 ASP 4217 4217 4217 ASP ASP A . n 
A 1 4218 THR 4218 4218 4218 THR THR A . n 
A 1 4219 VAL 4219 4219 4219 VAL VAL A . n 
A 1 4220 ASP 4220 4220 4220 ASP ASP A . n 
A 1 4221 THR 4221 4221 4221 THR THR A . n 
A 1 4222 TRP 4222 4222 4222 TRP TRP A . n 
A 1 4223 LEU 4223 4223 4223 LEU LEU A . n 
A 1 4224 ASP 4224 4224 4224 ASP ASP A . n 
A 1 4225 ASP 4225 4225 4225 ASP ASP A . n 
A 1 4226 THR 4226 4226 4226 THR THR A . n 
A 1 4227 ALA 4227 4227 4227 ALA ALA A . n 
A 1 4228 LYS 4228 4228 4228 LYS LYS A . n 
A 1 4229 GLY 4229 4229 4229 GLY GLY A . n 
A 1 4230 ARG 4230 4230 4230 ARG ARG A . n 
A 1 4231 GLN 4231 4231 4231 GLN GLN A . n 
A 1 4232 ASN 4232 4232 4232 ASN ASN A . n 
A 1 4233 ILE 4233 4233 4233 ILE ILE A . n 
A 1 4234 SER 4234 4234 4234 SER SER A . n 
A 1 4235 PRO 4235 4235 4235 PRO PRO A . n 
A 1 4236 ASP 4236 4236 4236 ASP ASP A . n 
A 1 4237 LYS 4237 4237 4237 LYS LYS A . n 
A 1 4238 ILE 4238 4238 4238 ILE ILE A . n 
A 1 4239 PRO 4239 4239 4239 PRO PRO A . n 
A 1 4240 TRP 4240 4240 4240 TRP TRP A . n 
A 1 4241 SER 4241 4241 4241 SER SER A . n 
A 1 4242 ALA 4242 4242 4242 ALA ALA A . n 
A 1 4243 LEU 4243 4243 4243 LEU LEU A . n 
A 1 4244 LYS 4244 4244 4244 LYS LYS A . n 
A 1 4245 THR 4245 4245 4245 THR THR A . n 
A 1 4246 LEU 4246 4246 4246 LEU LEU A . n 
A 1 4247 MET 4247 4247 4247 MET MET A . n 
A 1 4248 ALA 4248 4248 4248 ALA ALA A . n 
A 1 4249 GLN 4249 4249 4249 GLN GLN A . n 
A 1 4250 SER 4250 4250 4250 SER SER A . n 
A 1 4251 ILE 4251 4251 4251 ILE ILE A . n 
A 1 4252 TYR 4252 4252 4252 TYR TYR A . n 
A 1 4253 GLY 4253 4253 4253 GLY GLY A . n 
A 1 4254 GLY 4254 4254 4254 GLY GLY A . n 
A 1 4255 ARG 4255 4255 4255 ARG ARG A . n 
A 1 4256 VAL 4256 4256 4256 VAL VAL A . n 
A 1 4257 ASP 4257 4257 4257 ASP ASP A . n 
A 1 4258 ASN 4258 4258 4258 ASN ASN A . n 
A 1 4259 GLU 4259 4259 4259 GLU GLU A . n 
A 1 4260 PHE 4260 4260 4260 PHE PHE A . n 
A 1 4261 ASP 4261 4261 4261 ASP ASP A . n 
A 1 4262 GLN 4262 4262 4262 GLN GLN A . n 
A 1 4263 ARG 4263 4263 4263 ARG ARG A . n 
A 1 4264 LEU 4264 4264 4264 LEU LEU A . n 
A 1 4265 LEU 4265 4265 4265 LEU LEU A . n 
A 1 4266 ASN 4266 4266 4266 ASN ASN A . n 
A 1 4267 THR 4267 4267 4267 THR THR A . n 
A 1 4268 PHE 4268 4268 4268 PHE PHE A . n 
A 1 4269 LEU 4269 4269 4269 LEU LEU A . n 
A 1 4270 GLU 4270 4270 4270 GLU GLU A . n 
A 1 4271 ARG 4271 4271 4271 ARG ARG A . n 
A 1 4272 LEU 4272 4272 4272 LEU LEU A . n 
A 1 4273 PHE 4273 4273 4273 PHE PHE A . n 
A 1 4274 THR 4274 4274 4274 THR THR A . n 
A 1 4275 THR 4275 4275 4275 THR THR A . n 
A 1 4276 ARG 4276 4276 4276 ARG ARG A . n 
A 1 4277 SER 4277 4277 4277 SER SER A . n 
A 1 4278 PHE 4278 4278 4278 PHE PHE A . n 
A 1 4279 ASP 4279 4279 4279 ASP ASP A . n 
A 1 4280 SER 4280 4280 4280 SER SER A . n 
A 1 4281 GLU 4281 4281 4281 GLU GLU A . n 
A 1 4282 PHE 4282 4282 4282 PHE PHE A . n 
A 1 4283 LYS 4283 4283 4283 LYS LYS A . n 
A 1 4284 LEU 4284 4284 4284 LEU LEU A . n 
A 1 4285 ALA 4285 4285 4285 ALA ALA A . n 
A 1 4286 CYS 4286 4286 4286 CYS CYS A . n 
A 1 4287 LYS 4287 4287 4287 LYS LYS A . n 
A 1 4288 VAL 4288 4288 4288 VAL VAL A . n 
A 1 4289 ASP 4289 4289 4289 ASP ASP A . n 
A 1 4290 GLY 4290 4290 4290 GLY GLY A . n 
A 1 4291 HIS 4291 4291 4291 HIS HIS A . n 
A 1 4292 LYS 4292 4292 4292 LYS LYS A . n 
A 1 4293 ASP 4293 4293 4293 ASP ASP A . n 
A 1 4294 ILE 4294 4294 4294 ILE ILE A . n 
A 1 4295 GLN 4295 4295 4295 GLN GLN A . n 
A 1 4296 MET 4296 4296 4296 MET MET A . n 
A 1 4297 PRO 4297 4297 4297 PRO PRO A . n 
A 1 4298 ASP 4298 4298 4298 ASP ASP A . n 
A 1 4299 GLY 4299 4299 4299 GLY GLY A . n 
A 1 4300 ILE 4300 4300 4300 ILE ILE A . n 
A 1 4301 ARG 4301 4301 4301 ARG ARG A . n 
A 1 4302 ARG 4302 4302 4302 ARG ARG A . n 
A 1 4303 GLU 4303 4303 4303 GLU GLU A . n 
A 1 4304 GLU 4304 4304 4304 GLU GLU A . n 
A 1 4305 PHE 4305 4305 4305 PHE PHE A . n 
A 1 4306 VAL 4306 4306 4306 VAL VAL A . n 
A 1 4307 GLN 4307 4307 4307 GLN GLN A . n 
A 1 4308 TRP 4308 4308 4308 TRP TRP A . n 
A 1 4309 VAL 4309 4309 4309 VAL VAL A . n 
A 1 4310 GLU 4310 4310 4310 GLU GLU A . n 
A 1 4311 LEU 4311 4311 4311 LEU LEU A . n 
A 1 4312 LEU 4312 4312 4312 LEU LEU A . n 
A 1 4313 PRO 4313 4313 4313 PRO PRO A . n 
A 1 4314 ASP 4314 4314 4314 ASP ASP A . n 
A 1 4315 THR 4315 4315 4315 THR THR A . n 
A 1 4316 GLN 4316 4316 4316 GLN GLN A . n 
A 1 4317 THR 4317 4317 4317 THR THR A . n 
A 1 4318 PRO 4318 4318 4318 PRO PRO A . n 
A 1 4319 SER 4319 4319 4319 SER SER A . n 
A 1 4320 TRP 4320 4320 4320 TRP TRP A . n 
A 1 4321 LEU 4321 4321 4321 LEU LEU A . n 
A 1 4322 GLY 4322 4322 4322 GLY GLY A . n 
A 1 4323 LEU 4323 4323 4323 LEU LEU A . n 
A 1 4324 PRO 4324 4324 4324 PRO PRO A . n 
A 1 4325 ASN 4325 4325 4325 ASN ASN A . n 
A 1 4326 ASN 4326 4326 4326 ASN ASN A . n 
A 1 4327 ALA 4327 4327 4327 ALA ALA A . n 
A 1 4328 GLU 4328 4328 4328 GLU GLU A . n 
A 1 4329 ARG 4329 4329 4329 ARG ARG A . n 
A 1 4330 VAL 4330 4330 4330 VAL VAL A . n 
A 1 4331 LEU 4331 4331 4331 LEU LEU A . n 
A 1 4332 LEU 4332 4332 4332 LEU LEU A . n 
A 1 4333 THR 4333 4333 4333 THR THR A . n 
A 1 4334 THR 4334 4334 4334 THR THR A . n 
A 1 4335 GLN 4335 4335 4335 GLN GLN A . n 
A 1 4336 GLY 4336 4336 4336 GLY GLY A . n 
A 1 4337 VAL 4337 4337 4337 VAL VAL A . n 
A 1 4338 ASP 4338 4338 4338 ASP ASP A . n 
A 1 4339 MET 4339 4339 4339 MET MET A . n 
A 1 4340 ILE 4340 4340 4340 ILE ILE A . n 
A 1 4341 SER 4341 4341 4341 SER SER A . n 
A 1 4342 LYS 4342 4342 4342 LYS LYS A . n 
A 1 4343 MET 4343 4343 4343 MET MET A . n 
A 1 4344 LEU 4344 4344 4344 LEU LEU A . n 
A 1 4345 LYS 4345 4345 4345 LYS LYS A . n 
A 1 4346 MET 4346 4346 4346 MET MET A . n 
A 1 4347 GLN 4347 4347 4347 GLN GLN A . n 
A 1 4348 MET 4348 4348 ?    ?   ?   A . n 
A 1 4349 LEU 4349 4349 ?    ?   ?   A . n 
A 1 4350 GLU 4350 4350 ?    ?   ?   A . n 
A 1 4351 ASP 4351 4351 ?    ?   ?   A . n 
A 1 4352 GLU 4352 4352 ?    ?   ?   A . n 
A 1 4353 ASP 4353 4353 ?    ?   ?   A . n 
A 1 4354 ASP 4354 4354 ?    ?   ?   A . n 
A 1 4355 LEU 4355 4355 ?    ?   ?   A . n 
A 1 4356 ALA 4356 4356 ?    ?   ?   A . n 
A 1 4357 TYR 4357 4357 ?    ?   ?   A . n 
A 1 4358 ALA 4358 4358 ?    ?   ?   A . n 
A 1 4359 GLU 4359 4359 ?    ?   ?   A . n 
A 1 4360 THR 4360 4360 ?    ?   ?   A . n 
A 1 4361 GLU 4361 4361 ?    ?   ?   A . n 
A 1 4362 LYS 4362 4362 ?    ?   ?   A . n 
A 1 4363 LYS 4363 4363 ?    ?   ?   A . n 
A 1 4364 THR 4364 4364 ?    ?   ?   A . n 
A 1 4365 ARG 4365 4365 ?    ?   ?   A . n 
A 1 4366 THR 4366 4366 ?    ?   ?   A . n 
A 1 4367 ASP 4367 4367 ?    ?   ?   A . n 
A 1 4368 SER 4368 4368 ?    ?   ?   A . n 
A 1 4369 THR 4369 4369 ?    ?   ?   A . n 
A 1 4370 SER 4370 4370 ?    ?   ?   A . n 
A 1 4371 ASP 4371 4371 ?    ?   ?   A . n 
A 1 4372 GLY 4372 4372 ?    ?   ?   A . n 
A 1 4373 ARG 4373 4373 ?    ?   ?   A . n 
A 1 4374 PRO 4374 4374 4374 PRO PRO A . n 
A 1 4375 ALA 4375 4375 4375 ALA ALA A . n 
A 1 4376 TRP 4376 4376 4376 TRP TRP A . n 
A 1 4377 MET 4377 4377 4377 MET MET A . n 
A 1 4378 ARG 4378 4378 4378 ARG ARG A . n 
A 1 4379 THR 4379 4379 4379 THR THR A . n 
A 1 4380 LEU 4380 4380 4380 LEU LEU A . n 
A 1 4381 HIS 4381 4381 4381 HIS HIS A . n 
A 1 4382 THR 4382 4382 4382 THR THR A . n 
A 1 4383 THR 4383 4383 4383 THR THR A . n 
A 1 4384 ALA 4384 4384 4384 ALA ALA A . n 
A 1 4385 SER 4385 4385 4385 SER SER A . n 
A 1 4386 ASN 4386 4386 4386 ASN ASN A . n 
A 1 4387 TRP 4387 4387 4387 TRP TRP A . n 
A 1 4388 LEU 4388 4388 4388 LEU LEU A . n 
A 1 4389 HIS 4389 4389 4389 HIS HIS A . n 
A 1 4390 LEU 4390 4390 4390 LEU LEU A . n 
A 1 4391 ILE 4391 4391 4391 ILE ILE A . n 
A 1 4392 PRO 4392 4392 4392 PRO PRO A . n 
A 1 4393 GLN 4393 4393 4393 GLN GLN A . n 
A 1 4394 THR 4394 4394 4394 THR THR A . n 
A 1 4395 LEU 4395 4395 4395 LEU LEU A . n 
A 1 4396 SER 4396 4396 4396 SER SER A . n 
A 1 4397 HIS 4397 4397 4397 HIS HIS A . n 
A 1 4398 LEU 4398 4398 4398 LEU LEU A . n 
A 1 4399 LYS 4399 4399 4399 LYS LYS A . n 
A 1 4400 ARG 4400 4400 4400 ARG ARG A . n 
A 1 4401 THR 4401 4401 4401 THR THR A . n 
A 1 4402 VAL 4402 4402 4402 VAL VAL A . n 
A 1 4403 GLU 4403 4403 4403 GLU GLU A . n 
A 1 4404 ASN 4404 4404 4404 ASN ASN A . n 
A 1 4405 ILE 4405 4405 4405 ILE ILE A . n 
A 1 4406 LYS 4406 4406 4406 LYS LYS A . n 
A 1 4407 ASP 4407 4407 4407 ASP ASP A . n 
A 1 4408 PRO 4408 4408 4408 PRO PRO A . n 
A 1 4409 LEU 4409 4409 4409 LEU LEU A . n 
A 1 4410 PHE 4410 4410 4410 PHE PHE A . n 
A 1 4411 ARG 4411 4411 4411 ARG ARG A . n 
A 1 4412 PHE 4412 4412 4412 PHE PHE A . n 
A 1 4413 PHE 4413 4413 4413 PHE PHE A . n 
A 1 4414 GLU 4414 4414 4414 GLU GLU A . n 
A 1 4415 ARG 4415 4415 4415 ARG ARG A . n 
A 1 4416 GLU 4416 4416 4416 GLU GLU A . n 
A 1 4417 VAL 4417 4417 4417 VAL VAL A . n 
A 1 4418 LYS 4418 4418 4418 LYS LYS A . n 
A 1 4419 MET 4419 4419 4419 MET MET A . n 
A 1 4420 GLY 4420 4420 4420 GLY GLY A . n 
A 1 4421 ALA 4421 4421 4421 ALA ALA A . n 
A 1 4422 LYS 4422 4422 4422 LYS LYS A . n 
A 1 4423 LEU 4423 4423 4423 LEU LEU A . n 
A 1 4424 LEU 4424 4424 4424 LEU LEU A . n 
A 1 4425 GLN 4425 4425 4425 GLN GLN A . n 
A 1 4426 ASP 4426 4426 4426 ASP ASP A . n 
A 1 4427 VAL 4427 4427 4427 VAL VAL A . n 
A 1 4428 ARG 4428 4428 4428 ARG ARG A . n 
A 1 4429 GLN 4429 4429 4429 GLN GLN A . n 
A 1 4430 ASP 4430 4430 4430 ASP ASP A . n 
A 1 4431 LEU 4431 4431 4431 LEU LEU A . n 
A 1 4432 ALA 4432 4432 4432 ALA ALA A . n 
A 1 4433 ASP 4433 4433 4433 ASP ASP A . n 
A 1 4434 VAL 4434 4434 4434 VAL VAL A . n 
A 1 4435 VAL 4435 4435 4435 VAL VAL A . n 
A 1 4436 GLN 4436 4436 4436 GLN GLN A . n 
A 1 4437 VAL 4437 4437 4437 VAL VAL A . n 
A 1 4438 CYS 4438 4438 4438 CYS CYS A . n 
A 1 4439 GLU 4439 4439 4439 GLU GLU A . n 
A 1 4440 GLY 4440 4440 4440 GLY GLY A . n 
A 1 4441 LYS 4441 4441 4441 LYS LYS A . n 
A 1 4442 LYS 4442 4442 4442 LYS LYS A . n 
A 1 4443 LYS 4443 4443 4443 LYS LYS A . n 
A 1 4444 GLN 4444 4444 4444 GLN GLN A . n 
A 1 4445 THR 4445 4445 4445 THR THR A . n 
A 1 4446 ASN 4446 4446 4446 ASN ASN A . n 
A 1 4447 TYR 4447 4447 4447 TYR TYR A . n 
A 1 4448 LEU 4448 4448 4448 LEU LEU A . n 
A 1 4449 ARG 4449 4449 4449 ARG ARG A . n 
A 1 4450 THR 4450 4450 4450 THR THR A . n 
A 1 4451 LEU 4451 4451 4451 LEU LEU A . n 
A 1 4452 ILE 4452 4452 4452 ILE ILE A . n 
A 1 4453 ASN 4453 4453 4453 ASN ASN A . n 
A 1 4454 GLU 4454 4454 4454 GLU GLU A . n 
A 1 4455 LEU 4455 4455 4455 LEU LEU A . n 
A 1 4456 VAL 4456 4456 4456 VAL VAL A . n 
A 1 4457 LYS 4457 4457 4457 LYS LYS A . n 
A 1 4458 GLY 4458 4458 4458 GLY GLY A . n 
A 1 4459 ILE 4459 4459 4459 ILE ILE A . n 
A 1 4460 LEU 4460 4460 4460 LEU LEU A . n 
A 1 4461 PRO 4461 4461 4461 PRO PRO A . n 
A 1 4462 ARG 4462 4462 4462 ARG ARG A . n 
A 1 4463 SER 4463 4463 4463 SER SER A . n 
A 1 4464 TRP 4464 4464 4464 TRP TRP A . n 
A 1 4465 SER 4465 4465 4465 SER SER A . n 
A 1 4466 HIS 4466 4466 4466 HIS HIS A . n 
A 1 4467 TYR 4467 4467 4467 TYR TYR A . n 
A 1 4468 THR 4468 4468 4468 THR THR A . n 
A 1 4469 VAL 4469 4469 4469 VAL VAL A . n 
A 1 4470 PRO 4470 4470 4470 PRO PRO A . n 
A 1 4471 ALA 4471 4471 4471 ALA ALA A . n 
A 1 4472 GLY 4472 4472 4472 GLY GLY A . n 
A 1 4473 MET 4473 4473 4473 MET MET A . n 
A 1 4474 THR 4474 4474 4474 THR THR A . n 
A 1 4475 VAL 4475 4475 4475 VAL VAL A . n 
A 1 4476 ILE 4476 4476 4476 ILE ILE A . n 
A 1 4477 GLN 4477 4477 4477 GLN GLN A . n 
A 1 4478 TRP 4478 4478 4478 TRP TRP A . n 
A 1 4479 VAL 4479 4479 4479 VAL VAL A . n 
A 1 4480 SER 4480 4480 4480 SER SER A . n 
A 1 4481 ASP 4481 4481 4481 ASP ASP A . n 
A 1 4482 PHE 4482 4482 4482 PHE PHE A . n 
A 1 4483 SER 4483 4483 4483 SER SER A . n 
A 1 4484 GLU 4484 4484 4484 GLU GLU A . n 
A 1 4485 ARG 4485 4485 4485 ARG ARG A . n 
A 1 4486 ILE 4486 4486 4486 ILE ILE A . n 
A 1 4487 LYS 4487 4487 4487 LYS LYS A . n 
A 1 4488 GLN 4488 4488 4488 GLN GLN A . n 
A 1 4489 LEU 4489 4489 4489 LEU LEU A . n 
A 1 4490 GLN 4490 4490 4490 GLN GLN A . n 
A 1 4491 ASN 4491 4491 4491 ASN ASN A . n 
A 1 4492 ILE 4492 4492 4492 ILE ILE A . n 
A 1 4493 SER 4493 4493 4493 SER SER A . n 
A 1 4494 LEU 4494 4494 4494 LEU LEU A . n 
A 1 4495 ALA 4495 4495 4495 ALA ALA A . n 
A 1 4496 ALA 4496 4496 4496 ALA ALA A . n 
A 1 4497 ALA 4497 4497 4497 ALA ALA A . n 
A 1 4498 SER 4498 4498 4498 SER SER A . n 
A 1 4499 GLY 4499 4499 4499 GLY GLY A . n 
A 1 4500 GLY 4500 4500 4500 GLY GLY A . n 
A 1 4501 ALA 4501 4501 4501 ALA ALA A . n 
A 1 4502 LYS 4502 4502 4502 LYS LYS A . n 
A 1 4503 GLU 4503 4503 4503 GLU GLU A . n 
A 1 4504 LEU 4504 4504 4504 LEU LEU A . n 
A 1 4505 LYS 4505 4505 4505 LYS LYS A . n 
A 1 4506 ASN 4506 4506 4506 ASN ASN A . n 
A 1 4507 ILE 4507 4507 4507 ILE ILE A . n 
A 1 4508 HIS 4508 4508 4508 HIS HIS A . n 
A 1 4509 VAL 4509 4509 4509 VAL VAL A . n 
A 1 4510 CYS 4510 4510 4510 CYS CYS A . n 
A 1 4511 LEU 4511 4511 4511 LEU LEU A . n 
A 1 4512 GLY 4512 4512 4512 GLY GLY A . n 
A 1 4513 GLY 4513 4513 4513 GLY GLY A . n 
A 1 4514 LEU 4514 4514 4514 LEU LEU A . n 
A 1 4515 PHE 4515 4515 4515 PHE PHE A . n 
A 1 4516 VAL 4516 4516 4516 VAL VAL A . n 
A 1 4517 PRO 4517 4517 4517 PRO PRO A . n 
A 1 4518 GLU 4518 4518 4518 GLU GLU A . n 
A 1 4519 ALA 4519 4519 4519 ALA ALA A . n 
A 1 4520 TYR 4520 4520 4520 TYR TYR A . n 
A 1 4521 ILE 4521 4521 4521 ILE ILE A . n 
A 1 4522 THR 4522 4522 4522 THR THR A . n 
A 1 4523 ALA 4523 4523 4523 ALA ALA A . n 
A 1 4524 THR 4524 4524 4524 THR THR A . n 
A 1 4525 ARG 4525 4525 4525 ARG ARG A . n 
A 1 4526 GLN 4526 4526 4526 GLN GLN A . n 
A 1 4527 TYR 4527 4527 4527 TYR TYR A . n 
A 1 4528 VAL 4528 4528 4528 VAL VAL A . n 
A 1 4529 ALA 4529 4529 4529 ALA ALA A . n 
A 1 4530 GLN 4530 4530 4530 GLN GLN A . n 
A 1 4531 ALA 4531 4531 4531 ALA ALA A . n 
A 1 4532 ASN 4532 4532 4532 ASN ASN A . n 
A 1 4533 SER 4533 4533 4533 SER SER A . n 
A 1 4534 TRP 4534 4534 4534 TRP TRP A . n 
A 1 4535 SER 4535 4535 4535 SER SER A . n 
A 1 4536 LEU 4536 4536 4536 LEU LEU A . n 
A 1 4537 GLU 4537 4537 4537 GLU GLU A . n 
A 1 4538 GLU 4538 4538 4538 GLU GLU A . n 
A 1 4539 LEU 4539 4539 4539 LEU LEU A . n 
A 1 4540 CYS 4540 4540 4540 CYS CYS A . n 
A 1 4541 LEU 4541 4541 4541 LEU LEU A . n 
A 1 4542 GLU 4542 4542 4542 GLU GLU A . n 
A 1 4543 VAL 4543 4543 4543 VAL VAL A . n 
A 1 4544 ASN 4544 4544 4544 ASN ASN A . n 
A 1 4545 VAL 4545 4545 4545 VAL VAL A . n 
A 1 4546 THR 4546 4546 4546 THR THR A . n 
A 1 4547 THR 4547 4547 4547 THR THR A . n 
A 1 4548 SER 4548 4548 4548 SER SER A . n 
A 1 4549 GLN 4549 4549 4549 GLN GLN A . n 
A 1 4550 GLY 4550 4550 4550 GLY GLY A . n 
A 1 4551 ALA 4551 4551 4551 ALA ALA A . n 
A 1 4552 THR 4552 4552 4552 THR THR A . n 
A 1 4553 LEU 4553 4553 4553 LEU LEU A . n 
A 1 4554 ASP 4554 4554 4554 ASP ASP A . n 
A 1 4555 ALA 4555 4555 4555 ALA ALA A . n 
A 1 4556 CYS 4556 4556 4556 CYS CYS A . n 
A 1 4557 SER 4557 4557 4557 SER SER A . n 
A 1 4558 PHE 4558 4558 4558 PHE PHE A . n 
A 1 4559 GLY 4559 4559 4559 GLY GLY A . n 
A 1 4560 VAL 4560 4560 4560 VAL VAL A . n 
A 1 4561 THR 4561 4561 4561 THR THR A . n 
A 1 4562 GLY 4562 4562 4562 GLY GLY A . n 
A 1 4563 LEU 4563 4563 4563 LEU LEU A . n 
A 1 4564 LYS 4564 4564 4564 LYS LYS A . n 
A 1 4565 LEU 4565 4565 4565 LEU LEU A . n 
A 1 4566 GLN 4566 4566 4566 GLN GLN A . n 
A 1 4567 GLY 4567 4567 4567 GLY GLY A . n 
A 1 4568 ALA 4568 4568 4568 ALA ALA A . n 
A 1 4569 THR 4569 4569 4569 THR THR A . n 
A 1 4570 CYS 4570 4570 4570 CYS CYS A . n 
A 1 4571 ASN 4571 4571 4571 ASN ASN A . n 
A 1 4572 ASN 4572 4572 4572 ASN ASN A . n 
A 1 4573 ASN 4573 4573 4573 ASN ASN A . n 
A 1 4574 LYS 4574 4574 4574 LYS LYS A . n 
A 1 4575 LEU 4575 4575 4575 LEU LEU A . n 
A 1 4576 SER 4576 4576 4576 SER SER A . n 
A 1 4577 LEU 4577 4577 4577 LEU LEU A . n 
A 1 4578 SER 4578 4578 4578 SER SER A . n 
A 1 4579 ASN 4579 4579 4579 ASN ASN A . n 
A 1 4580 ALA 4580 4580 4580 ALA ALA A . n 
A 1 4581 ILE 4581 4581 4581 ILE ILE A . n 
A 1 4582 SER 4582 4582 4582 SER SER A . n 
A 1 4583 THR 4583 4583 4583 THR THR A . n 
A 1 4584 ALA 4584 4584 4584 ALA ALA A . n 
A 1 4585 LEU 4585 4585 4585 LEU LEU A . n 
A 1 4586 PRO 4586 4586 4586 PRO PRO A . n 
A 1 4587 LEU 4587 4587 4587 LEU LEU A . n 
A 1 4588 THR 4588 4588 4588 THR THR A . n 
A 1 4589 GLN 4589 4589 4589 GLN GLN A . n 
A 1 4590 LEU 4590 4590 4590 LEU LEU A . n 
A 1 4591 ARG 4591 4591 4591 ARG ARG A . n 
A 1 4592 TRP 4592 4592 4592 TRP TRP A . n 
A 1 4593 VAL 4593 4593 4593 VAL VAL A . n 
A 1 4594 LYS 4594 4594 4594 LYS LYS A . n 
A 1 4595 GLN 4595 4595 4595 GLN GLN A . n 
A 1 4596 THR 4596 4596 4596 THR THR A . n 
A 1 4597 ASN 4597 4597 4597 ASN ASN A . n 
A 1 4598 THR 4598 4598 4598 THR THR A . n 
A 1 4599 GLU 4599 4599 4599 GLU GLU A . n 
A 1 4600 LYS 4600 4600 4600 LYS LYS A . n 
A 1 4601 LYS 4601 4601 4601 LYS LYS A . n 
A 1 4602 ALA 4602 4602 4602 ALA ALA A . n 
A 1 4603 SER 4603 4603 4603 SER SER A . n 
A 1 4604 VAL 4604 4604 4604 VAL VAL A . n 
A 1 4605 VAL 4605 4605 4605 VAL VAL A . n 
A 1 4606 THR 4606 4606 4606 THR THR A . n 
A 1 4607 LEU 4607 4607 4607 LEU LEU A . n 
A 1 4608 PRO 4608 4608 4608 PRO PRO A . n 
A 1 4609 VAL 4609 4609 4609 VAL VAL A . n 
A 1 4610 TYR 4610 4610 4610 TYR TYR A . n 
A 1 4611 LEU 4611 4611 4611 LEU LEU A . n 
A 1 4612 ASN 4612 4612 4612 ASN ASN A . n 
A 1 4613 PHE 4613 4613 4613 PHE PHE A . n 
A 1 4614 THR 4614 4614 4614 THR THR A . n 
A 1 4615 ARG 4615 4615 4615 ARG ARG A . n 
A 1 4616 ALA 4616 4616 4616 ALA ALA A . n 
A 1 4617 ASP 4617 4617 4617 ASP ASP A . n 
A 1 4618 LEU 4618 4618 4618 LEU LEU A . n 
A 1 4619 ILE 4619 4619 4619 ILE ILE A . n 
A 1 4620 PHE 4620 4620 4620 PHE PHE A . n 
A 1 4621 THR 4621 4621 4621 THR THR A . n 
A 1 4622 VAL 4622 4622 4622 VAL VAL A . n 
A 1 4623 ASP 4623 4623 4623 ASP ASP A . n 
A 1 4624 PHE 4624 4624 4624 PHE PHE A . n 
A 1 4625 GLU 4625 4625 4625 GLU GLU A . n 
A 1 4626 ILE 4626 4626 4626 ILE ILE A . n 
A 1 4627 ALA 4627 4627 4627 ALA ALA A . n 
A 1 4628 THR 4628 4628 4628 THR THR A . n 
A 1 4629 LYS 4629 4629 4629 LYS LYS A . n 
A 1 4630 GLU 4630 4630 4630 GLU GLU A . n 
A 1 4631 ASP 4631 4631 4631 ASP ASP A . n 
A 1 4632 PRO 4632 4632 4632 PRO PRO A . n 
A 1 4633 ARG 4633 4633 4633 ARG ARG A . n 
A 1 4634 SER 4634 4634 4634 SER SER A . n 
A 1 4635 PHE 4635 4635 4635 PHE PHE A . n 
A 1 4636 TYR 4636 4636 4636 TYR TYR A . n 
A 1 4637 GLU 4637 4637 4637 GLU GLU A . n 
A 1 4638 ARG 4638 4638 4638 ARG ARG A . n 
A 1 4639 GLY 4639 4639 4639 GLY GLY A . n 
A 1 4640 VAL 4640 4640 4640 VAL VAL A . n 
A 1 4641 ALA 4641 4641 4641 ALA ALA A . n 
A 1 4642 VAL 4642 4642 4642 VAL VAL A . n 
A 1 4643 LEU 4643 4643 4643 LEU LEU A . n 
A 1 4644 CYS 4644 4644 4644 CYS CYS A . n 
A 1 4645 THR 4645 4645 4645 THR THR A . n 
A 1 4646 GLU 4646 4646 ?    ?   ?   A . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 ADP ? ? ADP ? ? 'SUBJECT OF INVESTIGATION' ? 
2 AOV ? ? AOV ? ? 'SUBJECT OF INVESTIGATION' ? 
3 ATP ? ? ATP ? ? 'SUBJECT OF INVESTIGATION' ? 
4 MG  ? ? MG  ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 AOV 1 4701 4701 AOV AOV A . 
C 3 ATP 1 4702 4702 ATP ATP A . 
D 4 ADP 1 4703 4703 ADP ADP A . 
E 4 ADP 1 4704 4704 ADP ADP A . 
F 5 MG  1 4705 4705 MG  MG  A . 
G 5 MG  1 4706 4706 MG  MG  A . 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9BMH 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     9BMH 
_struct.title                        'State-4 of motor domain from full-length human dynein-1 in 5mM ATPVi' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9BMH 
_struct_keywords.text            'dynein-1, MOTOR PROTEIN' 
_struct_keywords.pdbx_keywords   'MOTOR PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 4 ? 
F N N 5 ? 
G N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    DYHC1_HUMAN 
_struct_ref.pdbx_db_accession          Q14204 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSEPGGGGGEDGSAGLEVSAVQNVADVSVLQKHLRKLVPLLLEDGGEAPAALEAALEEKSALEQMRKFLSDPQVHTVLVE
RSTLKEDVGDEGEEEKEFISYNINIDIHYGVKSNSLAFIKRTPVIDADKPVSSQLRVLTLSEDSPYETLHSFISNAVAPF
FKSYIRESGKADRDGDKMAPSVEKKIAELEMGLLHLQQNIEIPEISLPIHPMITNVAKQCYERGEKPKVTDFGDKVEDPT
FLNQLQSGVNRWIREIQKVTKLDRDPASGTALQEISFWLNLERALYRIQEKRESPEVLLTLDILKHGKRFHATVSFDTDT
GLKQALETVNDYNPLMKDFPLNDLLSATELDKIRQALVAIFTHLRKIRNTKYPIQRALRLVEAISRDLSSQLLKVLGTRK
LMHVAYEEFEKVMVACFEVFQTWDDEYEKLQVLLRDIVKRKREENLKMVWRINPAHRKLQARLDQMRKFRRQHEQLRAVI
VRVLRPQVTAVAQQNQGEVPEPQDMKVAEVLFDAADANAIEEVNLAYENVKEVDGLDVSKEGTEAWEAAMKRYDERIDRV
ETRITARLRDQLGTAKNANEMFRIFSRFNALFVRPHIRGAIREYQTQLIQRVKDDIESLHDKFKVQYPQSQACKMSHVRD
LPPVSGSIIWAKQIDRQLTAYMKRVEDVLGKGWENHVEGQKLKQDGDSFRMKLNTQEIFDDWARKVQQRNLGVSGRIFTI
ESTRVRGRTGNVLKLKVNFLPEIITLSKEVRNLKWLGFRVPLAIVNKAHQANQLYPFAISLIESVRTYERTCEKVEERNT
ISLLVAGLKKEVQALIAEGIALVWESYKLDPYVQRLAETVFNFQEKVDDLLIIEEKIDLEVRSLETCMYDHKTFSEILNR
VQKAVDDLNLHSYSNLPIWVNKLDMEIERILGVRLQAGLRAWTQVLLGQAEDKAEVDMDTDAPQVSHKPGGEPKIKNVVH
ELRITNQVIYLNPPIEECRYKLYQEMFAWKMVVLSLPRIQSQRYQVGVHYELTEEEKFYRNALTRMPDGPVALEESYSAV
MGIVSEVEQYVKVWLQYQCLWDMQAENIYNRLGEDLNKWQALLVQIRKARGTFDNAETKKEFGPVVIDYGKVQSKVNLKY
DSWHKEVLSKFGQMLGSNMTEFHSQISKSRQELEQHSVDTASTSDAVTFITYVQSLKRKIKQFEKQVELYRNGQRLLEKQ
RFQFPPSWLYIDNIEGEWGAFNDIMRRKDSAIQQQVANLQMKIVQEDRAVESRTTDLLTDWEKTKPVTGNLRPEEALQAL
TIYEGKFGRLKDDREKCAKAKEALELTDTGLLSGSEERVQVALEELQDLKGVWSELSKVWEQIDQMKEQPWVSVQPRKLR
QNLDALLNQLKSFPARLRQYASYEFVQRLLKGYMKINMLVIELKSEALKDRHWKQLMKRLHVNWVVSELTLGQIWDVDLQ
KNEAIVKDVLLVAQGEMALEEFLKQIREVWNTYELDLVNYQNKCRLIRGWDDLFNKVKEHINSVSAMKLSPYYKVFEEDA
LSWEDKLNRIMALFDVWIDVQRRWVYLEGIFTGSADIKHLLPVETQRFQSISTEFLALMKKVSKSPLVMDVLNIQGVQRS
LERLADLLGKIQKALGEYLERERSSFPRFYFVGDEDLLEIIGNSKNVAKLQKHFKKMFAGVSSIILNEDNSVVLGISSRE
GEEVMFKTPVSITEHPKINEWLTLVEKEMRVTLAKLLAESVTEVEIFGKATSIDPNTYITWIDKYQAQLVVLSAQIAWSE
NVETALSSMGGGGDAAPLHSVLSNVEVTLNVLADSVLMEQPPLRRRKLEHLITELVHQRDVTRSLIKSKIDNAKSFEWLS
QMRFYFDPKQTDVLQQLSIQMANAKFNYGFEYLGVQDKLVQTPLTDRCYLTMTQALEARLGGSPFGPAGTGKTESVKALG
HQLGRFVLVFNCDETFDFQAMGRIFVGLCQVGAWGCFDEFNRLEERMLSAVSQQVQCIQEALREHSNPNYDKTSAPITCE
LLNKQVKVSPDMAIFITMNPGYAGRSNLPDNLKKLFRSLAMTKPDRQLIAQVMLYSQGFRTAEVLANKIVPFFKLCDEQL
SSQSHYDFGLRALKSVLVSAGNVKRERIQKIKREKEERGEAVDEGEIAENLPEQEILIQSVCETMVPKLVAEDIPLLFSL
LSDVFPGVQYHRGEMTALREELKKVCQEMYLTYGDGEEVGGMWVEKVLQLYQITQINHGLMMVGPSGSGKSMAWRVLLKA
LERLEGVEGVAHIIDPKAISKDHLYGTLDPNTREWTDGLFTHVLRKIIDSVRGELQKRQWIVFDGDVDPEWVENLNSVLD
DNKLLTLPNGERLSLPPNVRIMFEVQDLKYATLATVSRCGMVWFSEDVLSTDMIFNNFLARLRSIPLDEGEDEAQRRRKG
KEDEGEEAASPMLQIQRDAATIMQPYFTSNGLVTKALEHAFQLEHIMDLTRLRCLGSLFSMLHQACRNVAQYNANHPDFP
MQIEQLERYIQRYLVYAILWSLSGDSRLKMRAELGEYIRRITTVPLPTAPNIPIIDYEVSISGEWSPWQAKVPQIEVETH
KVAAPDVVVPTLDTVRHEALLYTWLAEHKPLVLCGPPGSGKTMTLFSALRALPDMEVVGLNFSSATTPELLLKTFDHYCE
YRRTPNGVVLAPVQLGKWLVLFCDEINLPDMDKYGTQRVISFIRQMVEHGGFYRTSDQTWVKLERIQFVGACNPPTDPGR
KPLSHRFLRHVPVVYVDYPGPASLTQIYGTFNRAMLRLIPSLRTYAEPLTAAMVEFYTMSQERFTQDTQPHYIYSPREMT
RWVRGIFEALRPLETLPVEGLIRIWAHEALRLFQDRLVEDEERRWTDENIDTVALKHFPNIDREKAMSRPILYSNWLSKD
YIPVDQEELRDYVKARLKVFYEEELDVPLVLFNEVLDHVLRIDRIFRQPQGHLLLIGVSGAGKTTLSRFVAWMNGLSVYQ
IKVHRKYTGEDFDEDLRTVLRRSGCKNEKIAFIMDESNVLDSGFLERMNTLLANGEVPGLFEGDEYATLMTQCKEGAQKE
GLMLDSHEELYKWFTSQVIRNLHVVFTMNPSSEGLKDRAATSPALFNRCVLNWFGDWSTEALYQVGKEFTSKMDLEKPNY
IVPDYMPVVYDKLPQPPSHREAIVNSCVFVHQTLHQANARLAKRGGRTMAITPRHYLDFINHYANLFHEKRSELEEQQMH
LNVGLRKIKETVDQVEELRRDLRIKSQELEVKNAAANDKLKKMVKDQQEAEKKKVMSQEIQEQLHKQQEVIADKQMSVKE
DLDKVEPAVIEAQNAVKSIKKQHLVEVRSMANPPAAVKLALESICLLLGESTTDWKQIRSIIMRENFIPTIVNFSAEEIS
DAIREKMKKNYMSNPSYNYEIVNRASLACGPMVKWAIAQLNYADMLKRVEPLRNELQKLEDDAKDNQQKANEVEQMIRDL
EASIARYKEEYAVLISEAQAIKADLAAVEAKVNRSTALLKSLSAERERWEKTSETFKNQMSTIAGDCLLSAAFIAYAGYF
DQQMRQNLFTTWSHHLQQANIQFRTDIARTEYLSNADERLRWQASSLPADDLCTENAIMLKRFNRYPLIIDPSGQATEFI
MNEYKDRKITRTSFLDDAFRKNLESALRFGNPLLVQDVESYDPVLNPVLNREVRRTGGRVLITLGDQDIDLSPSFVIFLS
TRDPTVEFPPDLCSRVTFVNFTVTRSSLQSQCLNEVLKAERPDVDEKRSDLLKLQGEFQLRLRQLEKSLLQALNEVKGRI
LDDDTIITTLENLKREAAEVTRKVEETDIVMQEVETVSQQYLPLSTACSSIYFTMESLKQIHFLYQYSLQFFLDIYHNVL
YENPNLKGVTDHTQRLSIITKDLFQVAFNRVARGMLHQDHITFAMLLARIKLKGTVGEPTYDAEFQHFLRGNEIVLSAGS
TPRIQGLTVEQAEAVVRLSCLPAFKDLIAKVQADEQFGIWLDSSSPEQTVPYLWSEETPATPIGQAIHRLLLIQAFRPDR
LLAMAHMFVSTNLGESFMSIMEQPLDLTHIVGTEVKPNTPVLMCSVPGYDASGHVEDLAAEQNTQITSIAIGSAEGFNQA
DKAINTAVKSGRWVMLKNVHLAPGWLMQLEKKLHSLQPHACFRLFLTMEINPKVPVNLLRAGRIFVFEPPPGVKANMLRT
FSSIPVSRICKSPNERARLYFLLAWFHAIIQERLRYAPLGWSKKYEFGESDLRSACDTVDTWLDDTAKGRQNISPDKIPW
SALKTLMAQSIYGGRVDNEFDQRLLNTFLERLFTTRSFDSEFKLACKVDGHKDIQMPDGIRREEFVQWVELLPDTQTPSW
LGLPNNAERVLLTTQGVDMISKMLKMQMLEDEDDLAYAETEKKTRTDSTSDGRPAWMRTLHTTASNWLHLIPQTLSHLKR
TVENIKDPLFRFFEREVKMGAKLLQDVRQDLADVVQVCEGKKKQTNYLRTLINELVKGILPRSWSHYTVPAGMTVIQWVS
DFSERIKQLQNISLAAASGGAKELKNIHVCLGGLFVPEAYITATRQYVAQANSWSLEELCLEVNVTTSQGATLDACSFGV
TGLKLQGATCNNNKLSLSNAISTALPLTQLRWVKQTNTEKKASVVTLPVYLNFTRADLIFTVDFEIATKEDPRSFYERGV
AVLCTE
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9BMH 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 4646 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q14204 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  4646 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       4646 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1   AA1 VAL A 1536 ? SER A 1554 ? VAL A 1536 SER A 1554 1 ? 19 
HELX_P HELX_P2   AA2 LEU A 1561 ? SER A 1583 ? LEU A 1561 SER A 1583 1 ? 23 
HELX_P HELX_P3   AA3 LEU A 1587 ? ASN A 1593 ? LEU A 1587 ASN A 1593 1 ? 7  
HELX_P HELX_P4   AA4 GLY A 1596 ? SER A 1625 ? GLY A 1596 SER A 1625 1 ? 30 
HELX_P HELX_P5   AA5 PHE A 1626 ? VAL A 1632 ? PHE A 1626 VAL A 1632 5 ? 7  
HELX_P HELX_P6   AA6 GLY A 1633 ? ASN A 1643 ? GLY A 1633 ASN A 1643 1 ? 11 
HELX_P HELX_P7   AA7 ALA A 1648 ? LYS A 1652 ? ALA A 1648 LYS A 1652 5 ? 5  
HELX_P HELX_P8   AA8 HIS A 1653 ? PHE A 1658 ? HIS A 1653 PHE A 1658 1 ? 6  
HELX_P HELX_P9   AA9 LYS A 1697 ? GLY A 1728 ? LYS A 1697 GLY A 1728 1 ? 32 
HELX_P HELX_P10  AB1 ASP A 1734 ? TYR A 1745 ? ASP A 1734 TYR A 1745 1 ? 12 
HELX_P HELX_P11  AB2 GLN A 1746 ? GLY A 1770 ? GLN A 1746 GLY A 1770 1 ? 25 
HELX_P HELX_P12  AB3 PRO A 1777 ? MET A 1798 ? PRO A 1777 MET A 1798 1 ? 22 
HELX_P HELX_P13  AB4 PRO A 1801 ? LYS A 1829 ? PRO A 1801 LYS A 1829 1 ? 29 
HELX_P HELX_P14  AB5 SER A 1835 ? SER A 1840 ? SER A 1835 SER A 1840 1 ? 6  
HELX_P HELX_P15  AB6 LEU A 1884 ? ALA A 1898 ? LEU A 1884 ALA A 1898 1 ? 15 
HELX_P HELX_P16  AB7 GLY A 1911 ? LEU A 1923 ? GLY A 1911 LEU A 1923 1 ? 13 
HELX_P HELX_P17  AB8 ASP A 1937 ? GLY A 1952 ? ASP A 1937 GLY A 1952 1 ? 16 
HELX_P HELX_P18  AB9 GLU A 1964 ? ASN A 1987 ? GLU A 1964 ASN A 1987 1 ? 24 
HELX_P HELX_P19  AC1 PRO A 2029 ? LYS A 2034 ? PRO A 2029 LYS A 2034 1 ? 6  
HELX_P HELX_P20  AC2 ASP A 2045 ? GLN A 2057 ? ASP A 2045 GLN A 2057 1 ? 13 
HELX_P HELX_P21  AC3 THR A 2061 ? LEU A 2080 ? THR A 2061 LEU A 2080 1 ? 20 
HELX_P HELX_P22  AC4 GLY A 2089 ? ARG A 2118 ? GLY A 2089 ARG A 2118 1 ? 30 
HELX_P HELX_P23  AC5 ASP A 2123 ? ASN A 2130 ? ASP A 2123 ASN A 2130 1 ? 8  
HELX_P HELX_P24  AC6 PRO A 2132 ? MET A 2145 ? PRO A 2132 MET A 2145 1 ? 14 
HELX_P HELX_P25  AC7 VAL A 2146 ? LEU A 2149 ? VAL A 2146 LEU A 2149 5 ? 4  
HELX_P HELX_P26  AC8 ASP A 2153 ? PHE A 2165 ? ASP A 2153 PHE A 2165 1 ? 13 
HELX_P HELX_P27  AC9 MET A 2175 ? MET A 2189 ? MET A 2175 MET A 2189 1 ? 15 
HELX_P HELX_P28  AD1 GLY A 2200 ? ASN A 2217 ? GLY A 2200 ASN A 2217 1 ? 18 
HELX_P HELX_P29  AD2 GLY A 2229 ? GLY A 2246 ? GLY A 2229 GLY A 2246 1 ? 18 
HELX_P HELX_P30  AD3 SER A 2260 ? TYR A 2265 ? SER A 2260 TYR A 2265 1 ? 6  
HELX_P HELX_P31  AD4 GLY A 2278 ? SER A 2290 ? GLY A 2278 SER A 2290 1 ? 13 
HELX_P HELX_P32  AD5 GLY A 2293 ? LYS A 2297 ? GLY A 2293 LYS A 2297 5 ? 5  
HELX_P HELX_P33  AD6 TRP A 2311 ? ASN A 2316 ? TRP A 2311 ASN A 2316 5 ? 6  
HELX_P HELX_P34  AD7 THR A 2352 ? SER A 2357 ? THR A 2352 SER A 2357 1 ? 6  
HELX_P HELX_P35  AD8 SER A 2370 ? ILE A 2385 ? SER A 2370 ILE A 2385 1 ? 16 
HELX_P HELX_P36  AD9 PRO A 2411 ? GLN A 2424 ? PRO A 2411 GLN A 2424 1 ? 14 
HELX_P HELX_P37  AE1 PRO A 2425 ? THR A 2428 ? PRO A 2425 THR A 2428 5 ? 4  
HELX_P HELX_P38  AE2 GLY A 2431 ? PHE A 2441 ? GLY A 2431 PHE A 2441 1 ? 11 
HELX_P HELX_P39  AE3 THR A 2450 ? HIS A 2476 ? THR A 2450 HIS A 2476 1 ? 27 
HELX_P HELX_P40  AE4 GLN A 2482 ? SER A 2503 ? GLN A 2482 SER A 2503 1 ? 22 
HELX_P HELX_P41  AE5 ARG A 2507 ? THR A 2522 ? ARG A 2507 THR A 2522 1 ? 16 
HELX_P HELX_P42  AE6 PRO A 2533 ? ILE A 2535 ? PRO A 2533 ILE A 2535 5 ? 3  
HELX_P HELX_P43  AE7 GLN A 2549 ? VAL A 2552 ? GLN A 2549 VAL A 2552 5 ? 4  
HELX_P HELX_P44  AE8 GLU A 2558 ? VAL A 2562 ? GLU A 2558 VAL A 2562 5 ? 5  
HELX_P HELX_P45  AE9 THR A 2571 ? GLU A 2587 ? THR A 2571 GLU A 2587 1 ? 17 
HELX_P HELX_P46  AF1 GLY A 2600 ? ARG A 2610 ? GLY A 2600 ARG A 2610 1 ? 11 
HELX_P HELX_P47  AF2 THR A 2627 ? TYR A 2638 ? THR A 2627 TYR A 2638 1 ? 12 
HELX_P HELX_P48  AF3 GLN A 2677 ? HIS A 2689 ? GLN A 2677 HIS A 2689 1 ? 13 
HELX_P HELX_P49  AF4 SER A 2724 ? ARG A 2729 ? SER A 2724 ARG A 2729 1 ? 6  
HELX_P HELX_P50  AF5 GLY A 2740 ? LEU A 2756 ? GLY A 2740 LEU A 2756 1 ? 17 
HELX_P HELX_P51  AF6 ARG A 2757 ? LEU A 2758 ? ARG A 2757 LEU A 2758 5 ? 2  
HELX_P HELX_P52  AF7 ILE A 2759 ? THR A 2764 ? ILE A 2759 THR A 2764 5 ? 6  
HELX_P HELX_P53  AF8 TYR A 2765 ? PHE A 2784 ? TYR A 2765 PHE A 2784 1 ? 20 
HELX_P HELX_P54  AF9 SER A 2795 ? ARG A 2811 ? SER A 2795 ARG A 2811 1 ? 17 
HELX_P HELX_P55  AG1 PRO A 2817 ? GLN A 2834 ? PRO A 2817 GLN A 2834 1 ? 18 
HELX_P HELX_P56  AG2 GLU A 2839 ? PHE A 2858 ? GLU A 2839 PHE A 2858 1 ? 20 
HELX_P HELX_P57  AG3 ASP A 2862 ? SER A 2868 ? ASP A 2862 SER A 2868 1 ? 7  
HELX_P HELX_P58  AG4 ASP A 2885 ? GLU A 2904 ? ASP A 2885 GLU A 2904 1 ? 20 
HELX_P HELX_P59  AG5 PHE A 2912 ? ARG A 2927 ? PHE A 2912 ARG A 2927 1 ? 16 
HELX_P HELX_P60  AG6 GLY A 2942 ? ASN A 2954 ? GLY A 2942 ASN A 2954 1 ? 13 
HELX_P HELX_P61  AG7 THR A 2968 ? CYS A 2985 ? THR A 2968 CYS A 2985 1 ? 18 
HELX_P HELX_P62  AG8 SER A 2997 ? VAL A 2999 ? SER A 2997 VAL A 2999 5 ? 3  
HELX_P HELX_P63  AG9 ASP A 3001 ? GLY A 3015 ? ASP A 3001 GLY A 3015 1 ? 15 
HELX_P HELX_P64  AH1 GLY A 3023 ? GLY A 3041 ? GLY A 3023 GLY A 3041 1 ? 19 
HELX_P HELX_P65  AH2 SER A 3046 ? ASN A 3061 ? SER A 3046 ASN A 3061 1 ? 16 
HELX_P HELX_P66  AH3 SER A 3071 ? SER A 3082 ? SER A 3071 SER A 3082 1 ? 12 
HELX_P HELX_P67  AH4 PRO A 3083 ? ARG A 3088 ? PRO A 3083 ARG A 3088 1 ? 6  
HELX_P HELX_P68  AH5 SER A 3098 ? THR A 3110 ? SER A 3098 THR A 3110 1 ? 13 
HELX_P HELX_P69  AH6 SER A 3138 ? ARG A 3164 ? SER A 3138 ARG A 3164 1 ? 27 
HELX_P HELX_P70  AH7 THR A 3172 ? LYS A 3241 ? THR A 3172 LYS A 3241 1 ? 70 
HELX_P HELX_P71  AH8 GLU A 3450 ? LEU A 3482 ? GLU A 3450 LEU A 3482 1 ? 33 
HELX_P HELX_P72  AH9 LEU A 3482 ? THR A 3495 ? LEU A 3482 THR A 3495 1 ? 14 
HELX_P HELX_P73  AI1 THR A 3495 ? ALA A 3517 ? THR A 3495 ALA A 3517 1 ? 23 
HELX_P HELX_P74  AI2 ASP A 3521 ? ALA A 3539 ? ASP A 3521 ALA A 3539 1 ? 19 
HELX_P HELX_P75  AI3 ALA A 3548 ? LEU A 3553 ? ALA A 3548 LEU A 3553 1 ? 6  
HELX_P HELX_P76  AI4 ASN A 3555 ? SER A 3565 ? ASN A 3555 SER A 3565 1 ? 11 
HELX_P HELX_P77  AI5 ASP A 3570 ? ARG A 3582 ? ASP A 3570 ARG A 3582 1 ? 13 
HELX_P HELX_P78  AI6 GLY A 3594 ? TYR A 3604 ? GLY A 3594 TYR A 3604 1 ? 11 
HELX_P HELX_P79  AI7 ALA A 3618 ? GLY A 3630 ? ALA A 3618 GLY A 3630 1 ? 13 
HELX_P HELX_P80  AI8 ASP A 3637 ? TYR A 3641 ? ASP A 3637 TYR A 3641 5 ? 5  
HELX_P HELX_P81  AI9 ASP A 3642 ? VAL A 3644 ? ASP A 3642 VAL A 3644 5 ? 3  
HELX_P HELX_P82  AJ1 LEU A 3645 ? ARG A 3651 ? LEU A 3645 ARG A 3651 1 ? 7  
HELX_P HELX_P83  AJ2 PRO A 3689 ? VAL A 3696 ? PRO A 3689 VAL A 3696 1 ? 8  
HELX_P HELX_P84  AJ3 THR A 3704 ? ARG A 3721 ? THR A 3704 ARG A 3721 1 ? 18 
HELX_P HELX_P85  AJ4 ARG A 3721 ? VAL A 3756 ? ARG A 3721 VAL A 3756 1 ? 36 
HELX_P HELX_P86  AJ5 ASP A 3763 ? GLN A 3799 ? ASP A 3763 GLN A 3799 1 ? 37 
HELX_P HELX_P87  AJ6 TYR A 3801 ? SER A 3817 ? TYR A 3801 SER A 3817 1 ? 17 
HELX_P HELX_P88  AJ7 LEU A 3818 ? ILE A 3821 ? LEU A 3818 ILE A 3821 5 ? 4  
HELX_P HELX_P89  AJ8 SER A 3828 ? TYR A 3841 ? SER A 3828 TYR A 3841 1 ? 14 
HELX_P HELX_P90  AJ9 ASN A 3843 ? LYS A 3847 ? ASN A 3843 LYS A 3847 5 ? 5  
HELX_P HELX_P91  AK1 ASP A 3851 ? ARG A 3873 ? ASP A 3851 ARG A 3873 1 ? 23 
HELX_P HELX_P92  AK2 GLY A 3874 ? MET A 3875 ? GLY A 3874 MET A 3875 5 ? 2  
HELX_P HELX_P93  AK3 LEU A 3876 ? GLN A 3878 ? LEU A 3876 GLN A 3878 5 ? 3  
HELX_P HELX_P94  AK4 ASP A 3879 ? GLY A 3894 ? ASP A 3879 GLY A 3894 1 ? 16 
HELX_P HELX_P95  AK5 TYR A 3901 ? GLY A 3911 ? TYR A 3901 GLY A 3911 1 ? 11 
HELX_P HELX_P96  AK6 THR A 3928 ? SER A 3939 ? THR A 3928 SER A 3939 1 ? 12 
HELX_P HELX_P97  AK7 CYS A 3940 ? LYS A 3945 ? CYS A 3940 LYS A 3945 5 ? 6  
HELX_P HELX_P98  AK8 LEU A 3947 ? ASP A 3954 ? LEU A 3947 ASP A 3954 1 ? 8  
HELX_P HELX_P99  AK9 GLN A 3956 ? ASP A 3962 ? GLN A 3956 ASP A 3962 1 ? 7  
HELX_P HELX_P100 AL1 SER A 3965 ? VAL A 3970 ? SER A 3965 VAL A 3970 5 ? 6  
HELX_P HELX_P101 AL2 THR A 3981 ? ARG A 3997 ? THR A 3981 ARG A 3997 1 ? 17 
HELX_P HELX_P102 AL3 ARG A 4000 ? GLY A 4014 ? ARG A 4000 GLY A 4014 1 ? 15 
HELX_P HELX_P103 AL4 ASP A 4026 ? THR A 4033 ? ASP A 4026 THR A 4033 1 ? 8  
HELX_P HELX_P104 AL5 ALA A 4051 ? GLN A 4062 ? ALA A 4051 GLN A 4062 1 ? 12 
HELX_P HELX_P105 AL6 SER A 4073 ? GLY A 4091 ? SER A 4073 GLY A 4091 1 ? 19 
HELX_P HELX_P106 AL7 VAL A 4099 ? LEU A 4101 ? VAL A 4099 LEU A 4101 5 ? 3  
HELX_P HELX_P107 AL8 ALA A 4102 ? SER A 4115 ? ALA A 4102 SER A 4115 1 ? 14 
HELX_P HELX_P108 AL9 PRO A 4135 ? GLY A 4142 ? PRO A 4135 GLY A 4142 1 ? 8  
HELX_P HELX_P109 AM1 GLY A 4152 ? ILE A 4164 ? GLY A 4152 ILE A 4164 1 ? 13 
HELX_P HELX_P110 AM2 PRO A 4165 ? CYS A 4170 ? PRO A 4165 CYS A 4170 1 ? 6  
HELX_P HELX_P111 AM3 ASN A 4174 ? ARG A 4193 ? ASN A 4174 ARG A 4193 1 ? 20 
HELX_P HELX_P112 AM4 TYR A 4196 ? TRP A 4201 ? TYR A 4196 TRP A 4201 1 ? 6  
HELX_P HELX_P113 AM5 GLY A 4208 ? ALA A 4227 ? GLY A 4208 ALA A 4227 1 ? 20 
HELX_P HELX_P114 AM6 PRO A 4239 ? SER A 4250 ? PRO A 4239 SER A 4250 1 ? 12 
HELX_P HELX_P115 AM7 ASN A 4258 ? PHE A 4273 ? ASN A 4258 PHE A 4273 1 ? 16 
HELX_P HELX_P116 AM8 THR A 4274 ? ASP A 4279 ? THR A 4274 ASP A 4279 5 ? 6  
HELX_P HELX_P117 AM9 ARG A 4301 ? LEU A 4311 ? ARG A 4301 LEU A 4311 1 ? 11 
HELX_P HELX_P118 AN1 THR A 4317 ? GLY A 4322 ? THR A 4317 GLY A 4322 5 ? 6  
HELX_P HELX_P119 AN2 PRO A 4324 ? ALA A 4327 ? PRO A 4324 ALA A 4327 5 ? 4  
HELX_P HELX_P120 AN3 GLU A 4328 ? MET A 4346 ? GLU A 4328 MET A 4346 1 ? 19 
HELX_P HELX_P121 AN4 ALA A 4375 ? ILE A 4391 ? ALA A 4375 ILE A 4391 1 ? 17 
HELX_P HELX_P122 AN5 THR A 4401 ? LYS A 4406 ? THR A 4401 LYS A 4406 1 ? 6  
HELX_P HELX_P123 AN6 ASP A 4407 ? GLU A 4439 ? ASP A 4407 GLU A 4439 1 ? 33 
HELX_P HELX_P124 AN7 THR A 4445 ? GLY A 4458 ? THR A 4445 GLY A 4458 1 ? 14 
HELX_P HELX_P125 AN8 THR A 4474 ? GLY A 4499 ? THR A 4474 GLY A 4499 1 ? 26 
HELX_P HELX_P126 AN9 LYS A 4502 ? ASN A 4506 ? LYS A 4502 ASN A 4506 5 ? 5  
HELX_P HELX_P127 AO1 GLY A 4512 ? LEU A 4514 ? GLY A 4512 LEU A 4514 5 ? 3  
HELX_P HELX_P128 AO2 VAL A 4516 ? SER A 4533 ? VAL A 4516 SER A 4533 1 ? 18 
HELX_P HELX_P129 AO3 SER A 4535 ? GLU A 4537 ? SER A 4535 GLU A 4537 5 ? 3  
HELX_P HELX_P130 AO4 ASP A 4631 ? ARG A 4638 ? ASP A 4631 ARG A 4638 1 ? 8  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A THR 1913 OG1 ? ? ? 1_555 G MG . MG ? ? A THR 1913 A MG 4706 1_555 ? ? ? ? ? ? ? 1.978 ? ? 
metalc2 metalc ? ? A GLU 2344 OE1 ? ? ? 1_555 F MG . MG ? ? A GLU 2344 A MG 4705 1_555 ? ? ? ? ? ? ? 2.850 ? ? 
metalc3 metalc ? ? B AOV .    O2B ? ? ? 1_555 G MG . MG ? ? A AOV 4701 A MG 4706 1_555 ? ? ? ? ? ? ? 2.634 ? ? 
metalc4 metalc ? ? B AOV .    O3B ? ? ? 1_555 G MG . MG ? ? A AOV 4701 A MG 4706 1_555 ? ? ? ? ? ? ? 2.265 ? ? 
metalc5 metalc ? ? C ATP .    O2G ? ? ? 1_555 F MG . MG ? ? A ATP 4702 A MG 4705 1_555 ? ? ? ? ? ? ? 2.588 ? ? 
metalc6 metalc ? ? C ATP .    O2B ? ? ? 1_555 F MG . MG ? ? A ATP 4702 A MG 4705 1_555 ? ? ? ? ? ? ? 2.006 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 OG1 ? A THR 1913 ? A THR 1913 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O2B ? B AOV . ? A AOV 4701 ? 1_555 82.5  ? 
2 OG1 ? A THR 1913 ? A THR 1913 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O3B ? B AOV . ? A AOV 4701 ? 1_555 139.6 ? 
3 O2B ? B AOV .    ? A AOV 4701 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O3B ? B AOV . ? A AOV 4701 ? 1_555 57.2  ? 
4 OE1 ? A GLU 2344 ? A GLU 2344 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 O2G ? C ATP . ? A ATP 4702 ? 1_555 148.8 ? 
5 OE1 ? A GLU 2344 ? A GLU 2344 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 O2B ? C ATP . ? A ATP 4702 ? 1_555 128.0 ? 
6 O2G ? C ATP .    ? A ATP 4702 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 O2B ? C ATP . ? A ATP 4702 ? 1_555 65.0  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
AA4 ? 3 ? 
AA5 ? 2 ? 
AA6 ? 5 ? 
AA7 ? 2 ? 
AA8 ? 2 ? 
AA9 ? 2 ? 
AB1 ? 5 ? 
AB2 ? 4 ? 
AB3 ? 5 ? 
AB4 ? 5 ? 
AB5 ? 3 ? 
AB6 ? 5 ? 
AB7 ? 2 ? 
AB8 ? 4 ? 
AB9 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA5 1 2 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? parallel      
AA6 3 4 ? parallel      
AA6 4 5 ? parallel      
AA7 1 2 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AB1 1 2 ? parallel      
AB1 2 3 ? parallel      
AB1 3 4 ? parallel      
AB1 4 5 ? parallel      
AB2 1 2 ? anti-parallel 
AB2 2 3 ? parallel      
AB2 3 4 ? anti-parallel 
AB3 1 2 ? parallel      
AB3 2 3 ? parallel      
AB3 3 4 ? parallel      
AB3 4 5 ? parallel      
AB4 1 2 ? parallel      
AB4 2 3 ? parallel      
AB4 3 4 ? parallel      
AB4 4 5 ? parallel      
AB5 1 2 ? anti-parallel 
AB5 2 3 ? anti-parallel 
AB6 1 2 ? parallel      
AB6 2 3 ? parallel      
AB6 3 4 ? parallel      
AB6 4 5 ? parallel      
AB7 1 2 ? anti-parallel 
AB8 1 2 ? parallel      
AB8 2 3 ? anti-parallel 
AB8 3 4 ? anti-parallel 
AB9 1 2 ? anti-parallel 
AB9 2 3 ? parallel      
AB9 3 4 ? anti-parallel 
AB9 4 5 ? parallel      
AB9 5 6 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 SER A 1663 ? LEU A 1666 ? SER A 1663 LEU A 1666 
AA1 2 VAL A 1672 ? SER A 1677 ? VAL A 1672 SER A 1677 
AA1 3 GLU A 1683 ? SER A 1691 ? GLU A 1683 SER A 1691 
AA2 1 MET A 1842 ? PHE A 1846 ? MET A 1842 PHE A 1846 
AA2 2 LEU A 1857 ? MET A 1861 ? LEU A 1857 MET A 1861 
AA2 3 ALA A 1864 ? ASN A 1867 ? ALA A 1864 ASN A 1867 
AA3 1 GLY A 1901 ? PHE A 1905 ? GLY A 1901 PHE A 1905 
AA3 2 PHE A 2036 ? ALA A 2040 ? PHE A 2036 ALA A 2040 
AA4 1 VAL A 1927 ? ASN A 1931 ? VAL A 1927 ASN A 1931 
AA4 2 TRP A 1954 ? ASP A 1958 ? TRP A 1954 ASP A 1958 
AA4 3 ALA A 2013 ? THR A 2017 ? ALA A 2013 THR A 2017 
AA5 1 THR A 1998 ? GLU A 2000 ? THR A 1998 GLU A 2000 
AA5 2 GLN A 2005 ? LYS A 2007 ? GLN A 2005 LYS A 2007 
AA6 1 GLY A 2249 ? ILE A 2254 ? GLY A 2249 ILE A 2254 
AA6 2 ARG A 2298 ? ASP A 2304 ? ARG A 2298 ASP A 2304 
AA6 3 VAL A 2339 ? VAL A 2345 ? VAL A 2339 VAL A 2345 
AA6 4 GLY A 2219 ? VAL A 2223 ? GLY A 2219 VAL A 2223 
AA6 5 GLY A 2360 ? TRP A 2363 ? GLY A 2360 TRP A 2363 
AA7 1 GLY A 2266 ? LEU A 2268 ? GLY A 2266 LEU A 2268 
AA7 2 TRP A 2275 ? ASP A 2277 ? TRP A 2275 ASP A 2277 
AA8 1 LEU A 2324 ? THR A 2326 ? LEU A 2324 THR A 2326 
AA8 2 ARG A 2332 ? SER A 2334 ? ARG A 2332 SER A 2334 
AA9 1 TYR A 2537 ? VAL A 2539 ? TYR A 2537 VAL A 2539 
AA9 2 TRP A 2545 ? PRO A 2547 ? TRP A 2545 PRO A 2547 
AB1 1 MET A 2615 ? LEU A 2620 ? MET A 2615 LEU A 2620 
AB1 2 TRP A 2658 ? CYS A 2663 ? TRP A 2658 CYS A 2663 
AB1 3 ILE A 2706 ? CYS A 2712 ? ILE A 2706 CYS A 2712 
AB1 4 LEU A 2591 ? CYS A 2594 ? LEU A 2591 CYS A 2594 
AB1 5 VAL A 2733 ? TYR A 2735 ? VAL A 2733 TYR A 2735 
AB2 1 CYS A 2639 ? THR A 2644 ? CYS A 2639 THR A 2644 
AB2 2 GLY A 2647 ? PRO A 2652 ? GLY A 2647 PRO A 2652 
AB2 3 THR A 2699 ? LEU A 2703 ? THR A 2699 LEU A 2703 
AB2 4 GLY A 2691 ? ARG A 2694 ? GLY A 2691 ARG A 2694 
AB3 1 SER A 2957 ? TYR A 2959 ? SER A 2957 TYR A 2959 
AB3 2 ILE A 2990 ? ASP A 2995 ? ILE A 2990 ASP A 2995 
AB3 3 LEU A 3062 ? MET A 3068 ? LEU A 3062 MET A 3068 
AB3 4 HIS A 2932 ? ILE A 2936 ? HIS A 2932 ILE A 2936 
AB3 5 CYS A 3089 ? TRP A 3093 ? CYS A 3089 TRP A 3093 
AB4 1 THR A 3610 ? THR A 3612 ? THR A 3610 THR A 3612 
AB4 2 PRO A 3632 ? VAL A 3635 ? PRO A 3632 VAL A 3635 
AB4 3 VAL A 3676 ? THR A 3681 ? VAL A 3676 THR A 3681 
AB4 4 PRO A 3587 ? ILE A 3590 ? PRO A 3587 ILE A 3590 
AB4 5 THR A 3697 ? ASN A 3700 ? THR A 3697 ASN A 3700 
AB5 1 ARG A 3654 ? THR A 3656 ? ARG A 3654 THR A 3656 
AB5 2 ARG A 3659 ? LEU A 3664 ? ARG A 3659 LEU A 3664 
AB5 3 GLN A 3667 ? ASP A 3670 ? GLN A 3667 ASP A 3670 
AB6 1 ILE A 4066 ? ALA A 4070 ? ILE A 4066 ALA A 4070 
AB6 2 TRP A 4093 ? LYS A 4097 ? TRP A 4093 LYS A 4097 
AB6 3 ARG A 4123 ? GLU A 4129 ? ARG A 4123 GLU A 4129 
AB6 4 VAL A 4041 ? SER A 4045 ? VAL A 4041 SER A 4045 
AB6 5 ARG A 4143 ? ILE A 4144 ? ARG A 4143 ILE A 4144 
AB7 1 LYS A 4283 ? ASP A 4289 ? LYS A 4283 ASP A 4289 
AB7 2 LYS A 4292 ? GLN A 4295 ? LYS A 4292 GLN A 4295 
AB8 1 VAL A 4509 ? CYS A 4510 ? VAL A 4509 CYS A 4510 
AB8 2 SER A 4557 ? THR A 4561 ? SER A 4557 THR A 4561 
AB8 3 LEU A 4587 ? LYS A 4594 ? LEU A 4587 LYS A 4594 
AB8 4 LEU A 4539 ? THR A 4546 ? LEU A 4539 THR A 4546 
AB9 1 LYS A 4564 ? ASN A 4571 ? LYS A 4564 ASN A 4571 
AB9 2 LYS A 4574 ? ALA A 4584 ? LYS A 4574 ALA A 4584 
AB9 3 LEU A 4618 ? ILE A 4626 ? LEU A 4618 ILE A 4626 
AB9 4 VAL A 4604 ? TYR A 4610 ? VAL A 4604 TYR A 4610 
AB9 5 ALA A 4641 ? LEU A 4643 ? ALA A 4641 LEU A 4643 
AB9 6 LYS A 4564 ? ASN A 4571 ? LYS A 4564 ASN A 4571 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ILE A 1665 ? N ILE A 1665 O GLY A 1675 ? O GLY A 1675 
AA1 2 3 N VAL A 1673 ? N VAL A 1673 O VAL A 1690 ? O VAL A 1690 
AA2 1 2 N ARG A 1843 ? N ARG A 1843 O GLN A 1860 ? O GLN A 1860 
AA2 2 3 N ILE A 1859 ? N ILE A 1859 O PHE A 1866 ? O PHE A 1866 
AA3 1 2 N PHE A 1905 ? N PHE A 1905 O LEU A 2039 ? O LEU A 2039 
AA4 1 2 N LEU A 1928 ? N LEU A 1928 O TRP A 1954 ? O TRP A 1954 
AA4 2 3 N PHE A 1957 ? N PHE A 1957 O PHE A 2015 ? O PHE A 2015 
AA5 1 2 N CYS A 1999 ? N CYS A 1999 O VAL A 2006 ? O VAL A 2006 
AA6 1 2 N ILE A 2254 ? N ILE A 2254 O VAL A 2302 ? O VAL A 2302 
AA6 2 3 N PHE A 2303 ? N PHE A 2303 O MET A 2342 ? O MET A 2342 
AA6 3 4 O PHE A 2343 ? O PHE A 2343 N MET A 2222 ? N MET A 2222 
AA6 4 5 N GLY A 2219 ? N GLY A 2219 O GLY A 2360 ? O GLY A 2360 
AA7 1 2 N THR A 2267 ? N THR A 2267 O THR A 2276 ? O THR A 2276 
AA8 1 2 N LEU A 2325 ? N LEU A 2325 O LEU A 2333 ? O LEU A 2333 
AA9 1 2 N GLU A 2538 ? N GLU A 2538 O SER A 2546 ? O SER A 2546 
AB1 1 2 N LEU A 2620 ? N LEU A 2620 O PHE A 2662 ? O PHE A 2662 
AB1 2 3 N LEU A 2659 ? N LEU A 2659 O GLN A 2707 ? O GLN A 2707 
AB1 3 4 O GLY A 2710 ? O GLY A 2710 N LEU A 2591 ? N LEU A 2591 
AB1 4 5 N CYS A 2594 ? N CYS A 2594 O VAL A 2734 ? O VAL A 2734 
AB2 1 2 N ARG A 2642 ? N ARG A 2642 O VAL A 2649 ? O VAL A 2649 
AB2 2 3 N VAL A 2648 ? N VAL A 2648 O LYS A 2702 ? O LYS A 2702 
AB2 3 4 O VAL A 2701 ? O VAL A 2701 N PHE A 2692 ? N PHE A 2692 
AB3 1 2 N SER A 2957 ? N SER A 2957 O ALA A 2991 ? O ALA A 2991 
AB3 2 3 N PHE A 2992 ? N PHE A 2992 O HIS A 3063 ? O HIS A 3063 
AB3 3 4 O VAL A 3064 ? O VAL A 3064 N LEU A 2933 ? N LEU A 2933 
AB3 4 5 N LEU A 2934 ? N LEU A 2934 O ASN A 3092 ? O ASN A 3092 
AB4 1 2 N THR A 3612 ? N THR A 3612 O LEU A 3634 ? O LEU A 3634 
AB4 2 3 N VAL A 3635 ? N VAL A 3635 O SER A 3680 ? O SER A 3680 
AB4 3 4 O LEU A 3679 ? O LEU A 3679 N ILE A 3589 ? N ILE A 3589 
AB4 4 5 N LEU A 3588 ? N LEU A 3588 O THR A 3697 ? O THR A 3697 
AB5 1 2 N ARG A 3654 ? N ARG A 3654 O LEU A 3661 ? O LEU A 3661 
AB5 2 3 N ILE A 3662 ? N ILE A 3662 O ILE A 3669 ? O ILE A 3669 
AB6 1 2 N ILE A 4069 ? N ILE A 4069 O LYS A 4097 ? O LYS A 4097 
AB6 2 3 N LEU A 4096 ? N LEU A 4096 O PHE A 4125 ? O PHE A 4125 
AB6 3 4 O LEU A 4124 ? O LEU A 4124 N VAL A 4041 ? N VAL A 4041 
AB6 4 5 N LEU A 4042 ? N LEU A 4042 O ARG A 4143 ? O ARG A 4143 
AB7 1 2 N ALA A 4285 ? N ALA A 4285 O ILE A 4294 ? O ILE A 4294 
AB8 1 2 N VAL A 4509 ? N VAL A 4509 O THR A 4561 ? O THR A 4561 
AB8 2 3 N VAL A 4560 ? N VAL A 4560 O THR A 4588 ? O THR A 4588 
AB8 3 4 O VAL A 4593 ? O VAL A 4593 N CYS A 4540 ? N CYS A 4540 
AB9 1 2 N LEU A 4565 ? N LEU A 4565 O THR A 4583 ? O THR A 4583 
AB9 2 3 N LEU A 4575 ? N LEU A 4575 O GLU A 4625 ? O GLU A 4625 
AB9 3 4 O PHE A 4624 ? O PHE A 4624 N VAL A 4605 ? N VAL A 4605 
AB9 4 5 N PRO A 4608 ? N PRO A 4608 O VAL A 4642 ? O VAL A 4642 
AB9 5 6 O LEU A 4643 ? O LEU A 4643 N LYS A 4564 ? N LYS A 4564 
# 
_pdbx_entry_details.entry_id                   9BMH 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OG  A SER 2231 ? ? MG  A MG  4705 ? ? 1.52 
2 1 OE2 A GLU 2344 ? ? MG  A MG  4705 ? ? 1.54 
3 1 OH  A TYR 3972 ? ? OE1 A GLU 3976 ? ? 2.13 
4 1 OH  A TYR 2967 ? ? OD2 A ASP 2975 ? ? 2.15 
5 1 OE2 A GLU 3639 ? ? NZ  A LYS 4111 ? ? 2.16 
6 1 OE1 A GLU 2688 ? ? NE2 A HIS 2730 ? ? 2.18 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 N A PRO 1883 ? ? CA A PRO 1883 ? ? CB A PRO 1883 ? ? 95.98 103.30 -7.32 1.20 N 
2 1 N A PRO 2020 ? ? CA A PRO 2020 ? ? CB A PRO 2020 ? ? 94.55 103.30 -8.75 1.20 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 PHE A 1626 ? ? 52.81   74.13   
2  1 LYS A 1729 ? ? 39.47   42.30   
3  1 ALA A 1862 ? ? 57.77   -119.25 
4  1 PRO A 1883 ? ? -53.26  -4.41   
5  1 PRO A 1907 ? ? -76.46  -161.60 
6  1 ASN A 2019 ? ? -112.92 79.23   
7  1 PHE A 2165 ? ? -114.11 72.71   
8  1 PRO A 2309 ? ? -66.76  3.34    
9  1 ASP A 2320 ? ? -107.89 -150.10 
10 1 LYS A 2673 ? ? -67.25  2.25    
11 1 VAL A 2838 ? ? -91.42  -61.96  
12 1 TYR A 2881 ? ? -90.86  58.18   
13 1 GLU A 2904 ? ? -126.53 -164.09 
14 1 LEU A 2905 ? ? -36.88  128.73  
15 1 PRO A 3643 ? ? -69.27  2.48    
16 1 GLU A 4034 ? ? 69.24   -3.43   
17 1 GLU A 4599 ? ? 59.64   -153.32 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9BMH 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         ? 
_em_3d_fitting.ref_protocol      ? 
# 
_em_3d_reconstruction.entry_id                    9BMH 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  2.8 
_em_3d_reconstruction.resolution_method           'FSC 0.143 CUT-OFF' 
_em_3d_reconstruction.magnification_calibration   ? 
_em_3d_reconstruction.nominal_pixel_size          ? 
_em_3d_reconstruction.actual_pixel_size           ? 
_em_3d_reconstruction.num_particles               248329 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       '25 mM HEPES pH 7.2, 150 mM KCl, 1 mM MgCl2, 5 mM DTT, 5 mM ATPVi' 
_em_buffer.pH            7.2 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 'state-4 of the motor domain from full-length human dynein-1 in 5mM ATPVi' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        9BMH 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'TFS GLACIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           'FEI TITAN KRIOS AUTOGRID HOLDER' 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            200 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      2.7 
_em_imaging.nominal_defocus_min             1200 
_em_imaging.nominal_defocus_max             5000 
_em_imaging.calibrated_defocus_min          3000 
_em_imaging.calibrated_defocus_max          3000 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           45000 
_em_imaging.calibrated_magnification        45000 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            30 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         NITROGEN 
# 
_em_vitrification.entry_id              9BMH 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              100 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   278 
_em_vitrification.instrument            'FEI VITROBOT MARK IV' 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                9BMH 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1    1 Y 1 A MET 1    ? A MET 1    
2    1 Y 1 A SER 2    ? A SER 2    
3    1 Y 1 A GLU 3    ? A GLU 3    
4    1 Y 1 A PRO 4    ? A PRO 4    
5    1 Y 1 A GLY 5    ? A GLY 5    
6    1 Y 1 A GLY 6    ? A GLY 6    
7    1 Y 1 A GLY 7    ? A GLY 7    
8    1 Y 1 A GLY 8    ? A GLY 8    
9    1 Y 1 A GLY 9    ? A GLY 9    
10   1 Y 1 A GLU 10   ? A GLU 10   
11   1 Y 1 A ASP 11   ? A ASP 11   
12   1 Y 1 A GLY 12   ? A GLY 12   
13   1 Y 1 A SER 13   ? A SER 13   
14   1 Y 1 A ALA 14   ? A ALA 14   
15   1 Y 1 A GLY 15   ? A GLY 15   
16   1 Y 1 A LEU 16   ? A LEU 16   
17   1 Y 1 A GLU 17   ? A GLU 17   
18   1 Y 1 A VAL 18   ? A VAL 18   
19   1 Y 1 A SER 19   ? A SER 19   
20   1 Y 1 A ALA 20   ? A ALA 20   
21   1 Y 1 A VAL 21   ? A VAL 21   
22   1 Y 1 A GLN 22   ? A GLN 22   
23   1 Y 1 A ASN 23   ? A ASN 23   
24   1 Y 1 A VAL 24   ? A VAL 24   
25   1 Y 1 A ALA 25   ? A ALA 25   
26   1 Y 1 A ASP 26   ? A ASP 26   
27   1 Y 1 A VAL 27   ? A VAL 27   
28   1 Y 1 A SER 28   ? A SER 28   
29   1 Y 1 A VAL 29   ? A VAL 29   
30   1 Y 1 A LEU 30   ? A LEU 30   
31   1 Y 1 A GLN 31   ? A GLN 31   
32   1 Y 1 A LYS 32   ? A LYS 32   
33   1 Y 1 A HIS 33   ? A HIS 33   
34   1 Y 1 A LEU 34   ? A LEU 34   
35   1 Y 1 A ARG 35   ? A ARG 35   
36   1 Y 1 A LYS 36   ? A LYS 36   
37   1 Y 1 A LEU 37   ? A LEU 37   
38   1 Y 1 A VAL 38   ? A VAL 38   
39   1 Y 1 A PRO 39   ? A PRO 39   
40   1 Y 1 A LEU 40   ? A LEU 40   
41   1 Y 1 A LEU 41   ? A LEU 41   
42   1 Y 1 A LEU 42   ? A LEU 42   
43   1 Y 1 A GLU 43   ? A GLU 43   
44   1 Y 1 A ASP 44   ? A ASP 44   
45   1 Y 1 A GLY 45   ? A GLY 45   
46   1 Y 1 A GLY 46   ? A GLY 46   
47   1 Y 1 A GLU 47   ? A GLU 47   
48   1 Y 1 A ALA 48   ? A ALA 48   
49   1 Y 1 A PRO 49   ? A PRO 49   
50   1 Y 1 A ALA 50   ? A ALA 50   
51   1 Y 1 A ALA 51   ? A ALA 51   
52   1 Y 1 A LEU 52   ? A LEU 52   
53   1 Y 1 A GLU 53   ? A GLU 53   
54   1 Y 1 A ALA 54   ? A ALA 54   
55   1 Y 1 A ALA 55   ? A ALA 55   
56   1 Y 1 A LEU 56   ? A LEU 56   
57   1 Y 1 A GLU 57   ? A GLU 57   
58   1 Y 1 A GLU 58   ? A GLU 58   
59   1 Y 1 A LYS 59   ? A LYS 59   
60   1 Y 1 A SER 60   ? A SER 60   
61   1 Y 1 A ALA 61   ? A ALA 61   
62   1 Y 1 A LEU 62   ? A LEU 62   
63   1 Y 1 A GLU 63   ? A GLU 63   
64   1 Y 1 A GLN 64   ? A GLN 64   
65   1 Y 1 A MET 65   ? A MET 65   
66   1 Y 1 A ARG 66   ? A ARG 66   
67   1 Y 1 A LYS 67   ? A LYS 67   
68   1 Y 1 A PHE 68   ? A PHE 68   
69   1 Y 1 A LEU 69   ? A LEU 69   
70   1 Y 1 A SER 70   ? A SER 70   
71   1 Y 1 A ASP 71   ? A ASP 71   
72   1 Y 1 A PRO 72   ? A PRO 72   
73   1 Y 1 A GLN 73   ? A GLN 73   
74   1 Y 1 A VAL 74   ? A VAL 74   
75   1 Y 1 A HIS 75   ? A HIS 75   
76   1 Y 1 A THR 76   ? A THR 76   
77   1 Y 1 A VAL 77   ? A VAL 77   
78   1 Y 1 A LEU 78   ? A LEU 78   
79   1 Y 1 A VAL 79   ? A VAL 79   
80   1 Y 1 A GLU 80   ? A GLU 80   
81   1 Y 1 A ARG 81   ? A ARG 81   
82   1 Y 1 A SER 82   ? A SER 82   
83   1 Y 1 A THR 83   ? A THR 83   
84   1 Y 1 A LEU 84   ? A LEU 84   
85   1 Y 1 A LYS 85   ? A LYS 85   
86   1 Y 1 A GLU 86   ? A GLU 86   
87   1 Y 1 A ASP 87   ? A ASP 87   
88   1 Y 1 A VAL 88   ? A VAL 88   
89   1 Y 1 A GLY 89   ? A GLY 89   
90   1 Y 1 A ASP 90   ? A ASP 90   
91   1 Y 1 A GLU 91   ? A GLU 91   
92   1 Y 1 A GLY 92   ? A GLY 92   
93   1 Y 1 A GLU 93   ? A GLU 93   
94   1 Y 1 A GLU 94   ? A GLU 94   
95   1 Y 1 A GLU 95   ? A GLU 95   
96   1 Y 1 A LYS 96   ? A LYS 96   
97   1 Y 1 A GLU 97   ? A GLU 97   
98   1 Y 1 A PHE 98   ? A PHE 98   
99   1 Y 1 A ILE 99   ? A ILE 99   
100  1 Y 1 A SER 100  ? A SER 100  
101  1 Y 1 A TYR 101  ? A TYR 101  
102  1 Y 1 A ASN 102  ? A ASN 102  
103  1 Y 1 A ILE 103  ? A ILE 103  
104  1 Y 1 A ASN 104  ? A ASN 104  
105  1 Y 1 A ILE 105  ? A ILE 105  
106  1 Y 1 A ASP 106  ? A ASP 106  
107  1 Y 1 A ILE 107  ? A ILE 107  
108  1 Y 1 A HIS 108  ? A HIS 108  
109  1 Y 1 A TYR 109  ? A TYR 109  
110  1 Y 1 A GLY 110  ? A GLY 110  
111  1 Y 1 A VAL 111  ? A VAL 111  
112  1 Y 1 A LYS 112  ? A LYS 112  
113  1 Y 1 A SER 113  ? A SER 113  
114  1 Y 1 A ASN 114  ? A ASN 114  
115  1 Y 1 A SER 115  ? A SER 115  
116  1 Y 1 A LEU 116  ? A LEU 116  
117  1 Y 1 A ALA 117  ? A ALA 117  
118  1 Y 1 A PHE 118  ? A PHE 118  
119  1 Y 1 A ILE 119  ? A ILE 119  
120  1 Y 1 A LYS 120  ? A LYS 120  
121  1 Y 1 A ARG 121  ? A ARG 121  
122  1 Y 1 A THR 122  ? A THR 122  
123  1 Y 1 A PRO 123  ? A PRO 123  
124  1 Y 1 A VAL 124  ? A VAL 124  
125  1 Y 1 A ILE 125  ? A ILE 125  
126  1 Y 1 A ASP 126  ? A ASP 126  
127  1 Y 1 A ALA 127  ? A ALA 127  
128  1 Y 1 A ASP 128  ? A ASP 128  
129  1 Y 1 A LYS 129  ? A LYS 129  
130  1 Y 1 A PRO 130  ? A PRO 130  
131  1 Y 1 A VAL 131  ? A VAL 131  
132  1 Y 1 A SER 132  ? A SER 132  
133  1 Y 1 A SER 133  ? A SER 133  
134  1 Y 1 A GLN 134  ? A GLN 134  
135  1 Y 1 A LEU 135  ? A LEU 135  
136  1 Y 1 A ARG 136  ? A ARG 136  
137  1 Y 1 A VAL 137  ? A VAL 137  
138  1 Y 1 A LEU 138  ? A LEU 138  
139  1 Y 1 A THR 139  ? A THR 139  
140  1 Y 1 A LEU 140  ? A LEU 140  
141  1 Y 1 A SER 141  ? A SER 141  
142  1 Y 1 A GLU 142  ? A GLU 142  
143  1 Y 1 A ASP 143  ? A ASP 143  
144  1 Y 1 A SER 144  ? A SER 144  
145  1 Y 1 A PRO 145  ? A PRO 145  
146  1 Y 1 A TYR 146  ? A TYR 146  
147  1 Y 1 A GLU 147  ? A GLU 147  
148  1 Y 1 A THR 148  ? A THR 148  
149  1 Y 1 A LEU 149  ? A LEU 149  
150  1 Y 1 A HIS 150  ? A HIS 150  
151  1 Y 1 A SER 151  ? A SER 151  
152  1 Y 1 A PHE 152  ? A PHE 152  
153  1 Y 1 A ILE 153  ? A ILE 153  
154  1 Y 1 A SER 154  ? A SER 154  
155  1 Y 1 A ASN 155  ? A ASN 155  
156  1 Y 1 A ALA 156  ? A ALA 156  
157  1 Y 1 A VAL 157  ? A VAL 157  
158  1 Y 1 A ALA 158  ? A ALA 158  
159  1 Y 1 A PRO 159  ? A PRO 159  
160  1 Y 1 A PHE 160  ? A PHE 160  
161  1 Y 1 A PHE 161  ? A PHE 161  
162  1 Y 1 A LYS 162  ? A LYS 162  
163  1 Y 1 A SER 163  ? A SER 163  
164  1 Y 1 A TYR 164  ? A TYR 164  
165  1 Y 1 A ILE 165  ? A ILE 165  
166  1 Y 1 A ARG 166  ? A ARG 166  
167  1 Y 1 A GLU 167  ? A GLU 167  
168  1 Y 1 A SER 168  ? A SER 168  
169  1 Y 1 A GLY 169  ? A GLY 169  
170  1 Y 1 A LYS 170  ? A LYS 170  
171  1 Y 1 A ALA 171  ? A ALA 171  
172  1 Y 1 A ASP 172  ? A ASP 172  
173  1 Y 1 A ARG 173  ? A ARG 173  
174  1 Y 1 A ASP 174  ? A ASP 174  
175  1 Y 1 A GLY 175  ? A GLY 175  
176  1 Y 1 A ASP 176  ? A ASP 176  
177  1 Y 1 A LYS 177  ? A LYS 177  
178  1 Y 1 A MET 178  ? A MET 178  
179  1 Y 1 A ALA 179  ? A ALA 179  
180  1 Y 1 A PRO 180  ? A PRO 180  
181  1 Y 1 A SER 181  ? A SER 181  
182  1 Y 1 A VAL 182  ? A VAL 182  
183  1 Y 1 A GLU 183  ? A GLU 183  
184  1 Y 1 A LYS 184  ? A LYS 184  
185  1 Y 1 A LYS 185  ? A LYS 185  
186  1 Y 1 A ILE 186  ? A ILE 186  
187  1 Y 1 A ALA 187  ? A ALA 187  
188  1 Y 1 A GLU 188  ? A GLU 188  
189  1 Y 1 A LEU 189  ? A LEU 189  
190  1 Y 1 A GLU 190  ? A GLU 190  
191  1 Y 1 A MET 191  ? A MET 191  
192  1 Y 1 A GLY 192  ? A GLY 192  
193  1 Y 1 A LEU 193  ? A LEU 193  
194  1 Y 1 A LEU 194  ? A LEU 194  
195  1 Y 1 A HIS 195  ? A HIS 195  
196  1 Y 1 A LEU 196  ? A LEU 196  
197  1 Y 1 A GLN 197  ? A GLN 197  
198  1 Y 1 A GLN 198  ? A GLN 198  
199  1 Y 1 A ASN 199  ? A ASN 199  
200  1 Y 1 A ILE 200  ? A ILE 200  
201  1 Y 1 A GLU 201  ? A GLU 201  
202  1 Y 1 A ILE 202  ? A ILE 202  
203  1 Y 1 A PRO 203  ? A PRO 203  
204  1 Y 1 A GLU 204  ? A GLU 204  
205  1 Y 1 A ILE 205  ? A ILE 205  
206  1 Y 1 A SER 206  ? A SER 206  
207  1 Y 1 A LEU 207  ? A LEU 207  
208  1 Y 1 A PRO 208  ? A PRO 208  
209  1 Y 1 A ILE 209  ? A ILE 209  
210  1 Y 1 A HIS 210  ? A HIS 210  
211  1 Y 1 A PRO 211  ? A PRO 211  
212  1 Y 1 A MET 212  ? A MET 212  
213  1 Y 1 A ILE 213  ? A ILE 213  
214  1 Y 1 A THR 214  ? A THR 214  
215  1 Y 1 A ASN 215  ? A ASN 215  
216  1 Y 1 A VAL 216  ? A VAL 216  
217  1 Y 1 A ALA 217  ? A ALA 217  
218  1 Y 1 A LYS 218  ? A LYS 218  
219  1 Y 1 A GLN 219  ? A GLN 219  
220  1 Y 1 A CYS 220  ? A CYS 220  
221  1 Y 1 A TYR 221  ? A TYR 221  
222  1 Y 1 A GLU 222  ? A GLU 222  
223  1 Y 1 A ARG 223  ? A ARG 223  
224  1 Y 1 A GLY 224  ? A GLY 224  
225  1 Y 1 A GLU 225  ? A GLU 225  
226  1 Y 1 A LYS 226  ? A LYS 226  
227  1 Y 1 A PRO 227  ? A PRO 227  
228  1 Y 1 A LYS 228  ? A LYS 228  
229  1 Y 1 A VAL 229  ? A VAL 229  
230  1 Y 1 A THR 230  ? A THR 230  
231  1 Y 1 A ASP 231  ? A ASP 231  
232  1 Y 1 A PHE 232  ? A PHE 232  
233  1 Y 1 A GLY 233  ? A GLY 233  
234  1 Y 1 A ASP 234  ? A ASP 234  
235  1 Y 1 A LYS 235  ? A LYS 235  
236  1 Y 1 A VAL 236  ? A VAL 236  
237  1 Y 1 A GLU 237  ? A GLU 237  
238  1 Y 1 A ASP 238  ? A ASP 238  
239  1 Y 1 A PRO 239  ? A PRO 239  
240  1 Y 1 A THR 240  ? A THR 240  
241  1 Y 1 A PHE 241  ? A PHE 241  
242  1 Y 1 A LEU 242  ? A LEU 242  
243  1 Y 1 A ASN 243  ? A ASN 243  
244  1 Y 1 A GLN 244  ? A GLN 244  
245  1 Y 1 A LEU 245  ? A LEU 245  
246  1 Y 1 A GLN 246  ? A GLN 246  
247  1 Y 1 A SER 247  ? A SER 247  
248  1 Y 1 A GLY 248  ? A GLY 248  
249  1 Y 1 A VAL 249  ? A VAL 249  
250  1 Y 1 A ASN 250  ? A ASN 250  
251  1 Y 1 A ARG 251  ? A ARG 251  
252  1 Y 1 A TRP 252  ? A TRP 252  
253  1 Y 1 A ILE 253  ? A ILE 253  
254  1 Y 1 A ARG 254  ? A ARG 254  
255  1 Y 1 A GLU 255  ? A GLU 255  
256  1 Y 1 A ILE 256  ? A ILE 256  
257  1 Y 1 A GLN 257  ? A GLN 257  
258  1 Y 1 A LYS 258  ? A LYS 258  
259  1 Y 1 A VAL 259  ? A VAL 259  
260  1 Y 1 A THR 260  ? A THR 260  
261  1 Y 1 A LYS 261  ? A LYS 261  
262  1 Y 1 A LEU 262  ? A LEU 262  
263  1 Y 1 A ASP 263  ? A ASP 263  
264  1 Y 1 A ARG 264  ? A ARG 264  
265  1 Y 1 A ASP 265  ? A ASP 265  
266  1 Y 1 A PRO 266  ? A PRO 266  
267  1 Y 1 A ALA 267  ? A ALA 267  
268  1 Y 1 A SER 268  ? A SER 268  
269  1 Y 1 A GLY 269  ? A GLY 269  
270  1 Y 1 A THR 270  ? A THR 270  
271  1 Y 1 A ALA 271  ? A ALA 271  
272  1 Y 1 A LEU 272  ? A LEU 272  
273  1 Y 1 A GLN 273  ? A GLN 273  
274  1 Y 1 A GLU 274  ? A GLU 274  
275  1 Y 1 A ILE 275  ? A ILE 275  
276  1 Y 1 A SER 276  ? A SER 276  
277  1 Y 1 A PHE 277  ? A PHE 277  
278  1 Y 1 A TRP 278  ? A TRP 278  
279  1 Y 1 A LEU 279  ? A LEU 279  
280  1 Y 1 A ASN 280  ? A ASN 280  
281  1 Y 1 A LEU 281  ? A LEU 281  
282  1 Y 1 A GLU 282  ? A GLU 282  
283  1 Y 1 A ARG 283  ? A ARG 283  
284  1 Y 1 A ALA 284  ? A ALA 284  
285  1 Y 1 A LEU 285  ? A LEU 285  
286  1 Y 1 A TYR 286  ? A TYR 286  
287  1 Y 1 A ARG 287  ? A ARG 287  
288  1 Y 1 A ILE 288  ? A ILE 288  
289  1 Y 1 A GLN 289  ? A GLN 289  
290  1 Y 1 A GLU 290  ? A GLU 290  
291  1 Y 1 A LYS 291  ? A LYS 291  
292  1 Y 1 A ARG 292  ? A ARG 292  
293  1 Y 1 A GLU 293  ? A GLU 293  
294  1 Y 1 A SER 294  ? A SER 294  
295  1 Y 1 A PRO 295  ? A PRO 295  
296  1 Y 1 A GLU 296  ? A GLU 296  
297  1 Y 1 A VAL 297  ? A VAL 297  
298  1 Y 1 A LEU 298  ? A LEU 298  
299  1 Y 1 A LEU 299  ? A LEU 299  
300  1 Y 1 A THR 300  ? A THR 300  
301  1 Y 1 A LEU 301  ? A LEU 301  
302  1 Y 1 A ASP 302  ? A ASP 302  
303  1 Y 1 A ILE 303  ? A ILE 303  
304  1 Y 1 A LEU 304  ? A LEU 304  
305  1 Y 1 A LYS 305  ? A LYS 305  
306  1 Y 1 A HIS 306  ? A HIS 306  
307  1 Y 1 A GLY 307  ? A GLY 307  
308  1 Y 1 A LYS 308  ? A LYS 308  
309  1 Y 1 A ARG 309  ? A ARG 309  
310  1 Y 1 A PHE 310  ? A PHE 310  
311  1 Y 1 A HIS 311  ? A HIS 311  
312  1 Y 1 A ALA 312  ? A ALA 312  
313  1 Y 1 A THR 313  ? A THR 313  
314  1 Y 1 A VAL 314  ? A VAL 314  
315  1 Y 1 A SER 315  ? A SER 315  
316  1 Y 1 A PHE 316  ? A PHE 316  
317  1 Y 1 A ASP 317  ? A ASP 317  
318  1 Y 1 A THR 318  ? A THR 318  
319  1 Y 1 A ASP 319  ? A ASP 319  
320  1 Y 1 A THR 320  ? A THR 320  
321  1 Y 1 A GLY 321  ? A GLY 321  
322  1 Y 1 A LEU 322  ? A LEU 322  
323  1 Y 1 A LYS 323  ? A LYS 323  
324  1 Y 1 A GLN 324  ? A GLN 324  
325  1 Y 1 A ALA 325  ? A ALA 325  
326  1 Y 1 A LEU 326  ? A LEU 326  
327  1 Y 1 A GLU 327  ? A GLU 327  
328  1 Y 1 A THR 328  ? A THR 328  
329  1 Y 1 A VAL 329  ? A VAL 329  
330  1 Y 1 A ASN 330  ? A ASN 330  
331  1 Y 1 A ASP 331  ? A ASP 331  
332  1 Y 1 A TYR 332  ? A TYR 332  
333  1 Y 1 A ASN 333  ? A ASN 333  
334  1 Y 1 A PRO 334  ? A PRO 334  
335  1 Y 1 A LEU 335  ? A LEU 335  
336  1 Y 1 A MET 336  ? A MET 336  
337  1 Y 1 A LYS 337  ? A LYS 337  
338  1 Y 1 A ASP 338  ? A ASP 338  
339  1 Y 1 A PHE 339  ? A PHE 339  
340  1 Y 1 A PRO 340  ? A PRO 340  
341  1 Y 1 A LEU 341  ? A LEU 341  
342  1 Y 1 A ASN 342  ? A ASN 342  
343  1 Y 1 A ASP 343  ? A ASP 343  
344  1 Y 1 A LEU 344  ? A LEU 344  
345  1 Y 1 A LEU 345  ? A LEU 345  
346  1 Y 1 A SER 346  ? A SER 346  
347  1 Y 1 A ALA 347  ? A ALA 347  
348  1 Y 1 A THR 348  ? A THR 348  
349  1 Y 1 A GLU 349  ? A GLU 349  
350  1 Y 1 A LEU 350  ? A LEU 350  
351  1 Y 1 A ASP 351  ? A ASP 351  
352  1 Y 1 A LYS 352  ? A LYS 352  
353  1 Y 1 A ILE 353  ? A ILE 353  
354  1 Y 1 A ARG 354  ? A ARG 354  
355  1 Y 1 A GLN 355  ? A GLN 355  
356  1 Y 1 A ALA 356  ? A ALA 356  
357  1 Y 1 A LEU 357  ? A LEU 357  
358  1 Y 1 A VAL 358  ? A VAL 358  
359  1 Y 1 A ALA 359  ? A ALA 359  
360  1 Y 1 A ILE 360  ? A ILE 360  
361  1 Y 1 A PHE 361  ? A PHE 361  
362  1 Y 1 A THR 362  ? A THR 362  
363  1 Y 1 A HIS 363  ? A HIS 363  
364  1 Y 1 A LEU 364  ? A LEU 364  
365  1 Y 1 A ARG 365  ? A ARG 365  
366  1 Y 1 A LYS 366  ? A LYS 366  
367  1 Y 1 A ILE 367  ? A ILE 367  
368  1 Y 1 A ARG 368  ? A ARG 368  
369  1 Y 1 A ASN 369  ? A ASN 369  
370  1 Y 1 A THR 370  ? A THR 370  
371  1 Y 1 A LYS 371  ? A LYS 371  
372  1 Y 1 A TYR 372  ? A TYR 372  
373  1 Y 1 A PRO 373  ? A PRO 373  
374  1 Y 1 A ILE 374  ? A ILE 374  
375  1 Y 1 A GLN 375  ? A GLN 375  
376  1 Y 1 A ARG 376  ? A ARG 376  
377  1 Y 1 A ALA 377  ? A ALA 377  
378  1 Y 1 A LEU 378  ? A LEU 378  
379  1 Y 1 A ARG 379  ? A ARG 379  
380  1 Y 1 A LEU 380  ? A LEU 380  
381  1 Y 1 A VAL 381  ? A VAL 381  
382  1 Y 1 A GLU 382  ? A GLU 382  
383  1 Y 1 A ALA 383  ? A ALA 383  
384  1 Y 1 A ILE 384  ? A ILE 384  
385  1 Y 1 A SER 385  ? A SER 385  
386  1 Y 1 A ARG 386  ? A ARG 386  
387  1 Y 1 A ASP 387  ? A ASP 387  
388  1 Y 1 A LEU 388  ? A LEU 388  
389  1 Y 1 A SER 389  ? A SER 389  
390  1 Y 1 A SER 390  ? A SER 390  
391  1 Y 1 A GLN 391  ? A GLN 391  
392  1 Y 1 A LEU 392  ? A LEU 392  
393  1 Y 1 A LEU 393  ? A LEU 393  
394  1 Y 1 A LYS 394  ? A LYS 394  
395  1 Y 1 A VAL 395  ? A VAL 395  
396  1 Y 1 A LEU 396  ? A LEU 396  
397  1 Y 1 A GLY 397  ? A GLY 397  
398  1 Y 1 A THR 398  ? A THR 398  
399  1 Y 1 A ARG 399  ? A ARG 399  
400  1 Y 1 A LYS 400  ? A LYS 400  
401  1 Y 1 A LEU 401  ? A LEU 401  
402  1 Y 1 A MET 402  ? A MET 402  
403  1 Y 1 A HIS 403  ? A HIS 403  
404  1 Y 1 A VAL 404  ? A VAL 404  
405  1 Y 1 A ALA 405  ? A ALA 405  
406  1 Y 1 A TYR 406  ? A TYR 406  
407  1 Y 1 A GLU 407  ? A GLU 407  
408  1 Y 1 A GLU 408  ? A GLU 408  
409  1 Y 1 A PHE 409  ? A PHE 409  
410  1 Y 1 A GLU 410  ? A GLU 410  
411  1 Y 1 A LYS 411  ? A LYS 411  
412  1 Y 1 A VAL 412  ? A VAL 412  
413  1 Y 1 A MET 413  ? A MET 413  
414  1 Y 1 A VAL 414  ? A VAL 414  
415  1 Y 1 A ALA 415  ? A ALA 415  
416  1 Y 1 A CYS 416  ? A CYS 416  
417  1 Y 1 A PHE 417  ? A PHE 417  
418  1 Y 1 A GLU 418  ? A GLU 418  
419  1 Y 1 A VAL 419  ? A VAL 419  
420  1 Y 1 A PHE 420  ? A PHE 420  
421  1 Y 1 A GLN 421  ? A GLN 421  
422  1 Y 1 A THR 422  ? A THR 422  
423  1 Y 1 A TRP 423  ? A TRP 423  
424  1 Y 1 A ASP 424  ? A ASP 424  
425  1 Y 1 A ASP 425  ? A ASP 425  
426  1 Y 1 A GLU 426  ? A GLU 426  
427  1 Y 1 A TYR 427  ? A TYR 427  
428  1 Y 1 A GLU 428  ? A GLU 428  
429  1 Y 1 A LYS 429  ? A LYS 429  
430  1 Y 1 A LEU 430  ? A LEU 430  
431  1 Y 1 A GLN 431  ? A GLN 431  
432  1 Y 1 A VAL 432  ? A VAL 432  
433  1 Y 1 A LEU 433  ? A LEU 433  
434  1 Y 1 A LEU 434  ? A LEU 434  
435  1 Y 1 A ARG 435  ? A ARG 435  
436  1 Y 1 A ASP 436  ? A ASP 436  
437  1 Y 1 A ILE 437  ? A ILE 437  
438  1 Y 1 A VAL 438  ? A VAL 438  
439  1 Y 1 A LYS 439  ? A LYS 439  
440  1 Y 1 A ARG 440  ? A ARG 440  
441  1 Y 1 A LYS 441  ? A LYS 441  
442  1 Y 1 A ARG 442  ? A ARG 442  
443  1 Y 1 A GLU 443  ? A GLU 443  
444  1 Y 1 A GLU 444  ? A GLU 444  
445  1 Y 1 A ASN 445  ? A ASN 445  
446  1 Y 1 A LEU 446  ? A LEU 446  
447  1 Y 1 A LYS 447  ? A LYS 447  
448  1 Y 1 A MET 448  ? A MET 448  
449  1 Y 1 A VAL 449  ? A VAL 449  
450  1 Y 1 A TRP 450  ? A TRP 450  
451  1 Y 1 A ARG 451  ? A ARG 451  
452  1 Y 1 A ILE 452  ? A ILE 452  
453  1 Y 1 A ASN 453  ? A ASN 453  
454  1 Y 1 A PRO 454  ? A PRO 454  
455  1 Y 1 A ALA 455  ? A ALA 455  
456  1 Y 1 A HIS 456  ? A HIS 456  
457  1 Y 1 A ARG 457  ? A ARG 457  
458  1 Y 1 A LYS 458  ? A LYS 458  
459  1 Y 1 A LEU 459  ? A LEU 459  
460  1 Y 1 A GLN 460  ? A GLN 460  
461  1 Y 1 A ALA 461  ? A ALA 461  
462  1 Y 1 A ARG 462  ? A ARG 462  
463  1 Y 1 A LEU 463  ? A LEU 463  
464  1 Y 1 A ASP 464  ? A ASP 464  
465  1 Y 1 A GLN 465  ? A GLN 465  
466  1 Y 1 A MET 466  ? A MET 466  
467  1 Y 1 A ARG 467  ? A ARG 467  
468  1 Y 1 A LYS 468  ? A LYS 468  
469  1 Y 1 A PHE 469  ? A PHE 469  
470  1 Y 1 A ARG 470  ? A ARG 470  
471  1 Y 1 A ARG 471  ? A ARG 471  
472  1 Y 1 A GLN 472  ? A GLN 472  
473  1 Y 1 A HIS 473  ? A HIS 473  
474  1 Y 1 A GLU 474  ? A GLU 474  
475  1 Y 1 A GLN 475  ? A GLN 475  
476  1 Y 1 A LEU 476  ? A LEU 476  
477  1 Y 1 A ARG 477  ? A ARG 477  
478  1 Y 1 A ALA 478  ? A ALA 478  
479  1 Y 1 A VAL 479  ? A VAL 479  
480  1 Y 1 A ILE 480  ? A ILE 480  
481  1 Y 1 A VAL 481  ? A VAL 481  
482  1 Y 1 A ARG 482  ? A ARG 482  
483  1 Y 1 A VAL 483  ? A VAL 483  
484  1 Y 1 A LEU 484  ? A LEU 484  
485  1 Y 1 A ARG 485  ? A ARG 485  
486  1 Y 1 A PRO 486  ? A PRO 486  
487  1 Y 1 A GLN 487  ? A GLN 487  
488  1 Y 1 A VAL 488  ? A VAL 488  
489  1 Y 1 A THR 489  ? A THR 489  
490  1 Y 1 A ALA 490  ? A ALA 490  
491  1 Y 1 A VAL 491  ? A VAL 491  
492  1 Y 1 A ALA 492  ? A ALA 492  
493  1 Y 1 A GLN 493  ? A GLN 493  
494  1 Y 1 A GLN 494  ? A GLN 494  
495  1 Y 1 A ASN 495  ? A ASN 495  
496  1 Y 1 A GLN 496  ? A GLN 496  
497  1 Y 1 A GLY 497  ? A GLY 497  
498  1 Y 1 A GLU 498  ? A GLU 498  
499  1 Y 1 A VAL 499  ? A VAL 499  
500  1 Y 1 A PRO 500  ? A PRO 500  
501  1 Y 1 A GLU 501  ? A GLU 501  
502  1 Y 1 A PRO 502  ? A PRO 502  
503  1 Y 1 A GLN 503  ? A GLN 503  
504  1 Y 1 A ASP 504  ? A ASP 504  
505  1 Y 1 A MET 505  ? A MET 505  
506  1 Y 1 A LYS 506  ? A LYS 506  
507  1 Y 1 A VAL 507  ? A VAL 507  
508  1 Y 1 A ALA 508  ? A ALA 508  
509  1 Y 1 A GLU 509  ? A GLU 509  
510  1 Y 1 A VAL 510  ? A VAL 510  
511  1 Y 1 A LEU 511  ? A LEU 511  
512  1 Y 1 A PHE 512  ? A PHE 512  
513  1 Y 1 A ASP 513  ? A ASP 513  
514  1 Y 1 A ALA 514  ? A ALA 514  
515  1 Y 1 A ALA 515  ? A ALA 515  
516  1 Y 1 A ASP 516  ? A ASP 516  
517  1 Y 1 A ALA 517  ? A ALA 517  
518  1 Y 1 A ASN 518  ? A ASN 518  
519  1 Y 1 A ALA 519  ? A ALA 519  
520  1 Y 1 A ILE 520  ? A ILE 520  
521  1 Y 1 A GLU 521  ? A GLU 521  
522  1 Y 1 A GLU 522  ? A GLU 522  
523  1 Y 1 A VAL 523  ? A VAL 523  
524  1 Y 1 A ASN 524  ? A ASN 524  
525  1 Y 1 A LEU 525  ? A LEU 525  
526  1 Y 1 A ALA 526  ? A ALA 526  
527  1 Y 1 A TYR 527  ? A TYR 527  
528  1 Y 1 A GLU 528  ? A GLU 528  
529  1 Y 1 A ASN 529  ? A ASN 529  
530  1 Y 1 A VAL 530  ? A VAL 530  
531  1 Y 1 A LYS 531  ? A LYS 531  
532  1 Y 1 A GLU 532  ? A GLU 532  
533  1 Y 1 A VAL 533  ? A VAL 533  
534  1 Y 1 A ASP 534  ? A ASP 534  
535  1 Y 1 A GLY 535  ? A GLY 535  
536  1 Y 1 A LEU 536  ? A LEU 536  
537  1 Y 1 A ASP 537  ? A ASP 537  
538  1 Y 1 A VAL 538  ? A VAL 538  
539  1 Y 1 A SER 539  ? A SER 539  
540  1 Y 1 A LYS 540  ? A LYS 540  
541  1 Y 1 A GLU 541  ? A GLU 541  
542  1 Y 1 A GLY 542  ? A GLY 542  
543  1 Y 1 A THR 543  ? A THR 543  
544  1 Y 1 A GLU 544  ? A GLU 544  
545  1 Y 1 A ALA 545  ? A ALA 545  
546  1 Y 1 A TRP 546  ? A TRP 546  
547  1 Y 1 A GLU 547  ? A GLU 547  
548  1 Y 1 A ALA 548  ? A ALA 548  
549  1 Y 1 A ALA 549  ? A ALA 549  
550  1 Y 1 A MET 550  ? A MET 550  
551  1 Y 1 A LYS 551  ? A LYS 551  
552  1 Y 1 A ARG 552  ? A ARG 552  
553  1 Y 1 A TYR 553  ? A TYR 553  
554  1 Y 1 A ASP 554  ? A ASP 554  
555  1 Y 1 A GLU 555  ? A GLU 555  
556  1 Y 1 A ARG 556  ? A ARG 556  
557  1 Y 1 A ILE 557  ? A ILE 557  
558  1 Y 1 A ASP 558  ? A ASP 558  
559  1 Y 1 A ARG 559  ? A ARG 559  
560  1 Y 1 A VAL 560  ? A VAL 560  
561  1 Y 1 A GLU 561  ? A GLU 561  
562  1 Y 1 A THR 562  ? A THR 562  
563  1 Y 1 A ARG 563  ? A ARG 563  
564  1 Y 1 A ILE 564  ? A ILE 564  
565  1 Y 1 A THR 565  ? A THR 565  
566  1 Y 1 A ALA 566  ? A ALA 566  
567  1 Y 1 A ARG 567  ? A ARG 567  
568  1 Y 1 A LEU 568  ? A LEU 568  
569  1 Y 1 A ARG 569  ? A ARG 569  
570  1 Y 1 A ASP 570  ? A ASP 570  
571  1 Y 1 A GLN 571  ? A GLN 571  
572  1 Y 1 A LEU 572  ? A LEU 572  
573  1 Y 1 A GLY 573  ? A GLY 573  
574  1 Y 1 A THR 574  ? A THR 574  
575  1 Y 1 A ALA 575  ? A ALA 575  
576  1 Y 1 A LYS 576  ? A LYS 576  
577  1 Y 1 A ASN 577  ? A ASN 577  
578  1 Y 1 A ALA 578  ? A ALA 578  
579  1 Y 1 A ASN 579  ? A ASN 579  
580  1 Y 1 A GLU 580  ? A GLU 580  
581  1 Y 1 A MET 581  ? A MET 581  
582  1 Y 1 A PHE 582  ? A PHE 582  
583  1 Y 1 A ARG 583  ? A ARG 583  
584  1 Y 1 A ILE 584  ? A ILE 584  
585  1 Y 1 A PHE 585  ? A PHE 585  
586  1 Y 1 A SER 586  ? A SER 586  
587  1 Y 1 A ARG 587  ? A ARG 587  
588  1 Y 1 A PHE 588  ? A PHE 588  
589  1 Y 1 A ASN 589  ? A ASN 589  
590  1 Y 1 A ALA 590  ? A ALA 590  
591  1 Y 1 A LEU 591  ? A LEU 591  
592  1 Y 1 A PHE 592  ? A PHE 592  
593  1 Y 1 A VAL 593  ? A VAL 593  
594  1 Y 1 A ARG 594  ? A ARG 594  
595  1 Y 1 A PRO 595  ? A PRO 595  
596  1 Y 1 A HIS 596  ? A HIS 596  
597  1 Y 1 A ILE 597  ? A ILE 597  
598  1 Y 1 A ARG 598  ? A ARG 598  
599  1 Y 1 A GLY 599  ? A GLY 599  
600  1 Y 1 A ALA 600  ? A ALA 600  
601  1 Y 1 A ILE 601  ? A ILE 601  
602  1 Y 1 A ARG 602  ? A ARG 602  
603  1 Y 1 A GLU 603  ? A GLU 603  
604  1 Y 1 A TYR 604  ? A TYR 604  
605  1 Y 1 A GLN 605  ? A GLN 605  
606  1 Y 1 A THR 606  ? A THR 606  
607  1 Y 1 A GLN 607  ? A GLN 607  
608  1 Y 1 A LEU 608  ? A LEU 608  
609  1 Y 1 A ILE 609  ? A ILE 609  
610  1 Y 1 A GLN 610  ? A GLN 610  
611  1 Y 1 A ARG 611  ? A ARG 611  
612  1 Y 1 A VAL 612  ? A VAL 612  
613  1 Y 1 A LYS 613  ? A LYS 613  
614  1 Y 1 A ASP 614  ? A ASP 614  
615  1 Y 1 A ASP 615  ? A ASP 615  
616  1 Y 1 A ILE 616  ? A ILE 616  
617  1 Y 1 A GLU 617  ? A GLU 617  
618  1 Y 1 A SER 618  ? A SER 618  
619  1 Y 1 A LEU 619  ? A LEU 619  
620  1 Y 1 A HIS 620  ? A HIS 620  
621  1 Y 1 A ASP 621  ? A ASP 621  
622  1 Y 1 A LYS 622  ? A LYS 622  
623  1 Y 1 A PHE 623  ? A PHE 623  
624  1 Y 1 A LYS 624  ? A LYS 624  
625  1 Y 1 A VAL 625  ? A VAL 625  
626  1 Y 1 A GLN 626  ? A GLN 626  
627  1 Y 1 A TYR 627  ? A TYR 627  
628  1 Y 1 A PRO 628  ? A PRO 628  
629  1 Y 1 A GLN 629  ? A GLN 629  
630  1 Y 1 A SER 630  ? A SER 630  
631  1 Y 1 A GLN 631  ? A GLN 631  
632  1 Y 1 A ALA 632  ? A ALA 632  
633  1 Y 1 A CYS 633  ? A CYS 633  
634  1 Y 1 A LYS 634  ? A LYS 634  
635  1 Y 1 A MET 635  ? A MET 635  
636  1 Y 1 A SER 636  ? A SER 636  
637  1 Y 1 A HIS 637  ? A HIS 637  
638  1 Y 1 A VAL 638  ? A VAL 638  
639  1 Y 1 A ARG 639  ? A ARG 639  
640  1 Y 1 A ASP 640  ? A ASP 640  
641  1 Y 1 A LEU 641  ? A LEU 641  
642  1 Y 1 A PRO 642  ? A PRO 642  
643  1 Y 1 A PRO 643  ? A PRO 643  
644  1 Y 1 A VAL 644  ? A VAL 644  
645  1 Y 1 A SER 645  ? A SER 645  
646  1 Y 1 A GLY 646  ? A GLY 646  
647  1 Y 1 A SER 647  ? A SER 647  
648  1 Y 1 A ILE 648  ? A ILE 648  
649  1 Y 1 A ILE 649  ? A ILE 649  
650  1 Y 1 A TRP 650  ? A TRP 650  
651  1 Y 1 A ALA 651  ? A ALA 651  
652  1 Y 1 A LYS 652  ? A LYS 652  
653  1 Y 1 A GLN 653  ? A GLN 653  
654  1 Y 1 A ILE 654  ? A ILE 654  
655  1 Y 1 A ASP 655  ? A ASP 655  
656  1 Y 1 A ARG 656  ? A ARG 656  
657  1 Y 1 A GLN 657  ? A GLN 657  
658  1 Y 1 A LEU 658  ? A LEU 658  
659  1 Y 1 A THR 659  ? A THR 659  
660  1 Y 1 A ALA 660  ? A ALA 660  
661  1 Y 1 A TYR 661  ? A TYR 661  
662  1 Y 1 A MET 662  ? A MET 662  
663  1 Y 1 A LYS 663  ? A LYS 663  
664  1 Y 1 A ARG 664  ? A ARG 664  
665  1 Y 1 A VAL 665  ? A VAL 665  
666  1 Y 1 A GLU 666  ? A GLU 666  
667  1 Y 1 A ASP 667  ? A ASP 667  
668  1 Y 1 A VAL 668  ? A VAL 668  
669  1 Y 1 A LEU 669  ? A LEU 669  
670  1 Y 1 A GLY 670  ? A GLY 670  
671  1 Y 1 A LYS 671  ? A LYS 671  
672  1 Y 1 A GLY 672  ? A GLY 672  
673  1 Y 1 A TRP 673  ? A TRP 673  
674  1 Y 1 A GLU 674  ? A GLU 674  
675  1 Y 1 A ASN 675  ? A ASN 675  
676  1 Y 1 A HIS 676  ? A HIS 676  
677  1 Y 1 A VAL 677  ? A VAL 677  
678  1 Y 1 A GLU 678  ? A GLU 678  
679  1 Y 1 A GLY 679  ? A GLY 679  
680  1 Y 1 A GLN 680  ? A GLN 680  
681  1 Y 1 A LYS 681  ? A LYS 681  
682  1 Y 1 A LEU 682  ? A LEU 682  
683  1 Y 1 A LYS 683  ? A LYS 683  
684  1 Y 1 A GLN 684  ? A GLN 684  
685  1 Y 1 A ASP 685  ? A ASP 685  
686  1 Y 1 A GLY 686  ? A GLY 686  
687  1 Y 1 A ASP 687  ? A ASP 687  
688  1 Y 1 A SER 688  ? A SER 688  
689  1 Y 1 A PHE 689  ? A PHE 689  
690  1 Y 1 A ARG 690  ? A ARG 690  
691  1 Y 1 A MET 691  ? A MET 691  
692  1 Y 1 A LYS 692  ? A LYS 692  
693  1 Y 1 A LEU 693  ? A LEU 693  
694  1 Y 1 A ASN 694  ? A ASN 694  
695  1 Y 1 A THR 695  ? A THR 695  
696  1 Y 1 A GLN 696  ? A GLN 696  
697  1 Y 1 A GLU 697  ? A GLU 697  
698  1 Y 1 A ILE 698  ? A ILE 698  
699  1 Y 1 A PHE 699  ? A PHE 699  
700  1 Y 1 A ASP 700  ? A ASP 700  
701  1 Y 1 A ASP 701  ? A ASP 701  
702  1 Y 1 A TRP 702  ? A TRP 702  
703  1 Y 1 A ALA 703  ? A ALA 703  
704  1 Y 1 A ARG 704  ? A ARG 704  
705  1 Y 1 A LYS 705  ? A LYS 705  
706  1 Y 1 A VAL 706  ? A VAL 706  
707  1 Y 1 A GLN 707  ? A GLN 707  
708  1 Y 1 A GLN 708  ? A GLN 708  
709  1 Y 1 A ARG 709  ? A ARG 709  
710  1 Y 1 A ASN 710  ? A ASN 710  
711  1 Y 1 A LEU 711  ? A LEU 711  
712  1 Y 1 A GLY 712  ? A GLY 712  
713  1 Y 1 A VAL 713  ? A VAL 713  
714  1 Y 1 A SER 714  ? A SER 714  
715  1 Y 1 A GLY 715  ? A GLY 715  
716  1 Y 1 A ARG 716  ? A ARG 716  
717  1 Y 1 A ILE 717  ? A ILE 717  
718  1 Y 1 A PHE 718  ? A PHE 718  
719  1 Y 1 A THR 719  ? A THR 719  
720  1 Y 1 A ILE 720  ? A ILE 720  
721  1 Y 1 A GLU 721  ? A GLU 721  
722  1 Y 1 A SER 722  ? A SER 722  
723  1 Y 1 A THR 723  ? A THR 723  
724  1 Y 1 A ARG 724  ? A ARG 724  
725  1 Y 1 A VAL 725  ? A VAL 725  
726  1 Y 1 A ARG 726  ? A ARG 726  
727  1 Y 1 A GLY 727  ? A GLY 727  
728  1 Y 1 A ARG 728  ? A ARG 728  
729  1 Y 1 A THR 729  ? A THR 729  
730  1 Y 1 A GLY 730  ? A GLY 730  
731  1 Y 1 A ASN 731  ? A ASN 731  
732  1 Y 1 A VAL 732  ? A VAL 732  
733  1 Y 1 A LEU 733  ? A LEU 733  
734  1 Y 1 A LYS 734  ? A LYS 734  
735  1 Y 1 A LEU 735  ? A LEU 735  
736  1 Y 1 A LYS 736  ? A LYS 736  
737  1 Y 1 A VAL 737  ? A VAL 737  
738  1 Y 1 A ASN 738  ? A ASN 738  
739  1 Y 1 A PHE 739  ? A PHE 739  
740  1 Y 1 A LEU 740  ? A LEU 740  
741  1 Y 1 A PRO 741  ? A PRO 741  
742  1 Y 1 A GLU 742  ? A GLU 742  
743  1 Y 1 A ILE 743  ? A ILE 743  
744  1 Y 1 A ILE 744  ? A ILE 744  
745  1 Y 1 A THR 745  ? A THR 745  
746  1 Y 1 A LEU 746  ? A LEU 746  
747  1 Y 1 A SER 747  ? A SER 747  
748  1 Y 1 A LYS 748  ? A LYS 748  
749  1 Y 1 A GLU 749  ? A GLU 749  
750  1 Y 1 A VAL 750  ? A VAL 750  
751  1 Y 1 A ARG 751  ? A ARG 751  
752  1 Y 1 A ASN 752  ? A ASN 752  
753  1 Y 1 A LEU 753  ? A LEU 753  
754  1 Y 1 A LYS 754  ? A LYS 754  
755  1 Y 1 A TRP 755  ? A TRP 755  
756  1 Y 1 A LEU 756  ? A LEU 756  
757  1 Y 1 A GLY 757  ? A GLY 757  
758  1 Y 1 A PHE 758  ? A PHE 758  
759  1 Y 1 A ARG 759  ? A ARG 759  
760  1 Y 1 A VAL 760  ? A VAL 760  
761  1 Y 1 A PRO 761  ? A PRO 761  
762  1 Y 1 A LEU 762  ? A LEU 762  
763  1 Y 1 A ALA 763  ? A ALA 763  
764  1 Y 1 A ILE 764  ? A ILE 764  
765  1 Y 1 A VAL 765  ? A VAL 765  
766  1 Y 1 A ASN 766  ? A ASN 766  
767  1 Y 1 A LYS 767  ? A LYS 767  
768  1 Y 1 A ALA 768  ? A ALA 768  
769  1 Y 1 A HIS 769  ? A HIS 769  
770  1 Y 1 A GLN 770  ? A GLN 770  
771  1 Y 1 A ALA 771  ? A ALA 771  
772  1 Y 1 A ASN 772  ? A ASN 772  
773  1 Y 1 A GLN 773  ? A GLN 773  
774  1 Y 1 A LEU 774  ? A LEU 774  
775  1 Y 1 A TYR 775  ? A TYR 775  
776  1 Y 1 A PRO 776  ? A PRO 776  
777  1 Y 1 A PHE 777  ? A PHE 777  
778  1 Y 1 A ALA 778  ? A ALA 778  
779  1 Y 1 A ILE 779  ? A ILE 779  
780  1 Y 1 A SER 780  ? A SER 780  
781  1 Y 1 A LEU 781  ? A LEU 781  
782  1 Y 1 A ILE 782  ? A ILE 782  
783  1 Y 1 A GLU 783  ? A GLU 783  
784  1 Y 1 A SER 784  ? A SER 784  
785  1 Y 1 A VAL 785  ? A VAL 785  
786  1 Y 1 A ARG 786  ? A ARG 786  
787  1 Y 1 A THR 787  ? A THR 787  
788  1 Y 1 A TYR 788  ? A TYR 788  
789  1 Y 1 A GLU 789  ? A GLU 789  
790  1 Y 1 A ARG 790  ? A ARG 790  
791  1 Y 1 A THR 791  ? A THR 791  
792  1 Y 1 A CYS 792  ? A CYS 792  
793  1 Y 1 A GLU 793  ? A GLU 793  
794  1 Y 1 A LYS 794  ? A LYS 794  
795  1 Y 1 A VAL 795  ? A VAL 795  
796  1 Y 1 A GLU 796  ? A GLU 796  
797  1 Y 1 A GLU 797  ? A GLU 797  
798  1 Y 1 A ARG 798  ? A ARG 798  
799  1 Y 1 A ASN 799  ? A ASN 799  
800  1 Y 1 A THR 800  ? A THR 800  
801  1 Y 1 A ILE 801  ? A ILE 801  
802  1 Y 1 A SER 802  ? A SER 802  
803  1 Y 1 A LEU 803  ? A LEU 803  
804  1 Y 1 A LEU 804  ? A LEU 804  
805  1 Y 1 A VAL 805  ? A VAL 805  
806  1 Y 1 A ALA 806  ? A ALA 806  
807  1 Y 1 A GLY 807  ? A GLY 807  
808  1 Y 1 A LEU 808  ? A LEU 808  
809  1 Y 1 A LYS 809  ? A LYS 809  
810  1 Y 1 A LYS 810  ? A LYS 810  
811  1 Y 1 A GLU 811  ? A GLU 811  
812  1 Y 1 A VAL 812  ? A VAL 812  
813  1 Y 1 A GLN 813  ? A GLN 813  
814  1 Y 1 A ALA 814  ? A ALA 814  
815  1 Y 1 A LEU 815  ? A LEU 815  
816  1 Y 1 A ILE 816  ? A ILE 816  
817  1 Y 1 A ALA 817  ? A ALA 817  
818  1 Y 1 A GLU 818  ? A GLU 818  
819  1 Y 1 A GLY 819  ? A GLY 819  
820  1 Y 1 A ILE 820  ? A ILE 820  
821  1 Y 1 A ALA 821  ? A ALA 821  
822  1 Y 1 A LEU 822  ? A LEU 822  
823  1 Y 1 A VAL 823  ? A VAL 823  
824  1 Y 1 A TRP 824  ? A TRP 824  
825  1 Y 1 A GLU 825  ? A GLU 825  
826  1 Y 1 A SER 826  ? A SER 826  
827  1 Y 1 A TYR 827  ? A TYR 827  
828  1 Y 1 A LYS 828  ? A LYS 828  
829  1 Y 1 A LEU 829  ? A LEU 829  
830  1 Y 1 A ASP 830  ? A ASP 830  
831  1 Y 1 A PRO 831  ? A PRO 831  
832  1 Y 1 A TYR 832  ? A TYR 832  
833  1 Y 1 A VAL 833  ? A VAL 833  
834  1 Y 1 A GLN 834  ? A GLN 834  
835  1 Y 1 A ARG 835  ? A ARG 835  
836  1 Y 1 A LEU 836  ? A LEU 836  
837  1 Y 1 A ALA 837  ? A ALA 837  
838  1 Y 1 A GLU 838  ? A GLU 838  
839  1 Y 1 A THR 839  ? A THR 839  
840  1 Y 1 A VAL 840  ? A VAL 840  
841  1 Y 1 A PHE 841  ? A PHE 841  
842  1 Y 1 A ASN 842  ? A ASN 842  
843  1 Y 1 A PHE 843  ? A PHE 843  
844  1 Y 1 A GLN 844  ? A GLN 844  
845  1 Y 1 A GLU 845  ? A GLU 845  
846  1 Y 1 A LYS 846  ? A LYS 846  
847  1 Y 1 A VAL 847  ? A VAL 847  
848  1 Y 1 A ASP 848  ? A ASP 848  
849  1 Y 1 A ASP 849  ? A ASP 849  
850  1 Y 1 A LEU 850  ? A LEU 850  
851  1 Y 1 A LEU 851  ? A LEU 851  
852  1 Y 1 A ILE 852  ? A ILE 852  
853  1 Y 1 A ILE 853  ? A ILE 853  
854  1 Y 1 A GLU 854  ? A GLU 854  
855  1 Y 1 A GLU 855  ? A GLU 855  
856  1 Y 1 A LYS 856  ? A LYS 856  
857  1 Y 1 A ILE 857  ? A ILE 857  
858  1 Y 1 A ASP 858  ? A ASP 858  
859  1 Y 1 A LEU 859  ? A LEU 859  
860  1 Y 1 A GLU 860  ? A GLU 860  
861  1 Y 1 A VAL 861  ? A VAL 861  
862  1 Y 1 A ARG 862  ? A ARG 862  
863  1 Y 1 A SER 863  ? A SER 863  
864  1 Y 1 A LEU 864  ? A LEU 864  
865  1 Y 1 A GLU 865  ? A GLU 865  
866  1 Y 1 A THR 866  ? A THR 866  
867  1 Y 1 A CYS 867  ? A CYS 867  
868  1 Y 1 A MET 868  ? A MET 868  
869  1 Y 1 A TYR 869  ? A TYR 869  
870  1 Y 1 A ASP 870  ? A ASP 870  
871  1 Y 1 A HIS 871  ? A HIS 871  
872  1 Y 1 A LYS 872  ? A LYS 872  
873  1 Y 1 A THR 873  ? A THR 873  
874  1 Y 1 A PHE 874  ? A PHE 874  
875  1 Y 1 A SER 875  ? A SER 875  
876  1 Y 1 A GLU 876  ? A GLU 876  
877  1 Y 1 A ILE 877  ? A ILE 877  
878  1 Y 1 A LEU 878  ? A LEU 878  
879  1 Y 1 A ASN 879  ? A ASN 879  
880  1 Y 1 A ARG 880  ? A ARG 880  
881  1 Y 1 A VAL 881  ? A VAL 881  
882  1 Y 1 A GLN 882  ? A GLN 882  
883  1 Y 1 A LYS 883  ? A LYS 883  
884  1 Y 1 A ALA 884  ? A ALA 884  
885  1 Y 1 A VAL 885  ? A VAL 885  
886  1 Y 1 A ASP 886  ? A ASP 886  
887  1 Y 1 A ASP 887  ? A ASP 887  
888  1 Y 1 A LEU 888  ? A LEU 888  
889  1 Y 1 A ASN 889  ? A ASN 889  
890  1 Y 1 A LEU 890  ? A LEU 890  
891  1 Y 1 A HIS 891  ? A HIS 891  
892  1 Y 1 A SER 892  ? A SER 892  
893  1 Y 1 A TYR 893  ? A TYR 893  
894  1 Y 1 A SER 894  ? A SER 894  
895  1 Y 1 A ASN 895  ? A ASN 895  
896  1 Y 1 A LEU 896  ? A LEU 896  
897  1 Y 1 A PRO 897  ? A PRO 897  
898  1 Y 1 A ILE 898  ? A ILE 898  
899  1 Y 1 A TRP 899  ? A TRP 899  
900  1 Y 1 A VAL 900  ? A VAL 900  
901  1 Y 1 A ASN 901  ? A ASN 901  
902  1 Y 1 A LYS 902  ? A LYS 902  
903  1 Y 1 A LEU 903  ? A LEU 903  
904  1 Y 1 A ASP 904  ? A ASP 904  
905  1 Y 1 A MET 905  ? A MET 905  
906  1 Y 1 A GLU 906  ? A GLU 906  
907  1 Y 1 A ILE 907  ? A ILE 907  
908  1 Y 1 A GLU 908  ? A GLU 908  
909  1 Y 1 A ARG 909  ? A ARG 909  
910  1 Y 1 A ILE 910  ? A ILE 910  
911  1 Y 1 A LEU 911  ? A LEU 911  
912  1 Y 1 A GLY 912  ? A GLY 912  
913  1 Y 1 A VAL 913  ? A VAL 913  
914  1 Y 1 A ARG 914  ? A ARG 914  
915  1 Y 1 A LEU 915  ? A LEU 915  
916  1 Y 1 A GLN 916  ? A GLN 916  
917  1 Y 1 A ALA 917  ? A ALA 917  
918  1 Y 1 A GLY 918  ? A GLY 918  
919  1 Y 1 A LEU 919  ? A LEU 919  
920  1 Y 1 A ARG 920  ? A ARG 920  
921  1 Y 1 A ALA 921  ? A ALA 921  
922  1 Y 1 A TRP 922  ? A TRP 922  
923  1 Y 1 A THR 923  ? A THR 923  
924  1 Y 1 A GLN 924  ? A GLN 924  
925  1 Y 1 A VAL 925  ? A VAL 925  
926  1 Y 1 A LEU 926  ? A LEU 926  
927  1 Y 1 A LEU 927  ? A LEU 927  
928  1 Y 1 A GLY 928  ? A GLY 928  
929  1 Y 1 A GLN 929  ? A GLN 929  
930  1 Y 1 A ALA 930  ? A ALA 930  
931  1 Y 1 A GLU 931  ? A GLU 931  
932  1 Y 1 A ASP 932  ? A ASP 932  
933  1 Y 1 A LYS 933  ? A LYS 933  
934  1 Y 1 A ALA 934  ? A ALA 934  
935  1 Y 1 A GLU 935  ? A GLU 935  
936  1 Y 1 A VAL 936  ? A VAL 936  
937  1 Y 1 A ASP 937  ? A ASP 937  
938  1 Y 1 A MET 938  ? A MET 938  
939  1 Y 1 A ASP 939  ? A ASP 939  
940  1 Y 1 A THR 940  ? A THR 940  
941  1 Y 1 A ASP 941  ? A ASP 941  
942  1 Y 1 A ALA 942  ? A ALA 942  
943  1 Y 1 A PRO 943  ? A PRO 943  
944  1 Y 1 A GLN 944  ? A GLN 944  
945  1 Y 1 A VAL 945  ? A VAL 945  
946  1 Y 1 A SER 946  ? A SER 946  
947  1 Y 1 A HIS 947  ? A HIS 947  
948  1 Y 1 A LYS 948  ? A LYS 948  
949  1 Y 1 A PRO 949  ? A PRO 949  
950  1 Y 1 A GLY 950  ? A GLY 950  
951  1 Y 1 A GLY 951  ? A GLY 951  
952  1 Y 1 A GLU 952  ? A GLU 952  
953  1 Y 1 A PRO 953  ? A PRO 953  
954  1 Y 1 A LYS 954  ? A LYS 954  
955  1 Y 1 A ILE 955  ? A ILE 955  
956  1 Y 1 A LYS 956  ? A LYS 956  
957  1 Y 1 A ASN 957  ? A ASN 957  
958  1 Y 1 A VAL 958  ? A VAL 958  
959  1 Y 1 A VAL 959  ? A VAL 959  
960  1 Y 1 A HIS 960  ? A HIS 960  
961  1 Y 1 A GLU 961  ? A GLU 961  
962  1 Y 1 A LEU 962  ? A LEU 962  
963  1 Y 1 A ARG 963  ? A ARG 963  
964  1 Y 1 A ILE 964  ? A ILE 964  
965  1 Y 1 A THR 965  ? A THR 965  
966  1 Y 1 A ASN 966  ? A ASN 966  
967  1 Y 1 A GLN 967  ? A GLN 967  
968  1 Y 1 A VAL 968  ? A VAL 968  
969  1 Y 1 A ILE 969  ? A ILE 969  
970  1 Y 1 A TYR 970  ? A TYR 970  
971  1 Y 1 A LEU 971  ? A LEU 971  
972  1 Y 1 A ASN 972  ? A ASN 972  
973  1 Y 1 A PRO 973  ? A PRO 973  
974  1 Y 1 A PRO 974  ? A PRO 974  
975  1 Y 1 A ILE 975  ? A ILE 975  
976  1 Y 1 A GLU 976  ? A GLU 976  
977  1 Y 1 A GLU 977  ? A GLU 977  
978  1 Y 1 A CYS 978  ? A CYS 978  
979  1 Y 1 A ARG 979  ? A ARG 979  
980  1 Y 1 A TYR 980  ? A TYR 980  
981  1 Y 1 A LYS 981  ? A LYS 981  
982  1 Y 1 A LEU 982  ? A LEU 982  
983  1 Y 1 A TYR 983  ? A TYR 983  
984  1 Y 1 A GLN 984  ? A GLN 984  
985  1 Y 1 A GLU 985  ? A GLU 985  
986  1 Y 1 A MET 986  ? A MET 986  
987  1 Y 1 A PHE 987  ? A PHE 987  
988  1 Y 1 A ALA 988  ? A ALA 988  
989  1 Y 1 A TRP 989  ? A TRP 989  
990  1 Y 1 A LYS 990  ? A LYS 990  
991  1 Y 1 A MET 991  ? A MET 991  
992  1 Y 1 A VAL 992  ? A VAL 992  
993  1 Y 1 A VAL 993  ? A VAL 993  
994  1 Y 1 A LEU 994  ? A LEU 994  
995  1 Y 1 A SER 995  ? A SER 995  
996  1 Y 1 A LEU 996  ? A LEU 996  
997  1 Y 1 A PRO 997  ? A PRO 997  
998  1 Y 1 A ARG 998  ? A ARG 998  
999  1 Y 1 A ILE 999  ? A ILE 999  
1000 1 Y 1 A GLN 1000 ? A GLN 1000 
1001 1 Y 1 A SER 1001 ? A SER 1001 
1002 1 Y 1 A GLN 1002 ? A GLN 1002 
1003 1 Y 1 A ARG 1003 ? A ARG 1003 
1004 1 Y 1 A TYR 1004 ? A TYR 1004 
1005 1 Y 1 A GLN 1005 ? A GLN 1005 
1006 1 Y 1 A VAL 1006 ? A VAL 1006 
1007 1 Y 1 A GLY 1007 ? A GLY 1007 
1008 1 Y 1 A VAL 1008 ? A VAL 1008 
1009 1 Y 1 A HIS 1009 ? A HIS 1009 
1010 1 Y 1 A TYR 1010 ? A TYR 1010 
1011 1 Y 1 A GLU 1011 ? A GLU 1011 
1012 1 Y 1 A LEU 1012 ? A LEU 1012 
1013 1 Y 1 A THR 1013 ? A THR 1013 
1014 1 Y 1 A GLU 1014 ? A GLU 1014 
1015 1 Y 1 A GLU 1015 ? A GLU 1015 
1016 1 Y 1 A GLU 1016 ? A GLU 1016 
1017 1 Y 1 A LYS 1017 ? A LYS 1017 
1018 1 Y 1 A PHE 1018 ? A PHE 1018 
1019 1 Y 1 A TYR 1019 ? A TYR 1019 
1020 1 Y 1 A ARG 1020 ? A ARG 1020 
1021 1 Y 1 A ASN 1021 ? A ASN 1021 
1022 1 Y 1 A ALA 1022 ? A ALA 1022 
1023 1 Y 1 A LEU 1023 ? A LEU 1023 
1024 1 Y 1 A THR 1024 ? A THR 1024 
1025 1 Y 1 A ARG 1025 ? A ARG 1025 
1026 1 Y 1 A MET 1026 ? A MET 1026 
1027 1 Y 1 A PRO 1027 ? A PRO 1027 
1028 1 Y 1 A ASP 1028 ? A ASP 1028 
1029 1 Y 1 A GLY 1029 ? A GLY 1029 
1030 1 Y 1 A PRO 1030 ? A PRO 1030 
1031 1 Y 1 A VAL 1031 ? A VAL 1031 
1032 1 Y 1 A ALA 1032 ? A ALA 1032 
1033 1 Y 1 A LEU 1033 ? A LEU 1033 
1034 1 Y 1 A GLU 1034 ? A GLU 1034 
1035 1 Y 1 A GLU 1035 ? A GLU 1035 
1036 1 Y 1 A SER 1036 ? A SER 1036 
1037 1 Y 1 A TYR 1037 ? A TYR 1037 
1038 1 Y 1 A SER 1038 ? A SER 1038 
1039 1 Y 1 A ALA 1039 ? A ALA 1039 
1040 1 Y 1 A VAL 1040 ? A VAL 1040 
1041 1 Y 1 A MET 1041 ? A MET 1041 
1042 1 Y 1 A GLY 1042 ? A GLY 1042 
1043 1 Y 1 A ILE 1043 ? A ILE 1043 
1044 1 Y 1 A VAL 1044 ? A VAL 1044 
1045 1 Y 1 A SER 1045 ? A SER 1045 
1046 1 Y 1 A GLU 1046 ? A GLU 1046 
1047 1 Y 1 A VAL 1047 ? A VAL 1047 
1048 1 Y 1 A GLU 1048 ? A GLU 1048 
1049 1 Y 1 A GLN 1049 ? A GLN 1049 
1050 1 Y 1 A TYR 1050 ? A TYR 1050 
1051 1 Y 1 A VAL 1051 ? A VAL 1051 
1052 1 Y 1 A LYS 1052 ? A LYS 1052 
1053 1 Y 1 A VAL 1053 ? A VAL 1053 
1054 1 Y 1 A TRP 1054 ? A TRP 1054 
1055 1 Y 1 A LEU 1055 ? A LEU 1055 
1056 1 Y 1 A GLN 1056 ? A GLN 1056 
1057 1 Y 1 A TYR 1057 ? A TYR 1057 
1058 1 Y 1 A GLN 1058 ? A GLN 1058 
1059 1 Y 1 A CYS 1059 ? A CYS 1059 
1060 1 Y 1 A LEU 1060 ? A LEU 1060 
1061 1 Y 1 A TRP 1061 ? A TRP 1061 
1062 1 Y 1 A ASP 1062 ? A ASP 1062 
1063 1 Y 1 A MET 1063 ? A MET 1063 
1064 1 Y 1 A GLN 1064 ? A GLN 1064 
1065 1 Y 1 A ALA 1065 ? A ALA 1065 
1066 1 Y 1 A GLU 1066 ? A GLU 1066 
1067 1 Y 1 A ASN 1067 ? A ASN 1067 
1068 1 Y 1 A ILE 1068 ? A ILE 1068 
1069 1 Y 1 A TYR 1069 ? A TYR 1069 
1070 1 Y 1 A ASN 1070 ? A ASN 1070 
1071 1 Y 1 A ARG 1071 ? A ARG 1071 
1072 1 Y 1 A LEU 1072 ? A LEU 1072 
1073 1 Y 1 A GLY 1073 ? A GLY 1073 
1074 1 Y 1 A GLU 1074 ? A GLU 1074 
1075 1 Y 1 A ASP 1075 ? A ASP 1075 
1076 1 Y 1 A LEU 1076 ? A LEU 1076 
1077 1 Y 1 A ASN 1077 ? A ASN 1077 
1078 1 Y 1 A LYS 1078 ? A LYS 1078 
1079 1 Y 1 A TRP 1079 ? A TRP 1079 
1080 1 Y 1 A GLN 1080 ? A GLN 1080 
1081 1 Y 1 A ALA 1081 ? A ALA 1081 
1082 1 Y 1 A LEU 1082 ? A LEU 1082 
1083 1 Y 1 A LEU 1083 ? A LEU 1083 
1084 1 Y 1 A VAL 1084 ? A VAL 1084 
1085 1 Y 1 A GLN 1085 ? A GLN 1085 
1086 1 Y 1 A ILE 1086 ? A ILE 1086 
1087 1 Y 1 A ARG 1087 ? A ARG 1087 
1088 1 Y 1 A LYS 1088 ? A LYS 1088 
1089 1 Y 1 A ALA 1089 ? A ALA 1089 
1090 1 Y 1 A ARG 1090 ? A ARG 1090 
1091 1 Y 1 A GLY 1091 ? A GLY 1091 
1092 1 Y 1 A THR 1092 ? A THR 1092 
1093 1 Y 1 A PHE 1093 ? A PHE 1093 
1094 1 Y 1 A ASP 1094 ? A ASP 1094 
1095 1 Y 1 A ASN 1095 ? A ASN 1095 
1096 1 Y 1 A ALA 1096 ? A ALA 1096 
1097 1 Y 1 A GLU 1097 ? A GLU 1097 
1098 1 Y 1 A THR 1098 ? A THR 1098 
1099 1 Y 1 A LYS 1099 ? A LYS 1099 
1100 1 Y 1 A LYS 1100 ? A LYS 1100 
1101 1 Y 1 A GLU 1101 ? A GLU 1101 
1102 1 Y 1 A PHE 1102 ? A PHE 1102 
1103 1 Y 1 A GLY 1103 ? A GLY 1103 
1104 1 Y 1 A PRO 1104 ? A PRO 1104 
1105 1 Y 1 A VAL 1105 ? A VAL 1105 
1106 1 Y 1 A VAL 1106 ? A VAL 1106 
1107 1 Y 1 A ILE 1107 ? A ILE 1107 
1108 1 Y 1 A ASP 1108 ? A ASP 1108 
1109 1 Y 1 A TYR 1109 ? A TYR 1109 
1110 1 Y 1 A GLY 1110 ? A GLY 1110 
1111 1 Y 1 A LYS 1111 ? A LYS 1111 
1112 1 Y 1 A VAL 1112 ? A VAL 1112 
1113 1 Y 1 A GLN 1113 ? A GLN 1113 
1114 1 Y 1 A SER 1114 ? A SER 1114 
1115 1 Y 1 A LYS 1115 ? A LYS 1115 
1116 1 Y 1 A VAL 1116 ? A VAL 1116 
1117 1 Y 1 A ASN 1117 ? A ASN 1117 
1118 1 Y 1 A LEU 1118 ? A LEU 1118 
1119 1 Y 1 A LYS 1119 ? A LYS 1119 
1120 1 Y 1 A TYR 1120 ? A TYR 1120 
1121 1 Y 1 A ASP 1121 ? A ASP 1121 
1122 1 Y 1 A SER 1122 ? A SER 1122 
1123 1 Y 1 A TRP 1123 ? A TRP 1123 
1124 1 Y 1 A HIS 1124 ? A HIS 1124 
1125 1 Y 1 A LYS 1125 ? A LYS 1125 
1126 1 Y 1 A GLU 1126 ? A GLU 1126 
1127 1 Y 1 A VAL 1127 ? A VAL 1127 
1128 1 Y 1 A LEU 1128 ? A LEU 1128 
1129 1 Y 1 A SER 1129 ? A SER 1129 
1130 1 Y 1 A LYS 1130 ? A LYS 1130 
1131 1 Y 1 A PHE 1131 ? A PHE 1131 
1132 1 Y 1 A GLY 1132 ? A GLY 1132 
1133 1 Y 1 A GLN 1133 ? A GLN 1133 
1134 1 Y 1 A MET 1134 ? A MET 1134 
1135 1 Y 1 A LEU 1135 ? A LEU 1135 
1136 1 Y 1 A GLY 1136 ? A GLY 1136 
1137 1 Y 1 A SER 1137 ? A SER 1137 
1138 1 Y 1 A ASN 1138 ? A ASN 1138 
1139 1 Y 1 A MET 1139 ? A MET 1139 
1140 1 Y 1 A THR 1140 ? A THR 1140 
1141 1 Y 1 A GLU 1141 ? A GLU 1141 
1142 1 Y 1 A PHE 1142 ? A PHE 1142 
1143 1 Y 1 A HIS 1143 ? A HIS 1143 
1144 1 Y 1 A SER 1144 ? A SER 1144 
1145 1 Y 1 A GLN 1145 ? A GLN 1145 
1146 1 Y 1 A ILE 1146 ? A ILE 1146 
1147 1 Y 1 A SER 1147 ? A SER 1147 
1148 1 Y 1 A LYS 1148 ? A LYS 1148 
1149 1 Y 1 A SER 1149 ? A SER 1149 
1150 1 Y 1 A ARG 1150 ? A ARG 1150 
1151 1 Y 1 A GLN 1151 ? A GLN 1151 
1152 1 Y 1 A GLU 1152 ? A GLU 1152 
1153 1 Y 1 A LEU 1153 ? A LEU 1153 
1154 1 Y 1 A GLU 1154 ? A GLU 1154 
1155 1 Y 1 A GLN 1155 ? A GLN 1155 
1156 1 Y 1 A HIS 1156 ? A HIS 1156 
1157 1 Y 1 A SER 1157 ? A SER 1157 
1158 1 Y 1 A VAL 1158 ? A VAL 1158 
1159 1 Y 1 A ASP 1159 ? A ASP 1159 
1160 1 Y 1 A THR 1160 ? A THR 1160 
1161 1 Y 1 A ALA 1161 ? A ALA 1161 
1162 1 Y 1 A SER 1162 ? A SER 1162 
1163 1 Y 1 A THR 1163 ? A THR 1163 
1164 1 Y 1 A SER 1164 ? A SER 1164 
1165 1 Y 1 A ASP 1165 ? A ASP 1165 
1166 1 Y 1 A ALA 1166 ? A ALA 1166 
1167 1 Y 1 A VAL 1167 ? A VAL 1167 
1168 1 Y 1 A THR 1168 ? A THR 1168 
1169 1 Y 1 A PHE 1169 ? A PHE 1169 
1170 1 Y 1 A ILE 1170 ? A ILE 1170 
1171 1 Y 1 A THR 1171 ? A THR 1171 
1172 1 Y 1 A TYR 1172 ? A TYR 1172 
1173 1 Y 1 A VAL 1173 ? A VAL 1173 
1174 1 Y 1 A GLN 1174 ? A GLN 1174 
1175 1 Y 1 A SER 1175 ? A SER 1175 
1176 1 Y 1 A LEU 1176 ? A LEU 1176 
1177 1 Y 1 A LYS 1177 ? A LYS 1177 
1178 1 Y 1 A ARG 1178 ? A ARG 1178 
1179 1 Y 1 A LYS 1179 ? A LYS 1179 
1180 1 Y 1 A ILE 1180 ? A ILE 1180 
1181 1 Y 1 A LYS 1181 ? A LYS 1181 
1182 1 Y 1 A GLN 1182 ? A GLN 1182 
1183 1 Y 1 A PHE 1183 ? A PHE 1183 
1184 1 Y 1 A GLU 1184 ? A GLU 1184 
1185 1 Y 1 A LYS 1185 ? A LYS 1185 
1186 1 Y 1 A GLN 1186 ? A GLN 1186 
1187 1 Y 1 A VAL 1187 ? A VAL 1187 
1188 1 Y 1 A GLU 1188 ? A GLU 1188 
1189 1 Y 1 A LEU 1189 ? A LEU 1189 
1190 1 Y 1 A TYR 1190 ? A TYR 1190 
1191 1 Y 1 A ARG 1191 ? A ARG 1191 
1192 1 Y 1 A ASN 1192 ? A ASN 1192 
1193 1 Y 1 A GLY 1193 ? A GLY 1193 
1194 1 Y 1 A GLN 1194 ? A GLN 1194 
1195 1 Y 1 A ARG 1195 ? A ARG 1195 
1196 1 Y 1 A LEU 1196 ? A LEU 1196 
1197 1 Y 1 A LEU 1197 ? A LEU 1197 
1198 1 Y 1 A GLU 1198 ? A GLU 1198 
1199 1 Y 1 A LYS 1199 ? A LYS 1199 
1200 1 Y 1 A GLN 1200 ? A GLN 1200 
1201 1 Y 1 A ARG 1201 ? A ARG 1201 
1202 1 Y 1 A PHE 1202 ? A PHE 1202 
1203 1 Y 1 A GLN 1203 ? A GLN 1203 
1204 1 Y 1 A PHE 1204 ? A PHE 1204 
1205 1 Y 1 A PRO 1205 ? A PRO 1205 
1206 1 Y 1 A PRO 1206 ? A PRO 1206 
1207 1 Y 1 A SER 1207 ? A SER 1207 
1208 1 Y 1 A TRP 1208 ? A TRP 1208 
1209 1 Y 1 A LEU 1209 ? A LEU 1209 
1210 1 Y 1 A TYR 1210 ? A TYR 1210 
1211 1 Y 1 A ILE 1211 ? A ILE 1211 
1212 1 Y 1 A ASP 1212 ? A ASP 1212 
1213 1 Y 1 A ASN 1213 ? A ASN 1213 
1214 1 Y 1 A ILE 1214 ? A ILE 1214 
1215 1 Y 1 A GLU 1215 ? A GLU 1215 
1216 1 Y 1 A GLY 1216 ? A GLY 1216 
1217 1 Y 1 A GLU 1217 ? A GLU 1217 
1218 1 Y 1 A TRP 1218 ? A TRP 1218 
1219 1 Y 1 A GLY 1219 ? A GLY 1219 
1220 1 Y 1 A ALA 1220 ? A ALA 1220 
1221 1 Y 1 A PHE 1221 ? A PHE 1221 
1222 1 Y 1 A ASN 1222 ? A ASN 1222 
1223 1 Y 1 A ASP 1223 ? A ASP 1223 
1224 1 Y 1 A ILE 1224 ? A ILE 1224 
1225 1 Y 1 A MET 1225 ? A MET 1225 
1226 1 Y 1 A ARG 1226 ? A ARG 1226 
1227 1 Y 1 A ARG 1227 ? A ARG 1227 
1228 1 Y 1 A LYS 1228 ? A LYS 1228 
1229 1 Y 1 A ASP 1229 ? A ASP 1229 
1230 1 Y 1 A SER 1230 ? A SER 1230 
1231 1 Y 1 A ALA 1231 ? A ALA 1231 
1232 1 Y 1 A ILE 1232 ? A ILE 1232 
1233 1 Y 1 A GLN 1233 ? A GLN 1233 
1234 1 Y 1 A GLN 1234 ? A GLN 1234 
1235 1 Y 1 A GLN 1235 ? A GLN 1235 
1236 1 Y 1 A VAL 1236 ? A VAL 1236 
1237 1 Y 1 A ALA 1237 ? A ALA 1237 
1238 1 Y 1 A ASN 1238 ? A ASN 1238 
1239 1 Y 1 A LEU 1239 ? A LEU 1239 
1240 1 Y 1 A GLN 1240 ? A GLN 1240 
1241 1 Y 1 A MET 1241 ? A MET 1241 
1242 1 Y 1 A LYS 1242 ? A LYS 1242 
1243 1 Y 1 A ILE 1243 ? A ILE 1243 
1244 1 Y 1 A VAL 1244 ? A VAL 1244 
1245 1 Y 1 A GLN 1245 ? A GLN 1245 
1246 1 Y 1 A GLU 1246 ? A GLU 1246 
1247 1 Y 1 A ASP 1247 ? A ASP 1247 
1248 1 Y 1 A ARG 1248 ? A ARG 1248 
1249 1 Y 1 A ALA 1249 ? A ALA 1249 
1250 1 Y 1 A VAL 1250 ? A VAL 1250 
1251 1 Y 1 A GLU 1251 ? A GLU 1251 
1252 1 Y 1 A SER 1252 ? A SER 1252 
1253 1 Y 1 A ARG 1253 ? A ARG 1253 
1254 1 Y 1 A THR 1254 ? A THR 1254 
1255 1 Y 1 A THR 1255 ? A THR 1255 
1256 1 Y 1 A ASP 1256 ? A ASP 1256 
1257 1 Y 1 A LEU 1257 ? A LEU 1257 
1258 1 Y 1 A LEU 1258 ? A LEU 1258 
1259 1 Y 1 A THR 1259 ? A THR 1259 
1260 1 Y 1 A ASP 1260 ? A ASP 1260 
1261 1 Y 1 A TRP 1261 ? A TRP 1261 
1262 1 Y 1 A GLU 1262 ? A GLU 1262 
1263 1 Y 1 A LYS 1263 ? A LYS 1263 
1264 1 Y 1 A THR 1264 ? A THR 1264 
1265 1 Y 1 A LYS 1265 ? A LYS 1265 
1266 1 Y 1 A PRO 1266 ? A PRO 1266 
1267 1 Y 1 A VAL 1267 ? A VAL 1267 
1268 1 Y 1 A THR 1268 ? A THR 1268 
1269 1 Y 1 A GLY 1269 ? A GLY 1269 
1270 1 Y 1 A ASN 1270 ? A ASN 1270 
1271 1 Y 1 A LEU 1271 ? A LEU 1271 
1272 1 Y 1 A ARG 1272 ? A ARG 1272 
1273 1 Y 1 A PRO 1273 ? A PRO 1273 
1274 1 Y 1 A GLU 1274 ? A GLU 1274 
1275 1 Y 1 A GLU 1275 ? A GLU 1275 
1276 1 Y 1 A ALA 1276 ? A ALA 1276 
1277 1 Y 1 A LEU 1277 ? A LEU 1277 
1278 1 Y 1 A GLN 1278 ? A GLN 1278 
1279 1 Y 1 A ALA 1279 ? A ALA 1279 
1280 1 Y 1 A LEU 1280 ? A LEU 1280 
1281 1 Y 1 A THR 1281 ? A THR 1281 
1282 1 Y 1 A ILE 1282 ? A ILE 1282 
1283 1 Y 1 A TYR 1283 ? A TYR 1283 
1284 1 Y 1 A GLU 1284 ? A GLU 1284 
1285 1 Y 1 A GLY 1285 ? A GLY 1285 
1286 1 Y 1 A LYS 1286 ? A LYS 1286 
1287 1 Y 1 A PHE 1287 ? A PHE 1287 
1288 1 Y 1 A GLY 1288 ? A GLY 1288 
1289 1 Y 1 A ARG 1289 ? A ARG 1289 
1290 1 Y 1 A LEU 1290 ? A LEU 1290 
1291 1 Y 1 A LYS 1291 ? A LYS 1291 
1292 1 Y 1 A ASP 1292 ? A ASP 1292 
1293 1 Y 1 A ASP 1293 ? A ASP 1293 
1294 1 Y 1 A ARG 1294 ? A ARG 1294 
1295 1 Y 1 A GLU 1295 ? A GLU 1295 
1296 1 Y 1 A LYS 1296 ? A LYS 1296 
1297 1 Y 1 A CYS 1297 ? A CYS 1297 
1298 1 Y 1 A ALA 1298 ? A ALA 1298 
1299 1 Y 1 A LYS 1299 ? A LYS 1299 
1300 1 Y 1 A ALA 1300 ? A ALA 1300 
1301 1 Y 1 A LYS 1301 ? A LYS 1301 
1302 1 Y 1 A GLU 1302 ? A GLU 1302 
1303 1 Y 1 A ALA 1303 ? A ALA 1303 
1304 1 Y 1 A LEU 1304 ? A LEU 1304 
1305 1 Y 1 A GLU 1305 ? A GLU 1305 
1306 1 Y 1 A LEU 1306 ? A LEU 1306 
1307 1 Y 1 A THR 1307 ? A THR 1307 
1308 1 Y 1 A ASP 1308 ? A ASP 1308 
1309 1 Y 1 A THR 1309 ? A THR 1309 
1310 1 Y 1 A GLY 1310 ? A GLY 1310 
1311 1 Y 1 A LEU 1311 ? A LEU 1311 
1312 1 Y 1 A LEU 1312 ? A LEU 1312 
1313 1 Y 1 A SER 1313 ? A SER 1313 
1314 1 Y 1 A GLY 1314 ? A GLY 1314 
1315 1 Y 1 A SER 1315 ? A SER 1315 
1316 1 Y 1 A GLU 1316 ? A GLU 1316 
1317 1 Y 1 A GLU 1317 ? A GLU 1317 
1318 1 Y 1 A ARG 1318 ? A ARG 1318 
1319 1 Y 1 A VAL 1319 ? A VAL 1319 
1320 1 Y 1 A GLN 1320 ? A GLN 1320 
1321 1 Y 1 A VAL 1321 ? A VAL 1321 
1322 1 Y 1 A ALA 1322 ? A ALA 1322 
1323 1 Y 1 A LEU 1323 ? A LEU 1323 
1324 1 Y 1 A GLU 1324 ? A GLU 1324 
1325 1 Y 1 A GLU 1325 ? A GLU 1325 
1326 1 Y 1 A LEU 1326 ? A LEU 1326 
1327 1 Y 1 A GLN 1327 ? A GLN 1327 
1328 1 Y 1 A ASP 1328 ? A ASP 1328 
1329 1 Y 1 A LEU 1329 ? A LEU 1329 
1330 1 Y 1 A LYS 1330 ? A LYS 1330 
1331 1 Y 1 A GLY 1331 ? A GLY 1331 
1332 1 Y 1 A VAL 1332 ? A VAL 1332 
1333 1 Y 1 A TRP 1333 ? A TRP 1333 
1334 1 Y 1 A SER 1334 ? A SER 1334 
1335 1 Y 1 A GLU 1335 ? A GLU 1335 
1336 1 Y 1 A LEU 1336 ? A LEU 1336 
1337 1 Y 1 A SER 1337 ? A SER 1337 
1338 1 Y 1 A LYS 1338 ? A LYS 1338 
1339 1 Y 1 A VAL 1339 ? A VAL 1339 
1340 1 Y 1 A TRP 1340 ? A TRP 1340 
1341 1 Y 1 A GLU 1341 ? A GLU 1341 
1342 1 Y 1 A GLN 1342 ? A GLN 1342 
1343 1 Y 1 A ILE 1343 ? A ILE 1343 
1344 1 Y 1 A ASP 1344 ? A ASP 1344 
1345 1 Y 1 A GLN 1345 ? A GLN 1345 
1346 1 Y 1 A MET 1346 ? A MET 1346 
1347 1 Y 1 A LYS 1347 ? A LYS 1347 
1348 1 Y 1 A GLU 1348 ? A GLU 1348 
1349 1 Y 1 A GLN 1349 ? A GLN 1349 
1350 1 Y 1 A PRO 1350 ? A PRO 1350 
1351 1 Y 1 A TRP 1351 ? A TRP 1351 
1352 1 Y 1 A VAL 1352 ? A VAL 1352 
1353 1 Y 1 A SER 1353 ? A SER 1353 
1354 1 Y 1 A VAL 1354 ? A VAL 1354 
1355 1 Y 1 A GLN 1355 ? A GLN 1355 
1356 1 Y 1 A PRO 1356 ? A PRO 1356 
1357 1 Y 1 A ARG 1357 ? A ARG 1357 
1358 1 Y 1 A LYS 1358 ? A LYS 1358 
1359 1 Y 1 A LEU 1359 ? A LEU 1359 
1360 1 Y 1 A ARG 1360 ? A ARG 1360 
1361 1 Y 1 A GLN 1361 ? A GLN 1361 
1362 1 Y 1 A ASN 1362 ? A ASN 1362 
1363 1 Y 1 A LEU 1363 ? A LEU 1363 
1364 1 Y 1 A ASP 1364 ? A ASP 1364 
1365 1 Y 1 A ALA 1365 ? A ALA 1365 
1366 1 Y 1 A LEU 1366 ? A LEU 1366 
1367 1 Y 1 A LEU 1367 ? A LEU 1367 
1368 1 Y 1 A ASN 1368 ? A ASN 1368 
1369 1 Y 1 A GLN 1369 ? A GLN 1369 
1370 1 Y 1 A LEU 1370 ? A LEU 1370 
1371 1 Y 1 A LYS 1371 ? A LYS 1371 
1372 1 Y 1 A SER 1372 ? A SER 1372 
1373 1 Y 1 A PHE 1373 ? A PHE 1373 
1374 1 Y 1 A PRO 1374 ? A PRO 1374 
1375 1 Y 1 A ALA 1375 ? A ALA 1375 
1376 1 Y 1 A ARG 1376 ? A ARG 1376 
1377 1 Y 1 A LEU 1377 ? A LEU 1377 
1378 1 Y 1 A ARG 1378 ? A ARG 1378 
1379 1 Y 1 A GLN 1379 ? A GLN 1379 
1380 1 Y 1 A TYR 1380 ? A TYR 1380 
1381 1 Y 1 A ALA 1381 ? A ALA 1381 
1382 1 Y 1 A SER 1382 ? A SER 1382 
1383 1 Y 1 A TYR 1383 ? A TYR 1383 
1384 1 Y 1 A GLU 1384 ? A GLU 1384 
1385 1 Y 1 A PHE 1385 ? A PHE 1385 
1386 1 Y 1 A VAL 1386 ? A VAL 1386 
1387 1 Y 1 A GLN 1387 ? A GLN 1387 
1388 1 Y 1 A ARG 1388 ? A ARG 1388 
1389 1 Y 1 A LEU 1389 ? A LEU 1389 
1390 1 Y 1 A LEU 1390 ? A LEU 1390 
1391 1 Y 1 A LYS 1391 ? A LYS 1391 
1392 1 Y 1 A GLY 1392 ? A GLY 1392 
1393 1 Y 1 A TYR 1393 ? A TYR 1393 
1394 1 Y 1 A MET 1394 ? A MET 1394 
1395 1 Y 1 A LYS 1395 ? A LYS 1395 
1396 1 Y 1 A ILE 1396 ? A ILE 1396 
1397 1 Y 1 A ASN 1397 ? A ASN 1397 
1398 1 Y 1 A MET 1398 ? A MET 1398 
1399 1 Y 1 A LEU 1399 ? A LEU 1399 
1400 1 Y 1 A VAL 1400 ? A VAL 1400 
1401 1 Y 1 A ILE 1401 ? A ILE 1401 
1402 1 Y 1 A GLU 1402 ? A GLU 1402 
1403 1 Y 1 A LEU 1403 ? A LEU 1403 
1404 1 Y 1 A LYS 1404 ? A LYS 1404 
1405 1 Y 1 A SER 1405 ? A SER 1405 
1406 1 Y 1 A GLU 1406 ? A GLU 1406 
1407 1 Y 1 A ALA 1407 ? A ALA 1407 
1408 1 Y 1 A LEU 1408 ? A LEU 1408 
1409 1 Y 1 A LYS 1409 ? A LYS 1409 
1410 1 Y 1 A ASP 1410 ? A ASP 1410 
1411 1 Y 1 A ARG 1411 ? A ARG 1411 
1412 1 Y 1 A HIS 1412 ? A HIS 1412 
1413 1 Y 1 A TRP 1413 ? A TRP 1413 
1414 1 Y 1 A LYS 1414 ? A LYS 1414 
1415 1 Y 1 A GLN 1415 ? A GLN 1415 
1416 1 Y 1 A LEU 1416 ? A LEU 1416 
1417 1 Y 1 A MET 1417 ? A MET 1417 
1418 1 Y 1 A LYS 1418 ? A LYS 1418 
1419 1 Y 1 A ARG 1419 ? A ARG 1419 
1420 1 Y 1 A LEU 1420 ? A LEU 1420 
1421 1 Y 1 A HIS 1421 ? A HIS 1421 
1422 1 Y 1 A VAL 1422 ? A VAL 1422 
1423 1 Y 1 A ASN 1423 ? A ASN 1423 
1424 1 Y 1 A TRP 1424 ? A TRP 1424 
1425 1 Y 1 A VAL 1425 ? A VAL 1425 
1426 1 Y 1 A VAL 1426 ? A VAL 1426 
1427 1 Y 1 A SER 1427 ? A SER 1427 
1428 1 Y 1 A GLU 1428 ? A GLU 1428 
1429 1 Y 1 A LEU 1429 ? A LEU 1429 
1430 1 Y 1 A THR 1430 ? A THR 1430 
1431 1 Y 1 A LEU 1431 ? A LEU 1431 
1432 1 Y 1 A GLY 1432 ? A GLY 1432 
1433 1 Y 1 A GLN 1433 ? A GLN 1433 
1434 1 Y 1 A ILE 1434 ? A ILE 1434 
1435 1 Y 1 A TRP 1435 ? A TRP 1435 
1436 1 Y 1 A ASP 1436 ? A ASP 1436 
1437 1 Y 1 A VAL 1437 ? A VAL 1437 
1438 1 Y 1 A ASP 1438 ? A ASP 1438 
1439 1 Y 1 A LEU 1439 ? A LEU 1439 
1440 1 Y 1 A GLN 1440 ? A GLN 1440 
1441 1 Y 1 A LYS 1441 ? A LYS 1441 
1442 1 Y 1 A ASN 1442 ? A ASN 1442 
1443 1 Y 1 A GLU 1443 ? A GLU 1443 
1444 1 Y 1 A ALA 1444 ? A ALA 1444 
1445 1 Y 1 A ILE 1445 ? A ILE 1445 
1446 1 Y 1 A VAL 1446 ? A VAL 1446 
1447 1 Y 1 A LYS 1447 ? A LYS 1447 
1448 1 Y 1 A ASP 1448 ? A ASP 1448 
1449 1 Y 1 A VAL 1449 ? A VAL 1449 
1450 1 Y 1 A LEU 1450 ? A LEU 1450 
1451 1 Y 1 A LEU 1451 ? A LEU 1451 
1452 1 Y 1 A VAL 1452 ? A VAL 1452 
1453 1 Y 1 A ALA 1453 ? A ALA 1453 
1454 1 Y 1 A GLN 1454 ? A GLN 1454 
1455 1 Y 1 A GLY 1455 ? A GLY 1455 
1456 1 Y 1 A GLU 1456 ? A GLU 1456 
1457 1 Y 1 A MET 1457 ? A MET 1457 
1458 1 Y 1 A ALA 1458 ? A ALA 1458 
1459 1 Y 1 A LEU 1459 ? A LEU 1459 
1460 1 Y 1 A GLU 1460 ? A GLU 1460 
1461 1 Y 1 A GLU 1461 ? A GLU 1461 
1462 1 Y 1 A PHE 1462 ? A PHE 1462 
1463 1 Y 1 A LEU 1463 ? A LEU 1463 
1464 1 Y 1 A LYS 1464 ? A LYS 1464 
1465 1 Y 1 A GLN 1465 ? A GLN 1465 
1466 1 Y 1 A ILE 1466 ? A ILE 1466 
1467 1 Y 1 A ARG 1467 ? A ARG 1467 
1468 1 Y 1 A GLU 1468 ? A GLU 1468 
1469 1 Y 1 A VAL 1469 ? A VAL 1469 
1470 1 Y 1 A TRP 1470 ? A TRP 1470 
1471 1 Y 1 A ASN 1471 ? A ASN 1471 
1472 1 Y 1 A THR 1472 ? A THR 1472 
1473 1 Y 1 A TYR 1473 ? A TYR 1473 
1474 1 Y 1 A GLU 1474 ? A GLU 1474 
1475 1 Y 1 A LEU 1475 ? A LEU 1475 
1476 1 Y 1 A ASP 1476 ? A ASP 1476 
1477 1 Y 1 A LEU 1477 ? A LEU 1477 
1478 1 Y 1 A VAL 1478 ? A VAL 1478 
1479 1 Y 1 A ASN 1479 ? A ASN 1479 
1480 1 Y 1 A TYR 1480 ? A TYR 1480 
1481 1 Y 1 A GLN 1481 ? A GLN 1481 
1482 1 Y 1 A ASN 1482 ? A ASN 1482 
1483 1 Y 1 A LYS 1483 ? A LYS 1483 
1484 1 Y 1 A CYS 1484 ? A CYS 1484 
1485 1 Y 1 A ARG 1485 ? A ARG 1485 
1486 1 Y 1 A LEU 1486 ? A LEU 1486 
1487 1 Y 1 A ILE 1487 ? A ILE 1487 
1488 1 Y 1 A ARG 1488 ? A ARG 1488 
1489 1 Y 1 A GLY 1489 ? A GLY 1489 
1490 1 Y 1 A TRP 1490 ? A TRP 1490 
1491 1 Y 1 A ASP 1491 ? A ASP 1491 
1492 1 Y 1 A ASP 1492 ? A ASP 1492 
1493 1 Y 1 A LEU 1493 ? A LEU 1493 
1494 1 Y 1 A PHE 1494 ? A PHE 1494 
1495 1 Y 1 A ASN 1495 ? A ASN 1495 
1496 1 Y 1 A LYS 1496 ? A LYS 1496 
1497 1 Y 1 A VAL 1497 ? A VAL 1497 
1498 1 Y 1 A LYS 1498 ? A LYS 1498 
1499 1 Y 1 A GLU 1499 ? A GLU 1499 
1500 1 Y 1 A HIS 1500 ? A HIS 1500 
1501 1 Y 1 A ILE 1501 ? A ILE 1501 
1502 1 Y 1 A ASN 1502 ? A ASN 1502 
1503 1 Y 1 A SER 1503 ? A SER 1503 
1504 1 Y 1 A VAL 1504 ? A VAL 1504 
1505 1 Y 1 A SER 1505 ? A SER 1505 
1506 1 Y 1 A ALA 1506 ? A ALA 1506 
1507 1 Y 1 A MET 1507 ? A MET 1507 
1508 1 Y 1 A LYS 1508 ? A LYS 1508 
1509 1 Y 1 A LEU 1509 ? A LEU 1509 
1510 1 Y 1 A SER 1510 ? A SER 1510 
1511 1 Y 1 A PRO 1511 ? A PRO 1511 
1512 1 Y 1 A TYR 1512 ? A TYR 1512 
1513 1 Y 1 A TYR 1513 ? A TYR 1513 
1514 1 Y 1 A LYS 1514 ? A LYS 1514 
1515 1 Y 1 A VAL 1515 ? A VAL 1515 
1516 1 Y 1 A PHE 1516 ? A PHE 1516 
1517 1 Y 1 A GLU 1517 ? A GLU 1517 
1518 1 Y 1 A GLU 1518 ? A GLU 1518 
1519 1 Y 1 A ASP 1519 ? A ASP 1519 
1520 1 Y 1 A ALA 1520 ? A ALA 1520 
1521 1 Y 1 A LEU 1521 ? A LEU 1521 
1522 1 Y 1 A SER 1522 ? A SER 1522 
1523 1 Y 1 A TRP 1523 ? A TRP 1523 
1524 1 Y 1 A GLU 1524 ? A GLU 1524 
1525 1 Y 1 A ASP 1525 ? A ASP 1525 
1526 1 Y 1 A LYS 1526 ? A LYS 1526 
1527 1 Y 1 A LEU 1527 ? A LEU 1527 
1528 1 Y 1 A ASN 1528 ? A ASN 1528 
1529 1 Y 1 A ARG 1529 ? A ARG 1529 
1530 1 Y 1 A ILE 1530 ? A ILE 1530 
1531 1 Y 1 A MET 1531 ? A MET 1531 
1532 1 Y 1 A ALA 1532 ? A ALA 1532 
1533 1 Y 1 A LEU 1533 ? A LEU 1533 
1534 1 Y 1 A PHE 1534 ? A PHE 1534 
1535 1 Y 1 A GLY 2390 ? A GLY 2390 
1536 1 Y 1 A GLU 2391 ? A GLU 2391 
1537 1 Y 1 A ASP 2392 ? A ASP 2392 
1538 1 Y 1 A GLU 2393 ? A GLU 2393 
1539 1 Y 1 A ALA 2394 ? A ALA 2394 
1540 1 Y 1 A GLN 2395 ? A GLN 2395 
1541 1 Y 1 A ARG 2396 ? A ARG 2396 
1542 1 Y 1 A ARG 2397 ? A ARG 2397 
1543 1 Y 1 A ARG 2398 ? A ARG 2398 
1544 1 Y 1 A LYS 2399 ? A LYS 2399 
1545 1 Y 1 A GLY 2400 ? A GLY 2400 
1546 1 Y 1 A LYS 2401 ? A LYS 2401 
1547 1 Y 1 A GLU 2402 ? A GLU 2402 
1548 1 Y 1 A ASP 2403 ? A ASP 2403 
1549 1 Y 1 A GLU 2404 ? A GLU 2404 
1550 1 Y 1 A GLY 2405 ? A GLY 2405 
1551 1 Y 1 A GLU 2406 ? A GLU 2406 
1552 1 Y 1 A GLU 2407 ? A GLU 2407 
1553 1 Y 1 A ALA 2408 ? A ALA 2408 
1554 1 Y 1 A ALA 2409 ? A ALA 2409 
1555 1 Y 1 A MET 3243 ? A MET 3243 
1556 1 Y 1 A VAL 3244 ? A VAL 3244 
1557 1 Y 1 A LYS 3245 ? A LYS 3245 
1558 1 Y 1 A ASP 3246 ? A ASP 3246 
1559 1 Y 1 A GLN 3247 ? A GLN 3247 
1560 1 Y 1 A GLN 3248 ? A GLN 3248 
1561 1 Y 1 A GLU 3249 ? A GLU 3249 
1562 1 Y 1 A ALA 3250 ? A ALA 3250 
1563 1 Y 1 A GLU 3251 ? A GLU 3251 
1564 1 Y 1 A LYS 3252 ? A LYS 3252 
1565 1 Y 1 A LYS 3253 ? A LYS 3253 
1566 1 Y 1 A LYS 3254 ? A LYS 3254 
1567 1 Y 1 A VAL 3255 ? A VAL 3255 
1568 1 Y 1 A MET 3256 ? A MET 3256 
1569 1 Y 1 A SER 3257 ? A SER 3257 
1570 1 Y 1 A GLN 3258 ? A GLN 3258 
1571 1 Y 1 A GLU 3259 ? A GLU 3259 
1572 1 Y 1 A ILE 3260 ? A ILE 3260 
1573 1 Y 1 A GLN 3261 ? A GLN 3261 
1574 1 Y 1 A GLU 3262 ? A GLU 3262 
1575 1 Y 1 A GLN 3263 ? A GLN 3263 
1576 1 Y 1 A LEU 3264 ? A LEU 3264 
1577 1 Y 1 A HIS 3265 ? A HIS 3265 
1578 1 Y 1 A LYS 3266 ? A LYS 3266 
1579 1 Y 1 A GLN 3267 ? A GLN 3267 
1580 1 Y 1 A GLN 3268 ? A GLN 3268 
1581 1 Y 1 A GLU 3269 ? A GLU 3269 
1582 1 Y 1 A VAL 3270 ? A VAL 3270 
1583 1 Y 1 A ILE 3271 ? A ILE 3271 
1584 1 Y 1 A ALA 3272 ? A ALA 3272 
1585 1 Y 1 A ASP 3273 ? A ASP 3273 
1586 1 Y 1 A LYS 3274 ? A LYS 3274 
1587 1 Y 1 A GLN 3275 ? A GLN 3275 
1588 1 Y 1 A MET 3276 ? A MET 3276 
1589 1 Y 1 A SER 3277 ? A SER 3277 
1590 1 Y 1 A VAL 3278 ? A VAL 3278 
1591 1 Y 1 A LYS 3279 ? A LYS 3279 
1592 1 Y 1 A GLU 3280 ? A GLU 3280 
1593 1 Y 1 A ASP 3281 ? A ASP 3281 
1594 1 Y 1 A LEU 3282 ? A LEU 3282 
1595 1 Y 1 A ASP 3283 ? A ASP 3283 
1596 1 Y 1 A LYS 3284 ? A LYS 3284 
1597 1 Y 1 A VAL 3285 ? A VAL 3285 
1598 1 Y 1 A GLU 3286 ? A GLU 3286 
1599 1 Y 1 A PRO 3287 ? A PRO 3287 
1600 1 Y 1 A ALA 3288 ? A ALA 3288 
1601 1 Y 1 A VAL 3289 ? A VAL 3289 
1602 1 Y 1 A ILE 3290 ? A ILE 3290 
1603 1 Y 1 A GLU 3291 ? A GLU 3291 
1604 1 Y 1 A ALA 3292 ? A ALA 3292 
1605 1 Y 1 A GLN 3293 ? A GLN 3293 
1606 1 Y 1 A ASN 3294 ? A ASN 3294 
1607 1 Y 1 A ALA 3295 ? A ALA 3295 
1608 1 Y 1 A VAL 3296 ? A VAL 3296 
1609 1 Y 1 A LYS 3297 ? A LYS 3297 
1610 1 Y 1 A SER 3298 ? A SER 3298 
1611 1 Y 1 A ILE 3299 ? A ILE 3299 
1612 1 Y 1 A LYS 3300 ? A LYS 3300 
1613 1 Y 1 A LYS 3301 ? A LYS 3301 
1614 1 Y 1 A GLN 3302 ? A GLN 3302 
1615 1 Y 1 A HIS 3303 ? A HIS 3303 
1616 1 Y 1 A LEU 3304 ? A LEU 3304 
1617 1 Y 1 A VAL 3305 ? A VAL 3305 
1618 1 Y 1 A GLU 3306 ? A GLU 3306 
1619 1 Y 1 A VAL 3307 ? A VAL 3307 
1620 1 Y 1 A ARG 3308 ? A ARG 3308 
1621 1 Y 1 A SER 3309 ? A SER 3309 
1622 1 Y 1 A MET 3310 ? A MET 3310 
1623 1 Y 1 A ALA 3311 ? A ALA 3311 
1624 1 Y 1 A ASN 3312 ? A ASN 3312 
1625 1 Y 1 A PRO 3313 ? A PRO 3313 
1626 1 Y 1 A PRO 3314 ? A PRO 3314 
1627 1 Y 1 A ALA 3315 ? A ALA 3315 
1628 1 Y 1 A ALA 3316 ? A ALA 3316 
1629 1 Y 1 A VAL 3317 ? A VAL 3317 
1630 1 Y 1 A LYS 3318 ? A LYS 3318 
1631 1 Y 1 A LEU 3319 ? A LEU 3319 
1632 1 Y 1 A ALA 3320 ? A ALA 3320 
1633 1 Y 1 A LEU 3321 ? A LEU 3321 
1634 1 Y 1 A GLU 3322 ? A GLU 3322 
1635 1 Y 1 A SER 3323 ? A SER 3323 
1636 1 Y 1 A ILE 3324 ? A ILE 3324 
1637 1 Y 1 A CYS 3325 ? A CYS 3325 
1638 1 Y 1 A LEU 3326 ? A LEU 3326 
1639 1 Y 1 A LEU 3327 ? A LEU 3327 
1640 1 Y 1 A LEU 3328 ? A LEU 3328 
1641 1 Y 1 A GLY 3329 ? A GLY 3329 
1642 1 Y 1 A GLU 3330 ? A GLU 3330 
1643 1 Y 1 A SER 3331 ? A SER 3331 
1644 1 Y 1 A THR 3332 ? A THR 3332 
1645 1 Y 1 A THR 3333 ? A THR 3333 
1646 1 Y 1 A ASP 3334 ? A ASP 3334 
1647 1 Y 1 A TRP 3335 ? A TRP 3335 
1648 1 Y 1 A LYS 3336 ? A LYS 3336 
1649 1 Y 1 A GLN 3337 ? A GLN 3337 
1650 1 Y 1 A ILE 3338 ? A ILE 3338 
1651 1 Y 1 A ARG 3339 ? A ARG 3339 
1652 1 Y 1 A SER 3340 ? A SER 3340 
1653 1 Y 1 A ILE 3341 ? A ILE 3341 
1654 1 Y 1 A ILE 3342 ? A ILE 3342 
1655 1 Y 1 A MET 3343 ? A MET 3343 
1656 1 Y 1 A ARG 3344 ? A ARG 3344 
1657 1 Y 1 A GLU 3345 ? A GLU 3345 
1658 1 Y 1 A ASN 3346 ? A ASN 3346 
1659 1 Y 1 A PHE 3347 ? A PHE 3347 
1660 1 Y 1 A ILE 3348 ? A ILE 3348 
1661 1 Y 1 A PRO 3349 ? A PRO 3349 
1662 1 Y 1 A THR 3350 ? A THR 3350 
1663 1 Y 1 A ILE 3351 ? A ILE 3351 
1664 1 Y 1 A VAL 3352 ? A VAL 3352 
1665 1 Y 1 A ASN 3353 ? A ASN 3353 
1666 1 Y 1 A PHE 3354 ? A PHE 3354 
1667 1 Y 1 A SER 3355 ? A SER 3355 
1668 1 Y 1 A ALA 3356 ? A ALA 3356 
1669 1 Y 1 A GLU 3357 ? A GLU 3357 
1670 1 Y 1 A GLU 3358 ? A GLU 3358 
1671 1 Y 1 A ILE 3359 ? A ILE 3359 
1672 1 Y 1 A SER 3360 ? A SER 3360 
1673 1 Y 1 A ASP 3361 ? A ASP 3361 
1674 1 Y 1 A ALA 3362 ? A ALA 3362 
1675 1 Y 1 A ILE 3363 ? A ILE 3363 
1676 1 Y 1 A ARG 3364 ? A ARG 3364 
1677 1 Y 1 A GLU 3365 ? A GLU 3365 
1678 1 Y 1 A LYS 3366 ? A LYS 3366 
1679 1 Y 1 A MET 3367 ? A MET 3367 
1680 1 Y 1 A LYS 3368 ? A LYS 3368 
1681 1 Y 1 A LYS 3369 ? A LYS 3369 
1682 1 Y 1 A ASN 3370 ? A ASN 3370 
1683 1 Y 1 A TYR 3371 ? A TYR 3371 
1684 1 Y 1 A MET 3372 ? A MET 3372 
1685 1 Y 1 A SER 3373 ? A SER 3373 
1686 1 Y 1 A ASN 3374 ? A ASN 3374 
1687 1 Y 1 A PRO 3375 ? A PRO 3375 
1688 1 Y 1 A SER 3376 ? A SER 3376 
1689 1 Y 1 A TYR 3377 ? A TYR 3377 
1690 1 Y 1 A ASN 3378 ? A ASN 3378 
1691 1 Y 1 A TYR 3379 ? A TYR 3379 
1692 1 Y 1 A GLU 3380 ? A GLU 3380 
1693 1 Y 1 A ILE 3381 ? A ILE 3381 
1694 1 Y 1 A VAL 3382 ? A VAL 3382 
1695 1 Y 1 A ASN 3383 ? A ASN 3383 
1696 1 Y 1 A ARG 3384 ? A ARG 3384 
1697 1 Y 1 A ALA 3385 ? A ALA 3385 
1698 1 Y 1 A SER 3386 ? A SER 3386 
1699 1 Y 1 A LEU 3387 ? A LEU 3387 
1700 1 Y 1 A ALA 3388 ? A ALA 3388 
1701 1 Y 1 A CYS 3389 ? A CYS 3389 
1702 1 Y 1 A GLY 3390 ? A GLY 3390 
1703 1 Y 1 A PRO 3391 ? A PRO 3391 
1704 1 Y 1 A MET 3392 ? A MET 3392 
1705 1 Y 1 A VAL 3393 ? A VAL 3393 
1706 1 Y 1 A LYS 3394 ? A LYS 3394 
1707 1 Y 1 A TRP 3395 ? A TRP 3395 
1708 1 Y 1 A ALA 3396 ? A ALA 3396 
1709 1 Y 1 A ILE 3397 ? A ILE 3397 
1710 1 Y 1 A ALA 3398 ? A ALA 3398 
1711 1 Y 1 A GLN 3399 ? A GLN 3399 
1712 1 Y 1 A LEU 3400 ? A LEU 3400 
1713 1 Y 1 A ASN 3401 ? A ASN 3401 
1714 1 Y 1 A TYR 3402 ? A TYR 3402 
1715 1 Y 1 A ALA 3403 ? A ALA 3403 
1716 1 Y 1 A ASP 3404 ? A ASP 3404 
1717 1 Y 1 A MET 3405 ? A MET 3405 
1718 1 Y 1 A LEU 3406 ? A LEU 3406 
1719 1 Y 1 A LYS 3407 ? A LYS 3407 
1720 1 Y 1 A ARG 3408 ? A ARG 3408 
1721 1 Y 1 A VAL 3409 ? A VAL 3409 
1722 1 Y 1 A GLU 3410 ? A GLU 3410 
1723 1 Y 1 A PRO 3411 ? A PRO 3411 
1724 1 Y 1 A LEU 3412 ? A LEU 3412 
1725 1 Y 1 A ARG 3413 ? A ARG 3413 
1726 1 Y 1 A ASN 3414 ? A ASN 3414 
1727 1 Y 1 A GLU 3415 ? A GLU 3415 
1728 1 Y 1 A LEU 3416 ? A LEU 3416 
1729 1 Y 1 A GLN 3417 ? A GLN 3417 
1730 1 Y 1 A LYS 3418 ? A LYS 3418 
1731 1 Y 1 A LEU 3419 ? A LEU 3419 
1732 1 Y 1 A GLU 3420 ? A GLU 3420 
1733 1 Y 1 A ASP 3421 ? A ASP 3421 
1734 1 Y 1 A ASP 3422 ? A ASP 3422 
1735 1 Y 1 A ALA 3423 ? A ALA 3423 
1736 1 Y 1 A LYS 3424 ? A LYS 3424 
1737 1 Y 1 A ASP 3425 ? A ASP 3425 
1738 1 Y 1 A ASN 3426 ? A ASN 3426 
1739 1 Y 1 A GLN 3427 ? A GLN 3427 
1740 1 Y 1 A GLN 3428 ? A GLN 3428 
1741 1 Y 1 A LYS 3429 ? A LYS 3429 
1742 1 Y 1 A ALA 3430 ? A ALA 3430 
1743 1 Y 1 A ASN 3431 ? A ASN 3431 
1744 1 Y 1 A GLU 3432 ? A GLU 3432 
1745 1 Y 1 A VAL 3433 ? A VAL 3433 
1746 1 Y 1 A GLU 3434 ? A GLU 3434 
1747 1 Y 1 A GLN 3435 ? A GLN 3435 
1748 1 Y 1 A MET 3436 ? A MET 3436 
1749 1 Y 1 A ILE 3437 ? A ILE 3437 
1750 1 Y 1 A ARG 3438 ? A ARG 3438 
1751 1 Y 1 A ASP 3439 ? A ASP 3439 
1752 1 Y 1 A LEU 3440 ? A LEU 3440 
1753 1 Y 1 A GLU 3441 ? A GLU 3441 
1754 1 Y 1 A ALA 3442 ? A ALA 3442 
1755 1 Y 1 A SER 3443 ? A SER 3443 
1756 1 Y 1 A ILE 3444 ? A ILE 3444 
1757 1 Y 1 A ALA 3445 ? A ALA 3445 
1758 1 Y 1 A ARG 3446 ? A ARG 3446 
1759 1 Y 1 A TYR 3447 ? A TYR 3447 
1760 1 Y 1 A LYS 3448 ? A LYS 3448 
1761 1 Y 1 A MET 4348 ? A MET 4348 
1762 1 Y 1 A LEU 4349 ? A LEU 4349 
1763 1 Y 1 A GLU 4350 ? A GLU 4350 
1764 1 Y 1 A ASP 4351 ? A ASP 4351 
1765 1 Y 1 A GLU 4352 ? A GLU 4352 
1766 1 Y 1 A ASP 4353 ? A ASP 4353 
1767 1 Y 1 A ASP 4354 ? A ASP 4354 
1768 1 Y 1 A LEU 4355 ? A LEU 4355 
1769 1 Y 1 A ALA 4356 ? A ALA 4356 
1770 1 Y 1 A TYR 4357 ? A TYR 4357 
1771 1 Y 1 A ALA 4358 ? A ALA 4358 
1772 1 Y 1 A GLU 4359 ? A GLU 4359 
1773 1 Y 1 A THR 4360 ? A THR 4360 
1774 1 Y 1 A GLU 4361 ? A GLU 4361 
1775 1 Y 1 A LYS 4362 ? A LYS 4362 
1776 1 Y 1 A LYS 4363 ? A LYS 4363 
1777 1 Y 1 A THR 4364 ? A THR 4364 
1778 1 Y 1 A ARG 4365 ? A ARG 4365 
1779 1 Y 1 A THR 4366 ? A THR 4366 
1780 1 Y 1 A ASP 4367 ? A ASP 4367 
1781 1 Y 1 A SER 4368 ? A SER 4368 
1782 1 Y 1 A THR 4369 ? A THR 4369 
1783 1 Y 1 A SER 4370 ? A SER 4370 
1784 1 Y 1 A ASP 4371 ? A ASP 4371 
1785 1 Y 1 A GLY 4372 ? A GLY 4372 
1786 1 Y 1 A ARG 4373 ? A ARG 4373 
1787 1 Y 1 A GLU 4646 ? A GLU 4646 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ADP PB     P  N N 1   
ADP O1B    O  N N 2   
ADP O2B    O  N N 3   
ADP O3B    O  N N 4   
ADP PA     P  N S 5   
ADP O1A    O  N N 6   
ADP O2A    O  N N 7   
ADP O3A    O  N N 8   
ADP "O5'"  O  N N 9   
ADP "C5'"  C  N N 10  
ADP "C4'"  C  N R 11  
ADP "O4'"  O  N N 12  
ADP "C3'"  C  N S 13  
ADP "O3'"  O  N N 14  
ADP "C2'"  C  N R 15  
ADP "O2'"  O  N N 16  
ADP "C1'"  C  N R 17  
ADP N9     N  Y N 18  
ADP C8     C  Y N 19  
ADP N7     N  Y N 20  
ADP C5     C  Y N 21  
ADP C6     C  Y N 22  
ADP N6     N  N N 23  
ADP N1     N  Y N 24  
ADP C2     C  Y N 25  
ADP N3     N  Y N 26  
ADP C4     C  Y N 27  
ADP HOB2   H  N N 28  
ADP HOB3   H  N N 29  
ADP HOA2   H  N N 30  
ADP "H5'1" H  N N 31  
ADP "H5'2" H  N N 32  
ADP "H4'"  H  N N 33  
ADP "H3'"  H  N N 34  
ADP "HO3'" H  N N 35  
ADP "H2'"  H  N N 36  
ADP "HO2'" H  N N 37  
ADP "H1'"  H  N N 38  
ADP H8     H  N N 39  
ADP HN61   H  N N 40  
ADP HN62   H  N N 41  
ADP H2     H  N N 42  
ALA N      N  N N 43  
ALA CA     C  N S 44  
ALA C      C  N N 45  
ALA O      O  N N 46  
ALA CB     C  N N 47  
ALA OXT    O  N N 48  
ALA H      H  N N 49  
ALA H2     H  N N 50  
ALA HA     H  N N 51  
ALA HB1    H  N N 52  
ALA HB2    H  N N 53  
ALA HB3    H  N N 54  
ALA HXT    H  N N 55  
AOV PB     P  N N 56  
AOV O1B    O  N N 57  
AOV O2B    O  N N 58  
AOV O3B    O  N N 59  
AOV PA     P  N N 60  
AOV O1A    O  N N 61  
AOV O2A    O  N N 62  
AOV O3A    O  N N 63  
AOV "O5'"  O  N N 64  
AOV "C5'"  C  N N 65  
AOV "C4'"  C  N R 66  
AOV "O4'"  O  N N 67  
AOV "C3'"  C  N S 68  
AOV "O3'"  O  N N 69  
AOV "C2'"  C  N R 70  
AOV "O2'"  O  N N 71  
AOV "C1'"  C  N R 72  
AOV N9     N  Y N 73  
AOV C8     C  Y N 74  
AOV N7     N  Y N 75  
AOV C5     C  Y N 76  
AOV C6     C  Y N 77  
AOV N6     N  N N 78  
AOV N1     N  Y N 79  
AOV C2     C  Y N 80  
AOV N3     N  Y N 81  
AOV C4     C  Y N 82  
AOV VG     V  N N 83  
AOV O1G    O  N N 84  
AOV O2G    O  N N 85  
AOV O3G    O  N N 86  
AOV O4G    O  N N 87  
AOV H2B    H  N N 88  
AOV H2A    H  N N 89  
AOV "H5'1" H  N N 90  
AOV "H5'2" H  N N 91  
AOV "H4'"  H  N N 92  
AOV "H3'"  H  N N 93  
AOV "H1'"  H  N N 94  
AOV HA     H  N N 95  
AOV "H2'"  H  N N 96  
AOV HB     H  N N 97  
AOV H8     H  N N 98  
AOV H61N   H  N N 99  
AOV H62N   H  N N 100 
AOV H2     H  N N 101 
AOV H2G1   H  N N 102 
AOV H3G1   H  N N 103 
AOV H4G1   H  N N 104 
ARG N      N  N N 105 
ARG CA     C  N S 106 
ARG C      C  N N 107 
ARG O      O  N N 108 
ARG CB     C  N N 109 
ARG CG     C  N N 110 
ARG CD     C  N N 111 
ARG NE     N  N N 112 
ARG CZ     C  N N 113 
ARG NH1    N  N N 114 
ARG NH2    N  N N 115 
ARG OXT    O  N N 116 
ARG H      H  N N 117 
ARG H2     H  N N 118 
ARG HA     H  N N 119 
ARG HB2    H  N N 120 
ARG HB3    H  N N 121 
ARG HG2    H  N N 122 
ARG HG3    H  N N 123 
ARG HD2    H  N N 124 
ARG HD3    H  N N 125 
ARG HE     H  N N 126 
ARG HH11   H  N N 127 
ARG HH12   H  N N 128 
ARG HH21   H  N N 129 
ARG HH22   H  N N 130 
ARG HXT    H  N N 131 
ASN N      N  N N 132 
ASN CA     C  N S 133 
ASN C      C  N N 134 
ASN O      O  N N 135 
ASN CB     C  N N 136 
ASN CG     C  N N 137 
ASN OD1    O  N N 138 
ASN ND2    N  N N 139 
ASN OXT    O  N N 140 
ASN H      H  N N 141 
ASN H2     H  N N 142 
ASN HA     H  N N 143 
ASN HB2    H  N N 144 
ASN HB3    H  N N 145 
ASN HD21   H  N N 146 
ASN HD22   H  N N 147 
ASN HXT    H  N N 148 
ASP N      N  N N 149 
ASP CA     C  N S 150 
ASP C      C  N N 151 
ASP O      O  N N 152 
ASP CB     C  N N 153 
ASP CG     C  N N 154 
ASP OD1    O  N N 155 
ASP OD2    O  N N 156 
ASP OXT    O  N N 157 
ASP H      H  N N 158 
ASP H2     H  N N 159 
ASP HA     H  N N 160 
ASP HB2    H  N N 161 
ASP HB3    H  N N 162 
ASP HD2    H  N N 163 
ASP HXT    H  N N 164 
ATP PG     P  N N 165 
ATP O1G    O  N N 166 
ATP O2G    O  N N 167 
ATP O3G    O  N N 168 
ATP PB     P  N R 169 
ATP O1B    O  N N 170 
ATP O2B    O  N N 171 
ATP O3B    O  N N 172 
ATP PA     P  N R 173 
ATP O1A    O  N N 174 
ATP O2A    O  N N 175 
ATP O3A    O  N N 176 
ATP "O5'"  O  N N 177 
ATP "C5'"  C  N N 178 
ATP "C4'"  C  N R 179 
ATP "O4'"  O  N N 180 
ATP "C3'"  C  N S 181 
ATP "O3'"  O  N N 182 
ATP "C2'"  C  N R 183 
ATP "O2'"  O  N N 184 
ATP "C1'"  C  N R 185 
ATP N9     N  Y N 186 
ATP C8     C  Y N 187 
ATP N7     N  Y N 188 
ATP C5     C  Y N 189 
ATP C6     C  Y N 190 
ATP N6     N  N N 191 
ATP N1     N  Y N 192 
ATP C2     C  Y N 193 
ATP N3     N  Y N 194 
ATP C4     C  Y N 195 
ATP HOG2   H  N N 196 
ATP HOG3   H  N N 197 
ATP HOB2   H  N N 198 
ATP HOA2   H  N N 199 
ATP "H5'1" H  N N 200 
ATP "H5'2" H  N N 201 
ATP "H4'"  H  N N 202 
ATP "H3'"  H  N N 203 
ATP "HO3'" H  N N 204 
ATP "H2'"  H  N N 205 
ATP "HO2'" H  N N 206 
ATP "H1'"  H  N N 207 
ATP H8     H  N N 208 
ATP HN61   H  N N 209 
ATP HN62   H  N N 210 
ATP H2     H  N N 211 
CYS N      N  N N 212 
CYS CA     C  N R 213 
CYS C      C  N N 214 
CYS O      O  N N 215 
CYS CB     C  N N 216 
CYS SG     S  N N 217 
CYS OXT    O  N N 218 
CYS H      H  N N 219 
CYS H2     H  N N 220 
CYS HA     H  N N 221 
CYS HB2    H  N N 222 
CYS HB3    H  N N 223 
CYS HG     H  N N 224 
CYS HXT    H  N N 225 
GLN N      N  N N 226 
GLN CA     C  N S 227 
GLN C      C  N N 228 
GLN O      O  N N 229 
GLN CB     C  N N 230 
GLN CG     C  N N 231 
GLN CD     C  N N 232 
GLN OE1    O  N N 233 
GLN NE2    N  N N 234 
GLN OXT    O  N N 235 
GLN H      H  N N 236 
GLN H2     H  N N 237 
GLN HA     H  N N 238 
GLN HB2    H  N N 239 
GLN HB3    H  N N 240 
GLN HG2    H  N N 241 
GLN HG3    H  N N 242 
GLN HE21   H  N N 243 
GLN HE22   H  N N 244 
GLN HXT    H  N N 245 
GLU N      N  N N 246 
GLU CA     C  N S 247 
GLU C      C  N N 248 
GLU O      O  N N 249 
GLU CB     C  N N 250 
GLU CG     C  N N 251 
GLU CD     C  N N 252 
GLU OE1    O  N N 253 
GLU OE2    O  N N 254 
GLU OXT    O  N N 255 
GLU H      H  N N 256 
GLU H2     H  N N 257 
GLU HA     H  N N 258 
GLU HB2    H  N N 259 
GLU HB3    H  N N 260 
GLU HG2    H  N N 261 
GLU HG3    H  N N 262 
GLU HE2    H  N N 263 
GLU HXT    H  N N 264 
GLY N      N  N N 265 
GLY CA     C  N N 266 
GLY C      C  N N 267 
GLY O      O  N N 268 
GLY OXT    O  N N 269 
GLY H      H  N N 270 
GLY H2     H  N N 271 
GLY HA2    H  N N 272 
GLY HA3    H  N N 273 
GLY HXT    H  N N 274 
HIS N      N  N N 275 
HIS CA     C  N S 276 
HIS C      C  N N 277 
HIS O      O  N N 278 
HIS CB     C  N N 279 
HIS CG     C  Y N 280 
HIS ND1    N  Y N 281 
HIS CD2    C  Y N 282 
HIS CE1    C  Y N 283 
HIS NE2    N  Y N 284 
HIS OXT    O  N N 285 
HIS H      H  N N 286 
HIS H2     H  N N 287 
HIS HA     H  N N 288 
HIS HB2    H  N N 289 
HIS HB3    H  N N 290 
HIS HD1    H  N N 291 
HIS HD2    H  N N 292 
HIS HE1    H  N N 293 
HIS HE2    H  N N 294 
HIS HXT    H  N N 295 
ILE N      N  N N 296 
ILE CA     C  N S 297 
ILE C      C  N N 298 
ILE O      O  N N 299 
ILE CB     C  N S 300 
ILE CG1    C  N N 301 
ILE CG2    C  N N 302 
ILE CD1    C  N N 303 
ILE OXT    O  N N 304 
ILE H      H  N N 305 
ILE H2     H  N N 306 
ILE HA     H  N N 307 
ILE HB     H  N N 308 
ILE HG12   H  N N 309 
ILE HG13   H  N N 310 
ILE HG21   H  N N 311 
ILE HG22   H  N N 312 
ILE HG23   H  N N 313 
ILE HD11   H  N N 314 
ILE HD12   H  N N 315 
ILE HD13   H  N N 316 
ILE HXT    H  N N 317 
LEU N      N  N N 318 
LEU CA     C  N S 319 
LEU C      C  N N 320 
LEU O      O  N N 321 
LEU CB     C  N N 322 
LEU CG     C  N N 323 
LEU CD1    C  N N 324 
LEU CD2    C  N N 325 
LEU OXT    O  N N 326 
LEU H      H  N N 327 
LEU H2     H  N N 328 
LEU HA     H  N N 329 
LEU HB2    H  N N 330 
LEU HB3    H  N N 331 
LEU HG     H  N N 332 
LEU HD11   H  N N 333 
LEU HD12   H  N N 334 
LEU HD13   H  N N 335 
LEU HD21   H  N N 336 
LEU HD22   H  N N 337 
LEU HD23   H  N N 338 
LEU HXT    H  N N 339 
LYS N      N  N N 340 
LYS CA     C  N S 341 
LYS C      C  N N 342 
LYS O      O  N N 343 
LYS CB     C  N N 344 
LYS CG     C  N N 345 
LYS CD     C  N N 346 
LYS CE     C  N N 347 
LYS NZ     N  N N 348 
LYS OXT    O  N N 349 
LYS H      H  N N 350 
LYS H2     H  N N 351 
LYS HA     H  N N 352 
LYS HB2    H  N N 353 
LYS HB3    H  N N 354 
LYS HG2    H  N N 355 
LYS HG3    H  N N 356 
LYS HD2    H  N N 357 
LYS HD3    H  N N 358 
LYS HE2    H  N N 359 
LYS HE3    H  N N 360 
LYS HZ1    H  N N 361 
LYS HZ2    H  N N 362 
LYS HZ3    H  N N 363 
LYS HXT    H  N N 364 
MET N      N  N N 365 
MET CA     C  N S 366 
MET C      C  N N 367 
MET O      O  N N 368 
MET CB     C  N N 369 
MET CG     C  N N 370 
MET SD     S  N N 371 
MET CE     C  N N 372 
MET OXT    O  N N 373 
MET H      H  N N 374 
MET H2     H  N N 375 
MET HA     H  N N 376 
MET HB2    H  N N 377 
MET HB3    H  N N 378 
MET HG2    H  N N 379 
MET HG3    H  N N 380 
MET HE1    H  N N 381 
MET HE2    H  N N 382 
MET HE3    H  N N 383 
MET HXT    H  N N 384 
MG  MG     MG N N 385 
PHE N      N  N N 386 
PHE CA     C  N S 387 
PHE C      C  N N 388 
PHE O      O  N N 389 
PHE CB     C  N N 390 
PHE CG     C  Y N 391 
PHE CD1    C  Y N 392 
PHE CD2    C  Y N 393 
PHE CE1    C  Y N 394 
PHE CE2    C  Y N 395 
PHE CZ     C  Y N 396 
PHE OXT    O  N N 397 
PHE H      H  N N 398 
PHE H2     H  N N 399 
PHE HA     H  N N 400 
PHE HB2    H  N N 401 
PHE HB3    H  N N 402 
PHE HD1    H  N N 403 
PHE HD2    H  N N 404 
PHE HE1    H  N N 405 
PHE HE2    H  N N 406 
PHE HZ     H  N N 407 
PHE HXT    H  N N 408 
PRO N      N  N N 409 
PRO CA     C  N S 410 
PRO C      C  N N 411 
PRO O      O  N N 412 
PRO CB     C  N N 413 
PRO CG     C  N N 414 
PRO CD     C  N N 415 
PRO OXT    O  N N 416 
PRO H      H  N N 417 
PRO HA     H  N N 418 
PRO HB2    H  N N 419 
PRO HB3    H  N N 420 
PRO HG2    H  N N 421 
PRO HG3    H  N N 422 
PRO HD2    H  N N 423 
PRO HD3    H  N N 424 
PRO HXT    H  N N 425 
SER N      N  N N 426 
SER CA     C  N S 427 
SER C      C  N N 428 
SER O      O  N N 429 
SER CB     C  N N 430 
SER OG     O  N N 431 
SER OXT    O  N N 432 
SER H      H  N N 433 
SER H2     H  N N 434 
SER HA     H  N N 435 
SER HB2    H  N N 436 
SER HB3    H  N N 437 
SER HG     H  N N 438 
SER HXT    H  N N 439 
THR N      N  N N 440 
THR CA     C  N S 441 
THR C      C  N N 442 
THR O      O  N N 443 
THR CB     C  N R 444 
THR OG1    O  N N 445 
THR CG2    C  N N 446 
THR OXT    O  N N 447 
THR H      H  N N 448 
THR H2     H  N N 449 
THR HA     H  N N 450 
THR HB     H  N N 451 
THR HG1    H  N N 452 
THR HG21   H  N N 453 
THR HG22   H  N N 454 
THR HG23   H  N N 455 
THR HXT    H  N N 456 
TRP N      N  N N 457 
TRP CA     C  N S 458 
TRP C      C  N N 459 
TRP O      O  N N 460 
TRP CB     C  N N 461 
TRP CG     C  Y N 462 
TRP CD1    C  Y N 463 
TRP CD2    C  Y N 464 
TRP NE1    N  Y N 465 
TRP CE2    C  Y N 466 
TRP CE3    C  Y N 467 
TRP CZ2    C  Y N 468 
TRP CZ3    C  Y N 469 
TRP CH2    C  Y N 470 
TRP OXT    O  N N 471 
TRP H      H  N N 472 
TRP H2     H  N N 473 
TRP HA     H  N N 474 
TRP HB2    H  N N 475 
TRP HB3    H  N N 476 
TRP HD1    H  N N 477 
TRP HE1    H  N N 478 
TRP HE3    H  N N 479 
TRP HZ2    H  N N 480 
TRP HZ3    H  N N 481 
TRP HH2    H  N N 482 
TRP HXT    H  N N 483 
TYR N      N  N N 484 
TYR CA     C  N S 485 
TYR C      C  N N 486 
TYR O      O  N N 487 
TYR CB     C  N N 488 
TYR CG     C  Y N 489 
TYR CD1    C  Y N 490 
TYR CD2    C  Y N 491 
TYR CE1    C  Y N 492 
TYR CE2    C  Y N 493 
TYR CZ     C  Y N 494 
TYR OH     O  N N 495 
TYR OXT    O  N N 496 
TYR H      H  N N 497 
TYR H2     H  N N 498 
TYR HA     H  N N 499 
TYR HB2    H  N N 500 
TYR HB3    H  N N 501 
TYR HD1    H  N N 502 
TYR HD2    H  N N 503 
TYR HE1    H  N N 504 
TYR HE2    H  N N 505 
TYR HH     H  N N 506 
TYR HXT    H  N N 507 
VAL N      N  N N 508 
VAL CA     C  N S 509 
VAL C      C  N N 510 
VAL O      O  N N 511 
VAL CB     C  N N 512 
VAL CG1    C  N N 513 
VAL CG2    C  N N 514 
VAL OXT    O  N N 515 
VAL H      H  N N 516 
VAL H2     H  N N 517 
VAL HA     H  N N 518 
VAL HB     H  N N 519 
VAL HG11   H  N N 520 
VAL HG12   H  N N 521 
VAL HG13   H  N N 522 
VAL HG21   H  N N 523 
VAL HG22   H  N N 524 
VAL HG23   H  N N 525 
VAL HXT    H  N N 526 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ADP PB    O1B    doub N N 1   
ADP PB    O2B    sing N N 2   
ADP PB    O3B    sing N N 3   
ADP PB    O3A    sing N N 4   
ADP O2B   HOB2   sing N N 5   
ADP O3B   HOB3   sing N N 6   
ADP PA    O1A    doub N N 7   
ADP PA    O2A    sing N N 8   
ADP PA    O3A    sing N N 9   
ADP PA    "O5'"  sing N N 10  
ADP O2A   HOA2   sing N N 11  
ADP "O5'" "C5'"  sing N N 12  
ADP "C5'" "C4'"  sing N N 13  
ADP "C5'" "H5'1" sing N N 14  
ADP "C5'" "H5'2" sing N N 15  
ADP "C4'" "O4'"  sing N N 16  
ADP "C4'" "C3'"  sing N N 17  
ADP "C4'" "H4'"  sing N N 18  
ADP "O4'" "C1'"  sing N N 19  
ADP "C3'" "O3'"  sing N N 20  
ADP "C3'" "C2'"  sing N N 21  
ADP "C3'" "H3'"  sing N N 22  
ADP "O3'" "HO3'" sing N N 23  
ADP "C2'" "O2'"  sing N N 24  
ADP "C2'" "C1'"  sing N N 25  
ADP "C2'" "H2'"  sing N N 26  
ADP "O2'" "HO2'" sing N N 27  
ADP "C1'" N9     sing N N 28  
ADP "C1'" "H1'"  sing N N 29  
ADP N9    C8     sing Y N 30  
ADP N9    C4     sing Y N 31  
ADP C8    N7     doub Y N 32  
ADP C8    H8     sing N N 33  
ADP N7    C5     sing Y N 34  
ADP C5    C6     sing Y N 35  
ADP C5    C4     doub Y N 36  
ADP C6    N6     sing N N 37  
ADP C6    N1     doub Y N 38  
ADP N6    HN61   sing N N 39  
ADP N6    HN62   sing N N 40  
ADP N1    C2     sing Y N 41  
ADP C2    N3     doub Y N 42  
ADP C2    H2     sing N N 43  
ADP N3    C4     sing Y N 44  
ALA N     CA     sing N N 45  
ALA N     H      sing N N 46  
ALA N     H2     sing N N 47  
ALA CA    C      sing N N 48  
ALA CA    CB     sing N N 49  
ALA CA    HA     sing N N 50  
ALA C     O      doub N N 51  
ALA C     OXT    sing N N 52  
ALA CB    HB1    sing N N 53  
ALA CB    HB2    sing N N 54  
ALA CB    HB3    sing N N 55  
ALA OXT   HXT    sing N N 56  
AOV PB    O1B    doub N N 57  
AOV PB    O2B    sing N N 58  
AOV PB    O3B    sing N N 59  
AOV PB    O3A    sing N N 60  
AOV O3B   VG     sing N N 61  
AOV PA    O1A    doub N N 62  
AOV PA    O2A    sing N N 63  
AOV PA    O3A    sing N N 64  
AOV PA    "O5'"  sing N N 65  
AOV "O5'" "C5'"  sing N N 66  
AOV "C5'" "C4'"  sing N N 67  
AOV "C4'" "O4'"  sing N N 68  
AOV "C4'" "C3'"  sing N N 69  
AOV "O4'" "C1'"  sing N N 70  
AOV "C3'" "O3'"  sing N N 71  
AOV "C3'" "C2'"  sing N N 72  
AOV "C2'" "O2'"  sing N N 73  
AOV "C2'" "C1'"  sing N N 74  
AOV "C1'" N9     sing N N 75  
AOV N9    C8     sing Y N 76  
AOV N9    C4     sing Y N 77  
AOV C8    N7     doub Y N 78  
AOV N7    C5     sing Y N 79  
AOV C5    C6     sing Y N 80  
AOV C5    C4     doub Y N 81  
AOV C6    N6     sing N N 82  
AOV C6    N1     doub Y N 83  
AOV N1    C2     sing Y N 84  
AOV C2    N3     doub Y N 85  
AOV N3    C4     sing Y N 86  
AOV VG    O1G    doub N N 87  
AOV VG    O2G    sing N N 88  
AOV VG    O3G    sing N N 89  
AOV VG    O4G    sing N N 90  
AOV O2B   H2B    sing N N 91  
AOV O2A   H2A    sing N N 92  
AOV "C5'" "H5'1" sing N N 93  
AOV "C5'" "H5'2" sing N N 94  
AOV "C4'" "H4'"  sing N N 95  
AOV "C3'" "H3'"  sing N N 96  
AOV "C1'" "H1'"  sing N N 97  
AOV "O3'" HA     sing N N 98  
AOV "C2'" "H2'"  sing N N 99  
AOV "O2'" HB     sing N N 100 
AOV C8    H8     sing N N 101 
AOV N6    H61N   sing N N 102 
AOV N6    H62N   sing N N 103 
AOV C2    H2     sing N N 104 
AOV O2G   H2G1   sing N N 105 
AOV O3G   H3G1   sing N N 106 
AOV O4G   H4G1   sing N N 107 
ARG N     CA     sing N N 108 
ARG N     H      sing N N 109 
ARG N     H2     sing N N 110 
ARG CA    C      sing N N 111 
ARG CA    CB     sing N N 112 
ARG CA    HA     sing N N 113 
ARG C     O      doub N N 114 
ARG C     OXT    sing N N 115 
ARG CB    CG     sing N N 116 
ARG CB    HB2    sing N N 117 
ARG CB    HB3    sing N N 118 
ARG CG    CD     sing N N 119 
ARG CG    HG2    sing N N 120 
ARG CG    HG3    sing N N 121 
ARG CD    NE     sing N N 122 
ARG CD    HD2    sing N N 123 
ARG CD    HD3    sing N N 124 
ARG NE    CZ     sing N N 125 
ARG NE    HE     sing N N 126 
ARG CZ    NH1    sing N N 127 
ARG CZ    NH2    doub N N 128 
ARG NH1   HH11   sing N N 129 
ARG NH1   HH12   sing N N 130 
ARG NH2   HH21   sing N N 131 
ARG NH2   HH22   sing N N 132 
ARG OXT   HXT    sing N N 133 
ASN N     CA     sing N N 134 
ASN N     H      sing N N 135 
ASN N     H2     sing N N 136 
ASN CA    C      sing N N 137 
ASN CA    CB     sing N N 138 
ASN CA    HA     sing N N 139 
ASN C     O      doub N N 140 
ASN C     OXT    sing N N 141 
ASN CB    CG     sing N N 142 
ASN CB    HB2    sing N N 143 
ASN CB    HB3    sing N N 144 
ASN CG    OD1    doub N N 145 
ASN CG    ND2    sing N N 146 
ASN ND2   HD21   sing N N 147 
ASN ND2   HD22   sing N N 148 
ASN OXT   HXT    sing N N 149 
ASP N     CA     sing N N 150 
ASP N     H      sing N N 151 
ASP N     H2     sing N N 152 
ASP CA    C      sing N N 153 
ASP CA    CB     sing N N 154 
ASP CA    HA     sing N N 155 
ASP C     O      doub N N 156 
ASP C     OXT    sing N N 157 
ASP CB    CG     sing N N 158 
ASP CB    HB2    sing N N 159 
ASP CB    HB3    sing N N 160 
ASP CG    OD1    doub N N 161 
ASP CG    OD2    sing N N 162 
ASP OD2   HD2    sing N N 163 
ASP OXT   HXT    sing N N 164 
ATP PG    O1G    doub N N 165 
ATP PG    O2G    sing N N 166 
ATP PG    O3G    sing N N 167 
ATP PG    O3B    sing N N 168 
ATP O2G   HOG2   sing N N 169 
ATP O3G   HOG3   sing N N 170 
ATP PB    O1B    doub N N 171 
ATP PB    O2B    sing N N 172 
ATP PB    O3B    sing N N 173 
ATP PB    O3A    sing N N 174 
ATP O2B   HOB2   sing N N 175 
ATP PA    O1A    doub N N 176 
ATP PA    O2A    sing N N 177 
ATP PA    O3A    sing N N 178 
ATP PA    "O5'"  sing N N 179 
ATP O2A   HOA2   sing N N 180 
ATP "O5'" "C5'"  sing N N 181 
ATP "C5'" "C4'"  sing N N 182 
ATP "C5'" "H5'1" sing N N 183 
ATP "C5'" "H5'2" sing N N 184 
ATP "C4'" "O4'"  sing N N 185 
ATP "C4'" "C3'"  sing N N 186 
ATP "C4'" "H4'"  sing N N 187 
ATP "O4'" "C1'"  sing N N 188 
ATP "C3'" "O3'"  sing N N 189 
ATP "C3'" "C2'"  sing N N 190 
ATP "C3'" "H3'"  sing N N 191 
ATP "O3'" "HO3'" sing N N 192 
ATP "C2'" "O2'"  sing N N 193 
ATP "C2'" "C1'"  sing N N 194 
ATP "C2'" "H2'"  sing N N 195 
ATP "O2'" "HO2'" sing N N 196 
ATP "C1'" N9     sing N N 197 
ATP "C1'" "H1'"  sing N N 198 
ATP N9    C8     sing Y N 199 
ATP N9    C4     sing Y N 200 
ATP C8    N7     doub Y N 201 
ATP C8    H8     sing N N 202 
ATP N7    C5     sing Y N 203 
ATP C5    C6     sing Y N 204 
ATP C5    C4     doub Y N 205 
ATP C6    N6     sing N N 206 
ATP C6    N1     doub Y N 207 
ATP N6    HN61   sing N N 208 
ATP N6    HN62   sing N N 209 
ATP N1    C2     sing Y N 210 
ATP C2    N3     doub Y N 211 
ATP C2    H2     sing N N 212 
ATP N3    C4     sing Y N 213 
CYS N     CA     sing N N 214 
CYS N     H      sing N N 215 
CYS N     H2     sing N N 216 
CYS CA    C      sing N N 217 
CYS CA    CB     sing N N 218 
CYS CA    HA     sing N N 219 
CYS C     O      doub N N 220 
CYS C     OXT    sing N N 221 
CYS CB    SG     sing N N 222 
CYS CB    HB2    sing N N 223 
CYS CB    HB3    sing N N 224 
CYS SG    HG     sing N N 225 
CYS OXT   HXT    sing N N 226 
GLN N     CA     sing N N 227 
GLN N     H      sing N N 228 
GLN N     H2     sing N N 229 
GLN CA    C      sing N N 230 
GLN CA    CB     sing N N 231 
GLN CA    HA     sing N N 232 
GLN C     O      doub N N 233 
GLN C     OXT    sing N N 234 
GLN CB    CG     sing N N 235 
GLN CB    HB2    sing N N 236 
GLN CB    HB3    sing N N 237 
GLN CG    CD     sing N N 238 
GLN CG    HG2    sing N N 239 
GLN CG    HG3    sing N N 240 
GLN CD    OE1    doub N N 241 
GLN CD    NE2    sing N N 242 
GLN NE2   HE21   sing N N 243 
GLN NE2   HE22   sing N N 244 
GLN OXT   HXT    sing N N 245 
GLU N     CA     sing N N 246 
GLU N     H      sing N N 247 
GLU N     H2     sing N N 248 
GLU CA    C      sing N N 249 
GLU CA    CB     sing N N 250 
GLU CA    HA     sing N N 251 
GLU C     O      doub N N 252 
GLU C     OXT    sing N N 253 
GLU CB    CG     sing N N 254 
GLU CB    HB2    sing N N 255 
GLU CB    HB3    sing N N 256 
GLU CG    CD     sing N N 257 
GLU CG    HG2    sing N N 258 
GLU CG    HG3    sing N N 259 
GLU CD    OE1    doub N N 260 
GLU CD    OE2    sing N N 261 
GLU OE2   HE2    sing N N 262 
GLU OXT   HXT    sing N N 263 
GLY N     CA     sing N N 264 
GLY N     H      sing N N 265 
GLY N     H2     sing N N 266 
GLY CA    C      sing N N 267 
GLY CA    HA2    sing N N 268 
GLY CA    HA3    sing N N 269 
GLY C     O      doub N N 270 
GLY C     OXT    sing N N 271 
GLY OXT   HXT    sing N N 272 
HIS N     CA     sing N N 273 
HIS N     H      sing N N 274 
HIS N     H2     sing N N 275 
HIS CA    C      sing N N 276 
HIS CA    CB     sing N N 277 
HIS CA    HA     sing N N 278 
HIS C     O      doub N N 279 
HIS C     OXT    sing N N 280 
HIS CB    CG     sing N N 281 
HIS CB    HB2    sing N N 282 
HIS CB    HB3    sing N N 283 
HIS CG    ND1    sing Y N 284 
HIS CG    CD2    doub Y N 285 
HIS ND1   CE1    doub Y N 286 
HIS ND1   HD1    sing N N 287 
HIS CD2   NE2    sing Y N 288 
HIS CD2   HD2    sing N N 289 
HIS CE1   NE2    sing Y N 290 
HIS CE1   HE1    sing N N 291 
HIS NE2   HE2    sing N N 292 
HIS OXT   HXT    sing N N 293 
ILE N     CA     sing N N 294 
ILE N     H      sing N N 295 
ILE N     H2     sing N N 296 
ILE CA    C      sing N N 297 
ILE CA    CB     sing N N 298 
ILE CA    HA     sing N N 299 
ILE C     O      doub N N 300 
ILE C     OXT    sing N N 301 
ILE CB    CG1    sing N N 302 
ILE CB    CG2    sing N N 303 
ILE CB    HB     sing N N 304 
ILE CG1   CD1    sing N N 305 
ILE CG1   HG12   sing N N 306 
ILE CG1   HG13   sing N N 307 
ILE CG2   HG21   sing N N 308 
ILE CG2   HG22   sing N N 309 
ILE CG2   HG23   sing N N 310 
ILE CD1   HD11   sing N N 311 
ILE CD1   HD12   sing N N 312 
ILE CD1   HD13   sing N N 313 
ILE OXT   HXT    sing N N 314 
LEU N     CA     sing N N 315 
LEU N     H      sing N N 316 
LEU N     H2     sing N N 317 
LEU CA    C      sing N N 318 
LEU CA    CB     sing N N 319 
LEU CA    HA     sing N N 320 
LEU C     O      doub N N 321 
LEU C     OXT    sing N N 322 
LEU CB    CG     sing N N 323 
LEU CB    HB2    sing N N 324 
LEU CB    HB3    sing N N 325 
LEU CG    CD1    sing N N 326 
LEU CG    CD2    sing N N 327 
LEU CG    HG     sing N N 328 
LEU CD1   HD11   sing N N 329 
LEU CD1   HD12   sing N N 330 
LEU CD1   HD13   sing N N 331 
LEU CD2   HD21   sing N N 332 
LEU CD2   HD22   sing N N 333 
LEU CD2   HD23   sing N N 334 
LEU OXT   HXT    sing N N 335 
LYS N     CA     sing N N 336 
LYS N     H      sing N N 337 
LYS N     H2     sing N N 338 
LYS CA    C      sing N N 339 
LYS CA    CB     sing N N 340 
LYS CA    HA     sing N N 341 
LYS C     O      doub N N 342 
LYS C     OXT    sing N N 343 
LYS CB    CG     sing N N 344 
LYS CB    HB2    sing N N 345 
LYS CB    HB3    sing N N 346 
LYS CG    CD     sing N N 347 
LYS CG    HG2    sing N N 348 
LYS CG    HG3    sing N N 349 
LYS CD    CE     sing N N 350 
LYS CD    HD2    sing N N 351 
LYS CD    HD3    sing N N 352 
LYS CE    NZ     sing N N 353 
LYS CE    HE2    sing N N 354 
LYS CE    HE3    sing N N 355 
LYS NZ    HZ1    sing N N 356 
LYS NZ    HZ2    sing N N 357 
LYS NZ    HZ3    sing N N 358 
LYS OXT   HXT    sing N N 359 
MET N     CA     sing N N 360 
MET N     H      sing N N 361 
MET N     H2     sing N N 362 
MET CA    C      sing N N 363 
MET CA    CB     sing N N 364 
MET CA    HA     sing N N 365 
MET C     O      doub N N 366 
MET C     OXT    sing N N 367 
MET CB    CG     sing N N 368 
MET CB    HB2    sing N N 369 
MET CB    HB3    sing N N 370 
MET CG    SD     sing N N 371 
MET CG    HG2    sing N N 372 
MET CG    HG3    sing N N 373 
MET SD    CE     sing N N 374 
MET CE    HE1    sing N N 375 
MET CE    HE2    sing N N 376 
MET CE    HE3    sing N N 377 
MET OXT   HXT    sing N N 378 
PHE N     CA     sing N N 379 
PHE N     H      sing N N 380 
PHE N     H2     sing N N 381 
PHE CA    C      sing N N 382 
PHE CA    CB     sing N N 383 
PHE CA    HA     sing N N 384 
PHE C     O      doub N N 385 
PHE C     OXT    sing N N 386 
PHE CB    CG     sing N N 387 
PHE CB    HB2    sing N N 388 
PHE CB    HB3    sing N N 389 
PHE CG    CD1    doub Y N 390 
PHE CG    CD2    sing Y N 391 
PHE CD1   CE1    sing Y N 392 
PHE CD1   HD1    sing N N 393 
PHE CD2   CE2    doub Y N 394 
PHE CD2   HD2    sing N N 395 
PHE CE1   CZ     doub Y N 396 
PHE CE1   HE1    sing N N 397 
PHE CE2   CZ     sing Y N 398 
PHE CE2   HE2    sing N N 399 
PHE CZ    HZ     sing N N 400 
PHE OXT   HXT    sing N N 401 
PRO N     CA     sing N N 402 
PRO N     CD     sing N N 403 
PRO N     H      sing N N 404 
PRO CA    C      sing N N 405 
PRO CA    CB     sing N N 406 
PRO CA    HA     sing N N 407 
PRO C     O      doub N N 408 
PRO C     OXT    sing N N 409 
PRO CB    CG     sing N N 410 
PRO CB    HB2    sing N N 411 
PRO CB    HB3    sing N N 412 
PRO CG    CD     sing N N 413 
PRO CG    HG2    sing N N 414 
PRO CG    HG3    sing N N 415 
PRO CD    HD2    sing N N 416 
PRO CD    HD3    sing N N 417 
PRO OXT   HXT    sing N N 418 
SER N     CA     sing N N 419 
SER N     H      sing N N 420 
SER N     H2     sing N N 421 
SER CA    C      sing N N 422 
SER CA    CB     sing N N 423 
SER CA    HA     sing N N 424 
SER C     O      doub N N 425 
SER C     OXT    sing N N 426 
SER CB    OG     sing N N 427 
SER CB    HB2    sing N N 428 
SER CB    HB3    sing N N 429 
SER OG    HG     sing N N 430 
SER OXT   HXT    sing N N 431 
THR N     CA     sing N N 432 
THR N     H      sing N N 433 
THR N     H2     sing N N 434 
THR CA    C      sing N N 435 
THR CA    CB     sing N N 436 
THR CA    HA     sing N N 437 
THR C     O      doub N N 438 
THR C     OXT    sing N N 439 
THR CB    OG1    sing N N 440 
THR CB    CG2    sing N N 441 
THR CB    HB     sing N N 442 
THR OG1   HG1    sing N N 443 
THR CG2   HG21   sing N N 444 
THR CG2   HG22   sing N N 445 
THR CG2   HG23   sing N N 446 
THR OXT   HXT    sing N N 447 
TRP N     CA     sing N N 448 
TRP N     H      sing N N 449 
TRP N     H2     sing N N 450 
TRP CA    C      sing N N 451 
TRP CA    CB     sing N N 452 
TRP CA    HA     sing N N 453 
TRP C     O      doub N N 454 
TRP C     OXT    sing N N 455 
TRP CB    CG     sing N N 456 
TRP CB    HB2    sing N N 457 
TRP CB    HB3    sing N N 458 
TRP CG    CD1    doub Y N 459 
TRP CG    CD2    sing Y N 460 
TRP CD1   NE1    sing Y N 461 
TRP CD1   HD1    sing N N 462 
TRP CD2   CE2    doub Y N 463 
TRP CD2   CE3    sing Y N 464 
TRP NE1   CE2    sing Y N 465 
TRP NE1   HE1    sing N N 466 
TRP CE2   CZ2    sing Y N 467 
TRP CE3   CZ3    doub Y N 468 
TRP CE3   HE3    sing N N 469 
TRP CZ2   CH2    doub Y N 470 
TRP CZ2   HZ2    sing N N 471 
TRP CZ3   CH2    sing Y N 472 
TRP CZ3   HZ3    sing N N 473 
TRP CH2   HH2    sing N N 474 
TRP OXT   HXT    sing N N 475 
TYR N     CA     sing N N 476 
TYR N     H      sing N N 477 
TYR N     H2     sing N N 478 
TYR CA    C      sing N N 479 
TYR CA    CB     sing N N 480 
TYR CA    HA     sing N N 481 
TYR C     O      doub N N 482 
TYR C     OXT    sing N N 483 
TYR CB    CG     sing N N 484 
TYR CB    HB2    sing N N 485 
TYR CB    HB3    sing N N 486 
TYR CG    CD1    doub Y N 487 
TYR CG    CD2    sing Y N 488 
TYR CD1   CE1    sing Y N 489 
TYR CD1   HD1    sing N N 490 
TYR CD2   CE2    doub Y N 491 
TYR CD2   HD2    sing N N 492 
TYR CE1   CZ     doub Y N 493 
TYR CE1   HE1    sing N N 494 
TYR CE2   CZ     sing Y N 495 
TYR CE2   HE2    sing N N 496 
TYR CZ    OH     sing N N 497 
TYR OH    HH     sing N N 498 
TYR OXT   HXT    sing N N 499 
VAL N     CA     sing N N 500 
VAL N     H      sing N N 501 
VAL N     H2     sing N N 502 
VAL CA    C      sing N N 503 
VAL CA    CB     sing N N 504 
VAL CA    HA     sing N N 505 
VAL C     O      doub N N 506 
VAL C     OXT    sing N N 507 
VAL CB    CG1    sing N N 508 
VAL CB    CG2    sing N N 509 
VAL CB    HB     sing N N 510 
VAL CG1   HG11   sing N N 511 
VAL CG1   HG12   sing N N 512 
VAL CG1   HG13   sing N N 513 
VAL CG2   HG21   sing N N 514 
VAL CG2   HG22   sing N N 515 
VAL CG2   HG23   sing N N 516 
VAL OXT   HXT    sing N N 517 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-05-02 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9BMH 
_em_admin.last_update        2025-04-30 
_em_admin.map_release_date   2025-04-23 
_em_admin.title              'State-4 of motor domain from full-length human dynein-1 in 5mM ATPVi' 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
_em_entity_assembly_molwt.entity_assembly_id   1 
_em_entity_assembly_molwt.experimental_flag    YES 
_em_entity_assembly_molwt.id                   1 
_em_entity_assembly_molwt.units                MEGADALTONS 
_em_entity_assembly_molwt.value                1.5 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          9606 
_em_entity_assembly_naturalsource.organism             'Homo sapiens' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          7108 
_em_entity_assembly_recombinant.organism             'Spodoptera frugiperda' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         40 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 (6k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'       ? 1  1 ? ? ?         ? 
'IMAGE ACQUISITION'        ? 2  ? ? 1 SerialEM  4 
MASKING                    ? 3  ? ? ? ?         ? 
'CTF CORRECTION'           ? 4  1 ? ? ?         ? 
'LAYERLINE INDEXING'       ? 5  ? ? ? ?         ? 
'DIFFRACTION INDEXING'     ? 6  ? ? ? ?         ? 
'MODEL FITTING'            ? 7  ? ? ? ?         ? 
'MODEL REFINEMENT'         ? 8  ? ? ? ?         ? 
OTHER                      ? 9  ? ? ? ?         ? 
'INITIAL EULER ASSIGNMENT' ? 10 1 ? ? ?         ? 
'FINAL EULER ASSIGNMENT'   ? 11 1 ? ? cryoSPARC 4 
CLASSIFICATION             ? 12 1 ? ? ?         ? 
RECONSTRUCTION             ? 13 1 ? ? cryoSPARC 4 
# 
_em_specimen.concentration           2 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' R35GM142959 1 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' R35GM139483 2 
# 
_atom_sites.entry_id                    9BMH 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   1.000000 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   1.000000 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   1.000000 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
MG 
N  
O  
P  
S  
V  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N     . ASP A 1 1535 ? 183.775 209.105 214.255 1.00 106.61 ? 1535 ASP A N     1 
ATOM   2     C  CA    . ASP A 1 1535 ? 184.678 209.918 215.061 1.00 110.11 ? 1535 ASP A CA    1 
ATOM   3     C  C     . ASP A 1 1535 ? 183.929 210.570 216.217 1.00 110.41 ? 1535 ASP A C     1 
ATOM   4     O  O     . ASP A 1 1535 ? 184.473 211.420 216.923 1.00 109.63 ? 1535 ASP A O     1 
ATOM   5     C  CB    . ASP A 1 1535 ? 185.353 210.985 214.199 1.00 109.26 ? 1535 ASP A CB    1 
ATOM   6     C  CG    . ASP A 1 1535 ? 186.333 210.395 213.203 1.00 108.60 ? 1535 ASP A CG    1 
ATOM   7     O  OD1   . ASP A 1 1535 ? 186.944 209.352 213.516 1.00 108.68 ? 1535 ASP A OD1   1 
ATOM   8     O  OD2   . ASP A 1 1535 ? 186.490 210.972 212.107 1.00 106.64 ? 1535 ASP A OD2   1 
ATOM   9     N  N     . VAL A 1 1536 ? 182.675 210.163 216.404 1.00 114.33 ? 1536 VAL A N     1 
ATOM   10    C  CA    . VAL A 1 1536 ? 181.831 210.724 217.443 1.00 115.08 ? 1536 VAL A CA    1 
ATOM   11    C  C     . VAL A 1 1536 ? 181.522 209.721 218.552 1.00 114.04 ? 1536 VAL A C     1 
ATOM   12    O  O     . VAL A 1 1536 ? 181.427 210.120 219.719 1.00 112.32 ? 1536 VAL A O     1 
ATOM   13    C  CB    . VAL A 1 1536 ? 180.526 211.284 216.834 1.00 112.95 ? 1536 VAL A CB    1 
ATOM   14    C  CG1   . VAL A 1 1536 ? 179.643 211.898 217.911 1.00 111.99 ? 1536 VAL A CG1   1 
ATOM   15    C  CG2   . VAL A 1 1536 ? 180.842 212.304 215.753 1.00 109.82 ? 1536 VAL A CG2   1 
ATOM   16    N  N     . TRP A 1 1537 ? 181.379 208.433 218.226 1.00 116.18 ? 1537 TRP A N     1 
ATOM   17    C  CA    . TRP A 1 1537 ? 180.971 207.450 219.227 1.00 117.46 ? 1537 TRP A CA    1 
ATOM   18    C  C     . TRP A 1 1537 ? 181.980 207.360 220.367 1.00 117.73 ? 1537 TRP A C     1 
ATOM   19    O  O     . TRP A 1 1537 ? 181.593 207.273 221.538 1.00 116.74 ? 1537 TRP A O     1 
ATOM   20    C  CB    . TRP A 1 1537 ? 180.779 206.082 218.571 1.00 116.31 ? 1537 TRP A CB    1 
ATOM   21    C  CG    . TRP A 1 1537 ? 179.876 205.159 219.339 1.00 117.45 ? 1537 TRP A CG    1 
ATOM   22    C  CD1   . TRP A 1 1537 ? 179.905 204.910 220.681 1.00 115.51 ? 1537 TRP A CD1   1 
ATOM   23    C  CD2   . TRP A 1 1537 ? 178.809 204.364 218.808 1.00 118.38 ? 1537 TRP A CD2   1 
ATOM   24    N  NE1   . TRP A 1 1537 ? 178.923 204.011 221.018 1.00 114.94 ? 1537 TRP A NE1   1 
ATOM   25    C  CE2   . TRP A 1 1537 ? 178.236 203.659 219.886 1.00 117.28 ? 1537 TRP A CE2   1 
ATOM   26    C  CE3   . TRP A 1 1537 ? 178.282 204.180 217.526 1.00 116.00 ? 1537 TRP A CE3   1 
ATOM   27    C  CZ2   . TRP A 1 1537 ? 177.164 202.785 219.722 1.00 115.40 ? 1537 TRP A CZ2   1 
ATOM   28    C  CZ3   . TRP A 1 1537 ? 177.217 203.311 217.365 1.00 114.84 ? 1537 TRP A CZ3   1 
ATOM   29    C  CH2   . TRP A 1 1537 ? 176.670 202.625 218.457 1.00 115.82 ? 1537 TRP A CH2   1 
ATOM   30    N  N     . ILE A 1 1538 ? 183.276 207.376 220.047 1.00 114.50 ? 1538 ILE A N     1 
ATOM   31    C  CA    . ILE A 1 1538 ? 184.297 207.270 221.086 1.00 114.80 ? 1538 ILE A CA    1 
ATOM   32    C  C     . ILE A 1 1538 ? 184.233 208.464 222.033 1.00 116.31 ? 1538 ILE A C     1 
ATOM   33    O  O     . ILE A 1 1538 ? 184.313 208.307 223.259 1.00 113.36 ? 1538 ILE A O     1 
ATOM   34    C  CB    . ILE A 1 1538 ? 185.693 207.112 220.450 1.00 114.21 ? 1538 ILE A CB    1 
ATOM   35    C  CG1   . ILE A 1 1538 ? 186.772 207.034 221.534 1.00 113.94 ? 1538 ILE A CG1   1 
ATOM   36    C  CG2   . ILE A 1 1538 ? 185.976 208.228 219.447 1.00 111.11 ? 1538 ILE A CG2   1 
ATOM   37    C  CD1   . ILE A 1 1538 ? 188.121 206.586 221.021 1.00 112.41 ? 1538 ILE A CD1   1 
ATOM   38    N  N     . ASP A 1 1539 ? 184.080 209.673 221.484 1.00 115.94 ? 1539 ASP A N     1 
ATOM   39    C  CA    . ASP A 1 1539 ? 184.041 210.867 222.321 1.00 115.16 ? 1539 ASP A CA    1 
ATOM   40    C  C     . ASP A 1 1539 ? 182.823 210.863 223.235 1.00 114.43 ? 1539 ASP A C     1 
ATOM   41    O  O     . ASP A 1 1539 ? 182.934 211.155 224.432 1.00 111.84 ? 1539 ASP A O     1 
ATOM   42    C  CB    . ASP A 1 1539 ? 184.050 212.120 221.445 1.00 114.17 ? 1539 ASP A CB    1 
ATOM   43    C  CG    . ASP A 1 1539 ? 185.336 212.270 220.657 1.00 114.18 ? 1539 ASP A CG    1 
ATOM   44    O  OD1   . ASP A 1 1539 ? 186.402 211.881 221.179 1.00 113.53 ? 1539 ASP A OD1   1 
ATOM   45    O  OD2   . ASP A 1 1539 ? 185.281 212.776 219.517 1.00 112.72 ? 1539 ASP A OD2   1 
ATOM   46    N  N     . VAL A 1 1540 ? 181.652 210.528 222.688 1.00 115.76 ? 1540 VAL A N     1 
ATOM   47    C  CA    . VAL A 1 1540 ? 180.435 210.492 223.492 1.00 116.82 ? 1540 VAL A CA    1 
ATOM   48    C  C     . VAL A 1 1540 ? 180.535 209.414 224.562 1.00 116.27 ? 1540 VAL A C     1 
ATOM   49    O  O     . VAL A 1 1540 ? 180.120 209.619 225.710 1.00 115.18 ? 1540 VAL A O     1 
ATOM   50    C  CB    . VAL A 1 1540 ? 179.206 210.285 222.588 1.00 114.65 ? 1540 VAL A CB    1 
ATOM   51    C  CG1   . VAL A 1 1540 ? 177.940 210.144 223.424 1.00 113.21 ? 1540 VAL A CG1   1 
ATOM   52    C  CG2   . VAL A 1 1540 ? 179.075 211.436 221.606 1.00 112.64 ? 1540 VAL A CG2   1 
ATOM   53    N  N     . GLN A 1 1541 ? 181.085 208.251 224.206 1.00 112.90 ? 1541 GLN A N     1 
ATOM   54    C  CA    . GLN A 1 1541 ? 181.253 207.176 225.177 1.00 114.30 ? 1541 GLN A CA    1 
ATOM   55    C  C     . GLN A 1 1541 ? 182.160 207.607 226.322 1.00 115.90 ? 1541 GLN A C     1 
ATOM   56    O  O     . GLN A 1 1541 ? 181.835 207.399 227.496 1.00 113.63 ? 1541 GLN A O     1 
ATOM   57    C  CB    . GLN A 1 1541 ? 181.811 205.931 224.487 1.00 113.82 ? 1541 GLN A CB    1 
ATOM   58    C  CG    . GLN A 1 1541 ? 182.147 204.793 225.436 1.00 113.04 ? 1541 GLN A CG    1 
ATOM   59    C  CD    . GLN A 1 1541 ? 182.713 203.585 224.717 1.00 113.61 ? 1541 GLN A CD    1 
ATOM   60    O  OE1   . GLN A 1 1541 ? 182.034 202.960 223.902 1.00 114.63 ? 1541 GLN A OE1   1 
ATOM   61    N  NE2   . GLN A 1 1541 ? 183.962 203.250 225.015 1.00 112.27 ? 1541 GLN A NE2   1 
ATOM   62    N  N     . ARG A 1 1542 ? 183.301 208.225 225.998 1.00 119.27 ? 1542 ARG A N     1 
ATOM   63    C  CA    . ARG A 1 1542 ? 184.214 208.680 227.043 1.00 119.26 ? 1542 ARG A CA    1 
ATOM   64    C  C     . ARG A 1 1542 ? 183.559 209.734 227.927 1.00 118.13 ? 1542 ARG A C     1 
ATOM   65    O  O     . ARG A 1 1542 ? 183.683 209.690 229.162 1.00 116.27 ? 1542 ARG A O     1 
ATOM   66    C  CB    . ARG A 1 1542 ? 185.494 209.234 226.416 1.00 117.27 ? 1542 ARG A CB    1 
ATOM   67    C  CG    . ARG A 1 1542 ? 186.286 210.154 227.336 1.00 117.30 ? 1542 ARG A CG    1 
ATOM   68    C  CD    . ARG A 1 1542 ? 187.440 210.822 226.607 1.00 116.72 ? 1542 ARG A CD    1 
ATOM   69    N  NE    . ARG A 1 1542 ? 187.022 211.401 225.335 1.00 120.03 ? 1542 ARG A NE    1 
ATOM   70    C  CZ    . ARG A 1 1542 ? 186.474 212.601 225.203 1.00 119.06 ? 1542 ARG A CZ    1 
ATOM   71    N  NH1   . ARG A 1 1542 ? 186.262 213.384 226.248 1.00 117.72 ? 1542 ARG A NH1   1 
ATOM   72    N  NH2   . ARG A 1 1542 ? 186.133 213.028 223.990 1.00 115.64 ? 1542 ARG A NH2   1 
ATOM   73    N  N     . ARG A 1 1543 ? 182.863 210.694 227.309 1.00 116.90 ? 1543 ARG A N     1 
ATOM   74    C  CA    . ARG A 1 1543 ? 182.217 211.753 228.075 1.00 117.26 ? 1543 ARG A CA    1 
ATOM   75    C  C     . ARG A 1 1543 ? 181.177 211.181 229.025 1.00 118.35 ? 1543 ARG A C     1 
ATOM   76    O  O     . ARG A 1 1543 ? 181.141 211.542 230.209 1.00 117.40 ? 1543 ARG A O     1 
ATOM   77    C  CB    . ARG A 1 1543 ? 181.589 212.775 227.128 1.00 117.73 ? 1543 ARG A CB    1 
ATOM   78    C  CG    . ARG A 1 1543 ? 182.604 213.648 226.402 1.00 118.08 ? 1543 ARG A CG    1 
ATOM   79    C  CD    . ARG A 1 1543 ? 181.981 214.331 225.195 1.00 118.35 ? 1543 ARG A CD    1 
ATOM   80    N  NE    . ARG A 1 1543 ? 182.988 214.869 224.288 1.00 118.12 ? 1543 ARG A NE    1 
ATOM   81    C  CZ    . ARG A 1 1543 ? 183.352 216.144 224.242 1.00 117.88 ? 1543 ARG A CZ    1 
ATOM   82    N  NH1   . ARG A 1 1543 ? 182.812 217.046 225.045 1.00 117.85 ? 1543 ARG A NH1   1 
ATOM   83    N  NH2   . ARG A 1 1543 ? 184.279 216.523 223.367 1.00 115.38 ? 1543 ARG A NH2   1 
ATOM   84    N  N     . TRP A 1 1544 ? 180.343 210.262 228.531 1.00 118.32 ? 1544 TRP A N     1 
ATOM   85    C  CA    . TRP A 1 1544 ? 179.365 209.621 229.397 1.00 119.73 ? 1544 TRP A CA    1 
ATOM   86    C  C     . TRP A 1 1544 ? 180.039 208.828 230.505 1.00 118.39 ? 1544 TRP A C     1 
ATOM   87    O  O     . TRP A 1 1544 ? 179.564 208.847 231.643 1.00 116.04 ? 1544 TRP A O     1 
ATOM   88    C  CB    . TRP A 1 1544 ? 178.440 208.713 228.586 1.00 117.88 ? 1544 TRP A CB    1 
ATOM   89    C  CG    . TRP A 1 1544 ? 177.297 208.172 229.394 1.00 118.65 ? 1544 TRP A CG    1 
ATOM   90    C  CD1   . TRP A 1 1544 ? 176.044 208.703 229.497 1.00 118.86 ? 1544 TRP A CD1   1 
ATOM   91    C  CD2   . TRP A 1 1544 ? 177.303 206.998 230.217 1.00 118.22 ? 1544 TRP A CD2   1 
ATOM   92    N  NE1   . TRP A 1 1544 ? 175.270 207.934 230.331 1.00 118.38 ? 1544 TRP A NE1   1 
ATOM   93    C  CE2   . TRP A 1 1544 ? 176.019 206.881 230.786 1.00 118.17 ? 1544 TRP A CE2   1 
ATOM   94    C  CE3   . TRP A 1 1544 ? 178.269 206.035 230.526 1.00 116.79 ? 1544 TRP A CE3   1 
ATOM   95    C  CZ2   . TRP A 1 1544 ? 175.676 205.839 231.647 1.00 116.54 ? 1544 TRP A CZ2   1 
ATOM   96    C  CZ3   . TRP A 1 1544 ? 177.927 205.002 231.381 1.00 118.21 ? 1544 TRP A CZ3   1 
ATOM   97    C  CH2   . TRP A 1 1544 ? 176.641 204.913 231.931 1.00 118.30 ? 1544 TRP A CH2   1 
ATOM   98    N  N     . VAL A 1 1545 ? 181.144 208.141 230.204 1.00 115.38 ? 1545 VAL A N     1 
ATOM   99    C  CA    . VAL A 1 1545 ? 181.804 207.326 231.220 1.00 116.22 ? 1545 VAL A CA    1 
ATOM   100   C  C     . VAL A 1 1545 ? 182.307 208.196 232.365 1.00 116.03 ? 1545 VAL A C     1 
ATOM   101   O  O     . VAL A 1 1545 ? 182.020 207.924 233.539 1.00 114.67 ? 1545 VAL A O     1 
ATOM   102   C  CB    . VAL A 1 1545 ? 182.943 206.498 230.597 1.00 116.01 ? 1545 VAL A CB    1 
ATOM   103   C  CG1   . VAL A 1 1545 ? 183.857 205.960 231.686 1.00 114.37 ? 1545 VAL A CG1   1 
ATOM   104   C  CG2   . VAL A 1 1545 ? 182.375 205.346 229.784 1.00 114.50 ? 1545 VAL A CG2   1 
ATOM   105   N  N     . TYR A 1 1546 ? 183.049 209.266 232.055 1.00 115.62 ? 1546 TYR A N     1 
ATOM   106   C  CA    . TYR A 1 1546 ? 183.582 210.022 233.187 1.00 116.10 ? 1546 TYR A CA    1 
ATOM   107   C  C     . TYR A 1 1546 ? 182.515 210.881 233.858 1.00 117.29 ? 1546 TYR A C     1 
ATOM   108   O  O     . TYR A 1 1546 ? 182.594 211.107 235.071 1.00 115.31 ? 1546 TYR A O     1 
ATOM   109   C  CB    . TYR A 1 1546 ? 184.804 210.883 232.822 1.00 115.62 ? 1546 TYR A CB    1 
ATOM   110   C  CG    . TYR A 1 1546 ? 184.624 212.034 231.856 1.00 117.52 ? 1546 TYR A CG    1 
ATOM   111   C  CD1   . TYR A 1 1546 ? 184.979 211.909 230.524 1.00 117.27 ? 1546 TYR A CD1   1 
ATOM   112   C  CD2   . TYR A 1 1546 ? 184.116 213.255 232.286 1.00 115.50 ? 1546 TYR A CD2   1 
ATOM   113   C  CE1   . TYR A 1 1546 ? 184.842 212.963 229.646 1.00 115.93 ? 1546 TYR A CE1   1 
ATOM   114   C  CE2   . TYR A 1 1546 ? 183.959 214.312 231.410 1.00 115.68 ? 1546 TYR A CE2   1 
ATOM   115   C  CZ    . TYR A 1 1546 ? 184.321 214.157 230.089 1.00 117.22 ? 1546 TYR A CZ    1 
ATOM   116   O  OH    . TYR A 1 1546 ? 184.172 215.202 229.207 1.00 116.39 ? 1546 TYR A OH    1 
ATOM   117   N  N     . LEU A 1 1547 ? 181.499 211.344 233.121 1.00 116.28 ? 1547 LEU A N     1 
ATOM   118   C  CA    . LEU A 1 1547 ? 180.415 212.065 233.780 1.00 115.67 ? 1547 LEU A CA    1 
ATOM   119   C  C     . LEU A 1 1547 ? 179.622 211.148 234.702 1.00 115.01 ? 1547 LEU A C     1 
ATOM   120   O  O     . LEU A 1 1547 ? 179.222 211.558 235.797 1.00 113.59 ? 1547 LEU A O     1 
ATOM   121   C  CB    . LEU A 1 1547 ? 179.504 212.717 232.743 1.00 114.18 ? 1547 LEU A CB    1 
ATOM   122   C  CG    . LEU A 1 1547 ? 179.930 214.128 232.332 1.00 115.22 ? 1547 LEU A CG    1 
ATOM   123   C  CD1   . LEU A 1 1547 ? 178.835 214.806 231.538 1.00 114.99 ? 1547 LEU A CD1   1 
ATOM   124   C  CD2   . LEU A 1 1547 ? 180.303 214.959 233.552 1.00 113.69 ? 1547 LEU A CD2   1 
ATOM   125   N  N     . GLU A 1 1548 ? 179.390 209.901 234.282 1.00 112.17 ? 1548 GLU A N     1 
ATOM   126   C  CA    . GLU A 1 1548 ? 178.728 208.935 235.150 1.00 112.06 ? 1548 GLU A CA    1 
ATOM   127   C  C     . GLU A 1 1548 ? 179.573 208.631 236.376 1.00 111.80 ? 1548 GLU A C     1 
ATOM   128   O  O     . GLU A 1 1548 ? 179.044 208.510 237.485 1.00 109.27 ? 1548 GLU A O     1 
ATOM   129   C  CB    . GLU A 1 1548 ? 178.424 207.654 234.373 1.00 110.82 ? 1548 GLU A CB    1 
ATOM   130   C  CG    . GLU A 1 1548 ? 177.487 206.699 235.095 1.00 110.78 ? 1548 GLU A CG    1 
ATOM   131   C  CD    . GLU A 1 1548 ? 178.229 205.688 235.949 1.00 111.35 ? 1548 GLU A CD    1 
ATOM   132   O  OE1   . GLU A 1 1548 ? 179.434 205.471 235.702 1.00 110.54 ? 1548 GLU A OE1   1 
ATOM   133   O  OE2   . GLU A 1 1548 ? 177.610 205.117 236.871 1.00 111.66 ? 1548 GLU A OE2   1 
ATOM   134   N  N     . GLY A 1 1549 ? 180.889 208.499 236.197 1.00 107.29 ? 1549 GLY A N     1 
ATOM   135   C  CA    . GLY A 1 1549 ? 181.755 208.301 237.349 1.00 106.96 ? 1549 GLY A CA    1 
ATOM   136   C  C     . GLY A 1 1549 ? 181.683 209.454 238.332 1.00 108.28 ? 1549 GLY A C     1 
ATOM   137   O  O     . GLY A 1 1549 ? 181.576 209.245 239.544 1.00 106.69 ? 1549 GLY A O     1 
ATOM   138   N  N     . ILE A 1 1550 ? 181.717 210.687 237.819 1.00 109.21 ? 1550 ILE A N     1 
ATOM   139   C  CA    . ILE A 1 1550 ? 181.636 211.863 238.680 1.00 110.75 ? 1550 ILE A CA    1 
ATOM   140   C  C     . ILE A 1 1550 ? 180.297 211.909 239.408 1.00 111.81 ? 1550 ILE A C     1 
ATOM   141   O  O     . ILE A 1 1550 ? 180.242 212.160 240.618 1.00 110.23 ? 1550 ILE A O     1 
ATOM   142   C  CB    . ILE A 1 1550 ? 181.876 213.139 237.852 1.00 111.16 ? 1550 ILE A CB    1 
ATOM   143   C  CG1   . ILE A 1 1550 ? 183.366 213.306 237.547 1.00 108.27 ? 1550 ILE A CG1   1 
ATOM   144   C  CG2   . ILE A 1 1550 ? 181.329 214.363 238.575 1.00 109.23 ? 1550 ILE A CG2   1 
ATOM   145   C  CD1   . ILE A 1 1550 ? 183.649 214.238 236.389 1.00 107.21 ? 1550 ILE A CD1   1 
ATOM   146   N  N     . PHE A 1 1551 ? 179.199 211.661 238.690 1.00 112.47 ? 1551 PHE A N     1 
ATOM   147   C  CA    . PHE A 1 1551 ? 177.879 211.762 239.302 1.00 112.07 ? 1551 PHE A CA    1 
ATOM   148   C  C     . PHE A 1 1551 ? 177.631 210.648 240.312 1.00 110.42 ? 1551 PHE A C     1 
ATOM   149   O  O     . PHE A 1 1551 ? 176.992 210.885 241.344 1.00 108.94 ? 1551 PHE A O     1 
ATOM   150   C  CB    . PHE A 1 1551 ? 176.795 211.750 238.221 1.00 112.69 ? 1551 PHE A CB    1 
ATOM   151   C  CG    . PHE A 1 1551 ? 176.425 213.118 237.717 1.00 114.28 ? 1551 PHE A CG    1 
ATOM   152   C  CD1   . PHE A 1 1551 ? 175.695 213.989 238.509 1.00 111.63 ? 1551 PHE A CD1   1 
ATOM   153   C  CD2   . PHE A 1 1551 ? 176.804 213.531 236.450 1.00 112.71 ? 1551 PHE A CD2   1 
ATOM   154   C  CE1   . PHE A 1 1551 ? 175.353 215.247 238.049 1.00 112.24 ? 1551 PHE A CE1   1 
ATOM   155   C  CE2   . PHE A 1 1551 ? 176.464 214.788 235.984 1.00 111.65 ? 1551 PHE A CE2   1 
ATOM   156   C  CZ    . PHE A 1 1551 ? 175.738 215.647 236.785 1.00 112.04 ? 1551 PHE A CZ    1 
ATOM   157   N  N     . THR A 1 1552 ? 178.119 209.436 240.042 1.00 107.37 ? 1552 THR A N     1 
ATOM   158   C  CA    . THR A 1 1552 ? 177.875 208.318 240.945 1.00 108.20 ? 1552 THR A CA    1 
ATOM   159   C  C     . THR A 1 1552 ? 178.777 208.378 242.172 1.00 107.38 ? 1552 THR A C     1 
ATOM   160   O  O     . THR A 1 1552 ? 178.320 208.118 243.291 1.00 104.26 ? 1552 THR A O     1 
ATOM   161   C  CB    . THR A 1 1552 ? 178.069 206.995 240.204 1.00 107.42 ? 1552 THR A CB    1 
ATOM   162   O  OG1   . THR A 1 1552 ? 177.155 206.926 239.102 1.00 105.74 ? 1552 THR A OG1   1 
ATOM   163   C  CG2   . THR A 1 1552 ? 177.812 205.819 241.134 1.00 105.15 ? 1552 THR A CG2   1 
ATOM   164   N  N     . GLY A 1 1553 ? 180.055 208.721 241.987 1.00 103.17 ? 1553 GLY A N     1 
ATOM   165   C  CA    . GLY A 1 1553 ? 180.948 208.831 243.129 1.00 101.85 ? 1553 GLY A CA    1 
ATOM   166   C  C     . GLY A 1 1553 ? 180.525 209.922 244.094 1.00 104.63 ? 1553 GLY A C     1 
ATOM   167   O  O     . GLY A 1 1553 ? 180.570 209.740 245.313 1.00 102.16 ? 1553 GLY A O     1 
ATOM   168   N  N     . SER A 1 1554 ? 180.100 211.066 243.562 1.00 107.67 ? 1554 SER A N     1 
ATOM   169   C  CA    . SER A 1 1554 ? 179.632 212.190 244.370 1.00 106.96 ? 1554 SER A CA    1 
ATOM   170   C  C     . SER A 1 1554 ? 178.110 212.114 244.430 1.00 110.30 ? 1554 SER A C     1 
ATOM   171   O  O     . SER A 1 1554 ? 177.406 212.677 243.591 1.00 110.73 ? 1554 SER A O     1 
ATOM   172   C  CB    . SER A 1 1554 ? 180.114 213.512 243.785 1.00 104.66 ? 1554 SER A CB    1 
ATOM   173   O  OG    . SER A 1 1554 ? 179.866 213.575 242.392 1.00 106.42 ? 1554 SER A OG    1 
ATOM   174   N  N     . ALA A 1 1555 ? 177.599 211.405 245.439 1.00 108.32 ? 1555 ALA A N     1 
ATOM   175   C  CA    . ALA A 1 1555 ? 176.156 211.256 245.589 1.00 106.90 ? 1555 ALA A CA    1 
ATOM   176   C  C     . ALA A 1 1555 ? 175.482 212.541 246.049 1.00 105.57 ? 1555 ALA A C     1 
ATOM   177   O  O     . ALA A 1 1555 ? 174.267 212.683 245.877 1.00 105.25 ? 1555 ALA A O     1 
ATOM   178   C  CB    . ALA A 1 1555 ? 175.840 210.126 246.569 1.00 104.41 ? 1555 ALA A CB    1 
ATOM   179   N  N     . ASP A 1 1556 ? 176.234 213.474 246.627 1.00 104.58 ? 1556 ASP A N     1 
ATOM   180   C  CA    . ASP A 1 1556 ? 175.683 214.734 247.105 1.00 104.57 ? 1556 ASP A CA    1 
ATOM   181   C  C     . ASP A 1 1556 ? 175.801 215.858 246.084 1.00 105.79 ? 1556 ASP A C     1 
ATOM   182   O  O     . ASP A 1 1556 ? 175.457 217.001 246.401 1.00 105.45 ? 1556 ASP A O     1 
ATOM   183   C  CB    . ASP A 1 1556 ? 176.371 215.148 248.410 1.00 104.74 ? 1556 ASP A CB    1 
ATOM   184   C  CG    . ASP A 1 1556 ? 176.098 214.179 249.544 1.00 106.88 ? 1556 ASP A CG    1 
ATOM   185   O  OD1   . ASP A 1 1556 ? 175.029 213.535 249.531 1.00 106.87 ? 1556 ASP A OD1   1 
ATOM   186   O  OD2   . ASP A 1 1556 ? 176.953 214.060 250.447 1.00 104.41 ? 1556 ASP A OD2   1 
ATOM   187   N  N     . ILE A 1 1557 ? 176.284 215.566 244.874 1.00 108.28 ? 1557 ILE A N     1 
ATOM   188   C  CA    . ILE A 1 1557 ? 176.385 216.592 243.845 1.00 109.41 ? 1557 ILE A CA    1 
ATOM   189   C  C     . ILE A 1 1557 ? 175.024 216.913 243.239 1.00 108.22 ? 1557 ILE A C     1 
ATOM   190   O  O     . ILE A 1 1557 ? 174.864 217.962 242.605 1.00 104.83 ? 1557 ILE A O     1 
ATOM   191   C  CB    . ILE A 1 1557 ? 177.386 216.160 242.755 1.00 109.00 ? 1557 ILE A CB    1 
ATOM   192   C  CG1   . ILE A 1 1557 ? 177.990 217.383 242.063 1.00 107.07 ? 1557 ILE A CG1   1 
ATOM   193   C  CG2   . ILE A 1 1557 ? 176.719 215.248 241.736 1.00 106.66 ? 1557 ILE A CG2   1 
ATOM   194   C  CD1   . ILE A 1 1557 ? 179.160 217.058 241.160 1.00 106.05 ? 1557 ILE A CD1   1 
ATOM   195   N  N     . LYS A 1 1558 ? 174.034 216.035 243.420 1.00 110.97 ? 1558 LYS A N     1 
ATOM   196   C  CA    . LYS A 1 1558 ? 172.717 216.273 242.840 1.00 111.45 ? 1558 LYS A CA    1 
ATOM   197   C  C     . LYS A 1 1558 ? 171.934 217.322 243.618 1.00 110.87 ? 1558 LYS A C     1 
ATOM   198   O  O     . LYS A 1 1558 ? 171.138 218.061 243.027 1.00 107.99 ? 1558 LYS A O     1 
ATOM   199   C  CB    . LYS A 1 1558 ? 171.924 214.969 242.780 1.00 110.22 ? 1558 LYS A CB    1 
ATOM   200   C  CG    . LYS A 1 1558 ? 172.024 214.124 244.037 1.00 108.48 ? 1558 LYS A CG    1 
ATOM   201   C  CD    . LYS A 1 1558 ? 171.213 212.846 243.906 1.00 108.57 ? 1558 LYS A CD    1 
ATOM   202   C  CE    . LYS A 1 1558 ? 169.796 213.138 243.433 1.00 110.55 ? 1558 LYS A CE    1 
ATOM   203   N  NZ    . LYS A 1 1558 ? 169.021 211.891 243.182 1.00 110.15 ? 1558 LYS A NZ    1 
ATOM   204   N  N     . HIS A 1 1559 ? 172.132 217.392 244.937 1.00 111.63 ? 1559 HIS A N     1 
ATOM   205   C  CA    . HIS A 1 1559 ? 171.409 218.368 245.746 1.00 112.44 ? 1559 HIS A CA    1 
ATOM   206   C  C     . HIS A 1 1559 ? 171.732 219.795 245.329 1.00 113.86 ? 1559 HIS A C     1 
ATOM   207   O  O     . HIS A 1 1559 ? 170.893 220.690 245.478 1.00 113.52 ? 1559 HIS A O     1 
ATOM   208   C  CB    . HIS A 1 1559 ? 171.738 218.179 247.227 1.00 111.09 ? 1559 HIS A CB    1 
ATOM   209   C  CG    . HIS A 1 1559 ? 171.619 216.764 247.699 1.00 114.12 ? 1559 HIS A CG    1 
ATOM   210   N  ND1   . HIS A 1 1559 ? 172.597 216.146 248.447 1.00 113.29 ? 1559 HIS A ND1   1 
ATOM   211   C  CD2   . HIS A 1 1559 ? 170.636 215.847 247.533 1.00 114.11 ? 1559 HIS A CD2   1 
ATOM   212   C  CE1   . HIS A 1 1559 ? 172.224 214.909 248.721 1.00 112.91 ? 1559 HIS A CE1   1 
ATOM   213   N  NE2   . HIS A 1 1559 ? 171.037 214.702 248.178 1.00 113.99 ? 1559 HIS A NE2   1 
ATOM   214   N  N     . LEU A 1 1560 ? 172.936 220.026 244.811 1.00 108.86 ? 1560 LEU A N     1 
ATOM   215   C  CA    . LEU A 1 1560 ? 173.399 221.367 244.495 1.00 109.64 ? 1560 LEU A CA    1 
ATOM   216   C  C     . LEU A 1 1560 ? 173.578 221.596 242.998 1.00 108.63 ? 1560 LEU A C     1 
ATOM   217   O  O     . LEU A 1 1560 ? 173.861 222.727 242.588 1.00 106.59 ? 1560 LEU A O     1 
ATOM   218   C  CB    . LEU A 1 1560 ? 174.703 221.637 245.261 1.00 108.65 ? 1560 LEU A CB    1 
ATOM   219   C  CG    . LEU A 1 1560 ? 175.363 223.010 245.306 1.00 108.00 ? 1560 LEU A CG    1 
ATOM   220   C  CD1   . LEU A 1 1560 ? 174.416 224.032 245.898 1.00 106.50 ? 1560 LEU A CD1   1 
ATOM   221   C  CD2   . LEU A 1 1560 ? 176.607 222.904 246.171 1.00 106.74 ? 1560 LEU A CD2   1 
ATOM   222   N  N     . LEU A 1 1561 ? 173.389 220.563 242.175 1.00 108.19 ? 1561 LEU A N     1 
ATOM   223   C  CA    . LEU A 1 1561 ? 173.397 220.675 240.715 1.00 108.94 ? 1561 LEU A CA    1 
ATOM   224   C  C     . LEU A 1 1561 ? 172.139 220.015 240.162 1.00 108.93 ? 1561 LEU A C     1 
ATOM   225   O  O     . LEU A 1 1561 ? 172.217 219.027 239.424 1.00 107.11 ? 1561 LEU A O     1 
ATOM   226   C  CB    . LEU A 1 1561 ? 174.649 220.030 240.117 1.00 109.29 ? 1561 LEU A CB    1 
ATOM   227   C  CG    . LEU A 1 1561 ? 176.031 220.532 240.532 1.00 109.22 ? 1561 LEU A CG    1 
ATOM   228   C  CD1   . LEU A 1 1561 ? 177.091 219.945 239.619 1.00 106.07 ? 1561 LEU A CD1   1 
ATOM   229   C  CD2   . LEU A 1 1561 ? 176.075 222.043 240.474 1.00 107.48 ? 1561 LEU A CD2   1 
ATOM   230   N  N     . PRO A 1 1562 ? 170.956 220.557 240.480 1.00 111.76 ? 1562 PRO A N     1 
ATOM   231   C  CA    . PRO A 1 1562 ? 169.707 219.826 240.208 1.00 110.58 ? 1562 PRO A CA    1 
ATOM   232   C  C     . PRO A 1 1562 ? 169.347 219.674 238.734 1.00 109.35 ? 1562 PRO A C     1 
ATOM   233   O  O     . PRO A 1 1562 ? 169.055 218.562 238.275 1.00 106.34 ? 1562 PRO A O     1 
ATOM   234   C  CB    . PRO A 1 1562 ? 168.654 220.660 240.947 1.00 109.32 ? 1562 PRO A CB    1 
ATOM   235   C  CG    . PRO A 1 1562 ? 169.212 222.041 240.970 1.00 108.20 ? 1562 PRO A CG    1 
ATOM   236   C  CD    . PRO A 1 1562 ? 170.711 221.916 240.996 1.00 108.23 ? 1562 PRO A CD    1 
ATOM   237   N  N     . VAL A 1 1563 ? 169.346 220.781 237.987 1.00 107.02 ? 1563 VAL A N     1 
ATOM   238   C  CA    . VAL A 1 1563 ? 168.829 220.749 236.621 1.00 107.24 ? 1563 VAL A CA    1 
ATOM   239   C  C     . VAL A 1 1563 ? 169.727 219.910 235.717 1.00 107.44 ? 1563 VAL A C     1 
ATOM   240   O  O     . VAL A 1 1563 ? 169.241 219.079 234.938 1.00 105.14 ? 1563 VAL A O     1 
ATOM   241   C  CB    . VAL A 1 1563 ? 168.631 222.182 236.088 1.00 106.99 ? 1563 VAL A CB    1 
ATOM   242   C  CG1   . VAL A 1 1563 ? 169.905 222.999 236.212 1.00 105.18 ? 1563 VAL A CG1   1 
ATOM   243   C  CG2   . VAL A 1 1563 ? 168.148 222.151 234.646 1.00 105.31 ? 1563 VAL A CG2   1 
ATOM   244   N  N     . GLU A 1 1564 ? 171.046 220.091 235.812 1.00 109.86 ? 1564 GLU A N     1 
ATOM   245   C  CA    . GLU A 1 1564 ? 171.935 219.231 235.041 1.00 109.32 ? 1564 GLU A CA    1 
ATOM   246   C  C     . GLU A 1 1564 ? 171.968 217.806 235.578 1.00 109.07 ? 1564 GLU A C     1 
ATOM   247   O  O     . GLU A 1 1564 ? 172.274 216.886 234.816 1.00 107.48 ? 1564 GLU A O     1 
ATOM   248   C  CB    . GLU A 1 1564 ? 173.348 219.819 234.979 1.00 107.31 ? 1564 GLU A CB    1 
ATOM   249   C  CG    . GLU A 1 1564 ? 174.016 220.068 236.315 1.00 108.76 ? 1564 GLU A CG    1 
ATOM   250   C  CD    . GLU A 1 1564 ? 173.841 221.500 236.778 1.00 109.55 ? 1564 GLU A CD    1 
ATOM   251   O  OE1   . GLU A 1 1564 ? 172.934 222.183 236.263 1.00 110.11 ? 1564 GLU A OE1   1 
ATOM   252   O  OE2   . GLU A 1 1564 ? 174.623 221.955 237.636 1.00 108.30 ? 1564 GLU A OE2   1 
ATOM   253   N  N     . THR A 1 1565 ? 171.622 217.591 236.850 1.00 109.91 ? 1565 THR A N     1 
ATOM   254   C  CA    . THR A 1 1565 ? 171.451 216.222 237.329 1.00 111.43 ? 1565 THR A CA    1 
ATOM   255   C  C     . THR A 1 1565 ? 170.283 215.540 236.628 1.00 111.86 ? 1565 THR A C     1 
ATOM   256   O  O     . THR A 1 1565 ? 170.391 214.382 236.213 1.00 110.44 ? 1565 THR A O     1 
ATOM   257   C  CB    . THR A 1 1565 ? 171.248 216.197 238.843 1.00 111.81 ? 1565 THR A CB    1 
ATOM   258   O  OG1   . THR A 1 1565 ? 172.452 216.616 239.496 1.00 111.56 ? 1565 THR A OG1   1 
ATOM   259   C  CG2   . THR A 1 1565 ? 170.890 214.792 239.310 1.00 109.80 ? 1565 THR A CG2   1 
ATOM   260   N  N     . GLN A 1 1566 ? 169.158 216.245 236.477 1.00 110.50 ? 1566 GLN A N     1 
ATOM   261   C  CA    . GLN A 1 1566 ? 168.034 215.677 235.734 1.00 110.10 ? 1566 GLN A CA    1 
ATOM   262   C  C     . GLN A 1 1566 ? 168.385 215.484 234.262 1.00 108.68 ? 1566 GLN A C     1 
ATOM   263   O  O     . GLN A 1 1566 ? 167.982 214.489 233.640 1.00 107.93 ? 1566 GLN A O     1 
ATOM   264   C  CB    . GLN A 1 1566 ? 166.798 216.565 235.881 1.00 107.63 ? 1566 GLN A CB    1 
ATOM   265   C  CG    . GLN A 1 1566 ? 166.459 216.926 237.316 1.00 109.25 ? 1566 GLN A CG    1 
ATOM   266   C  CD    . GLN A 1 1566 ? 166.325 215.706 238.206 1.00 110.43 ? 1566 GLN A CD    1 
ATOM   267   O  OE1   . GLN A 1 1566 ? 167.070 215.542 239.172 1.00 108.13 ? 1566 GLN A OE1   1 
ATOM   268   N  NE2   . GLN A 1 1566 ? 165.372 214.840 237.882 1.00 108.03 ? 1566 GLN A NE2   1 
ATOM   269   N  N     . ARG A 1 1567 ? 169.125 216.433 233.684 1.00 107.06 ? 1567 ARG A N     1 
ATOM   270   C  CA    . ARG A 1 1567 ? 169.550 216.287 232.296 1.00 109.31 ? 1567 ARG A CA    1 
ATOM   271   C  C     . ARG A 1 1567 ? 170.427 215.054 232.117 1.00 109.89 ? 1567 ARG A C     1 
ATOM   272   O  O     . ARG A 1 1567 ? 170.257 214.291 231.158 1.00 106.61 ? 1567 ARG A O     1 
ATOM   273   C  CB    . ARG A 1 1567 ? 170.285 217.546 231.837 1.00 108.01 ? 1567 ARG A CB    1 
ATOM   274   C  CG    . ARG A 1 1567 ? 169.390 218.767 231.696 1.00 106.48 ? 1567 ARG A CG    1 
ATOM   275   C  CD    . ARG A 1 1567 ? 170.211 220.036 231.549 1.00 108.18 ? 1567 ARG A CD    1 
ATOM   276   N  NE    . ARG A 1 1567 ? 169.405 221.239 231.724 1.00 109.02 ? 1567 ARG A NE    1 
ATOM   277   C  CZ    . ARG A 1 1567 ? 168.727 221.838 230.755 1.00 108.66 ? 1567 ARG A CZ    1 
ATOM   278   N  NH1   . ARG A 1 1567 ? 168.723 221.366 229.519 1.00 107.74 ? 1567 ARG A NH1   1 
ATOM   279   N  NH2   . ARG A 1 1567 ? 168.032 222.937 231.034 1.00 107.45 ? 1567 ARG A NH2   1 
ATOM   280   N  N     . PHE A 1 1568 ? 171.361 214.825 233.044 1.00 112.73 ? 1568 PHE A N     1 
ATOM   281   C  CA    . PHE A 1 1568 ? 172.181 213.624 232.966 1.00 112.14 ? 1568 PHE A CA    1 
ATOM   282   C  C     . PHE A 1 1568 ? 171.382 212.370 233.288 1.00 111.45 ? 1568 PHE A C     1 
ATOM   283   O  O     . PHE A 1 1568 ? 171.736 211.287 232.825 1.00 109.77 ? 1568 PHE A O     1 
ATOM   284   C  CB    . PHE A 1 1568 ? 173.385 213.721 233.898 1.00 112.43 ? 1568 PHE A CB    1 
ATOM   285   C  CG    . PHE A 1 1568 ? 174.306 212.542 233.797 1.00 115.07 ? 1568 PHE A CG    1 
ATOM   286   C  CD1   . PHE A 1 1568 ? 175.021 212.309 232.635 1.00 113.87 ? 1568 PHE A CD1   1 
ATOM   287   C  CD2   . PHE A 1 1568 ? 174.427 211.647 234.845 1.00 113.05 ? 1568 PHE A CD2   1 
ATOM   288   C  CE1   . PHE A 1 1568 ? 175.859 211.219 232.528 1.00 113.80 ? 1568 PHE A CE1   1 
ATOM   289   C  CE2   . PHE A 1 1568 ? 175.264 210.554 234.745 1.00 111.79 ? 1568 PHE A CE2   1 
ATOM   290   C  CZ    . PHE A 1 1568 ? 175.979 210.340 233.583 1.00 114.45 ? 1568 PHE A CZ    1 
ATOM   291   N  N     . GLN A 1 1569 ? 170.318 212.484 234.084 1.00 106.81 ? 1569 GLN A N     1 
ATOM   292   C  CA    . GLN A 1 1569 ? 169.431 211.342 234.289 1.00 107.50 ? 1569 GLN A CA    1 
ATOM   293   C  C     . GLN A 1 1569 ? 168.772 210.931 232.979 1.00 107.79 ? 1569 GLN A C     1 
ATOM   294   O  O     . GLN A 1 1569 ? 168.716 209.740 232.642 1.00 105.68 ? 1569 GLN A O     1 
ATOM   295   C  CB    . GLN A 1 1569 ? 168.377 211.684 235.343 1.00 104.40 ? 1569 GLN A CB    1 
ATOM   296   C  CG    . GLN A 1 1569 ? 167.323 210.609 235.561 1.00 106.45 ? 1569 GLN A CG    1 
ATOM   297   C  CD    . GLN A 1 1569 ? 167.922 209.260 235.906 1.00 107.01 ? 1569 GLN A CD    1 
ATOM   298   O  OE1   . GLN A 1 1569 ? 167.624 208.253 235.264 1.00 104.79 ? 1569 GLN A OE1   1 
ATOM   299   N  NE2   . GLN A 1 1569 ? 168.770 209.234 236.928 1.00 106.91 ? 1569 GLN A NE2   1 
ATOM   300   N  N     . SER A 1 1570 ? 168.285 211.912 232.217 1.00 109.22 ? 1570 SER A N     1 
ATOM   301   C  CA    . SER A 1 1570 ? 167.735 211.621 230.896 1.00 108.57 ? 1570 SER A CA    1 
ATOM   302   C  C     . SER A 1 1570 ? 168.805 211.057 229.964 1.00 108.22 ? 1570 SER A C     1 
ATOM   303   O  O     . SER A 1 1570 ? 168.542 210.126 229.191 1.00 104.14 ? 1570 SER A O     1 
ATOM   304   C  CB    . SER A 1 1570 ? 167.110 212.882 230.300 1.00 106.06 ? 1570 SER A CB    1 
ATOM   305   O  OG    . SER A 1 1570 ? 166.209 213.481 231.213 1.00 103.51 ? 1570 SER A OG    1 
ATOM   306   N  N     . ILE A 1 1571 ? 170.018 211.613 230.026 1.00 112.81 ? 1571 ILE A N     1 
ATOM   307   C  CA    . ILE A 1 1571 ? 171.114 211.118 229.195 1.00 113.76 ? 1571 ILE A CA    1 
ATOM   308   C  C     . ILE A 1 1571 ? 171.451 209.675 229.555 1.00 113.46 ? 1571 ILE A C     1 
ATOM   309   O  O     . ILE A 1 1571 ? 171.744 208.854 228.680 1.00 110.65 ? 1571 ILE A O     1 
ATOM   310   C  CB    . ILE A 1 1571 ? 172.340 212.042 229.329 1.00 113.22 ? 1571 ILE A CB    1 
ATOM   311   C  CG1   . ILE A 1 1571 ? 172.069 213.385 228.648 1.00 111.89 ? 1571 ILE A CG1   1 
ATOM   312   C  CG2   . ILE A 1 1571 ? 173.579 211.387 228.739 1.00 111.40 ? 1571 ILE A CG2   1 
ATOM   313   C  CD1   . ILE A 1 1571 ? 173.203 214.378 228.782 1.00 112.07 ? 1571 ILE A CD1   1 
ATOM   314   N  N     . SER A 1 1572 ? 171.414 209.343 230.846 1.00 111.80 ? 1572 SER A N     1 
ATOM   315   C  CA    . SER A 1 1572 ? 171.693 207.980 231.282 1.00 111.81 ? 1572 SER A CA    1 
ATOM   316   C  C     . SER A 1 1572 ? 170.586 207.028 230.854 1.00 110.68 ? 1572 SER A C     1 
ATOM   317   O  O     . SER A 1 1572 ? 170.848 205.865 230.534 1.00 108.12 ? 1572 SER A O     1 
ATOM   318   C  CB    . SER A 1 1572 ? 171.878 207.941 232.799 1.00 110.68 ? 1572 SER A CB    1 
ATOM   319   O  OG    . SER A 1 1572 ? 172.940 208.785 233.207 1.00 109.89 ? 1572 SER A OG    1 
ATOM   320   N  N     . THR A 1 1573 ? 169.337 207.500 230.853 1.00 109.71 ? 1573 THR A N     1 
ATOM   321   C  CA    . THR A 1 1573 ? 168.252 206.686 230.312 1.00 109.66 ? 1573 THR A CA    1 
ATOM   322   C  C     . THR A 1 1573 ? 168.471 206.405 228.829 1.00 110.64 ? 1573 THR A C     1 
ATOM   323   O  O     . THR A 1 1573 ? 168.276 205.274 228.363 1.00 108.85 ? 1573 THR A O     1 
ATOM   324   C  CB    . THR A 1 1573 ? 166.908 207.379 230.535 1.00 109.22 ? 1573 THR A CB    1 
ATOM   325   O  OG1   . THR A 1 1573 ? 166.844 207.883 231.875 1.00 109.73 ? 1573 THR A OG1   1 
ATOM   326   C  CG2   . THR A 1 1573 ? 165.762 206.403 230.310 1.00 107.63 ? 1573 THR A CG2   1 
ATOM   327   N  N     . GLU A 1 1574 ? 168.889 207.424 228.075 1.00 111.54 ? 1574 GLU A N     1 
ATOM   328   C  CA    . GLU A 1 1574 ? 169.209 207.220 226.664 1.00 112.13 ? 1574 GLU A CA    1 
ATOM   329   C  C     . GLU A 1 1574 ? 170.370 206.245 226.497 1.00 112.41 ? 1574 GLU A C     1 
ATOM   330   O  O     . GLU A 1 1574 ? 170.360 205.401 225.593 1.00 109.78 ? 1574 GLU A O     1 
ATOM   331   C  CB    . GLU A 1 1574 ? 169.535 208.558 226.001 1.00 111.00 ? 1574 GLU A CB    1 
ATOM   332   C  CG    . GLU A 1 1574 ? 168.334 209.467 225.805 1.00 111.33 ? 1574 GLU A CG    1 
ATOM   333   C  CD    . GLU A 1 1574 ? 167.567 209.149 224.538 1.00 111.68 ? 1574 GLU A CD    1 
ATOM   334   O  OE1   . GLU A 1 1574 ? 168.058 209.491 223.442 1.00 111.17 ? 1574 GLU A OE1   1 
ATOM   335   O  OE2   . GLU A 1 1574 ? 166.473 208.556 224.638 1.00 110.61 ? 1574 GLU A OE2   1 
ATOM   336   N  N     . PHE A 1 1575 ? 171.384 206.357 227.356 1.00 116.69 ? 1575 PHE A N     1 
ATOM   337   C  CA    . PHE A 1 1575 ? 172.526 205.451 227.293 1.00 116.46 ? 1575 PHE A CA    1 
ATOM   338   C  C     . PHE A 1 1575 ? 172.112 204.018 227.597 1.00 116.52 ? 1575 PHE A C     1 
ATOM   339   O  O     . PHE A 1 1575 ? 172.613 203.077 226.975 1.00 116.78 ? 1575 PHE A O     1 
ATOM   340   C  CB    . PHE A 1 1575 ? 173.613 205.912 228.263 1.00 114.81 ? 1575 PHE A CB    1 
ATOM   341   C  CG    . PHE A 1 1575 ? 174.998 205.493 227.866 1.00 115.70 ? 1575 PHE A CG    1 
ATOM   342   C  CD1   . PHE A 1 1575 ? 175.719 206.225 226.938 1.00 115.16 ? 1575 PHE A CD1   1 
ATOM   343   C  CD2   . PHE A 1 1575 ? 175.582 204.368 228.426 1.00 115.57 ? 1575 PHE A CD2   1 
ATOM   344   C  CE1   . PHE A 1 1575 ? 176.997 205.841 226.572 1.00 115.54 ? 1575 PHE A CE1   1 
ATOM   345   C  CE2   . PHE A 1 1575 ? 176.859 203.980 228.066 1.00 115.97 ? 1575 PHE A CE2   1 
ATOM   346   C  CZ    . PHE A 1 1575 ? 177.568 204.717 227.137 1.00 116.35 ? 1575 PHE A CZ    1 
ATOM   347   N  N     . LEU A 1 1576 ? 171.209 203.831 228.561 1.00 109.36 ? 1576 LEU A N     1 
ATOM   348   C  CA    . LEU A 1 1576 ? 170.704 202.494 228.856 1.00 110.71 ? 1576 LEU A CA    1 
ATOM   349   C  C     . LEU A 1 1576 ? 169.902 201.939 227.686 1.00 109.89 ? 1576 LEU A C     1 
ATOM   350   O  O     . LEU A 1 1576 ? 169.986 200.743 227.376 1.00 107.71 ? 1576 LEU A O     1 
ATOM   351   C  CB    . LEU A 1 1576 ? 169.855 202.520 230.127 1.00 109.53 ? 1576 LEU A CB    1 
ATOM   352   C  CG    . LEU A 1 1576 ? 170.604 202.722 231.447 1.00 108.98 ? 1576 LEU A CG    1 
ATOM   353   C  CD1   . LEU A 1 1576 ? 169.744 202.280 232.620 1.00 107.15 ? 1576 LEU A CD1   1 
ATOM   354   C  CD2   . LEU A 1 1576 ? 171.932 201.978 231.441 1.00 107.69 ? 1576 LEU A CD2   1 
ATOM   355   N  N     . ALA A 1 1577 ? 169.111 202.791 227.028 1.00 108.21 ? 1577 ALA A N     1 
ATOM   356   C  CA    . ALA A 1 1577 ? 168.396 202.352 225.833 1.00 109.15 ? 1577 ALA A CA    1 
ATOM   357   C  C     . ALA A 1 1577 ? 169.367 201.920 224.740 1.00 109.93 ? 1577 ALA A C     1 
ATOM   358   O  O     . ALA A 1 1577 ? 169.171 200.883 224.094 1.00 108.18 ? 1577 ALA A O     1 
ATOM   359   C  CB    . ALA A 1 1577 ? 167.478 203.466 225.330 1.00 106.29 ? 1577 ALA A CB    1 
ATOM   360   N  N     . LEU A 1 1578 ? 170.432 202.697 224.531 1.00 109.90 ? 1578 LEU A N     1 
ATOM   361   C  CA    . LEU A 1 1578 ? 171.451 202.312 223.558 1.00 108.98 ? 1578 LEU A CA    1 
ATOM   362   C  C     . LEU A 1 1578 ? 172.124 201.003 223.954 1.00 107.19 ? 1578 LEU A C     1 
ATOM   363   O  O     . LEU A 1 1578 ? 172.393 200.152 223.101 1.00 106.42 ? 1578 LEU A O     1 
ATOM   364   C  CB    . LEU A 1 1578 ? 172.489 203.425 223.406 1.00 108.73 ? 1578 LEU A CB    1 
ATOM   365   C  CG    . LEU A 1 1578 ? 172.296 204.411 222.250 1.00 108.97 ? 1578 LEU A CG    1 
ATOM   366   C  CD1   . LEU A 1 1578 ? 171.084 205.303 222.473 1.00 106.64 ? 1578 LEU A CD1   1 
ATOM   367   C  CD2   . LEU A 1 1578 ? 173.551 205.249 222.047 1.00 107.05 ? 1578 LEU A CD2   1 
ATOM   368   N  N     . MET A 1 1579 ? 172.404 200.828 225.247 1.00 110.18 ? 1579 MET A N     1 
ATOM   369   C  CA    . MET A 1 1579 ? 173.031 199.600 225.724 1.00 113.31 ? 1579 MET A CA    1 
ATOM   370   C  C     . MET A 1 1579 ? 172.147 198.392 225.446 1.00 113.21 ? 1579 MET A C     1 
ATOM   371   O  O     . MET A 1 1579 ? 172.630 197.337 225.018 1.00 112.74 ? 1579 MET A O     1 
ATOM   372   C  CB    . MET A 1 1579 ? 173.326 199.719 227.221 1.00 112.67 ? 1579 MET A CB    1 
ATOM   373   C  CG    . MET A 1 1579 ? 174.121 198.563 227.809 1.00 112.41 ? 1579 MET A CG    1 
ATOM   374   S  SD    . MET A 1 1579 ? 175.800 198.451 227.164 1.00 118.27 ? 1579 MET A SD    1 
ATOM   375   C  CE    . MET A 1 1579 ? 176.155 196.719 227.453 1.00 111.25 ? 1579 MET A CE    1 
ATOM   376   N  N     . LYS A 1 1580 ? 170.842 198.531 225.681 1.00 110.74 ? 1580 LYS A N     1 
ATOM   377   C  CA    . LYS A 1 1580 ? 169.922 197.424 225.449 1.00 111.29 ? 1580 LYS A CA    1 
ATOM   378   C  C     . LYS A 1 1580 ? 169.583 197.229 223.977 1.00 112.65 ? 1580 LYS A C     1 
ATOM   379   O  O     . LYS A 1 1580 ? 169.059 196.168 223.619 1.00 111.66 ? 1580 LYS A O     1 
ATOM   380   C  CB    . LYS A 1 1580 ? 168.639 197.633 226.257 1.00 110.05 ? 1580 LYS A CB    1 
ATOM   381   C  CG    . LYS A 1 1580 ? 167.943 196.340 226.664 1.00 110.19 ? 1580 LYS A CG    1 
ATOM   382   C  CD    . LYS A 1 1580 ? 168.892 195.385 227.377 1.00 110.22 ? 1580 LYS A CD    1 
ATOM   383   C  CE    . LYS A 1 1580 ? 169.371 195.951 228.705 1.00 110.81 ? 1580 LYS A CE    1 
ATOM   384   N  NZ    . LYS A 1 1580 ? 170.318 195.027 229.388 1.00 108.89 ? 1580 LYS A NZ    1 
ATOM   385   N  N     . LYS A 1 1581 ? 169.862 198.210 223.119 1.00 113.91 ? 1581 LYS A N     1 
ATOM   386   C  CA    . LYS A 1 1581 ? 169.598 198.058 221.691 1.00 112.85 ? 1581 LYS A CA    1 
ATOM   387   C  C     . LYS A 1 1581 ? 170.797 197.551 220.896 1.00 111.83 ? 1581 LYS A C     1 
ATOM   388   O  O     . LYS A 1 1581 ? 170.661 196.585 220.140 1.00 109.48 ? 1581 LYS A O     1 
ATOM   389   C  CB    . LYS A 1 1581 ? 169.121 199.386 221.094 1.00 109.43 ? 1581 LYS A CB    1 
ATOM   390   C  CG    . LYS A 1 1581 ? 167.709 199.781 221.502 1.00 110.66 ? 1581 LYS A CG    1 
ATOM   391   C  CD    . LYS A 1 1581 ? 166.767 198.585 221.465 1.00 113.02 ? 1581 LYS A CD    1 
ATOM   392   C  CE    . LYS A 1 1581 ? 165.397 198.937 222.025 1.00 111.75 ? 1581 LYS A CE    1 
ATOM   393   N  NZ    . LYS A 1 1581 ? 164.670 199.903 221.156 1.00 110.05 ? 1581 LYS A NZ    1 
ATOM   394   N  N     . VAL A 1 1582 ? 171.971 198.170 221.043 1.00 108.93 ? 1582 VAL A N     1 
ATOM   395   C  CA    . VAL A 1 1582 ? 173.105 197.808 220.194 1.00 109.59 ? 1582 VAL A CA    1 
ATOM   396   C  C     . VAL A 1 1582 ? 173.719 196.469 220.589 1.00 110.20 ? 1582 VAL A C     1 
ATOM   397   O  O     . VAL A 1 1582 ? 174.257 195.765 219.724 1.00 107.29 ? 1582 VAL A O     1 
ATOM   398   C  CB    . VAL A 1 1582 ? 174.183 198.909 220.208 1.00 107.72 ? 1582 VAL A CB    1 
ATOM   399   C  CG1   . VAL A 1 1582 ? 174.828 199.037 221.582 1.00 106.10 ? 1582 VAL A CG1   1 
ATOM   400   C  CG2   . VAL A 1 1582 ? 175.233 198.659 219.133 1.00 106.96 ? 1582 VAL A CG2   1 
ATOM   401   N  N     . SER A 1 1583 ? 173.640 196.082 221.864 1.00 109.05 ? 1583 SER A N     1 
ATOM   402   C  CA    . SER A 1 1583 ? 174.243 194.831 222.303 1.00 108.14 ? 1583 SER A CA    1 
ATOM   403   C  C     . SER A 1 1583 ? 173.449 193.608 221.863 1.00 107.93 ? 1583 SER A C     1 
ATOM   404   O  O     . SER A 1 1583 ? 173.987 192.496 221.887 1.00 105.82 ? 1583 SER A O     1 
ATOM   405   C  CB    . SER A 1 1583 ? 174.393 194.823 223.826 1.00 106.09 ? 1583 SER A CB    1 
ATOM   406   O  OG    . SER A 1 1583 ? 173.205 194.371 224.452 1.00 105.46 ? 1583 SER A OG    1 
ATOM   407   N  N     . LYS A 1 1584 ? 172.185 193.786 221.469 1.00 109.77 ? 1584 LYS A N     1 
ATOM   408   C  CA    . LYS A 1 1584 ? 171.392 192.655 220.998 1.00 109.70 ? 1584 LYS A CA    1 
ATOM   409   C  C     . LYS A 1 1584 ? 171.960 192.082 219.705 1.00 109.34 ? 1584 LYS A C     1 
ATOM   410   O  O     . LYS A 1 1584 ? 171.993 190.860 219.520 1.00 107.12 ? 1584 LYS A O     1 
ATOM   411   C  CB    . LYS A 1 1584 ? 169.936 193.079 220.809 1.00 108.27 ? 1584 LYS A CB    1 
ATOM   412   C  CG    . LYS A 1 1584 ? 169.149 193.173 222.106 1.00 108.44 ? 1584 LYS A CG    1 
ATOM   413   C  CD    . LYS A 1 1584 ? 167.652 193.228 221.848 1.00 108.07 ? 1584 LYS A CD    1 
ATOM   414   C  CE    . LYS A 1 1584 ? 167.268 194.481 221.080 1.00 109.30 ? 1584 LYS A CE    1 
ATOM   415   N  NZ    . LYS A 1 1584 ? 165.794 194.587 220.896 1.00 107.65 ? 1584 LYS A NZ    1 
ATOM   416   N  N     . SER A 1 1585 ? 172.412 192.949 218.800 1.00 109.72 ? 1585 SER A N     1 
ATOM   417   C  CA    . SER A 1 1585 ? 173.007 192.523 217.537 1.00 110.15 ? 1585 SER A CA    1 
ATOM   418   C  C     . SER A 1 1585 ? 174.476 192.925 217.513 1.00 109.53 ? 1585 SER A C     1 
ATOM   419   O  O     . SER A 1 1585 ? 174.794 194.095 217.250 1.00 108.40 ? 1585 SER A O     1 
ATOM   420   C  CB    . SER A 1 1585 ? 172.261 193.141 216.351 1.00 108.81 ? 1585 SER A CB    1 
ATOM   421   O  OG    . SER A 1 1585 ? 170.888 192.792 216.377 1.00 106.80 ? 1585 SER A OG    1 
ATOM   422   N  N     . PRO A 1 1586 ? 175.409 192.001 217.775 1.00 110.86 ? 1586 PRO A N     1 
ATOM   423   C  CA    . PRO A 1 1586 ? 176.838 192.333 217.837 1.00 110.29 ? 1586 PRO A CA    1 
ATOM   424   C  C     . PRO A 1 1586 ? 177.528 192.367 216.474 1.00 109.96 ? 1586 PRO A C     1 
ATOM   425   O  O     . PRO A 1 1586 ? 178.571 191.744 216.269 1.00 108.43 ? 1586 PRO A O     1 
ATOM   426   C  CB    . PRO A 1 1586 ? 177.401 191.220 218.725 1.00 106.94 ? 1586 PRO A CB    1 
ATOM   427   C  CG    . PRO A 1 1586 ? 176.524 190.046 218.436 1.00 106.71 ? 1586 PRO A CG    1 
ATOM   428   C  CD    . PRO A 1 1586 ? 175.153 190.586 218.097 1.00 106.87 ? 1586 PRO A CD    1 
ATOM   429   N  N     . LEU A 1 1587 ? 176.940 193.102 215.532 1.00 111.62 ? 1587 LEU A N     1 
ATOM   430   C  CA    . LEU A 1 1587 ? 177.508 193.262 214.201 1.00 111.40 ? 1587 LEU A CA    1 
ATOM   431   C  C     . LEU A 1 1587 ? 177.444 194.725 213.790 1.00 111.43 ? 1587 LEU A C     1 
ATOM   432   O  O     . LEU A 1 1587 ? 176.451 195.411 214.053 1.00 110.39 ? 1587 LEU A O     1 
ATOM   433   C  CB    . LEU A 1 1587 ? 176.777 192.393 213.168 1.00 110.38 ? 1587 LEU A CB    1 
ATOM   434   C  CG    . LEU A 1 1587 ? 177.594 191.997 211.934 1.00 111.17 ? 1587 LEU A CG    1 
ATOM   435   C  CD1   . LEU A 1 1587 ? 178.947 191.432 212.342 1.00 108.83 ? 1587 LEU A CD1   1 
ATOM   436   C  CD2   . LEU A 1 1587 ? 176.832 191.002 211.071 1.00 108.95 ? 1587 LEU A CD2   1 
ATOM   437   N  N     . VAL A 1 1588 ? 178.512 195.198 213.144 1.00 114.31 ? 1588 VAL A N     1 
ATOM   438   C  CA    . VAL A 1 1588 ? 178.569 196.590 212.707 1.00 115.06 ? 1588 VAL A CA    1 
ATOM   439   C  C     . VAL A 1 1588 ? 177.522 196.862 211.630 1.00 112.97 ? 1588 VAL A C     1 
ATOM   440   O  O     . VAL A 1 1588 ? 176.842 197.898 211.650 1.00 109.91 ? 1588 VAL A O     1 
ATOM   441   C  CB    . VAL A 1 1588 ? 179.995 196.933 212.231 1.00 113.48 ? 1588 VAL A CB    1 
ATOM   442   C  CG1   . VAL A 1 1588 ? 180.463 195.957 211.155 1.00 111.56 ? 1588 VAL A CG1   1 
ATOM   443   C  CG2   . VAL A 1 1588 ? 180.066 198.364 211.724 1.00 110.60 ? 1588 VAL A CG2   1 
ATOM   444   N  N     . MET A 1 1589 ? 177.366 195.935 210.682 1.00 116.48 ? 1589 MET A N     1 
ATOM   445   C  CA    . MET A 1 1589 ? 176.376 196.109 209.625 1.00 116.75 ? 1589 MET A CA    1 
ATOM   446   C  C     . MET A 1 1589 ? 174.961 196.068 210.186 1.00 117.12 ? 1589 MET A C     1 
ATOM   447   O  O     . MET A 1 1589 ? 174.069 196.769 209.694 1.00 115.33 ? 1589 MET A O     1 
ATOM   448   C  CB    . MET A 1 1589 ? 176.563 195.035 208.555 1.00 115.85 ? 1589 MET A CB    1 
ATOM   449   C  CG    . MET A 1 1589 ? 177.658 195.343 207.550 1.00 115.26 ? 1589 MET A CG    1 
ATOM   450   S  SD    . MET A 1 1589 ? 177.376 194.567 205.950 1.00 120.67 ? 1589 MET A SD    1 
ATOM   451   C  CE    . MET A 1 1589 ? 178.318 195.654 204.885 1.00 113.91 ? 1589 MET A CE    1 
ATOM   452   N  N     . ASP A 1 1590 ? 174.737 195.244 211.212 1.00 115.35 ? 1590 ASP A N     1 
ATOM   453   C  CA    . ASP A 1 1590 ? 173.414 195.125 211.812 1.00 115.36 ? 1590 ASP A CA    1 
ATOM   454   C  C     . ASP A 1 1590 ? 173.007 196.372 212.586 1.00 116.61 ? 1590 ASP A C     1 
ATOM   455   O  O     . ASP A 1 1590 ? 171.815 196.552 212.858 1.00 117.14 ? 1590 ASP A O     1 
ATOM   456   C  CB    . ASP A 1 1590 ? 173.370 193.905 212.733 1.00 114.64 ? 1590 ASP A CB    1 
ATOM   457   C  CG    . ASP A 1 1590 ? 173.422 192.596 211.971 1.00 116.98 ? 1590 ASP A CG    1 
ATOM   458   O  OD1   . ASP A 1 1590 ? 173.760 192.618 210.769 1.00 115.75 ? 1590 ASP A OD1   1 
ATOM   459   O  OD2   . ASP A 1 1590 ? 173.133 191.542 212.578 1.00 116.14 ? 1590 ASP A OD2   1 
ATOM   460   N  N     . VAL A 1 1591 ? 173.958 197.229 212.953 1.00 111.65 ? 1591 VAL A N     1 
ATOM   461   C  CA    . VAL A 1 1591 ? 173.655 198.411 213.749 1.00 111.58 ? 1591 VAL A CA    1 
ATOM   462   C  C     . VAL A 1 1591 ? 173.766 199.716 212.967 1.00 110.13 ? 1591 VAL A C     1 
ATOM   463   O  O     . VAL A 1 1591 ? 173.104 200.696 213.345 1.00 107.83 ? 1591 VAL A O     1 
ATOM   464   C  CB    . VAL A 1 1591 ? 174.528 198.474 215.020 1.00 110.09 ? 1591 VAL A CB    1 
ATOM   465   C  CG1   . VAL A 1 1591 ? 174.363 197.204 215.839 1.00 108.09 ? 1591 VAL A CG1   1 
ATOM   466   C  CG2   . VAL A 1 1591 ? 175.987 198.691 214.659 1.00 107.93 ? 1591 VAL A CG2   1 
ATOM   467   N  N     . LEU A 1 1592 ? 174.572 199.778 211.903 1.00 109.54 ? 1592 LEU A N     1 
ATOM   468   C  CA    . LEU A 1 1592 ? 174.570 200.996 211.095 1.00 110.99 ? 1592 LEU A CA    1 
ATOM   469   C  C     . LEU A 1 1592 ? 173.352 201.099 210.185 1.00 109.45 ? 1592 LEU A C     1 
ATOM   470   O  O     . LEU A 1 1592 ? 173.074 202.188 209.672 1.00 107.35 ? 1592 LEU A O     1 
ATOM   471   C  CB    . LEU A 1 1592 ? 175.852 201.120 210.265 1.00 108.41 ? 1592 LEU A CB    1 
ATOM   472   C  CG    . LEU A 1 1592 ? 177.099 201.715 210.932 1.00 107.28 ? 1592 LEU A CG    1 
ATOM   473   C  CD1   . LEU A 1 1592 ? 176.831 203.167 211.309 1.00 105.71 ? 1592 LEU A CD1   1 
ATOM   474   C  CD2   . LEU A 1 1592 ? 177.555 200.933 212.150 1.00 105.93 ? 1592 LEU A CD2   1 
ATOM   475   N  N     . ASN A 1 1593 ? 172.621 200.007 209.968 1.00 108.96 ? 1593 ASN A N     1 
ATOM   476   C  CA    . ASN A 1 1593 ? 171.428 200.083 209.133 1.00 110.04 ? 1593 ASN A CA    1 
ATOM   477   C  C     . ASN A 1 1593 ? 170.214 200.617 209.884 1.00 109.37 ? 1593 ASN A C     1 
ATOM   478   O  O     . ASN A 1 1593 ? 169.183 200.879 209.254 1.00 106.53 ? 1593 ASN A O     1 
ATOM   479   C  CB    . ASN A 1 1593 ? 171.104 198.709 208.539 1.00 107.57 ? 1593 ASN A CB    1 
ATOM   480   C  CG    . ASN A 1 1593 ? 170.266 198.805 207.278 1.00 108.28 ? 1593 ASN A CG    1 
ATOM   481   O  OD1   . ASN A 1 1593 ? 170.213 199.853 206.635 1.00 107.47 ? 1593 ASN A OD1   1 
ATOM   482   N  ND2   . ASN A 1 1593 ? 169.604 197.712 206.920 1.00 108.35 ? 1593 ASN A ND2   1 
ATOM   483   N  N     . ILE A 1 1594 ? 170.311 200.792 211.199 1.00 109.70 ? 1594 ILE A N     1 
ATOM   484   C  CA    . ILE A 1 1594 ? 169.184 201.256 212.001 1.00 110.10 ? 1594 ILE A CA    1 
ATOM   485   C  C     . ILE A 1 1594 ? 169.112 202.775 211.934 1.00 110.41 ? 1594 ILE A C     1 
ATOM   486   O  O     . ILE A 1 1594 ? 170.092 203.471 212.229 1.00 109.44 ? 1594 ILE A O     1 
ATOM   487   C  CB    . ILE A 1 1594 ? 169.317 200.768 213.452 1.00 109.89 ? 1594 ILE A CB    1 
ATOM   488   C  CG1   . ILE A 1 1594 ? 169.616 199.268 213.481 1.00 107.40 ? 1594 ILE A CG1   1 
ATOM   489   C  CG2   . ILE A 1 1594 ? 168.051 201.077 214.238 1.00 107.44 ? 1594 ILE A CG2   1 
ATOM   490   C  CD1   . ILE A 1 1594 ? 169.813 198.710 214.872 1.00 105.48 ? 1594 ILE A CD1   1 
ATOM   491   N  N     . GLN A 1 1595 ? 167.950 203.294 211.547 1.00 112.19 ? 1595 GLN A N     1 
ATOM   492   C  CA    . GLN A 1 1595 ? 167.748 204.731 211.446 1.00 111.33 ? 1595 GLN A CA    1 
ATOM   493   C  C     . GLN A 1 1595 ? 167.601 205.356 212.832 1.00 110.30 ? 1595 GLN A C     1 
ATOM   494   O  O     . GLN A 1 1595 ? 167.237 204.695 213.809 1.00 108.31 ? 1595 GLN A O     1 
ATOM   495   C  CB    . GLN A 1 1595 ? 166.516 205.043 210.597 1.00 110.12 ? 1595 GLN A CB    1 
ATOM   496   C  CG    . GLN A 1 1595 ? 165.194 204.743 211.287 1.00 110.35 ? 1595 GLN A CG    1 
ATOM   497   C  CD    . GLN A 1 1595 ? 164.766 203.298 211.121 1.00 111.32 ? 1595 GLN A CD    1 
ATOM   498   O  OE1   . GLN A 1 1595 ? 165.176 202.622 210.177 1.00 109.57 ? 1595 GLN A OE1   1 
ATOM   499   N  NE2   . GLN A 1 1595 ? 163.936 202.817 212.040 1.00 109.55 ? 1595 GLN A NE2   1 
ATOM   500   N  N     . GLY A 1 1596 ? 167.891 206.654 212.905 1.00 100.36 ? 1596 GLY A N     1 
ATOM   501   C  CA    . GLY A 1 1596 ? 167.795 207.390 214.146 1.00 101.00 ? 1596 GLY A CA    1 
ATOM   502   C  C     . GLY A 1 1596 ? 168.983 207.254 215.071 1.00 103.06 ? 1596 GLY A C     1 
ATOM   503   O  O     . GLY A 1 1596 ? 168.947 207.799 216.181 1.00 101.35 ? 1596 GLY A O     1 
ATOM   504   N  N     . VAL A 1 1597 ? 170.033 206.546 214.656 1.00 108.39 ? 1597 VAL A N     1 
ATOM   505   C  CA    . VAL A 1 1597 ? 171.189 206.348 215.524 1.00 107.45 ? 1597 VAL A CA    1 
ATOM   506   C  C     . VAL A 1 1597 ? 172.158 207.518 215.411 1.00 105.43 ? 1597 VAL A C     1 
ATOM   507   O  O     . VAL A 1 1597 ? 172.668 208.016 216.419 1.00 101.01 ? 1597 VAL A O     1 
ATOM   508   C  CB    . VAL A 1 1597 ? 171.876 205.009 215.199 1.00 106.22 ? 1597 VAL A CB    1 
ATOM   509   C  CG1   . VAL A 1 1597 ? 173.116 204.826 216.060 1.00 104.37 ? 1597 VAL A CG1   1 
ATOM   510   C  CG2   . VAL A 1 1597 ? 170.907 203.854 215.399 1.00 104.17 ? 1597 VAL A CG2   1 
ATOM   511   N  N     . GLN A 1 1598 ? 172.427 207.977 214.186 1.00 112.94 ? 1598 GLN A N     1 
ATOM   512   C  CA    . GLN A 1 1598 ? 173.410 209.040 213.996 1.00 114.84 ? 1598 GLN A CA    1 
ATOM   513   C  C     . GLN A 1 1598 ? 172.883 210.388 214.480 1.00 115.09 ? 1598 GLN A C     1 
ATOM   514   O  O     . GLN A 1 1598 ? 173.624 211.165 215.096 1.00 113.06 ? 1598 GLN A O     1 
ATOM   515   C  CB    . GLN A 1 1598 ? 173.819 209.118 212.525 1.00 111.52 ? 1598 GLN A CB    1 
ATOM   516   C  CG    . GLN A 1 1598 ? 174.879 210.167 212.235 1.00 112.69 ? 1598 GLN A CG    1 
ATOM   517   C  CD    . GLN A 1 1598 ? 176.193 209.871 212.930 1.00 115.04 ? 1598 GLN A CD    1 
ATOM   518   O  OE1   . GLN A 1 1598 ? 176.558 210.536 213.899 1.00 114.60 ? 1598 GLN A OE1   1 
ATOM   519   N  NE2   . GLN A 1 1598 ? 176.910 208.868 212.439 1.00 112.04 ? 1598 GLN A NE2   1 
ATOM   520   N  N     . ARG A 1 1599 ? 171.613 210.691 214.199 1.00 114.83 ? 1599 ARG A N     1 
ATOM   521   C  CA    . ARG A 1 1599 ? 171.034 211.944 214.677 1.00 114.35 ? 1599 ARG A CA    1 
ATOM   522   C  C     . ARG A 1 1599 ? 170.997 211.983 216.199 1.00 113.79 ? 1599 ARG A C     1 
ATOM   523   O  O     . ARG A 1 1599 ? 171.344 213.000 216.814 1.00 110.43 ? 1599 ARG A O     1 
ATOM   524   C  CB    . ARG A 1 1599 ? 169.631 212.129 214.099 1.00 113.14 ? 1599 ARG A CB    1 
ATOM   525   C  CG    . ARG A 1 1599 ? 168.972 213.445 214.478 1.00 112.95 ? 1599 ARG A CG    1 
ATOM   526   C  CD    . ARG A 1 1599 ? 167.471 213.282 214.669 1.00 113.17 ? 1599 ARG A CD    1 
ATOM   527   N  NE    . ARG A 1 1599 ? 167.129 212.013 215.299 1.00 115.48 ? 1599 ARG A NE    1 
ATOM   528   C  CZ    . ARG A 1 1599 ? 167.164 211.792 216.606 1.00 114.25 ? 1599 ARG A CZ    1 
ATOM   529   N  NH1   . ARG A 1 1599 ? 167.528 212.737 217.457 1.00 112.86 ? 1599 ARG A NH1   1 
ATOM   530   N  NH2   . ARG A 1 1599 ? 166.825 210.593 217.070 1.00 112.89 ? 1599 ARG A NH2   1 
ATOM   531   N  N     . SER A 1 1600 ? 170.586 210.877 216.825 1.00 112.98 ? 1600 SER A N     1 
ATOM   532   C  CA    . SER A 1 1600 ? 170.602 210.802 218.281 1.00 114.12 ? 1600 SER A CA    1 
ATOM   533   C  C     . SER A 1 1600 ? 172.021 210.872 218.826 1.00 114.05 ? 1600 SER A C     1 
ATOM   534   O  O     . SER A 1 1600 ? 172.238 211.436 219.902 1.00 110.99 ? 1600 SER A O     1 
ATOM   535   C  CB    . SER A 1 1600 ? 169.914 209.521 218.752 1.00 112.77 ? 1600 SER A CB    1 
ATOM   536   O  OG    . SER A 1 1600 ? 170.520 208.376 218.178 1.00 111.80 ? 1600 SER A OG    1 
ATOM   537   N  N     . LEU A 1 1601 ? 172.996 210.314 218.104 1.00 115.84 ? 1601 LEU A N     1 
ATOM   538   C  CA    . LEU A 1 1601 ? 174.386 210.408 218.538 1.00 116.03 ? 1601 LEU A CA    1 
ATOM   539   C  C     . LEU A 1 1601 ? 174.874 211.851 218.520 1.00 114.79 ? 1601 LEU A C     1 
ATOM   540   O  O     . LEU A 1 1601 ? 175.558 212.294 219.449 1.00 113.91 ? 1601 LEU A O     1 
ATOM   541   C  CB    . LEU A 1 1601 ? 175.272 209.532 217.652 1.00 115.40 ? 1601 LEU A CB    1 
ATOM   542   C  CG    . LEU A 1 1601 ? 176.634 209.141 218.227 1.00 116.25 ? 1601 LEU A CG    1 
ATOM   543   C  CD1   . LEU A 1 1601 ? 176.463 208.385 219.536 1.00 113.98 ? 1601 LEU A CD1   1 
ATOM   544   C  CD2   . LEU A 1 1601 ? 177.425 208.314 217.225 1.00 113.73 ? 1601 LEU A CD2   1 
ATOM   545   N  N     . GLU A 1 1602 ? 174.534 212.600 217.469 1.00 116.97 ? 1602 GLU A N     1 
ATOM   546   C  CA    . GLU A 1 1602 ? 174.910 214.012 217.421 1.00 117.31 ? 1602 GLU A CA    1 
ATOM   547   C  C     . GLU A 1 1602 ? 174.211 214.809 218.517 1.00 117.84 ? 1602 GLU A C     1 
ATOM   548   O  O     . GLU A 1 1602 ? 174.823 215.684 219.146 1.00 116.51 ? 1602 GLU A O     1 
ATOM   549   C  CB    . GLU A 1 1602 ? 174.595 214.600 216.045 1.00 116.55 ? 1602 GLU A CB    1 
ATOM   550   C  CG    . GLU A 1 1602 ? 175.556 214.165 214.951 1.00 117.47 ? 1602 GLU A CG    1 
ATOM   551   C  CD    . GLU A 1 1602 ? 175.280 214.848 213.627 1.00 117.74 ? 1602 GLU A CD    1 
ATOM   552   O  OE1   . GLU A 1 1602 ? 174.222 215.501 213.503 1.00 117.12 ? 1602 GLU A OE1   1 
ATOM   553   O  OE2   . GLU A 1 1602 ? 176.121 214.735 212.711 1.00 116.74 ? 1602 GLU A OE2   1 
ATOM   554   N  N     . ARG A 1 1603 ? 172.928 214.525 218.757 1.00 118.05 ? 1603 ARG A N     1 
ATOM   555   C  CA    . ARG A 1 1603 ? 172.211 215.201 219.834 1.00 117.43 ? 1603 ARG A CA    1 
ATOM   556   C  C     . ARG A 1 1603 ? 172.842 214.898 221.189 1.00 117.42 ? 1603 ARG A C     1 
ATOM   557   O  O     . ARG A 1 1603 ? 172.988 215.793 222.031 1.00 115.11 ? 1603 ARG A O     1 
ATOM   558   C  CB    . ARG A 1 1603 ? 170.738 214.789 219.820 1.00 116.46 ? 1603 ARG A CB    1 
ATOM   559   C  CG    . ARG A 1 1603 ? 169.929 215.307 220.998 1.00 117.44 ? 1603 ARG A CG    1 
ATOM   560   C  CD    . ARG A 1 1603 ? 168.521 214.732 220.993 1.00 116.80 ? 1603 ARG A CD    1 
ATOM   561   N  NE    . ARG A 1 1603 ? 168.509 213.316 221.339 1.00 117.88 ? 1603 ARG A NE    1 
ATOM   562   C  CZ    . ARG A 1 1603 ? 167.527 212.478 221.036 1.00 117.12 ? 1603 ARG A CZ    1 
ATOM   563   N  NH1   . ARG A 1 1603 ? 166.458 212.878 220.369 1.00 116.64 ? 1603 ARG A NH1   1 
ATOM   564   N  NH2   . ARG A 1 1603 ? 167.622 211.205 221.411 1.00 116.17 ? 1603 ARG A NH2   1 
ATOM   565   N  N     . LEU A 1 1604 ? 173.228 213.640 221.411 1.00 113.81 ? 1604 LEU A N     1 
ATOM   566   C  CA    . LEU A 1 1604 ? 173.884 213.266 222.658 1.00 114.85 ? 1604 LEU A CA    1 
ATOM   567   C  C     . LEU A 1 1604 ? 175.245 213.934 222.789 1.00 113.77 ? 1604 LEU A C     1 
ATOM   568   O  O     . LEU A 1 1604 ? 175.643 214.328 223.887 1.00 110.15 ? 1604 LEU A O     1 
ATOM   569   C  CB    . LEU A 1 1604 ? 174.018 211.745 222.743 1.00 115.67 ? 1604 LEU A CB    1 
ATOM   570   C  CG    . LEU A 1 1604 ? 172.811 210.998 223.312 1.00 116.24 ? 1604 LEU A CG    1 
ATOM   571   C  CD1   . LEU A 1 1604 ? 172.989 209.494 223.173 1.00 112.40 ? 1604 LEU A CD1   1 
ATOM   572   C  CD2   . LEU A 1 1604 ? 172.583 211.382 224.765 1.00 113.73 ? 1604 LEU A CD2   1 
ATOM   573   N  N     . ALA A 1 1605 ? 175.980 214.059 221.682 1.00 113.29 ? 1605 ALA A N     1 
ATOM   574   C  CA    . ALA A 1 1605 ? 177.262 214.756 221.724 1.00 113.61 ? 1605 ALA A CA    1 
ATOM   575   C  C     . ALA A 1 1605 ? 177.079 216.217 222.110 1.00 112.20 ? 1605 ALA A C     1 
ATOM   576   O  O     . ALA A 1 1605 ? 177.824 216.747 222.945 1.00 110.37 ? 1605 ALA A O     1 
ATOM   577   C  CB    . ALA A 1 1605 ? 177.968 214.644 220.374 1.00 111.27 ? 1605 ALA A CB    1 
ATOM   578   N  N     . ASP A 1 1606 ? 176.087 216.883 221.514 1.00 112.45 ? 1606 ASP A N     1 
ATOM   579   C  CA    . ASP A 1 1606 ? 175.818 218.274 221.866 1.00 113.37 ? 1606 ASP A CA    1 
ATOM   580   C  C     . ASP A 1 1606 ? 175.406 218.405 223.328 1.00 114.87 ? 1606 ASP A C     1 
ATOM   581   O  O     . ASP A 1 1606 ? 175.872 219.310 224.032 1.00 111.28 ? 1606 ASP A O     1 
ATOM   582   C  CB    . ASP A 1 1606 ? 174.739 218.849 220.949 1.00 113.47 ? 1606 ASP A CB    1 
ATOM   583   C  CG    . ASP A 1 1606 ? 175.233 219.063 219.531 1.00 114.67 ? 1606 ASP A CG    1 
ATOM   584   O  OD1   . ASP A 1 1606 ? 176.440 219.327 219.354 1.00 114.12 ? 1606 ASP A OD1   1 
ATOM   585   O  OD2   . ASP A 1 1606 ? 174.413 218.968 218.593 1.00 112.97 ? 1606 ASP A OD2   1 
ATOM   586   N  N     . LEU A 1 1607 ? 174.544 217.502 223.805 1.00 115.63 ? 1607 LEU A N     1 
ATOM   587   C  CA    . LEU A 1 1607 ? 174.115 217.552 225.199 1.00 114.78 ? 1607 LEU A CA    1 
ATOM   588   C  C     . LEU A 1 1607 ? 175.280 217.305 226.150 1.00 115.03 ? 1607 LEU A C     1 
ATOM   589   O  O     . LEU A 1 1607 ? 175.394 217.971 227.186 1.00 111.98 ? 1607 LEU A O     1 
ATOM   590   C  CB    . LEU A 1 1607 ? 173.000 216.535 225.442 1.00 114.38 ? 1607 LEU A CB    1 
ATOM   591   C  CG    . LEU A 1 1607 ? 171.611 216.928 224.935 1.00 115.31 ? 1607 LEU A CG    1 
ATOM   592   C  CD1   . LEU A 1 1607 ? 170.589 215.850 225.266 1.00 112.65 ? 1607 LEU A CD1   1 
ATOM   593   C  CD2   . LEU A 1 1607 ? 171.189 218.271 225.511 1.00 112.50 ? 1607 LEU A CD2   1 
ATOM   594   N  N     . LEU A 1 1608 ? 176.150 216.346 225.820 1.00 113.92 ? 1608 LEU A N     1 
ATOM   595   C  CA    . LEU A 1 1608 ? 177.304 216.057 226.663 1.00 114.05 ? 1608 LEU A CA    1 
ATOM   596   C  C     . LEU A 1 1608 ? 178.263 217.238 226.707 1.00 115.13 ? 1608 LEU A C     1 
ATOM   597   O  O     . LEU A 1 1608 ? 178.774 217.592 227.775 1.00 113.55 ? 1608 LEU A O     1 
ATOM   598   C  CB    . LEU A 1 1608 ? 178.017 214.800 226.162 1.00 113.81 ? 1608 LEU A CB    1 
ATOM   599   C  CG    . LEU A 1 1608 ? 177.673 213.469 226.838 1.00 114.59 ? 1608 LEU A CG    1 
ATOM   600   C  CD1   . LEU A 1 1608 ? 178.197 213.442 228.262 1.00 112.93 ? 1608 LEU A CD1   1 
ATOM   601   C  CD2   . LEU A 1 1608 ? 176.176 213.201 226.817 1.00 112.12 ? 1608 LEU A CD2   1 
ATOM   602   N  N     . GLY A 1 1609 ? 178.516 217.865 225.557 1.00 110.24 ? 1609 GLY A N     1 
ATOM   603   C  CA    . GLY A 1 1609 ? 179.347 219.057 225.554 1.00 108.88 ? 1609 GLY A CA    1 
ATOM   604   C  C     . GLY A 1 1609 ? 178.746 220.181 226.377 1.00 109.83 ? 1609 GLY A C     1 
ATOM   605   O  O     . GLY A 1 1609 ? 179.452 220.858 227.131 1.00 107.94 ? 1609 GLY A O     1 
ATOM   606   N  N     . LYS A 1 1610 ? 177.431 220.384 226.258 1.00 107.87 ? 1610 LYS A N     1 
ATOM   607   C  CA    . LYS A 1 1610 ? 176.779 221.451 227.010 1.00 108.10 ? 1610 LYS A CA    1 
ATOM   608   C  C     . LYS A 1 1610 ? 176.832 221.189 228.511 1.00 108.42 ? 1610 LYS A C     1 
ATOM   609   O  O     . LYS A 1 1610 ? 177.095 222.108 229.294 1.00 105.57 ? 1610 LYS A O     1 
ATOM   610   C  CB    . LYS A 1 1610 ? 175.336 221.619 226.533 1.00 108.23 ? 1610 LYS A CB    1 
ATOM   611   C  CG    . LYS A 1 1610 ? 174.603 222.802 227.150 1.00 107.92 ? 1610 LYS A CG    1 
ATOM   612   C  CD    . LYS A 1 1610 ? 173.665 222.363 228.259 1.00 108.56 ? 1610 LYS A CD    1 
ATOM   613   C  CE    . LYS A 1 1610 ? 172.504 221.559 227.701 1.00 107.79 ? 1610 LYS A CE    1 
ATOM   614   N  NZ    . LYS A 1 1610 ? 171.585 221.102 228.774 1.00 106.16 ? 1610 LYS A NZ    1 
ATOM   615   N  N     . ILE A 1 1611 ? 176.590 219.946 228.936 1.00 107.10 ? 1611 ILE A N     1 
ATOM   616   C  CA    . ILE A 1 1611 ? 176.615 219.651 230.367 1.00 107.22 ? 1611 ILE A CA    1 
ATOM   617   C  C     . ILE A 1 1611 ? 178.042 219.713 230.905 1.00 108.34 ? 1611 ILE A C     1 
ATOM   618   O  O     . ILE A 1 1611 ? 178.266 220.125 232.048 1.00 107.42 ? 1611 ILE A O     1 
ATOM   619   C  CB    . ILE A 1 1611 ? 175.941 218.297 230.668 1.00 109.51 ? 1611 ILE A CB    1 
ATOM   620   C  CG1   . ILE A 1 1611 ? 175.897 218.044 232.177 1.00 109.37 ? 1611 ILE A CG1   1 
ATOM   621   C  CG2   . ILE A 1 1611 ? 176.657 217.158 229.985 1.00 106.18 ? 1611 ILE A CG2   1 
ATOM   622   C  CD1   . ILE A 1 1611 ? 175.047 216.860 232.573 1.00 108.30 ? 1611 ILE A CD1   1 
ATOM   623   N  N     . GLN A 1 1612 ? 179.031 219.315 230.098 1.00 109.53 ? 1612 GLN A N     1 
ATOM   624   C  CA    . GLN A 1 1612 ? 180.421 219.472 230.517 1.00 109.89 ? 1612 GLN A CA    1 
ATOM   625   C  C     . GLN A 1 1612 ? 180.779 220.943 230.691 1.00 109.86 ? 1612 GLN A C     1 
ATOM   626   O  O     . GLN A 1 1612 ? 181.446 221.319 231.664 1.00 107.18 ? 1612 GLN A O     1 
ATOM   627   C  CB    . GLN A 1 1612 ? 181.357 218.811 229.508 1.00 107.25 ? 1612 GLN A CB    1 
ATOM   628   C  CG    . GLN A 1 1612 ? 182.829 218.949 229.861 1.00 107.94 ? 1612 GLN A CG    1 
ATOM   629   C  CD    . GLN A 1 1612 ? 183.738 218.247 228.875 1.00 110.67 ? 1612 GLN A CD    1 
ATOM   630   O  OE1   . GLN A 1 1612 ? 184.528 217.381 229.250 1.00 110.44 ? 1612 GLN A OE1   1 
ATOM   631   N  NE2   . GLN A 1 1612 ? 183.633 218.618 227.604 1.00 108.16 ? 1612 GLN A NE2   1 
ATOM   632   N  N     . LYS A 1 1613 ? 180.344 221.791 229.755 1.00 103.23 ? 1613 LYS A N     1 
ATOM   633   C  CA    . LYS A 1 1613 ? 180.585 223.224 229.891 1.00 103.40 ? 1613 LYS A CA    1 
ATOM   634   C  C     . LYS A 1 1613 ? 179.885 223.782 231.124 1.00 104.03 ? 1613 LYS A C     1 
ATOM   635   O  O     . LYS A 1 1613 ? 180.442 224.627 231.833 1.00 102.82 ? 1613 LYS A O     1 
ATOM   636   C  CB    . LYS A 1 1613 ? 180.126 223.957 228.631 1.00 102.97 ? 1613 LYS A CB    1 
ATOM   637   C  CG    . LYS A 1 1613 ? 180.020 225.465 228.795 1.00 104.35 ? 1613 LYS A CG    1 
ATOM   638   C  CD    . LYS A 1 1613 ? 180.515 226.197 227.561 1.00 103.12 ? 1613 LYS A CD    1 
ATOM   639   C  CE    . LYS A 1 1613 ? 180.875 227.637 227.887 1.00 101.69 ? 1613 LYS A CE    1 
ATOM   640   N  NZ    . LYS A 1 1613 ? 180.874 228.500 226.674 1.00 101.36 ? 1613 LYS A NZ    1 
ATOM   641   N  N     . ALA A 1 1614 ? 178.661 223.324 231.392 1.00 101.90 ? 1614 ALA A N     1 
ATOM   642   C  CA    . ALA A 1 1614 ? 177.943 223.775 232.580 1.00 101.55 ? 1614 ALA A CA    1 
ATOM   643   C  C     . ALA A 1 1614 ? 178.670 223.363 233.853 1.00 100.37 ? 1614 ALA A C     1 
ATOM   644   O  O     . ALA A 1 1614 ? 178.771 224.150 234.800 1.00 99.78  ? 1614 ALA A O     1 
ATOM   645   C  CB    . ALA A 1 1614 ? 176.517 223.224 232.574 1.00 99.97  ? 1614 ALA A CB    1 
ATOM   646   N  N     . LEU A 1 1615 ? 179.184 222.132 233.893 1.00 100.25 ? 1615 LEU A N     1 
ATOM   647   C  CA    . LEU A 1 1615 ? 179.933 221.675 235.059 1.00 101.54 ? 1615 LEU A CA    1 
ATOM   648   C  C     . LEU A 1 1615 ? 181.211 222.485 235.243 1.00 103.58 ? 1615 LEU A C     1 
ATOM   649   O  O     . LEU A 1 1615 ? 181.571 222.842 236.370 1.00 100.41 ? 1615 LEU A O     1 
ATOM   650   C  CB    . LEU A 1 1615 ? 180.246 220.183 234.925 1.00 100.86 ? 1615 LEU A CB    1 
ATOM   651   C  CG    . LEU A 1 1615 ? 180.803 219.440 236.144 1.00 101.90 ? 1615 LEU A CG    1 
ATOM   652   C  CD1   . LEU A 1 1615 ? 180.254 218.023 236.192 1.00 99.99  ? 1615 LEU A CD1   1 
ATOM   653   C  CD2   . LEU A 1 1615 ? 182.324 219.411 236.122 1.00 98.93  ? 1615 LEU A CD2   1 
ATOM   654   N  N     . GLY A 1 1616 ? 181.908 222.787 234.146 1.00 100.05 ? 1616 GLY A N     1 
ATOM   655   C  CA    . GLY A 1 1616 ? 183.106 223.607 234.249 1.00 96.42  ? 1616 GLY A CA    1 
ATOM   656   C  C     . GLY A 1 1616 ? 182.815 225.017 234.730 1.00 98.17  ? 1616 GLY A C     1 
ATOM   657   O  O     . GLY A 1 1616 ? 183.540 225.560 235.570 1.00 96.82  ? 1616 GLY A O     1 
ATOM   658   N  N     . GLU A 1 1617 ? 181.751 225.630 234.204 1.00 104.47 ? 1617 GLU A N     1 
ATOM   659   C  CA    . GLU A 1 1617 ? 181.369 226.966 234.650 1.00 105.02 ? 1617 GLU A CA    1 
ATOM   660   C  C     . GLU A 1 1617 ? 180.947 226.957 236.112 1.00 103.43 ? 1617 GLU A C     1 
ATOM   661   O  O     . GLU A 1 1617 ? 181.259 227.893 236.859 1.00 103.45 ? 1617 GLU A O     1 
ATOM   662   C  CB    . GLU A 1 1617 ? 180.251 227.519 233.767 1.00 102.94 ? 1617 GLU A CB    1 
ATOM   663   C  CG    . GLU A 1 1617 ? 180.670 227.764 232.328 1.00 103.41 ? 1617 GLU A CG    1 
ATOM   664   C  CD    . GLU A 1 1617 ? 182.102 228.250 232.216 1.00 105.57 ? 1617 GLU A CD    1 
ATOM   665   O  OE1   . GLU A 1 1617 ? 182.371 229.406 232.605 1.00 102.88 ? 1617 GLU A OE1   1 
ATOM   666   O  OE2   . GLU A 1 1617 ? 182.961 227.476 231.743 1.00 105.94 ? 1617 GLU A OE2   1 
ATOM   667   N  N     . TYR A 1 1618 ? 180.242 225.909 236.542 1.00 103.47 ? 1618 TYR A N     1 
ATOM   668   C  CA    . TYR A 1 1618 ? 179.908 225.783 237.955 1.00 106.46 ? 1618 TYR A CA    1 
ATOM   669   C  C     . TYR A 1 1618 ? 181.156 225.648 238.815 1.00 106.10 ? 1618 TYR A C     1 
ATOM   670   O  O     . TYR A 1 1618 ? 181.231 226.230 239.902 1.00 102.43 ? 1618 TYR A O     1 
ATOM   671   C  CB    . TYR A 1 1618 ? 178.983 224.592 238.192 1.00 105.44 ? 1618 TYR A CB    1 
ATOM   672   C  CG    . TYR A 1 1618 ? 178.645 224.459 239.653 1.00 105.85 ? 1618 TYR A CG    1 
ATOM   673   C  CD1   . TYR A 1 1618 ? 177.716 225.298 240.248 1.00 105.48 ? 1618 TYR A CD1   1 
ATOM   674   C  CD2   . TYR A 1 1618 ? 179.292 223.524 240.449 1.00 104.56 ? 1618 TYR A CD2   1 
ATOM   675   C  CE1   . TYR A 1 1618 ? 177.424 225.195 241.585 1.00 106.17 ? 1618 TYR A CE1   1 
ATOM   676   C  CE2   . TYR A 1 1618 ? 179.007 223.413 241.787 1.00 105.04 ? 1618 TYR A CE2   1 
ATOM   677   C  CZ    . TYR A 1 1618 ? 178.072 224.252 242.348 1.00 106.39 ? 1618 TYR A CZ    1 
ATOM   678   O  OH    . TYR A 1 1618 ? 177.783 224.148 243.681 1.00 104.64 ? 1618 TYR A OH    1 
ATOM   679   N  N     . LEU A 1 1619 ? 182.132 224.859 238.364 1.00 104.39 ? 1619 LEU A N     1 
ATOM   680   C  CA    . LEU A 1 1619 ? 183.364 224.715 239.131 1.00 104.66 ? 1619 LEU A CA    1 
ATOM   681   C  C     . LEU A 1 1619 ? 184.089 226.048 239.247 1.00 103.37 ? 1619 LEU A C     1 
ATOM   682   O  O     . LEU A 1 1619 ? 184.584 226.404 240.323 1.00 102.02 ? 1619 LEU A O     1 
ATOM   683   C  CB    . LEU A 1 1619 ? 184.265 223.661 238.489 1.00 104.22 ? 1619 LEU A CB    1 
ATOM   684   C  CG    . LEU A 1 1619 ? 183.897 222.205 238.781 1.00 103.95 ? 1619 LEU A CG    1 
ATOM   685   C  CD1   . LEU A 1 1619 ? 184.857 221.256 238.084 1.00 102.92 ? 1619 LEU A CD1   1 
ATOM   686   C  CD2   . LEU A 1 1619 ? 183.875 221.946 240.277 1.00 103.42 ? 1619 LEU A CD2   1 
ATOM   687   N  N     . GLU A 1 1620 ? 184.141 226.811 238.153 1.00 101.94 ? 1620 GLU A N     1 
ATOM   688   C  CA    . GLU A 1 1620 ? 184.768 228.129 238.203 1.00 102.78 ? 1620 GLU A CA    1 
ATOM   689   C  C     . GLU A 1 1620 ? 184.025 229.063 239.153 1.00 102.51 ? 1620 GLU A C     1 
ATOM   690   O  O     . GLU A 1 1620 ? 184.649 229.786 239.940 1.00 100.66 ? 1620 GLU A O     1 
ATOM   691   C  CB    . GLU A 1 1620 ? 184.832 228.732 236.801 1.00 102.70 ? 1620 GLU A CB    1 
ATOM   692   C  CG    . GLU A 1 1620 ? 185.561 230.063 236.733 1.00 103.63 ? 1620 GLU A CG    1 
ATOM   693   C  CD    . GLU A 1 1620 ? 185.613 230.625 235.327 1.00 104.18 ? 1620 GLU A CD    1 
ATOM   694   O  OE1   . GLU A 1 1620 ? 185.050 229.988 234.411 1.00 102.61 ? 1620 GLU A OE1   1 
ATOM   695   O  OE2   . GLU A 1 1620 ? 186.215 231.703 235.137 1.00 103.31 ? 1620 GLU A OE2   1 
ATOM   696   N  N     . ARG A 1 1621 ? 182.690 229.062 239.096 1.00 105.56 ? 1621 ARG A N     1 
ATOM   697   C  CA    . ARG A 1 1621 ? 181.909 229.932 239.971 1.00 106.33 ? 1621 ARG A CA    1 
ATOM   698   C  C     . ARG A 1 1621 ? 182.091 229.552 241.435 1.00 105.44 ? 1621 ARG A C     1 
ATOM   699   O  O     . ARG A 1 1621 ? 182.205 230.426 242.302 1.00 102.24 ? 1621 ARG A O     1 
ATOM   700   C  CB    . ARG A 1 1621 ? 180.432 229.878 239.582 1.00 105.57 ? 1621 ARG A CB    1 
ATOM   701   C  CG    . ARG A 1 1621 ? 180.073 230.754 238.394 1.00 105.95 ? 1621 ARG A CG    1 
ATOM   702   C  CD    . ARG A 1 1621 ? 178.568 230.941 238.272 1.00 106.82 ? 1621 ARG A CD    1 
ATOM   703   N  NE    . ARG A 1 1621 ? 177.827 229.741 238.643 1.00 108.26 ? 1621 ARG A NE    1 
ATOM   704   C  CZ    . ARG A 1 1621 ? 177.671 228.682 237.859 1.00 107.46 ? 1621 ARG A CZ    1 
ATOM   705   N  NH1   . ARG A 1 1621 ? 178.204 228.632 236.649 1.00 106.06 ? 1621 ARG A NH1   1 
ATOM   706   N  NH2   . ARG A 1 1621 ? 176.961 227.648 238.300 1.00 104.85 ? 1621 ARG A NH2   1 
ATOM   707   N  N     . GLU A 1 1622 ? 182.115 228.251 241.729 1.00 104.66 ? 1622 GLU A N     1 
ATOM   708   C  CA    . GLU A 1 1622 ? 182.329 227.800 243.098 1.00 104.11 ? 1622 GLU A CA    1 
ATOM   709   C  C     . GLU A 1 1622 ? 183.753 228.072 243.561 1.00 105.08 ? 1622 GLU A C     1 
ATOM   710   O  O     . GLU A 1 1622 ? 183.998 228.191 244.766 1.00 105.07 ? 1622 GLU A O     1 
ATOM   711   C  CB    . GLU A 1 1622 ? 182.005 226.312 243.214 1.00 101.52 ? 1622 GLU A CB    1 
ATOM   712   C  CG    . GLU A 1 1622 ? 181.749 225.837 244.632 1.00 103.38 ? 1622 GLU A CG    1 
ATOM   713   C  CD    . GLU A 1 1622 ? 181.666 224.331 244.723 1.00 105.58 ? 1622 GLU A CD    1 
ATOM   714   O  OE1   . GLU A 1 1622 ? 181.604 223.682 243.660 1.00 104.43 ? 1622 GLU A OE1   1 
ATOM   715   O  OE2   . GLU A 1 1622 ? 181.664 223.796 245.851 1.00 106.49 ? 1622 GLU A OE2   1 
ATOM   716   N  N     . ARG A 1 1623 ? 184.703 228.156 242.628 1.00 100.38 ? 1623 ARG A N     1 
ATOM   717   C  CA    . ARG A 1 1623 ? 186.053 228.570 242.983 1.00 96.17  ? 1623 ARG A CA    1 
ATOM   718   C  C     . ARG A 1 1623 ? 186.148 230.071 243.215 1.00 95.72  ? 1623 ARG A C     1 
ATOM   719   O  O     . ARG A 1 1623 ? 187.025 230.514 243.964 1.00 96.55  ? 1623 ARG A O     1 
ATOM   720   C  CB    . ARG A 1 1623 ? 187.038 228.149 241.893 1.00 93.22  ? 1623 ARG A CB    1 
ATOM   721   C  CG    . ARG A 1 1623 ? 187.343 226.664 241.881 1.00 93.80  ? 1623 ARG A CG    1 
ATOM   722   C  CD    . ARG A 1 1623 ? 188.833 226.407 241.904 1.00 93.11  ? 1623 ARG A CD    1 
ATOM   723   N  NE    . ARG A 1 1623 ? 189.142 224.983 241.931 1.00 96.82  ? 1623 ARG A NE    1 
ATOM   724   C  CZ    . ARG A 1 1623 ? 189.282 224.227 240.851 1.00 97.62  ? 1623 ARG A CZ    1 
ATOM   725   N  NH1   . ARG A 1 1623 ? 189.150 224.730 239.635 1.00 95.69  ? 1623 ARG A NH1   1 
ATOM   726   N  NH2   . ARG A 1 1623 ? 189.562 222.935 240.995 1.00 95.21  ? 1623 ARG A NH2   1 
ATOM   727   N  N     . SER A 1 1624 ? 185.273 230.860 242.584 1.00 96.71  ? 1624 SER A N     1 
ATOM   728   C  CA    . SER A 1 1624 ? 185.271 232.300 242.828 1.00 95.31  ? 1624 SER A CA    1 
ATOM   729   C  C     . SER A 1 1624 ? 184.970 232.609 244.289 1.00 94.07  ? 1624 SER A C     1 
ATOM   730   O  O     . SER A 1 1624 ? 185.625 233.462 244.899 1.00 92.62  ? 1624 SER A O     1 
ATOM   731   C  CB    . SER A 1 1624 ? 184.260 232.989 241.912 1.00 92.50  ? 1624 SER A CB    1 
ATOM   732   O  OG    . SER A 1 1624 ? 184.697 232.972 240.565 1.00 91.75  ? 1624 SER A OG    1 
ATOM   733   N  N     . SER A 1 1625 ? 183.983 231.928 244.866 1.00 89.27  ? 1625 SER A N     1 
ATOM   734   C  CA    . SER A 1 1625 ? 183.747 232.006 246.299 1.00 88.45  ? 1625 SER A CA    1 
ATOM   735   C  C     . SER A 1 1625 ? 184.699 231.065 247.023 1.00 89.76  ? 1625 SER A C     1 
ATOM   736   O  O     . SER A 1 1625 ? 184.927 229.936 246.581 1.00 86.99  ? 1625 SER A O     1 
ATOM   737   C  CB    . SER A 1 1625 ? 182.298 231.645 246.627 1.00 87.73  ? 1625 SER A CB    1 
ATOM   738   O  OG    . SER A 1 1625 ? 182.112 231.499 248.024 1.00 89.42  ? 1625 SER A OG    1 
ATOM   739   N  N     . PHE A 1 1626 ? 185.250 231.534 248.145 1.00 82.37  ? 1626 PHE A N     1 
ATOM   740   C  CA    . PHE A 1 1626 ? 186.284 230.798 248.866 1.00 82.20  ? 1626 PHE A CA    1 
ATOM   741   C  C     . PHE A 1 1626 ? 187.413 230.436 247.908 1.00 82.11  ? 1626 PHE A C     1 
ATOM   742   O  O     . PHE A 1 1626 ? 187.537 229.274 247.502 1.00 79.33  ? 1626 PHE A O     1 
ATOM   743   C  CB    . PHE A 1 1626 ? 185.713 229.542 249.525 1.00 80.25  ? 1626 PHE A CB    1 
ATOM   744   C  CG    . PHE A 1 1626 ? 186.652 228.892 250.495 1.00 80.03  ? 1626 PHE A CG    1 
ATOM   745   C  CD1   . PHE A 1 1626 ? 187.009 229.533 251.667 1.00 78.09  ? 1626 PHE A CD1   1 
ATOM   746   C  CD2   . PHE A 1 1626 ? 187.183 227.642 250.233 1.00 78.45  ? 1626 PHE A CD2   1 
ATOM   747   C  CE1   . PHE A 1 1626 ? 187.873 228.940 252.560 1.00 78.95  ? 1626 PHE A CE1   1 
ATOM   748   C  CE2   . PHE A 1 1626 ? 188.047 227.044 251.122 1.00 77.89  ? 1626 PHE A CE2   1 
ATOM   749   C  CZ    . PHE A 1 1626 ? 188.394 227.694 252.287 1.00 80.63  ? 1626 PHE A CZ    1 
ATOM   750   N  N     . PRO A 1 1627 ? 188.245 231.405 247.517 1.00 76.27  ? 1627 PRO A N     1 
ATOM   751   C  CA    . PRO A 1 1627 ? 189.226 231.165 246.448 1.00 76.15  ? 1627 PRO A CA    1 
ATOM   752   C  C     . PRO A 1 1627 ? 190.270 230.110 246.779 1.00 76.34  ? 1627 PRO A C     1 
ATOM   753   O  O     . PRO A 1 1627 ? 191.077 229.749 245.916 1.00 77.89  ? 1627 PRO A O     1 
ATOM   754   C  CB    . PRO A 1 1627 ? 189.877 232.543 246.258 1.00 74.94  ? 1627 PRO A CB    1 
ATOM   755   C  CG    . PRO A 1 1627 ? 188.927 233.517 246.880 1.00 76.30  ? 1627 PRO A CG    1 
ATOM   756   C  CD    . PRO A 1 1627 ? 188.309 232.785 248.021 1.00 76.28  ? 1627 PRO A CD    1 
ATOM   757   N  N     . ARG A 1 1628 ? 190.262 229.598 248.013 1.00 72.03  ? 1628 ARG A N     1 
ATOM   758   C  CA    . ARG A 1 1628 ? 191.227 228.575 248.400 1.00 72.74  ? 1628 ARG A CA    1 
ATOM   759   C  C     . ARG A 1 1628 ? 191.071 227.294 247.592 1.00 73.32  ? 1628 ARG A C     1 
ATOM   760   O  O     . ARG A 1 1628 ? 191.989 226.468 247.579 1.00 75.12  ? 1628 ARG A O     1 
ATOM   761   C  CB    . ARG A 1 1628 ? 191.096 228.262 249.891 1.00 76.64  ? 1628 ARG A CB    1 
ATOM   762   C  CG    . ARG A 1 1628 ? 191.249 229.464 250.801 1.00 72.60  ? 1628 ARG A CG    1 
ATOM   763   C  CD    . ARG A 1 1628 ? 192.683 229.611 251.273 1.00 71.55  ? 1628 ARG A CD    1 
ATOM   764   N  NE    . ARG A 1 1628 ? 192.805 230.575 252.359 1.00 73.36  ? 1628 ARG A NE    1 
ATOM   765   C  CZ    . ARG A 1 1628 ? 193.731 230.521 253.306 1.00 73.85  ? 1628 ARG A CZ    1 
ATOM   766   N  NH1   . ARG A 1 1628 ? 194.640 229.561 253.329 1.00 73.39  ? 1628 ARG A NH1   1 
ATOM   767   N  NH2   . ARG A 1 1628 ? 193.748 231.456 254.251 1.00 70.57  ? 1628 ARG A NH2   1 
ATOM   768   N  N     . PHE A 1 1629 ? 189.932 227.108 246.921 1.00 83.88  ? 1629 PHE A N     1 
ATOM   769   C  CA    . PHE A 1 1629 ? 189.730 225.943 246.069 1.00 86.77  ? 1629 PHE A CA    1 
ATOM   770   C  C     . PHE A 1 1629 ? 190.621 225.952 244.834 1.00 87.46  ? 1629 PHE A C     1 
ATOM   771   O  O     . PHE A 1 1629 ? 190.699 224.934 244.141 1.00 87.92  ? 1629 PHE A O     1 
ATOM   772   C  CB    . PHE A 1 1629 ? 188.265 225.851 245.643 1.00 87.09  ? 1629 PHE A CB    1 
ATOM   773   C  CG    . PHE A 1 1629 ? 187.384 225.169 246.647 1.00 88.57  ? 1629 PHE A CG    1 
ATOM   774   C  CD1   . PHE A 1 1629 ? 187.866 224.120 247.413 1.00 87.81  ? 1629 PHE A CD1   1 
ATOM   775   C  CD2   . PHE A 1 1629 ? 186.071 225.572 246.823 1.00 88.18  ? 1629 PHE A CD2   1 
ATOM   776   C  CE1   . PHE A 1 1629 ? 187.055 223.489 248.336 1.00 85.26  ? 1629 PHE A CE1   1 
ATOM   777   C  CE2   . PHE A 1 1629 ? 185.256 224.945 247.744 1.00 88.03  ? 1629 PHE A CE2   1 
ATOM   778   C  CZ    . PHE A 1 1629 ? 185.749 223.903 248.501 1.00 86.55  ? 1629 PHE A CZ    1 
ATOM   779   N  N     . TYR A 1 1630 ? 191.280 227.071 244.534 1.00 79.95  ? 1630 TYR A N     1 
ATOM   780   C  CA    . TYR A 1 1630 ? 192.219 227.121 243.422 1.00 79.12  ? 1630 TYR A CA    1 
ATOM   781   C  C     . TYR A 1 1630 ? 193.485 226.318 243.684 1.00 78.81  ? 1630 TYR A C     1 
ATOM   782   O  O     . TYR A 1 1630 ? 194.272 226.115 242.754 1.00 78.77  ? 1630 TYR A O     1 
ATOM   783   C  CB    . TYR A 1 1630 ? 192.571 228.575 243.111 1.00 75.47  ? 1630 TYR A CB    1 
ATOM   784   C  CG    . TYR A 1 1630 ? 191.548 229.258 242.237 1.00 79.03  ? 1630 TYR A CG    1 
ATOM   785   C  CD1   . TYR A 1 1630 ? 190.946 230.441 242.635 1.00 78.21  ? 1630 TYR A CD1   1 
ATOM   786   C  CD2   . TYR A 1 1630 ? 191.204 228.733 241.000 1.00 78.18  ? 1630 TYR A CD2   1 
ATOM   787   C  CE1   . TYR A 1 1630 ? 190.009 231.066 241.839 1.00 80.77  ? 1630 TYR A CE1   1 
ATOM   788   C  CE2   . TYR A 1 1630 ? 190.271 229.355 240.195 1.00 80.03  ? 1630 TYR A CE2   1 
ATOM   789   C  CZ    . TYR A 1 1630 ? 189.679 230.523 240.619 1.00 85.48  ? 1630 TYR A CZ    1 
ATOM   790   O  OH    . TYR A 1 1630 ? 188.749 231.151 239.822 1.00 84.83  ? 1630 TYR A OH    1 
ATOM   791   N  N     . PHE A 1 1631 ? 193.702 225.863 244.916 1.00 71.97  ? 1631 PHE A N     1 
ATOM   792   C  CA    . PHE A 1 1631 ? 194.871 225.069 245.264 1.00 70.03  ? 1631 PHE A CA    1 
ATOM   793   C  C     . PHE A 1 1631 ? 194.596 223.571 245.270 1.00 74.32  ? 1631 PHE A C     1 
ATOM   794   O  O     . PHE A 1 1631 ? 195.494 222.794 245.608 1.00 73.64  ? 1631 PHE A O     1 
ATOM   795   C  CB    . PHE A 1 1631 ? 195.414 225.502 246.629 1.00 70.52  ? 1631 PHE A CB    1 
ATOM   796   C  CG    . PHE A 1 1631 ? 195.944 226.907 246.652 1.00 70.12  ? 1631 PHE A CG    1 
ATOM   797   C  CD1   . PHE A 1 1631 ? 196.423 227.499 245.495 1.00 68.39  ? 1631 PHE A CD1   1 
ATOM   798   C  CD2   . PHE A 1 1631 ? 195.969 227.635 247.828 1.00 70.02  ? 1631 PHE A CD2   1 
ATOM   799   C  CE1   . PHE A 1 1631 ? 196.910 228.788 245.511 1.00 68.22  ? 1631 PHE A CE1   1 
ATOM   800   C  CE2   . PHE A 1 1631 ? 196.458 228.925 247.848 1.00 70.21  ? 1631 PHE A CE2   1 
ATOM   801   C  CZ    . PHE A 1 1631 ? 196.929 229.501 246.688 1.00 70.20  ? 1631 PHE A CZ    1 
ATOM   802   N  N     . VAL A 1 1632 ? 193.389 223.146 244.905 1.00 86.54  ? 1632 VAL A N     1 
ATOM   803   C  CA    . VAL A 1 1632 ? 193.056 221.730 244.811 1.00 86.82  ? 1632 VAL A CA    1 
ATOM   804   C  C     . VAL A 1 1632 ? 192.659 221.421 243.376 1.00 87.13  ? 1632 VAL A C     1 
ATOM   805   O  O     . VAL A 1 1632 ? 192.215 222.299 242.629 1.00 85.09  ? 1632 VAL A O     1 
ATOM   806   C  CB    . VAL A 1 1632 ? 191.930 221.320 245.787 1.00 85.80  ? 1632 VAL A CB    1 
ATOM   807   C  CG1   . VAL A 1 1632 ? 192.426 221.351 247.217 1.00 84.30  ? 1632 VAL A CG1   1 
ATOM   808   C  CG2   . VAL A 1 1632 ? 190.721 222.217 245.620 1.00 85.12  ? 1632 VAL A CG2   1 
ATOM   809   N  N     . GLY A 1 1633 ? 192.820 220.159 242.993 1.00 92.08  ? 1633 GLY A N     1 
ATOM   810   C  CA    . GLY A 1 1633 ? 192.504 219.744 241.644 1.00 92.54  ? 1633 GLY A CA    1 
ATOM   811   C  C     . GLY A 1 1633 ? 191.012 219.728 241.376 1.00 94.88  ? 1633 GLY A C     1 
ATOM   812   O  O     . GLY A 1 1633 ? 190.177 219.803 242.278 1.00 96.30  ? 1633 GLY A O     1 
ATOM   813   N  N     . ASP A 1 1634 ? 190.676 219.635 240.087 1.00 98.78  ? 1634 ASP A N     1 
ATOM   814   C  CA    . ASP A 1 1634 ? 189.272 219.600 239.690 1.00 98.85  ? 1634 ASP A CA    1 
ATOM   815   C  C     . ASP A 1 1634 ? 188.574 218.366 240.244 1.00 98.32  ? 1634 ASP A C     1 
ATOM   816   O  O     . ASP A 1 1634 ? 187.461 218.458 240.777 1.00 98.74  ? 1634 ASP A O     1 
ATOM   817   C  CB    . ASP A 1 1634 ? 189.159 219.645 238.166 1.00 97.41  ? 1634 ASP A CB    1 
ATOM   818   C  CG    . ASP A 1 1634 ? 189.771 220.900 237.574 1.00 97.69  ? 1634 ASP A CG    1 
ATOM   819   O  OD1   . ASP A 1 1634 ? 190.218 221.768 238.352 1.00 95.78  ? 1634 ASP A OD1   1 
ATOM   820   O  OD2   . ASP A 1 1634 ? 189.803 221.018 236.331 1.00 96.18  ? 1634 ASP A OD2   1 
ATOM   821   N  N     . GLU A 1 1635 ? 189.216 217.200 240.140 1.00 98.91  ? 1635 GLU A N     1 
ATOM   822   C  CA    . GLU A 1 1635 ? 188.643 215.996 240.728 1.00 98.86  ? 1635 GLU A CA    1 
ATOM   823   C  C     . GLU A 1 1635 ? 188.646 216.065 242.250 1.00 97.44  ? 1635 GLU A C     1 
ATOM   824   O  O     . GLU A 1 1635 ? 187.712 215.574 242.892 1.00 97.26  ? 1635 GLU A O     1 
ATOM   825   C  CB    . GLU A 1 1635 ? 189.394 214.757 240.235 1.00 98.71  ? 1635 GLU A CB    1 
ATOM   826   C  CG    . GLU A 1 1635 ? 190.877 214.731 240.570 1.00 99.43  ? 1635 GLU A CG    1 
ATOM   827   C  CD    . GLU A 1 1635 ? 191.165 214.033 241.884 1.00 100.27 ? 1635 GLU A CD    1 
ATOM   828   O  OE1   . GLU A 1 1635 ? 190.306 213.250 242.342 1.00 99.63  ? 1635 GLU A OE1   1 
ATOM   829   O  OE2   . GLU A 1 1635 ? 192.247 214.267 242.460 1.00 98.33  ? 1635 GLU A OE2   1 
ATOM   830   N  N     . ASP A 1 1636 ? 189.673 216.678 242.842 1.00 94.78  ? 1636 ASP A N     1 
ATOM   831   C  CA    . ASP A 1 1636 ? 189.679 216.878 244.287 1.00 93.66  ? 1636 ASP A CA    1 
ATOM   832   C  C     . ASP A 1 1636 ? 188.552 217.810 244.715 1.00 95.90  ? 1636 ASP A C     1 
ATOM   833   O  O     . ASP A 1 1636 ? 187.892 217.571 245.734 1.00 100.47 ? 1636 ASP A O     1 
ATOM   834   C  CB    . ASP A 1 1636 ? 191.032 217.429 244.735 1.00 97.06  ? 1636 ASP A CB    1 
ATOM   835   C  CG    . ASP A 1 1636 ? 192.082 216.345 244.884 1.00 98.21  ? 1636 ASP A CG    1 
ATOM   836   O  OD1   . ASP A 1 1636 ? 191.881 215.431 245.710 1.00 97.33  ? 1636 ASP A OD1   1 
ATOM   837   O  OD2   . ASP A 1 1636 ? 193.108 216.408 244.176 1.00 97.79  ? 1636 ASP A OD2   1 
ATOM   838   N  N     . LEU A 1 1637 ? 188.315 218.876 243.948 1.00 95.52  ? 1637 LEU A N     1 
ATOM   839   C  CA    . LEU A 1 1637 ? 187.202 219.768 244.251 1.00 97.25  ? 1637 LEU A CA    1 
ATOM   840   C  C     . LEU A 1 1637 ? 185.867 219.045 244.125 1.00 97.95  ? 1637 LEU A C     1 
ATOM   841   O  O     . LEU A 1 1637 ? 184.966 219.246 244.946 1.00 97.04  ? 1637 LEU A O     1 
ATOM   842   C  CB    . LEU A 1 1637 ? 187.241 220.992 243.335 1.00 95.89  ? 1637 LEU A CB    1 
ATOM   843   C  CG    . LEU A 1 1637 ? 186.097 221.996 243.495 1.00 97.52  ? 1637 LEU A CG    1 
ATOM   844   C  CD1   . LEU A 1 1637 ? 185.905 222.377 244.953 1.00 95.71  ? 1637 LEU A CD1   1 
ATOM   845   C  CD2   . LEU A 1 1637 ? 186.350 223.230 242.653 1.00 97.88  ? 1637 LEU A CD2   1 
ATOM   846   N  N     . LEU A 1 1638 ? 185.718 218.201 243.101 1.00 100.17 ? 1638 LEU A N     1 
ATOM   847   C  CA    . LEU A 1 1638 ? 184.483 217.434 242.957 1.00 99.08  ? 1638 LEU A CA    1 
ATOM   848   C  C     . LEU A 1 1638 ? 184.295 216.468 244.121 1.00 98.08  ? 1638 LEU A C     1 
ATOM   849   O  O     . LEU A 1 1638 ? 183.173 216.276 244.605 1.00 99.61  ? 1638 LEU A O     1 
ATOM   850   C  CB    . LEU A 1 1638 ? 184.485 216.684 241.626 1.00 98.22  ? 1638 LEU A CB    1 
ATOM   851   C  CG    . LEU A 1 1638 ? 184.141 217.520 240.393 1.00 99.13  ? 1638 LEU A CG    1 
ATOM   852   C  CD1   . LEU A 1 1638 ? 184.177 216.664 239.140 1.00 98.94  ? 1638 LEU A CD1   1 
ATOM   853   C  CD2   . LEU A 1 1638 ? 182.783 218.186 240.553 1.00 97.54  ? 1638 LEU A CD2   1 
ATOM   854   N  N     . GLU A 1 1639 ? 185.383 215.843 244.576 1.00 98.75  ? 1639 GLU A N     1 
ATOM   855   C  CA    . GLU A 1 1639 ? 185.314 214.977 245.749 1.00 99.17  ? 1639 GLU A CA    1 
ATOM   856   C  C     . GLU A 1 1639 ? 184.884 215.759 246.983 1.00 98.64  ? 1639 GLU A C     1 
ATOM   857   O  O     . GLU A 1 1639 ? 184.089 215.269 247.794 1.00 98.64  ? 1639 GLU A O     1 
ATOM   858   C  CB    . GLU A 1 1639 ? 186.667 214.307 245.983 1.00 98.27  ? 1639 GLU A CB    1 
ATOM   859   C  CG    . GLU A 1 1639 ? 186.707 213.399 247.197 1.00 98.68  ? 1639 GLU A CG    1 
ATOM   860   C  CD    . GLU A 1 1639 ? 188.083 212.821 247.451 1.00 100.67 ? 1639 GLU A CD    1 
ATOM   861   O  OE1   . GLU A 1 1639 ? 189.013 213.134 246.678 1.00 99.29  ? 1639 GLU A OE1   1 
ATOM   862   O  OE2   . GLU A 1 1639 ? 188.236 212.056 248.426 1.00 99.23  ? 1639 GLU A OE2   1 
ATOM   863   N  N     . ILE A 1 1640 ? 185.409 216.975 247.145 1.00 96.29  ? 1640 ILE A N     1 
ATOM   864   C  CA    . ILE A 1 1640 ? 184.990 217.828 248.255 1.00 97.45  ? 1640 ILE A CA    1 
ATOM   865   C  C     . ILE A 1 1640 ? 183.505 218.153 248.145 1.00 99.72  ? 1640 ILE A C     1 
ATOM   866   O  O     . ILE A 1 1640 ? 182.776 218.151 249.144 1.00 99.74  ? 1640 ILE A O     1 
ATOM   867   C  CB    . ILE A 1 1640 ? 185.850 219.105 248.298 1.00 97.96  ? 1640 ILE A CB    1 
ATOM   868   C  CG1   . ILE A 1 1640 ? 187.276 218.771 248.738 1.00 97.23  ? 1640 ILE A CG1   1 
ATOM   869   C  CG2   . ILE A 1 1640 ? 185.228 220.149 249.214 1.00 97.70  ? 1640 ILE A CG2   1 
ATOM   870   C  CD1   . ILE A 1 1640 ? 188.222 219.949 248.693 1.00 96.70  ? 1640 ILE A CD1   1 
ATOM   871   N  N     . ILE A 1 1641 ? 183.038 218.436 246.928 1.00 99.23  ? 1641 ILE A N     1 
ATOM   872   C  CA    . ILE A 1 1641 ? 181.631 218.768 246.718 1.00 98.71  ? 1641 ILE A CA    1 
ATOM   873   C  C     . ILE A 1 1641 ? 180.742 217.593 247.103 1.00 100.60 ? 1641 ILE A C     1 
ATOM   874   O  O     . ILE A 1 1641 ? 179.745 217.753 247.817 1.00 100.08 ? 1641 ILE A O     1 
ATOM   875   C  CB    . ILE A 1 1641 ? 181.394 219.186 245.255 1.00 98.25  ? 1641 ILE A CB    1 
ATOM   876   C  CG1   . ILE A 1 1641 ? 182.047 220.535 244.960 1.00 98.84  ? 1641 ILE A CG1   1 
ATOM   877   C  CG2   . ILE A 1 1641 ? 179.905 219.242 244.950 1.00 96.98  ? 1641 ILE A CG2   1 
ATOM   878   C  CD1   . ILE A 1 1641 ? 182.479 220.680 243.517 1.00 98.02  ? 1641 ILE A CD1   1 
ATOM   879   N  N     . GLY A 1 1642 ? 181.094 216.391 246.641 1.00 98.38  ? 1642 GLY A N     1 
ATOM   880   C  CA    . GLY A 1 1642 ? 180.252 215.231 246.877 1.00 98.39  ? 1642 GLY A CA    1 
ATOM   881   C  C     . GLY A 1 1642 ? 180.323 214.665 248.277 1.00 101.30 ? 1642 GLY A C     1 
ATOM   882   O  O     . GLY A 1 1642 ? 179.413 213.936 248.683 1.00 101.52 ? 1642 GLY A O     1 
ATOM   883   N  N     . ASN A 1 1643 ? 181.377 214.981 249.024 1.00 99.44  ? 1643 ASN A N     1 
ATOM   884   C  CA    . ASN A 1 1643 ? 181.563 214.482 250.382 1.00 95.76  ? 1643 ASN A CA    1 
ATOM   885   C  C     . ASN A 1 1643 ? 181.475 215.607 251.408 1.00 95.77  ? 1643 ASN A C     1 
ATOM   886   O  O     . ASN A 1 1643 ? 182.259 215.668 252.356 1.00 96.19  ? 1643 ASN A O     1 
ATOM   887   C  CB    . ASN A 1 1643 ? 182.893 213.746 250.515 1.00 93.90  ? 1643 ASN A CB    1 
ATOM   888   C  CG    . ASN A 1 1643 ? 183.115 212.739 249.406 1.00 97.10  ? 1643 ASN A CG    1 
ATOM   889   O  OD1   . ASN A 1 1643 ? 182.170 212.289 248.759 1.00 95.24  ? 1643 ASN A OD1   1 
ATOM   890   N  ND2   . ASN A 1 1643 ? 184.370 212.374 249.185 1.00 98.79  ? 1643 ASN A ND2   1 
ATOM   891   N  N     . SER A 1 1644 ? 180.523 216.522 251.218 1.00 95.33  ? 1644 SER A N     1 
ATOM   892   C  CA    . SER A 1 1644 ? 180.296 217.561 252.213 1.00 97.87  ? 1644 SER A CA    1 
ATOM   893   C  C     . SER A 1 1644 ? 179.576 217.020 253.441 1.00 99.38  ? 1644 SER A C     1 
ATOM   894   O  O     . SER A 1 1644 ? 179.719 217.580 254.534 1.00 95.44  ? 1644 SER A O     1 
ATOM   895   C  CB    . SER A 1 1644 ? 179.500 218.714 251.602 1.00 95.32  ? 1644 SER A CB    1 
ATOM   896   O  OG    . SER A 1 1644 ? 179.307 219.753 252.546 1.00 96.01  ? 1644 SER A OG    1 
ATOM   897   N  N     . LYS A 1 1645 ? 178.801 215.943 253.284 1.00 99.12  ? 1645 LYS A N     1 
ATOM   898   C  CA    . LYS A 1 1645 ? 178.095 215.365 254.423 1.00 99.28  ? 1645 LYS A CA    1 
ATOM   899   C  C     . LYS A 1 1645 ? 179.061 214.713 255.404 1.00 99.01  ? 1645 LYS A C     1 
ATOM   900   O  O     . LYS A 1 1645 ? 178.946 214.909 256.619 1.00 97.22  ? 1645 LYS A O     1 
ATOM   901   C  CB    . LYS A 1 1645 ? 177.056 214.354 253.940 1.00 100.70 ? 1645 LYS A CB    1 
ATOM   902   C  CG    . LYS A 1 1645 ? 176.206 213.758 255.052 1.00 100.05 ? 1645 LYS A CG    1 
ATOM   903   C  CD    . LYS A 1 1645 ? 175.162 212.803 254.497 1.00 99.66  ? 1645 LYS A CD    1 
ATOM   904   C  CE    . LYS A 1 1645 ? 174.251 212.277 255.593 1.00 98.05  ? 1645 LYS A CE    1 
ATOM   905   N  NZ    . LYS A 1 1645 ? 174.977 211.391 256.544 1.00 97.15  ? 1645 LYS A NZ    1 
ATOM   906   N  N     . ASN A 1 1646 ? 180.016 213.936 254.901 1.00 98.51  ? 1646 ASN A N     1 
ATOM   907   C  CA    . ASN A 1 1646 ? 181.019 213.289 255.738 1.00 97.76  ? 1646 ASN A CA    1 
ATOM   908   C  C     . ASN A 1 1646 ? 182.299 214.114 255.699 1.00 97.26  ? 1646 ASN A C     1 
ATOM   909   O  O     . ASN A 1 1646 ? 182.916 214.267 254.639 1.00 96.35  ? 1646 ASN A O     1 
ATOM   910   C  CB    . ASN A 1 1646 ? 181.276 211.852 255.283 1.00 95.96  ? 1646 ASN A CB    1 
ATOM   911   C  CG    . ASN A 1 1646 ? 181.604 211.755 253.808 1.00 98.05  ? 1646 ASN A CG    1 
ATOM   912   O  OD1   . ASN A 1 1646 ? 181.092 212.523 252.995 1.00 99.09  ? 1646 ASN A OD1   1 
ATOM   913   N  ND2   . ASN A 1 1646 ? 182.463 210.805 253.454 1.00 95.43  ? 1646 ASN A ND2   1 
ATOM   914   N  N     . VAL A 1 1647 ? 182.696 214.642 256.861 1.00 95.24  ? 1647 VAL A N     1 
ATOM   915   C  CA    . VAL A 1 1647 ? 183.844 215.537 256.946 1.00 96.23  ? 1647 VAL A CA    1 
ATOM   916   C  C     . VAL A 1 1647 ? 185.142 214.806 257.255 1.00 94.80  ? 1647 VAL A C     1 
ATOM   917   O  O     . VAL A 1 1647 ? 186.196 215.451 257.351 1.00 95.04  ? 1647 VAL A O     1 
ATOM   918   C  CB    . VAL A 1 1647 ? 183.582 216.629 258.000 1.00 95.09  ? 1647 VAL A CB    1 
ATOM   919   C  CG1   . VAL A 1 1647 ? 182.514 217.585 257.507 1.00 93.44  ? 1647 VAL A CG1   1 
ATOM   920   C  CG2   . VAL A 1 1647 ? 183.137 215.988 259.298 1.00 93.86  ? 1647 VAL A CG2   1 
ATOM   921   N  N     . ALA A 1 1648 ? 185.104 213.483 257.421 1.00 89.02  ? 1648 ALA A N     1 
ATOM   922   C  CA    . ALA A 1 1648 ? 186.338 212.734 257.633 1.00 89.86  ? 1648 ALA A CA    1 
ATOM   923   C  C     . ALA A 1 1648 ? 187.199 212.724 256.377 1.00 91.75  ? 1648 ALA A C     1 
ATOM   924   O  O     . ALA A 1 1648 ? 188.432 212.773 256.460 1.00 89.54  ? 1648 ALA A O     1 
ATOM   925   C  CB    . ALA A 1 1648 ? 186.018 211.308 258.078 1.00 87.38  ? 1648 ALA A CB    1 
ATOM   926   N  N     . LYS A 1 1649 ? 186.567 212.657 255.203 1.00 94.96  ? 1649 LYS A N     1 
ATOM   927   C  CA    . LYS A 1 1649 ? 187.310 212.650 253.949 1.00 94.08  ? 1649 LYS A CA    1 
ATOM   928   C  C     . LYS A 1 1649 ? 187.911 214.012 253.626 1.00 93.67  ? 1649 LYS A C     1 
ATOM   929   O  O     . LYS A 1 1649 ? 188.880 214.083 252.862 1.00 93.21  ? 1649 LYS A O     1 
ATOM   930   C  CB    . LYS A 1 1649 ? 186.398 212.200 252.807 1.00 94.18  ? 1649 LYS A CB    1 
ATOM   931   C  CG    . LYS A 1 1649 ? 186.170 210.698 252.747 1.00 92.88  ? 1649 LYS A CG    1 
ATOM   932   C  CD    . LYS A 1 1649 ? 185.689 210.269 251.371 1.00 93.12  ? 1649 LYS A CD    1 
ATOM   933   C  CE    . LYS A 1 1649 ? 184.839 209.011 251.449 1.00 93.58  ? 1649 LYS A CE    1 
ATOM   934   N  NZ    . LYS A 1 1649 ? 185.628 207.781 251.168 1.00 91.40  ? 1649 LYS A NZ    1 
ATOM   935   N  N     . LEU A 1 1650 ? 187.361 215.088 254.187 1.00 90.82  ? 1650 LEU A N     1 
ATOM   936   C  CA    . LEU A 1 1650 ? 187.862 216.435 253.949 1.00 90.48  ? 1650 LEU A CA    1 
ATOM   937   C  C     . LEU A 1 1650 ? 189.176 216.723 254.661 1.00 89.07  ? 1650 LEU A C     1 
ATOM   938   O  O     . LEU A 1 1650 ? 189.826 217.723 254.341 1.00 87.27  ? 1650 LEU A O     1 
ATOM   939   C  CB    . LEU A 1 1650 ? 186.817 217.463 254.388 1.00 89.88  ? 1650 LEU A CB    1 
ATOM   940   C  CG    . LEU A 1 1650 ? 185.784 217.899 253.351 1.00 90.43  ? 1650 LEU A CG    1 
ATOM   941   C  CD1   . LEU A 1 1650 ? 184.579 218.521 254.033 1.00 90.35  ? 1650 LEU A CD1   1 
ATOM   942   C  CD2   . LEU A 1 1650 ? 186.409 218.877 252.378 1.00 89.23  ? 1650 LEU A CD2   1 
ATOM   943   N  N     . GLN A 1 1651 ? 189.583 215.878 255.611 1.00 89.51  ? 1651 GLN A N     1 
ATOM   944   C  CA    . GLN A 1 1651 ? 190.744 216.182 256.439 1.00 91.21  ? 1651 GLN A CA    1 
ATOM   945   C  C     . GLN A 1 1651 ? 192.054 216.133 255.664 1.00 88.59  ? 1651 GLN A C     1 
ATOM   946   O  O     . GLN A 1 1651 ? 193.025 216.776 256.077 1.00 88.47  ? 1651 GLN A O     1 
ATOM   947   C  CB    . GLN A 1 1651 ? 190.808 215.216 257.622 1.00 88.03  ? 1651 GLN A CB    1 
ATOM   948   C  CG    . GLN A 1 1651 ? 189.617 215.306 258.558 1.00 84.21  ? 1651 GLN A CG    1 
ATOM   949   C  CD    . GLN A 1 1651 ? 189.763 216.412 259.581 1.00 85.98  ? 1651 GLN A CD    1 
ATOM   950   O  OE1   . GLN A 1 1651 ? 189.835 217.589 259.233 1.00 87.16  ? 1651 GLN A OE1   1 
ATOM   951   N  NE2   . GLN A 1 1651 ? 189.805 216.038 260.853 1.00 87.82  ? 1651 GLN A NE2   1 
ATOM   952   N  N     . LYS A 1 1652 ? 192.109 215.395 254.560 1.00 88.81  ? 1652 LYS A N     1 
ATOM   953   C  CA    . LYS A 1 1652 ? 193.340 215.245 253.797 1.00 88.60  ? 1652 LYS A CA    1 
ATOM   954   C  C     . LYS A 1 1652 ? 193.576 216.384 252.815 1.00 91.49  ? 1652 LYS A C     1 
ATOM   955   O  O     . LYS A 1 1652 ? 194.615 216.400 252.148 1.00 91.55  ? 1652 LYS A O     1 
ATOM   956   C  CB    . LYS A 1 1652 ? 193.335 213.909 253.048 1.00 88.70  ? 1652 LYS A CB    1 
ATOM   957   C  CG    . LYS A 1 1652 ? 192.302 213.818 251.938 1.00 89.17  ? 1652 LYS A CG    1 
ATOM   958   C  CD    . LYS A 1 1652 ? 192.477 212.550 251.118 1.00 87.69  ? 1652 LYS A CD    1 
ATOM   959   C  CE    . LYS A 1 1652 ? 192.451 211.308 251.995 1.00 90.10  ? 1652 LYS A CE    1 
ATOM   960   N  NZ    . LYS A 1 1652 ? 191.287 211.299 252.923 1.00 90.85  ? 1652 LYS A NZ    1 
ATOM   961   N  N     . HIS A 1 1653 ? 192.646 217.333 252.710 1.00 91.59  ? 1653 HIS A N     1 
ATOM   962   C  CA    . HIS A 1 1653 ? 192.776 218.445 251.782 1.00 89.54  ? 1653 HIS A CA    1 
ATOM   963   C  C     . HIS A 1 1653 ? 193.078 219.773 252.459 1.00 87.53  ? 1653 HIS A C     1 
ATOM   964   O  O     . HIS A 1 1653 ? 193.424 220.734 251.765 1.00 89.12  ? 1653 HIS A O     1 
ATOM   965   C  CB    . HIS A 1 1653 ? 191.497 218.587 250.945 1.00 87.92  ? 1653 HIS A CB    1 
ATOM   966   C  CG    . HIS A 1 1653 ? 191.219 217.408 250.067 1.00 91.52  ? 1653 HIS A CG    1 
ATOM   967   N  ND1   . HIS A 1 1653 ? 189.979 217.165 249.516 1.00 91.46  ? 1653 HIS A ND1   1 
ATOM   968   C  CD2   . HIS A 1 1653 ? 192.022 216.405 249.640 1.00 91.54  ? 1653 HIS A CD2   1 
ATOM   969   C  CE1   . HIS A 1 1653 ? 190.030 216.063 248.790 1.00 91.54  ? 1653 HIS A CE1   1 
ATOM   970   N  NE2   . HIS A 1 1653 ? 191.258 215.582 248.849 1.00 93.29  ? 1653 HIS A NE2   1 
ATOM   971   N  N     . PHE A 1 1654 ? 192.960 219.858 253.785 1.00 85.70  ? 1654 PHE A N     1 
ATOM   972   C  CA    . PHE A 1 1654 ? 193.240 221.111 254.475 1.00 84.96  ? 1654 PHE A CA    1 
ATOM   973   C  C     . PHE A 1 1654 ? 194.721 221.458 254.476 1.00 85.23  ? 1654 PHE A C     1 
ATOM   974   O  O     . PHE A 1 1654 ? 195.066 222.636 254.613 1.00 86.51  ? 1654 PHE A O     1 
ATOM   975   C  CB    . PHE A 1 1654 ? 192.722 221.051 255.913 1.00 84.57  ? 1654 PHE A CB    1 
ATOM   976   C  CG    . PHE A 1 1654 ? 191.226 221.070 256.019 1.00 87.38  ? 1654 PHE A CG    1 
ATOM   977   C  CD1   . PHE A 1 1654 ? 190.508 222.203 255.672 1.00 84.28  ? 1654 PHE A CD1   1 
ATOM   978   C  CD2   . PHE A 1 1654 ? 190.536 219.960 256.471 1.00 86.44  ? 1654 PHE A CD2   1 
ATOM   979   C  CE1   . PHE A 1 1654 ? 189.132 222.226 255.771 1.00 81.84  ? 1654 PHE A CE1   1 
ATOM   980   C  CE2   . PHE A 1 1654 ? 189.158 219.978 256.571 1.00 87.34  ? 1654 PHE A CE2   1 
ATOM   981   C  CZ    . PHE A 1 1654 ? 188.456 221.113 256.220 1.00 84.54  ? 1654 PHE A CZ    1 
ATOM   982   N  N     . LYS A 1 1655 ? 195.603 220.467 254.325 1.00 87.95  ? 1655 LYS A N     1 
ATOM   983   C  CA    . LYS A 1 1655 ? 197.034 220.749 254.325 1.00 86.74  ? 1655 LYS A CA    1 
ATOM   984   C  C     . LYS A 1 1655 ? 197.452 221.565 253.107 1.00 90.18  ? 1655 LYS A C     1 
ATOM   985   O  O     . LYS A 1 1655 ? 198.353 222.404 253.209 1.00 91.20  ? 1655 LYS A O     1 
ATOM   986   C  CB    . LYS A 1 1655 ? 197.831 219.446 254.388 1.00 82.81  ? 1655 LYS A CB    1 
ATOM   987   C  CG    . LYS A 1 1655 ? 197.511 218.463 253.277 1.00 86.03  ? 1655 LYS A CG    1 
ATOM   988   C  CD    . LYS A 1 1655 ? 198.472 217.288 253.281 1.00 89.06  ? 1655 LYS A CD    1 
ATOM   989   C  CE    . LYS A 1 1655 ? 197.992 216.188 252.350 1.00 90.69  ? 1655 LYS A CE    1 
ATOM   990   N  NZ    . LYS A 1 1655 ? 197.820 216.680 250.955 1.00 89.03  ? 1655 LYS A NZ    1 
ATOM   991   N  N     . LYS A 1 1656 ? 196.822 221.336 251.956 1.00 90.30  ? 1656 LYS A N     1 
ATOM   992   C  CA    . LYS A 1 1656 ? 197.189 222.038 250.734 1.00 88.53  ? 1656 LYS A CA    1 
ATOM   993   C  C     . LYS A 1 1656 ? 196.400 223.322 250.514 1.00 86.70  ? 1656 LYS A C     1 
ATOM   994   O  O     . LYS A 1 1656 ? 196.805 224.143 249.685 1.00 87.81  ? 1656 LYS A O     1 
ATOM   995   C  CB    . LYS A 1 1656 ? 197.018 221.114 249.523 1.00 88.32  ? 1656 LYS A CB    1 
ATOM   996   C  CG    . LYS A 1 1656 ? 195.609 220.590 249.322 1.00 88.73  ? 1656 LYS A CG    1 
ATOM   997   C  CD    . LYS A 1 1656 ? 195.527 219.725 248.074 1.00 90.32  ? 1656 LYS A CD    1 
ATOM   998   C  CE    . LYS A 1 1656 ? 194.554 218.572 248.260 1.00 90.79  ? 1656 LYS A CE    1 
ATOM   999   N  NZ    . LYS A 1 1656 ? 195.162 217.452 249.029 1.00 88.08  ? 1656 LYS A NZ    1 
ATOM   1000  N  N     . MET A 1 1657 ? 195.296 223.522 251.234 1.00 78.17  ? 1657 MET A N     1 
ATOM   1001  C  CA    . MET A 1 1657 ? 194.529 224.754 251.141 1.00 81.83  ? 1657 MET A CA    1 
ATOM   1002  C  C     . MET A 1 1657 ? 194.866 225.759 252.232 1.00 83.56  ? 1657 MET A C     1 
ATOM   1003  O  O     . MET A 1 1657 ? 194.341 226.878 252.200 1.00 83.66  ? 1657 MET A O     1 
ATOM   1004  C  CB    . MET A 1 1657 ? 193.024 224.450 251.184 1.00 82.11  ? 1657 MET A CB    1 
ATOM   1005  C  CG    . MET A 1 1657 ? 192.578 223.399 250.185 1.00 84.21  ? 1657 MET A CG    1 
ATOM   1006  S  SD    . MET A 1 1657 ? 190.931 222.755 250.531 1.00 89.47  ? 1657 MET A SD    1 
ATOM   1007  C  CE    . MET A 1 1657 ? 190.115 224.223 251.145 1.00 79.64  ? 1657 MET A CE    1 
ATOM   1008  N  N     . PHE A 1 1658 ? 195.719 225.397 253.188 1.00 76.01  ? 1658 PHE A N     1 
ATOM   1009  C  CA    . PHE A 1 1658 ? 196.093 226.285 254.278 1.00 67.66  ? 1658 PHE A CA    1 
ATOM   1010  C  C     . PHE A 1 1658 ? 197.577 226.121 254.575 1.00 69.85  ? 1658 PHE A C     1 
ATOM   1011  O  O     . PHE A 1 1658 ? 198.181 225.087 254.282 1.00 69.43  ? 1658 PHE A O     1 
ATOM   1012  C  CB    . PHE A 1 1658 ? 195.272 226.011 255.541 1.00 67.87  ? 1658 PHE A CB    1 
ATOM   1013  C  CG    . PHE A 1 1658 ? 193.826 226.403 255.427 1.00 74.26  ? 1658 PHE A CG    1 
ATOM   1014  C  CD1   . PHE A 1 1658 ? 192.896 225.530 254.891 1.00 73.44  ? 1658 PHE A CD1   1 
ATOM   1015  C  CD2   . PHE A 1 1658 ? 193.397 227.644 255.863 1.00 72.73  ? 1658 PHE A CD2   1 
ATOM   1016  C  CE1   . PHE A 1 1658 ? 191.569 225.889 254.787 1.00 71.72  ? 1658 PHE A CE1   1 
ATOM   1017  C  CE2   . PHE A 1 1658 ? 192.072 228.008 255.763 1.00 72.46  ? 1658 PHE A CE2   1 
ATOM   1018  C  CZ    . PHE A 1 1658 ? 191.156 227.130 255.224 1.00 72.77  ? 1658 PHE A CZ    1 
ATOM   1019  N  N     . ALA A 1 1659 ? 198.160 227.166 255.167 1.00 70.28  ? 1659 ALA A N     1 
ATOM   1020  C  CA    . ALA A 1 1659 ? 199.595 227.164 255.434 1.00 66.80  ? 1659 ALA A CA    1 
ATOM   1021  C  C     . ALA A 1 1659 ? 199.961 226.148 256.508 1.00 69.94  ? 1659 ALA A C     1 
ATOM   1022  O  O     . ALA A 1 1659 ? 200.954 225.423 256.376 1.00 70.74  ? 1659 ALA A O     1 
ATOM   1023  C  CB    . ALA A 1 1659 ? 200.055 228.563 255.838 1.00 64.03  ? 1659 ALA A CB    1 
ATOM   1024  N  N     . GLY A 1 1660 ? 199.176 226.081 257.580 1.00 72.70  ? 1660 GLY A N     1 
ATOM   1025  C  CA    . GLY A 1 1660 ? 199.520 225.215 258.690 1.00 68.04  ? 1660 GLY A CA    1 
ATOM   1026  C  C     . GLY A 1 1660 ? 198.370 224.407 259.251 1.00 67.13  ? 1660 GLY A C     1 
ATOM   1027  O  O     . GLY A 1 1660 ? 198.550 223.664 260.219 1.00 69.77  ? 1660 GLY A O     1 
ATOM   1028  N  N     . VAL A 1 1661 ? 197.185 224.537 258.658 1.00 71.86  ? 1661 VAL A N     1 
ATOM   1029  C  CA    . VAL A 1 1661 ? 196.001 223.818 259.126 1.00 70.40  ? 1661 VAL A CA    1 
ATOM   1030  C  C     . VAL A 1 1661 ? 196.094 222.390 258.596 1.00 69.45  ? 1661 VAL A C     1 
ATOM   1031  O  O     . VAL A 1 1661 ? 195.746 222.120 257.447 1.00 69.58  ? 1661 VAL A O     1 
ATOM   1032  C  CB    . VAL A 1 1661 ? 194.706 224.500 258.681 1.00 69.85  ? 1661 VAL A CB    1 
ATOM   1033  C  CG1   . VAL A 1 1661 ? 193.498 223.770 259.243 1.00 66.61  ? 1661 VAL A CG1   1 
ATOM   1034  C  CG2   . VAL A 1 1661 ? 194.708 225.957 259.097 1.00 72.26  ? 1661 VAL A CG2   1 
ATOM   1035  N  N     . SER A 1 1662 ? 196.566 221.468 259.435 1.00 73.19  ? 1662 SER A N     1 
ATOM   1036  C  CA    . SER A 1 1662 ? 196.623 220.068 259.031 1.00 74.17  ? 1662 SER A CA    1 
ATOM   1037  C  C     . SER A 1 1662 ? 195.238 219.435 259.023 1.00 76.10  ? 1662 SER A C     1 
ATOM   1038  O  O     . SER A 1 1662 ? 194.905 218.676 258.106 1.00 78.13  ? 1662 SER A O     1 
ATOM   1039  C  CB    . SER A 1 1662 ? 197.556 219.290 259.958 1.00 73.80  ? 1662 SER A CB    1 
ATOM   1040  O  OG    . SER A 1 1662 ? 197.704 217.950 259.522 1.00 74.38  ? 1662 SER A OG    1 
ATOM   1041  N  N     . SER A 1 1663 ? 194.422 219.738 260.028 1.00 76.08  ? 1663 SER A N     1 
ATOM   1042  C  CA    . SER A 1 1663 ? 193.079 219.189 260.122 1.00 76.30  ? 1663 SER A CA    1 
ATOM   1043  C  C     . SER A 1 1663 ? 192.241 220.112 260.992 1.00 73.85  ? 1663 SER A C     1 
ATOM   1044  O  O     . SER A 1 1663 ? 192.770 220.946 261.730 1.00 75.81  ? 1663 SER A O     1 
ATOM   1045  C  CB    . SER A 1 1663 ? 193.092 217.767 260.692 1.00 75.75  ? 1663 SER A CB    1 
ATOM   1046  O  OG    . SER A 1 1663 ? 193.613 217.752 262.009 1.00 73.54  ? 1663 SER A OG    1 
ATOM   1047  N  N     . ILE A 1 1664 ? 190.927 219.953 260.895 1.00 72.40  ? 1664 ILE A N     1 
ATOM   1048  C  CA    . ILE A 1 1664 ? 189.994 220.723 261.706 1.00 75.85  ? 1664 ILE A CA    1 
ATOM   1049  C  C     . ILE A 1 1664 ? 189.567 219.877 262.895 1.00 78.01  ? 1664 ILE A C     1 
ATOM   1050  O  O     . ILE A 1 1664 ? 189.543 218.642 262.834 1.00 78.86  ? 1664 ILE A O     1 
ATOM   1051  C  CB    . ILE A 1 1664 ? 188.772 221.192 260.887 1.00 76.71  ? 1664 ILE A CB    1 
ATOM   1052  C  CG1   . ILE A 1 1664 ? 187.989 219.991 260.352 1.00 78.44  ? 1664 ILE A CG1   1 
ATOM   1053  C  CG2   . ILE A 1 1664 ? 189.212 222.101 259.752 1.00 77.75  ? 1664 ILE A CG2   1 
ATOM   1054  C  CD1   . ILE A 1 1664 ? 186.799 220.370 259.498 1.00 77.03  ? 1664 ILE A CD1   1 
ATOM   1055  N  N     . ILE A 1 1665 ? 189.235 220.548 263.993 1.00 80.22  ? 1665 ILE A N     1 
ATOM   1056  C  CA    . ILE A 1 1665 ? 188.793 219.893 265.218 1.00 79.02  ? 1665 ILE A CA    1 
ATOM   1057  C  C     . ILE A 1 1665 ? 187.273 219.897 265.239 1.00 80.31  ? 1665 ILE A C     1 
ATOM   1058  O  O     . ILE A 1 1665 ? 186.642 220.944 265.044 1.00 78.92  ? 1665 ILE A O     1 
ATOM   1059  C  CB    . ILE A 1 1665 ? 189.365 220.590 266.464 1.00 80.13  ? 1665 ILE A CB    1 
ATOM   1060  C  CG1   . ILE A 1 1665 ? 190.893 220.511 266.464 1.00 79.75  ? 1665 ILE A CG1   1 
ATOM   1061  C  CG2   . ILE A 1 1665 ? 188.801 219.966 267.729 1.00 77.75  ? 1665 ILE A CG2   1 
ATOM   1062  C  CD1   . ILE A 1 1665 ? 191.433 219.125 266.202 1.00 77.92  ? 1665 ILE A CD1   1 
ATOM   1063  N  N     . LEU A 1 1666 ? 186.683 218.728 265.473 1.00 87.77  ? 1666 LEU A N     1 
ATOM   1064  C  CA    . LEU A 1 1666 ? 185.242 218.554 265.416 1.00 90.09  ? 1666 LEU A CA    1 
ATOM   1065  C  C     . LEU A 1 1666 ? 184.761 217.828 266.663 1.00 92.91  ? 1666 LEU A C     1 
ATOM   1066  O  O     . LEU A 1 1666 ? 185.510 217.090 267.308 1.00 88.22  ? 1666 LEU A O     1 
ATOM   1067  C  CB    . LEU A 1 1666 ? 184.832 217.773 264.162 1.00 88.24  ? 1666 LEU A CB    1 
ATOM   1068  C  CG    . LEU A 1 1666 ? 185.096 218.481 262.834 1.00 88.94  ? 1666 LEU A CG    1 
ATOM   1069  C  CD1   . LEU A 1 1666 ? 185.217 217.469 261.719 1.00 86.22  ? 1666 LEU A CD1   1 
ATOM   1070  C  CD2   . LEU A 1 1666 ? 183.989 219.473 262.533 1.00 88.61  ? 1666 LEU A CD2   1 
ATOM   1071  N  N     . ASN A 1 1667 ? 183.492 218.049 266.996 1.00 95.92  ? 1667 ASN A N     1 
ATOM   1072  C  CA    . ASN A 1 1667 ? 182.873 217.360 268.116 1.00 92.42  ? 1667 ASN A CA    1 
ATOM   1073  C  C     . ASN A 1 1667 ? 182.572 215.911 267.734 1.00 94.79  ? 1667 ASN A C     1 
ATOM   1074  O  O     . ASN A 1 1667 ? 182.879 215.449 266.632 1.00 93.67  ? 1667 ASN A O     1 
ATOM   1075  C  CB    . ASN A 1 1667 ? 181.602 218.086 268.547 1.00 88.94  ? 1667 ASN A CB    1 
ATOM   1076  C  CG    . ASN A 1 1667 ? 180.625 218.276 267.405 1.00 91.48  ? 1667 ASN A CG    1 
ATOM   1077  O  OD1   . ASN A 1 1667 ? 180.981 218.119 266.238 1.00 91.83  ? 1667 ASN A OD1   1 
ATOM   1078  N  ND2   . ASN A 1 1667 ? 179.385 218.613 267.736 1.00 91.79  ? 1667 ASN A ND2   1 
ATOM   1079  N  N     . GLU A 1 1668 ? 181.961 215.180 268.668 1.00 100.70 ? 1668 GLU A N     1 
ATOM   1080  C  CA    . GLU A 1 1668 ? 181.577 213.802 268.382 1.00 100.03 ? 1668 GLU A CA    1 
ATOM   1081  C  C     . GLU A 1 1668 ? 180.486 213.733 267.321 1.00 97.86  ? 1668 GLU A C     1 
ATOM   1082  O  O     . GLU A 1 1668 ? 180.404 212.746 266.582 1.00 95.78  ? 1668 GLU A O     1 
ATOM   1083  C  CB    . GLU A 1 1668 ? 181.121 213.105 269.664 1.00 98.23  ? 1668 GLU A CB    1 
ATOM   1084  C  CG    . GLU A 1 1668 ? 180.228 213.955 270.552 1.00 98.79  ? 1668 GLU A CG    1 
ATOM   1085  C  CD    . GLU A 1 1668 ? 179.795 213.226 271.809 1.00 100.73 ? 1668 GLU A CD    1 
ATOM   1086  O  OE1   . GLU A 1 1668 ? 180.096 212.020 271.931 1.00 100.16 ? 1668 GLU A OE1   1 
ATOM   1087  O  OE2   . GLU A 1 1668 ? 179.153 213.857 272.675 1.00 100.23 ? 1668 GLU A OE2   1 
ATOM   1088  N  N     . ASP A 1 1669 ? 179.647 214.766 267.227 1.00 94.16  ? 1669 ASP A N     1 
ATOM   1089  C  CA    . ASP A 1 1669 ? 178.584 214.797 266.231 1.00 94.28  ? 1669 ASP A CA    1 
ATOM   1090  C  C     . ASP A 1 1669 ? 179.092 215.118 264.831 1.00 97.32  ? 1669 ASP A C     1 
ATOM   1091  O  O     . ASP A 1 1669 ? 178.387 214.832 263.856 1.00 96.60  ? 1669 ASP A O     1 
ATOM   1092  C  CB    . ASP A 1 1669 ? 177.520 215.821 266.631 1.00 94.86  ? 1669 ASP A CB    1 
ATOM   1093  C  CG    . ASP A 1 1669 ? 176.124 215.409 266.208 1.00 97.62  ? 1669 ASP A CG    1 
ATOM   1094  O  OD1   . ASP A 1 1669 ? 176.001 214.543 265.318 1.00 97.10  ? 1669 ASP A OD1   1 
ATOM   1095  O  OD2   . ASP A 1 1669 ? 175.149 215.956 266.764 1.00 97.38  ? 1669 ASP A OD2   1 
ATOM   1096  N  N     . ASN A 1 1670 ? 180.289 215.697 264.713 1.00 95.59  ? 1670 ASN A N     1 
ATOM   1097  C  CA    . ASN A 1 1670 ? 180.840 216.131 263.426 1.00 94.71  ? 1670 ASN A CA    1 
ATOM   1098  C  C     . ASN A 1 1670 ? 179.894 217.099 262.717 1.00 92.75  ? 1670 ASN A C     1 
ATOM   1099  O  O     . ASN A 1 1670 ? 179.714 217.043 261.500 1.00 90.44  ? 1670 ASN A O     1 
ATOM   1100  C  CB    . ASN A 1 1670 ? 181.169 214.936 262.527 1.00 92.95  ? 1670 ASN A CB    1 
ATOM   1101  C  CG    . ASN A 1 1670 ? 182.453 214.240 262.930 1.00 94.26  ? 1670 ASN A CG    1 
ATOM   1102  O  OD1   . ASN A 1 1670 ? 182.773 214.138 264.113 1.00 93.72  ? 1670 ASN A OD1   1 
ATOM   1103  N  ND2   . ASN A 1 1670 ? 183.197 213.754 261.943 1.00 92.90  ? 1670 ASN A ND2   1 
ATOM   1104  N  N     . SER A 1 1671 ? 179.287 218.001 263.489 1.00 86.44  ? 1671 SER A N     1 
ATOM   1105  C  CA    . SER A 1 1671 ? 178.343 218.969 262.957 1.00 87.09  ? 1671 SER A CA    1 
ATOM   1106  C  C     . SER A 1 1671 ? 178.721 220.415 263.239 1.00 88.41  ? 1671 SER A C     1 
ATOM   1107  O  O     . SER A 1 1671 ? 178.107 221.317 262.659 1.00 88.06  ? 1671 SER A O     1 
ATOM   1108  C  CB    . SER A 1 1671 ? 176.936 218.707 263.515 1.00 87.98  ? 1671 SER A CB    1 
ATOM   1109  O  OG    . SER A 1 1671 ? 176.883 218.966 264.907 1.00 88.28  ? 1671 SER A OG    1 
ATOM   1110  N  N     . VAL A 1 1672 ? 179.694 220.664 264.110 1.00 81.81  ? 1672 VAL A N     1 
ATOM   1111  C  CA    . VAL A 1 1672 ? 180.167 222.010 264.410 1.00 82.13  ? 1672 VAL A CA    1 
ATOM   1112  C  C     . VAL A 1 1672 ? 181.689 221.980 264.429 1.00 85.84  ? 1672 VAL A C     1 
ATOM   1113  O  O     . VAL A 1 1672 ? 182.291 220.999 264.882 1.00 84.70  ? 1672 VAL A O     1 
ATOM   1114  C  CB    . VAL A 1 1672 ? 179.597 222.536 265.745 1.00 82.64  ? 1672 VAL A CB    1 
ATOM   1115  C  CG1   . VAL A 1 1672 ? 180.099 221.715 266.919 1.00 83.54  ? 1672 VAL A CG1   1 
ATOM   1116  C  CG2   . VAL A 1 1672 ? 179.931 224.007 265.935 1.00 80.21  ? 1672 VAL A CG2   1 
ATOM   1117  N  N     . VAL A 1 1673 ? 182.310 223.035 263.908 1.00 83.84  ? 1673 VAL A N     1 
ATOM   1118  C  CA    . VAL A 1 1673 ? 183.764 223.103 263.813 1.00 81.65  ? 1673 VAL A CA    1 
ATOM   1119  C  C     . VAL A 1 1673 ? 184.292 223.810 265.057 1.00 80.27  ? 1673 VAL A C     1 
ATOM   1120  O  O     . VAL A 1 1673 ? 184.185 225.032 265.181 1.00 79.86  ? 1673 VAL A O     1 
ATOM   1121  C  CB    . VAL A 1 1673 ? 184.210 223.821 262.535 1.00 80.14  ? 1673 VAL A CB    1 
ATOM   1122  C  CG1   . VAL A 1 1673 ? 185.693 223.595 262.290 1.00 79.88  ? 1673 VAL A CG1   1 
ATOM   1123  C  CG2   . VAL A 1 1673 ? 183.388 223.345 261.348 1.00 77.19  ? 1673 VAL A CG2   1 
ATOM   1124  N  N     . LEU A 1 1674 ? 184.864 223.039 265.983 1.00 78.69  ? 1674 LEU A N     1 
ATOM   1125  C  CA    . LEU A 1 1674 ? 185.408 223.620 267.206 1.00 80.05  ? 1674 LEU A CA    1 
ATOM   1126  C  C     . LEU A 1 1674 ? 186.675 224.416 266.920 1.00 80.19  ? 1674 LEU A C     1 
ATOM   1127  O  O     . LEU A 1 1674 ? 186.842 225.540 267.406 1.00 83.10  ? 1674 LEU A O     1 
ATOM   1128  C  CB    . LEU A 1 1674 ? 185.681 222.522 268.235 1.00 80.41  ? 1674 LEU A CB    1 
ATOM   1129  C  CG    . LEU A 1 1674 ? 184.578 221.488 268.455 1.00 80.97  ? 1674 LEU A CG    1 
ATOM   1130  C  CD1   . LEU A 1 1674 ? 184.960 220.540 269.578 1.00 80.53  ? 1674 LEU A CD1   1 
ATOM   1131  C  CD2   . LEU A 1 1674 ? 183.262 222.179 268.764 1.00 78.44  ? 1674 LEU A CD2   1 
ATOM   1132  N  N     . GLY A 1 1675 ? 187.582 223.847 266.136 1.00 77.63  ? 1675 GLY A N     1 
ATOM   1133  C  CA    . GLY A 1 1675 ? 188.840 224.503 265.869 1.00 77.01  ? 1675 GLY A CA    1 
ATOM   1134  C  C     . GLY A 1 1675 ? 189.630 223.782 264.800 1.00 76.38  ? 1675 GLY A C     1 
ATOM   1135  O  O     . GLY A 1 1675 ? 189.100 222.953 264.058 1.00 78.18  ? 1675 GLY A O     1 
ATOM   1136  N  N     . ILE A 1 1676 ? 190.914 224.124 264.727 1.00 70.58  ? 1676 ILE A N     1 
ATOM   1137  C  CA    . ILE A 1 1676 ? 191.832 223.581 263.738 1.00 70.89  ? 1676 ILE A CA    1 
ATOM   1138  C  C     . ILE A 1 1676 ? 193.112 223.160 264.443 1.00 71.10  ? 1676 ILE A C     1 
ATOM   1139  O  O     . ILE A 1 1676 ? 193.417 223.609 265.550 1.00 77.66  ? 1676 ILE A O     1 
ATOM   1140  C  CB    . ILE A 1 1676 ? 192.138 224.594 262.620 1.00 72.77  ? 1676 ILE A CB    1 
ATOM   1141  C  CG1   . ILE A 1 1676 ? 192.815 225.822 263.221 1.00 70.44  ? 1676 ILE A CG1   1 
ATOM   1142  C  CG2   . ILE A 1 1676 ? 190.872 224.976 261.871 1.00 74.85  ? 1676 ILE A CG2   1 
ATOM   1143  C  CD1   . ILE A 1 1676 ? 193.364 226.778 262.223 1.00 69.31  ? 1676 ILE A CD1   1 
ATOM   1144  N  N     . SER A 1 1677 ? 193.870 222.290 263.782 1.00 67.91  ? 1677 SER A N     1 
ATOM   1145  C  CA    . SER A 1 1677 ? 195.099 221.748 264.339 1.00 69.65  ? 1677 SER A CA    1 
ATOM   1146  C  C     . SER A 1 1677 ? 196.214 221.820 263.306 1.00 70.07  ? 1677 SER A C     1 
ATOM   1147  O  O     . SER A 1 1677 ? 195.968 221.786 262.098 1.00 73.48  ? 1677 SER A O     1 
ATOM   1148  C  CB    . SER A 1 1677 ? 194.912 220.296 264.799 1.00 73.78  ? 1677 SER A CB    1 
ATOM   1149  O  OG    . SER A 1 1677 ? 196.120 219.761 265.309 1.00 74.37  ? 1677 SER A OG    1 
ATOM   1150  N  N     . SER A 1 1678 ? 197.445 221.924 263.796 1.00 69.48  ? 1678 SER A N     1 
ATOM   1151  C  CA    . SER A 1 1678 ? 198.618 221.941 262.938 1.00 69.87  ? 1678 SER A CA    1 
ATOM   1152  C  C     . SER A 1 1678 ? 199.199 220.536 262.801 1.00 72.43  ? 1678 SER A C     1 
ATOM   1153  O  O     . SER A 1 1678 ? 198.761 219.584 263.451 1.00 74.47  ? 1678 SER A O     1 
ATOM   1154  C  CB    . SER A 1 1678 ? 199.671 222.902 263.487 1.00 70.87  ? 1678 SER A CB    1 
ATOM   1155  O  OG    . SER A 1 1678 ? 200.235 222.406 264.687 1.00 70.84  ? 1678 SER A OG    1 
ATOM   1156  N  N     . ARG A 1 1679 ? 200.206 220.413 261.932 1.00 78.37  ? 1679 ARG A N     1 
ATOM   1157  C  CA    . ARG A 1 1679 ? 200.844 219.117 261.721 1.00 79.17  ? 1679 ARG A CA    1 
ATOM   1158  C  C     . ARG A 1 1679 ? 201.574 218.639 262.968 1.00 78.01  ? 1679 ARG A C     1 
ATOM   1159  O  O     . ARG A 1 1679 ? 201.726 217.429 263.172 1.00 77.22  ? 1679 ARG A O     1 
ATOM   1160  C  CB    . ARG A 1 1679 ? 201.808 219.190 260.537 1.00 78.12  ? 1679 ARG A CB    1 
ATOM   1161  C  CG    . ARG A 1 1679 ? 201.128 219.374 259.192 1.00 80.33  ? 1679 ARG A CG    1 
ATOM   1162  C  CD    . ARG A 1 1679 ? 202.116 219.232 258.045 1.00 84.25  ? 1679 ARG A CD    1 
ATOM   1163  N  NE    . ARG A 1 1679 ? 203.142 220.268 258.059 1.00 86.35  ? 1679 ARG A NE    1 
ATOM   1164  C  CZ    . ARG A 1 1679 ? 203.020 221.449 257.470 1.00 86.21  ? 1679 ARG A CZ    1 
ATOM   1165  N  NH1   . ARG A 1 1679 ? 201.921 221.785 256.816 1.00 81.08  ? 1679 ARG A NH1   1 
ATOM   1166  N  NH2   . ARG A 1 1679 ? 204.028 222.315 257.538 1.00 84.65  ? 1679 ARG A NH2   1 
ATOM   1167  N  N     . GLU A 1 1680 ? 202.034 219.565 263.809 1.00 76.26  ? 1680 GLU A N     1 
ATOM   1168  C  CA    . GLU A 1 1680 ? 202.738 219.201 265.032 1.00 77.63  ? 1680 GLU A CA    1 
ATOM   1169  C  C     . GLU A 1 1680 ? 201.792 218.869 266.177 1.00 77.69  ? 1680 GLU A C     1 
ATOM   1170  O  O     . GLU A 1 1680 ? 202.263 218.522 267.265 1.00 74.49  ? 1680 GLU A O     1 
ATOM   1171  C  CB    . GLU A 1 1680 ? 203.677 220.332 265.457 1.00 77.10  ? 1680 GLU A CB    1 
ATOM   1172  C  CG    . GLU A 1 1680 ? 204.645 220.784 264.375 1.00 77.34  ? 1680 GLU A CG    1 
ATOM   1173  C  CD    . GLU A 1 1680 ? 204.047 221.836 263.462 1.00 79.05  ? 1680 GLU A CD    1 
ATOM   1174  O  OE1   . GLU A 1 1680 ? 202.925 222.303 263.752 1.00 80.56  ? 1680 GLU A OE1   1 
ATOM   1175  O  OE2   . GLU A 1 1680 ? 204.694 222.192 262.455 1.00 78.38  ? 1680 GLU A OE2   1 
ATOM   1176  N  N     . GLY A 1 1681 ? 200.482 218.974 265.965 1.00 76.64  ? 1681 GLY A N     1 
ATOM   1177  C  CA    . GLY A 1 1681 ? 199.500 218.745 266.995 1.00 76.77  ? 1681 GLY A CA    1 
ATOM   1178  C  C     . GLY A 1 1681 ? 198.987 220.004 267.661 1.00 76.67  ? 1681 GLY A C     1 
ATOM   1179  O  O     . GLY A 1 1681 ? 197.966 219.948 268.356 1.00 77.09  ? 1681 GLY A O     1 
ATOM   1180  N  N     . GLU A 1 1682 ? 199.668 221.131 267.469 1.00 73.60  ? 1682 GLU A N     1 
ATOM   1181  C  CA    . GLU A 1 1682 ? 199.221 222.392 268.042 1.00 70.64  ? 1682 GLU A CA    1 
ATOM   1182  C  C     . GLU A 1 1682 ? 197.901 222.818 267.416 1.00 71.64  ? 1682 GLU A C     1 
ATOM   1183  O  O     . GLU A 1 1682 ? 197.689 222.657 266.212 1.00 74.25  ? 1682 GLU A O     1 
ATOM   1184  C  CB    . GLU A 1 1682 ? 200.284 223.469 267.831 1.00 71.39  ? 1682 GLU A CB    1 
ATOM   1185  C  CG    . GLU A 1 1682 ? 199.983 224.780 268.528 1.00 69.18  ? 1682 GLU A CG    1 
ATOM   1186  C  CD    . GLU A 1 1682 ? 200.975 225.862 268.176 1.00 70.18  ? 1682 GLU A CD    1 
ATOM   1187  O  OE1   . GLU A 1 1682 ? 200.991 226.299 267.007 1.00 69.88  ? 1682 GLU A OE1   1 
ATOM   1188  O  OE2   . GLU A 1 1682 ? 201.741 226.276 269.069 1.00 74.12  ? 1682 GLU A OE2   1 
ATOM   1189  N  N     . GLU A 1 1683 ? 197.016 223.363 268.242 1.00 73.52  ? 1683 GLU A N     1 
ATOM   1190  C  CA    . GLU A 1 1683 ? 195.659 223.681 267.834 1.00 73.44  ? 1683 GLU A CA    1 
ATOM   1191  C  C     . GLU A 1 1683 ? 195.241 225.036 268.389 1.00 75.00  ? 1683 GLU A C     1 
ATOM   1192  O  O     . GLU A 1 1683 ? 195.796 225.524 269.377 1.00 82.72  ? 1683 GLU A O     1 
ATOM   1193  C  CB    . GLU A 1 1683 ? 194.691 222.592 268.308 1.00 74.64  ? 1683 GLU A CB    1 
ATOM   1194  C  CG    . GLU A 1 1683 ? 194.443 222.608 269.800 1.00 77.38  ? 1683 GLU A CG    1 
ATOM   1195  C  CD    . GLU A 1 1683 ? 193.412 221.590 270.230 1.00 83.08  ? 1683 GLU A CD    1 
ATOM   1196  O  OE1   . GLU A 1 1683 ? 192.925 220.833 269.364 1.00 81.04  ? 1683 GLU A OE1   1 
ATOM   1197  O  OE2   . GLU A 1 1683 ? 193.082 221.553 271.434 1.00 82.60  ? 1683 GLU A OE2   1 
ATOM   1198  N  N     . VAL A 1 1684 ? 194.257 225.646 267.733 1.00 73.78  ? 1684 VAL A N     1 
ATOM   1199  C  CA    . VAL A 1 1684 ? 193.637 226.882 268.202 1.00 78.52  ? 1684 VAL A CA    1 
ATOM   1200  C  C     . VAL A 1 1684 ? 192.142 226.600 268.299 1.00 75.84  ? 1684 VAL A C     1 
ATOM   1201  O  O     . VAL A 1 1684 ? 191.564 225.956 267.416 1.00 75.46  ? 1684 VAL A O     1 
ATOM   1202  C  CB    . VAL A 1 1684 ? 193.928 228.085 267.291 1.00 76.79  ? 1684 VAL A CB    1 
ATOM   1203  C  CG1   . VAL A 1 1684 ? 195.427 228.300 267.148 1.00 71.82  ? 1684 VAL A CG1   1 
ATOM   1204  C  CG2   . VAL A 1 1684 ? 193.282 227.932 265.931 1.00 73.54  ? 1684 VAL A CG2   1 
ATOM   1205  N  N     . MET A 1 1685 ? 191.522 227.032 269.392 1.00 76.71  ? 1685 MET A N     1 
ATOM   1206  C  CA    . MET A 1 1685 ? 190.082 226.882 269.545 1.00 76.43  ? 1685 MET A CA    1 
ATOM   1207  C  C     . MET A 1 1685 ? 189.369 228.163 269.141 1.00 78.39  ? 1685 MET A C     1 
ATOM   1208  O  O     . MET A 1 1685 ? 189.709 229.253 269.609 1.00 81.45  ? 1685 MET A O     1 
ATOM   1209  C  CB    . MET A 1 1685 ? 189.736 226.505 270.984 1.00 76.67  ? 1685 MET A CB    1 
ATOM   1210  C  CG    . MET A 1 1685 ? 190.393 225.224 271.466 1.00 79.13  ? 1685 MET A CG    1 
ATOM   1211  S  SD    . MET A 1 1685 ? 189.601 223.762 270.760 1.00 85.27  ? 1685 MET A SD    1 
ATOM   1212  C  CE    . MET A 1 1685 ? 190.704 223.373 269.409 1.00 80.41  ? 1685 MET A CE    1 
ATOM   1213  N  N     . PHE A 1 1686 ? 188.378 228.023 268.266 1.00 71.03  ? 1686 PHE A N     1 
ATOM   1214  C  CA    . PHE A 1 1686 ? 187.641 229.173 267.768 1.00 72.28  ? 1686 PHE A CA    1 
ATOM   1215  C  C     . PHE A 1 1686 ? 186.874 229.844 268.898 1.00 74.49  ? 1686 PHE A C     1 
ATOM   1216  O  O     . PHE A 1 1686 ? 186.324 229.177 269.778 1.00 72.83  ? 1686 PHE A O     1 
ATOM   1217  C  CB    . PHE A 1 1686 ? 186.673 228.742 266.667 1.00 72.21  ? 1686 PHE A CB    1 
ATOM   1218  C  CG    . PHE A 1 1686 ? 187.346 228.268 265.409 1.00 75.50  ? 1686 PHE A CG    1 
ATOM   1219  C  CD1   . PHE A 1 1686 ? 188.705 228.448 265.214 1.00 75.94  ? 1686 PHE A CD1   1 
ATOM   1220  C  CD2   . PHE A 1 1686 ? 186.614 227.634 264.422 1.00 77.27  ? 1686 PHE A CD2   1 
ATOM   1221  C  CE1   . PHE A 1 1686 ? 189.316 228.008 264.059 1.00 74.01  ? 1686 PHE A CE1   1 
ATOM   1222  C  CE2   . PHE A 1 1686 ? 187.221 227.192 263.266 1.00 73.97  ? 1686 PHE A CE2   1 
ATOM   1223  C  CZ    . PHE A 1 1686 ? 188.572 227.380 263.084 1.00 72.89  ? 1686 PHE A CZ    1 
ATOM   1224  N  N     . LYS A 1 1687 ? 186.849 231.178 268.878 1.00 75.67  ? 1687 LYS A N     1 
ATOM   1225  C  CA    . LYS A 1 1687 ? 186.042 231.906 269.851 1.00 75.50  ? 1687 LYS A CA    1 
ATOM   1226  C  C     . LYS A 1 1687 ? 184.563 231.596 269.666 1.00 77.11  ? 1687 LYS A C     1 
ATOM   1227  O  O     . LYS A 1 1687 ? 183.838 231.375 270.643 1.00 78.46  ? 1687 LYS A O     1 
ATOM   1228  C  CB    . LYS A 1 1687 ? 186.298 233.407 269.730 1.00 74.77  ? 1687 LYS A CB    1 
ATOM   1229  C  CG    . LYS A 1 1687 ? 187.742 233.806 269.975 1.00 72.18  ? 1687 LYS A CG    1 
ATOM   1230  C  CD    . LYS A 1 1687 ? 188.270 233.221 271.270 1.00 68.52  ? 1687 LYS A CD    1 
ATOM   1231  C  CE    . LYS A 1 1687 ? 189.379 234.078 271.847 1.00 74.11  ? 1687 LYS A CE    1 
ATOM   1232  N  NZ    . LYS A 1 1687 ? 190.410 233.250 272.527 1.00 75.67  ? 1687 LYS A NZ    1 
ATOM   1233  N  N     . THR A 1 1688 ? 184.101 231.574 268.419 1.00 76.54  ? 1688 THR A N     1 
ATOM   1234  C  CA    . THR A 1 1688 ? 182.733 231.181 268.082 1.00 77.76  ? 1688 THR A CA    1 
ATOM   1235  C  C     . THR A 1 1688 ? 182.791 230.012 267.110 1.00 74.79  ? 1688 THR A C     1 
ATOM   1236  O  O     . THR A 1 1688 ? 183.047 230.215 265.909 1.00 75.26  ? 1688 THR A O     1 
ATOM   1237  C  CB    . THR A 1 1688 ? 181.958 232.348 267.472 1.00 78.18  ? 1688 THR A CB    1 
ATOM   1238  O  OG1   . THR A 1 1688 ? 182.602 232.770 266.264 1.00 76.15  ? 1688 THR A OG1   1 
ATOM   1239  C  CG2   . THR A 1 1688 ? 181.902 233.516 268.445 1.00 75.49  ? 1688 THR A CG2   1 
ATOM   1240  N  N     . PRO A 1 1689 ? 182.576 228.780 267.572 1.00 78.18  ? 1689 PRO A N     1 
ATOM   1241  C  CA    . PRO A 1 1689 ? 182.677 227.625 266.671 1.00 80.03  ? 1689 PRO A CA    1 
ATOM   1242  C  C     . PRO A 1 1689 ? 181.699 227.725 265.509 1.00 77.82  ? 1689 PRO A C     1 
ATOM   1243  O  O     . PRO A 1 1689 ? 180.583 228.228 265.650 1.00 79.95  ? 1689 PRO A O     1 
ATOM   1244  C  CB    . PRO A 1 1689 ? 182.350 226.435 267.579 1.00 80.18  ? 1689 PRO A CB    1 
ATOM   1245  C  CG    . PRO A 1 1689 ? 182.658 226.902 268.955 1.00 79.69  ? 1689 PRO A CG    1 
ATOM   1246  C  CD    . PRO A 1 1689 ? 182.419 228.383 268.981 1.00 76.08  ? 1689 PRO A CD    1 
ATOM   1247  N  N     . VAL A 1 1690 ? 182.135 227.237 264.352 1.00 79.60  ? 1690 VAL A N     1 
ATOM   1248  C  CA    . VAL A 1 1690 ? 181.352 227.310 263.124 1.00 80.18  ? 1690 VAL A CA    1 
ATOM   1249  C  C     . VAL A 1 1690 ? 180.496 226.056 263.008 1.00 80.77  ? 1690 VAL A C     1 
ATOM   1250  O  O     . VAL A 1 1690 ? 181.014 224.934 263.033 1.00 83.78  ? 1690 VAL A O     1 
ATOM   1251  C  CB    . VAL A 1 1690 ? 182.268 227.468 261.900 1.00 81.55  ? 1690 VAL A CB    1 
ATOM   1252  C  CG1   . VAL A 1 1690 ? 181.458 227.419 260.616 1.00 80.40  ? 1690 VAL A CG1   1 
ATOM   1253  C  CG2   . VAL A 1 1690 ? 183.049 228.767 261.995 1.00 81.47  ? 1690 VAL A CG2   1 
ATOM   1254  N  N     . SER A 1 1691 ? 179.188 226.247 262.869 1.00 84.36  ? 1691 SER A N     1 
ATOM   1255  C  CA    . SER A 1 1691 ? 178.228 225.151 262.840 1.00 86.54  ? 1691 SER A CA    1 
ATOM   1256  C  C     . SER A 1 1691 ? 177.946 224.760 261.395 1.00 85.32  ? 1691 SER A C     1 
ATOM   1257  O  O     . SER A 1 1691 ? 177.459 225.580 260.609 1.00 85.53  ? 1691 SER A O     1 
ATOM   1258  C  CB    . SER A 1 1691 ? 176.935 225.546 263.551 1.00 87.54  ? 1691 SER A CB    1 
ATOM   1259  O  OG    . SER A 1 1691 ? 176.467 226.802 263.091 1.00 86.60  ? 1691 SER A OG    1 
ATOM   1260  N  N     . ILE A 1 1692 ? 178.249 223.506 261.052 1.00 84.40  ? 1692 ILE A N     1 
ATOM   1261  C  CA    . ILE A 1 1692 ? 177.986 223.017 259.703 1.00 85.53  ? 1692 ILE A CA    1 
ATOM   1262  C  C     . ILE A 1 1692 ? 176.488 222.886 259.454 1.00 89.19  ? 1692 ILE A C     1 
ATOM   1263  O  O     . ILE A 1 1692 ? 176.020 223.092 258.328 1.00 87.12  ? 1692 ILE A O     1 
ATOM   1264  C  CB    . ILE A 1 1692 ? 178.722 221.684 259.472 1.00 83.44  ? 1692 ILE A CB    1 
ATOM   1265  C  CG1   . ILE A 1 1692 ? 180.218 221.853 259.743 1.00 84.64  ? 1692 ILE A CG1   1 
ATOM   1266  C  CG2   . ILE A 1 1692 ? 178.498 221.178 258.057 1.00 85.80  ? 1692 ILE A CG2   1 
ATOM   1267  C  CD1   . ILE A 1 1692 ? 181.044 220.637 259.393 1.00 85.46  ? 1692 ILE A CD1   1 
ATOM   1268  N  N     . THR A 1 1693 ? 175.713 222.542 260.486 1.00 94.38  ? 1693 THR A N     1 
ATOM   1269  C  CA    . THR A 1 1693 ? 174.272 222.376 260.308 1.00 92.51  ? 1693 THR A CA    1 
ATOM   1270  C  C     . THR A 1 1693 ? 173.605 223.684 259.900 1.00 90.84  ? 1693 THR A C     1 
ATOM   1271  O  O     . THR A 1 1693 ? 172.711 223.692 259.047 1.00 87.75  ? 1693 THR A O     1 
ATOM   1272  C  CB    . THR A 1 1693 ? 173.640 221.833 261.590 1.00 92.90  ? 1693 THR A CB    1 
ATOM   1273  O  OG1   . THR A 1 1693 ? 173.895 222.736 262.673 1.00 92.68  ? 1693 THR A OG1   1 
ATOM   1274  C  CG2   . THR A 1 1693 ? 174.211 220.467 261.926 1.00 89.74  ? 1693 THR A CG2   1 
ATOM   1275  N  N     . GLU A 1 1694 ? 174.019 224.801 260.503 1.00 93.37  ? 1694 GLU A N     1 
ATOM   1276  C  CA    . GLU A 1 1694 ? 173.441 226.090 260.143 1.00 93.33  ? 1694 GLU A CA    1 
ATOM   1277  C  C     . GLU A 1 1694 ? 173.941 226.595 258.796 1.00 95.60  ? 1694 GLU A C     1 
ATOM   1278  O  O     . GLU A 1 1694 ? 173.303 227.471 258.203 1.00 95.31  ? 1694 GLU A O     1 
ATOM   1279  C  CB    . GLU A 1 1694 ? 173.738 227.125 261.229 1.00 92.19  ? 1694 GLU A CB    1 
ATOM   1280  C  CG    . GLU A 1 1694 ? 173.108 226.811 262.576 1.00 94.27  ? 1694 GLU A CG    1 
ATOM   1281  C  CD    . GLU A 1 1694 ? 173.013 228.030 263.474 1.00 96.95  ? 1694 GLU A CD    1 
ATOM   1282  O  OE1   . GLU A 1 1694 ? 173.242 229.153 262.979 1.00 96.45  ? 1694 GLU A OE1   1 
ATOM   1283  O  OE2   . GLU A 1 1694 ? 172.707 227.864 264.674 1.00 95.19  ? 1694 GLU A OE2   1 
ATOM   1284  N  N     . HIS A 1 1695 ? 175.060 226.069 258.303 1.00 92.76  ? 1695 HIS A N     1 
ATOM   1285  C  CA    . HIS A 1 1695 ? 175.625 226.453 257.009 1.00 92.62  ? 1695 HIS A CA    1 
ATOM   1286  C  C     . HIS A 1 1695 ? 175.947 225.188 256.224 1.00 94.97  ? 1695 HIS A C     1 
ATOM   1287  O  O     . HIS A 1 1695 ? 177.113 224.793 256.104 1.00 94.08  ? 1695 HIS A O     1 
ATOM   1288  C  CB    . HIS A 1 1695 ? 176.864 227.328 257.193 1.00 89.38  ? 1695 HIS A CB    1 
ATOM   1289  C  CG    . HIS A 1 1695 ? 176.594 228.602 257.930 1.00 92.89  ? 1695 HIS A CG    1 
ATOM   1290  N  ND1   . HIS A 1 1695 ? 176.170 229.751 257.300 1.00 93.68  ? 1695 HIS A ND1   1 
ATOM   1291  C  CD2   . HIS A 1 1695 ? 176.681 228.906 259.247 1.00 92.20  ? 1695 HIS A CD2   1 
ATOM   1292  C  CE1   . HIS A 1 1695 ? 176.011 230.709 258.195 1.00 90.50  ? 1695 HIS A CE1   1 
ATOM   1293  N  NE2   . HIS A 1 1695 ? 176.315 230.222 259.385 1.00 92.49  ? 1695 HIS A NE2   1 
ATOM   1294  N  N     . PRO A 1 1696 ? 174.925 224.520 255.683 1.00 95.97  ? 1696 PRO A N     1 
ATOM   1295  C  CA    . PRO A 1 1696 ? 175.156 223.209 255.051 1.00 94.08  ? 1696 PRO A CA    1 
ATOM   1296  C  C     . PRO A 1 1696 ? 176.091 223.249 253.854 1.00 92.75  ? 1696 PRO A C     1 
ATOM   1297  O  O     . PRO A 1 1696 ? 176.816 222.274 253.621 1.00 91.57  ? 1696 PRO A O     1 
ATOM   1298  C  CB    . PRO A 1 1696 ? 173.744 222.755 254.645 1.00 93.84  ? 1696 PRO A CB    1 
ATOM   1299  C  CG    . PRO A 1 1696 ? 172.791 223.701 255.316 1.00 93.04  ? 1696 PRO A CG    1 
ATOM   1300  C  CD    . PRO A 1 1696 ? 173.529 224.968 255.561 1.00 92.24  ? 1696 PRO A CD    1 
ATOM   1301  N  N     . LYS A 1 1697 ? 176.094 224.335 253.085 1.00 93.78  ? 1697 LYS A N     1 
ATOM   1302  C  CA    . LYS A 1 1697 ? 176.913 224.394 251.882 1.00 95.26  ? 1697 LYS A CA    1 
ATOM   1303  C  C     . LYS A 1 1697 ? 178.397 224.415 252.232 1.00 95.17  ? 1697 LYS A C     1 
ATOM   1304  O  O     . LYS A 1 1697 ? 178.819 225.076 253.184 1.00 96.40  ? 1697 LYS A O     1 
ATOM   1305  C  CB    . LYS A 1 1697 ? 176.544 225.620 251.048 1.00 94.74  ? 1697 LYS A CB    1 
ATOM   1306  C  CG    . LYS A 1 1697 ? 175.338 225.398 250.148 1.00 94.65  ? 1697 LYS A CG    1 
ATOM   1307  C  CD    . LYS A 1 1697 ? 175.157 226.531 249.154 1.00 93.94  ? 1697 LYS A CD    1 
ATOM   1308  C  CE    . LYS A 1 1697 ? 175.155 227.883 249.847 1.00 93.17  ? 1697 LYS A CE    1 
ATOM   1309  N  NZ    . LYS A 1 1697 ? 174.128 227.955 250.923 1.00 93.06  ? 1697 LYS A NZ    1 
ATOM   1310  N  N     . ILE A 1 1698 ? 179.189 223.685 251.441 1.00 87.29  ? 1698 ILE A N     1 
ATOM   1311  C  CA    . ILE A 1 1698 ? 180.613 223.524 251.730 1.00 88.66  ? 1698 ILE A CA    1 
ATOM   1312  C  C     . ILE A 1 1698 ? 181.334 224.869 251.706 1.00 89.32  ? 1698 ILE A C     1 
ATOM   1313  O  O     . ILE A 1 1698 ? 182.121 225.183 252.611 1.00 91.59  ? 1698 ILE A O     1 
ATOM   1314  C  CB    . ILE A 1 1698 ? 181.238 222.506 250.750 1.00 89.28  ? 1698 ILE A CB    1 
ATOM   1315  C  CG1   . ILE A 1 1698 ? 182.640 222.082 251.199 1.00 84.19  ? 1698 ILE A CG1   1 
ATOM   1316  C  CG2   . ILE A 1 1698 ? 181.215 223.001 249.301 1.00 89.88  ? 1698 ILE A CG2   1 
ATOM   1317  C  CD1   . ILE A 1 1698 ? 182.668 221.310 252.480 1.00 86.05  ? 1698 ILE A CD1   1 
ATOM   1318  N  N     . ASN A 1 1699 ? 181.063 225.693 250.691 1.00 90.20  ? 1699 ASN A N     1 
ATOM   1319  C  CA    . ASN A 1 1699 ? 181.810 226.936 250.529 1.00 90.67  ? 1699 ASN A CA    1 
ATOM   1320  C  C     . ASN A 1 1699 ? 181.544 227.898 251.679 1.00 90.38  ? 1699 ASN A C     1 
ATOM   1321  O  O     . ASN A 1 1699 ? 182.473 228.536 252.187 1.00 89.14  ? 1699 ASN A O     1 
ATOM   1322  C  CB    . ASN A 1 1699 ? 181.472 227.578 249.182 1.00 90.71  ? 1699 ASN A CB    1 
ATOM   1323  C  CG    . ASN A 1 1699 ? 180.043 228.082 249.113 1.00 91.75  ? 1699 ASN A CG    1 
ATOM   1324  O  OD1   . ASN A 1 1699 ? 179.125 227.335 248.776 1.00 89.14  ? 1699 ASN A OD1   1 
ATOM   1325  N  ND2   . ASN A 1 1699 ? 179.850 229.357 249.429 1.00 89.67  ? 1699 ASN A ND2   1 
ATOM   1326  N  N     . GLU A 1 1700 ? 180.287 227.998 252.117 1.00 90.78  ? 1700 GLU A N     1 
ATOM   1327  C  CA    . GLU A 1 1700 ? 179.944 228.943 253.174 1.00 89.21  ? 1700 GLU A CA    1 
ATOM   1328  C  C     . GLU A 1 1700 ? 180.655 228.600 254.476 1.00 88.40  ? 1700 GLU A C     1 
ATOM   1329  O  O     . GLU A 1 1700 ? 181.271 229.468 255.104 1.00 88.78  ? 1700 GLU A O     1 
ATOM   1330  C  CB    . GLU A 1 1700 ? 178.431 228.976 253.381 1.00 90.96  ? 1700 GLU A CB    1 
ATOM   1331  C  CG    . GLU A 1 1700 ? 177.671 229.716 252.295 1.00 91.66  ? 1700 GLU A CG    1 
ATOM   1332  C  CD    . GLU A 1 1700 ? 176.183 229.777 252.570 1.00 94.50  ? 1700 GLU A CD    1 
ATOM   1333  O  OE1   . GLU A 1 1700 ? 175.725 229.106 253.520 1.00 93.68  ? 1700 GLU A OE1   1 
ATOM   1334  O  OE2   . GLU A 1 1700 ? 175.469 230.493 251.836 1.00 92.86  ? 1700 GLU A OE2   1 
ATOM   1335  N  N     . TRP A 1 1701 ? 180.597 227.335 254.896 1.00 82.81  ? 1701 TRP A N     1 
ATOM   1336  C  CA    . TRP A 1 1701 ? 181.204 227.003 256.178 1.00 83.05  ? 1701 TRP A CA    1 
ATOM   1337  C  C     . TRP A 1 1701 ? 182.723 226.912 256.091 1.00 85.37  ? 1701 TRP A C     1 
ATOM   1338  O  O     . TRP A 1 1701 ? 183.397 227.177 257.089 1.00 87.70  ? 1701 TRP A O     1 
ATOM   1339  C  CB    . TRP A 1 1701 ? 180.586 225.724 256.759 1.00 82.57  ? 1701 TRP A CB    1 
ATOM   1340  C  CG    . TRP A 1 1701 ? 181.057 224.420 256.200 1.00 79.49  ? 1701 TRP A CG    1 
ATOM   1341  C  CD1   . TRP A 1 1701 ? 180.415 223.652 255.277 1.00 78.78  ? 1701 TRP A CD1   1 
ATOM   1342  C  CD2   . TRP A 1 1701 ? 182.236 223.696 256.572 1.00 80.21  ? 1701 TRP A CD2   1 
ATOM   1343  N  NE1   . TRP A 1 1701 ? 181.131 222.510 255.030 1.00 80.08  ? 1701 TRP A NE1   1 
ATOM   1344  C  CE2   . TRP A 1 1701 ? 182.256 222.512 255.811 1.00 80.62  ? 1701 TRP A CE2   1 
ATOM   1345  C  CE3   . TRP A 1 1701 ? 183.285 223.941 257.462 1.00 82.50  ? 1701 TRP A CE3   1 
ATOM   1346  C  CZ2   . TRP A 1 1701 ? 183.281 221.576 255.913 1.00 80.80  ? 1701 TRP A CZ2   1 
ATOM   1347  C  CZ3   . TRP A 1 1701 ? 184.302 223.011 257.561 1.00 81.06  ? 1701 TRP A CZ3   1 
ATOM   1348  C  CH2   . TRP A 1 1701 ? 184.293 221.843 256.792 1.00 80.03  ? 1701 TRP A CH2   1 
ATOM   1349  N  N     . LEU A 1 1702 ? 183.297 226.593 254.925 1.00 79.15  ? 1702 LEU A N     1 
ATOM   1350  C  CA    . LEU A 1 1702 ? 184.748 226.729 254.798 1.00 77.74  ? 1702 LEU A CA    1 
ATOM   1351  C  C     . LEU A 1 1702 ? 185.185 228.188 254.894 1.00 80.59  ? 1702 LEU A C     1 
ATOM   1352  O  O     . LEU A 1 1702 ? 186.195 228.500 255.543 1.00 83.32  ? 1702 LEU A O     1 
ATOM   1353  C  CB    . LEU A 1 1702 ? 185.241 226.106 253.493 1.00 79.64  ? 1702 LEU A CB    1 
ATOM   1354  C  CG    . LEU A 1 1702 ? 185.144 224.587 253.381 1.00 82.38  ? 1702 LEU A CG    1 
ATOM   1355  C  CD1   . LEU A 1 1702 ? 185.536 224.137 251.989 1.00 81.51  ? 1702 LEU A CD1   1 
ATOM   1356  C  CD2   . LEU A 1 1702 ? 186.038 223.937 254.421 1.00 79.49  ? 1702 LEU A CD2   1 
ATOM   1357  N  N     . THR A 1 1703 ? 184.441 229.098 254.259 1.00 81.12  ? 1703 THR A N     1 
ATOM   1358  C  CA    . THR A 1 1703 ? 184.758 230.517 254.374 1.00 80.33  ? 1703 THR A CA    1 
ATOM   1359  C  C     . THR A 1 1703 ? 184.627 230.989 255.815 1.00 80.28  ? 1703 THR A C     1 
ATOM   1360  O  O     . THR A 1 1703 ? 185.459 231.763 256.304 1.00 83.81  ? 1703 THR A O     1 
ATOM   1361  C  CB    . THR A 1 1703 ? 183.847 231.335 253.458 1.00 80.00  ? 1703 THR A CB    1 
ATOM   1362  O  OG1   . THR A 1 1703 ? 184.016 230.904 252.102 1.00 83.64  ? 1703 THR A OG1   1 
ATOM   1363  C  CG2   . THR A 1 1703 ? 184.179 232.815 253.556 1.00 78.17  ? 1703 THR A CG2   1 
ATOM   1364  N  N     . LEU A 1 1704 ? 183.586 230.528 256.511 1.00 77.87  ? 1704 LEU A N     1 
ATOM   1365  C  CA    . LEU A 1 1704 ? 183.423 230.882 257.917 1.00 76.18  ? 1704 LEU A CA    1 
ATOM   1366  C  C     . LEU A 1 1704 ? 184.547 230.309 258.769 1.00 75.21  ? 1704 LEU A C     1 
ATOM   1367  O  O     . LEU A 1 1704 ? 184.996 230.955 259.717 1.00 78.08  ? 1704 LEU A O     1 
ATOM   1368  C  CB    . LEU A 1 1704 ? 182.062 230.412 258.426 1.00 78.00  ? 1704 LEU A CB    1 
ATOM   1369  C  CG    . LEU A 1 1704 ? 180.856 231.107 257.794 1.00 80.28  ? 1704 LEU A CG    1 
ATOM   1370  C  CD1   . LEU A 1 1704 ? 179.565 230.472 258.264 1.00 79.06  ? 1704 LEU A CD1   1 
ATOM   1371  C  CD2   . LEU A 1 1704 ? 180.869 232.593 258.108 1.00 76.85  ? 1704 LEU A CD2   1 
ATOM   1372  N  N     . VAL A 1 1705 ? 185.014 229.100 258.449 1.00 72.25  ? 1705 VAL A N     1 
ATOM   1373  C  CA    . VAL A 1 1705 ? 186.131 228.515 259.185 1.00 72.40  ? 1705 VAL A CA    1 
ATOM   1374  C  C     . VAL A 1 1705 ? 187.386 229.357 259.007 1.00 72.10  ? 1705 VAL A C     1 
ATOM   1375  O  O     . VAL A 1 1705 ? 188.108 229.629 259.972 1.00 74.24  ? 1705 VAL A O     1 
ATOM   1376  C  CB    . VAL A 1 1705 ? 186.358 227.056 258.746 1.00 71.20  ? 1705 VAL A CB    1 
ATOM   1377  C  CG1   . VAL A 1 1705 ? 187.758 226.597 259.119 1.00 72.42  ? 1705 VAL A CG1   1 
ATOM   1378  C  CG2   . VAL A 1 1705 ? 185.323 226.148 259.382 1.00 73.39  ? 1705 VAL A CG2   1 
ATOM   1379  N  N     . GLU A 1 1706 ? 187.666 229.787 257.775 1.00 71.51  ? 1706 GLU A N     1 
ATOM   1380  C  CA    . GLU A 1 1706 ? 188.836 230.634 257.541 1.00 72.02  ? 1706 GLU A CA    1 
ATOM   1381  C  C     . GLU A 1 1706 ? 188.710 231.975 258.265 1.00 72.78  ? 1706 GLU A C     1 
ATOM   1382  O  O     . GLU A 1 1706 ? 189.661 232.439 258.919 1.00 73.76  ? 1706 GLU A O     1 
ATOM   1383  C  CB    . GLU A 1 1706 ? 189.028 230.847 256.040 1.00 72.08  ? 1706 GLU A CB    1 
ATOM   1384  C  CG    . GLU A 1 1706 ? 190.122 231.835 255.679 1.00 75.63  ? 1706 GLU A CG    1 
ATOM   1385  C  CD    . GLU A 1 1706 ? 190.028 232.305 254.240 1.00 75.85  ? 1706 GLU A CD    1 
ATOM   1386  O  OE1   . GLU A 1 1706 ? 189.040 232.986 253.897 1.00 75.93  ? 1706 GLU A OE1   1 
ATOM   1387  O  OE2   . GLU A 1 1706 ? 190.943 231.992 253.451 1.00 76.58  ? 1706 GLU A OE2   1 
ATOM   1388  N  N     . LYS A 1 1707 ? 187.539 232.606 258.169 1.00 70.42  ? 1707 LYS A N     1 
ATOM   1389  C  CA    . LYS A 1 1707 ? 187.327 233.890 258.827 1.00 69.36  ? 1707 LYS A CA    1 
ATOM   1390  C  C     . LYS A 1 1707 ? 187.464 233.759 260.338 1.00 72.42  ? 1707 LYS A C     1 
ATOM   1391  O  O     . LYS A 1 1707 ? 188.070 234.612 260.996 1.00 75.60  ? 1707 LYS A O     1 
ATOM   1392  C  CB    . LYS A 1 1707 ? 185.952 234.444 258.453 1.00 69.95  ? 1707 LYS A CB    1 
ATOM   1393  C  CG    . LYS A 1 1707 ? 185.533 235.667 259.248 1.00 72.75  ? 1707 LYS A CG    1 
ATOM   1394  C  CD    . LYS A 1 1707 ? 184.138 236.125 258.854 1.00 73.12  ? 1707 LYS A CD    1 
ATOM   1395  C  CE    . LYS A 1 1707 ? 183.708 237.340 259.659 1.00 72.66  ? 1707 LYS A CE    1 
ATOM   1396  N  NZ    . LYS A 1 1707 ? 183.527 237.017 261.102 1.00 69.52  ? 1707 LYS A NZ    1 
ATOM   1397  N  N     . GLU A 1 1708 ? 186.915 232.684 260.908 1.00 70.95  ? 1708 GLU A N     1 
ATOM   1398  C  CA    . GLU A 1 1708 ? 187.005 232.483 262.347 1.00 66.79  ? 1708 GLU A CA    1 
ATOM   1399  C  C     . GLU A 1 1708 ? 188.420 232.132 262.775 1.00 66.55  ? 1708 GLU A C     1 
ATOM   1400  O  O     . GLU A 1 1708 ? 188.835 232.497 263.875 1.00 72.95  ? 1708 GLU A O     1 
ATOM   1401  C  CB    . GLU A 1 1708 ? 186.025 231.398 262.789 1.00 68.84  ? 1708 GLU A CB    1 
ATOM   1402  C  CG    . GLU A 1 1708 ? 185.904 231.271 264.294 1.00 73.95  ? 1708 GLU A CG    1 
ATOM   1403  C  CD    . GLU A 1 1708 ? 185.601 232.593 264.972 1.00 76.11  ? 1708 GLU A CD    1 
ATOM   1404  O  OE1   . GLU A 1 1708 ? 184.774 233.365 264.443 1.00 73.72  ? 1708 GLU A OE1   1 
ATOM   1405  O  OE2   . GLU A 1 1708 ? 186.197 232.864 266.035 1.00 73.97  ? 1708 GLU A OE2   1 
ATOM   1406  N  N     . MET A 1 1709 ? 189.172 231.423 261.930 1.00 63.17  ? 1709 MET A N     1 
ATOM   1407  C  CA    . MET A 1 1709 ? 190.600 231.251 262.173 1.00 63.04  ? 1709 MET A CA    1 
ATOM   1408  C  C     . MET A 1 1709 ? 191.286 232.595 262.345 1.00 68.37  ? 1709 MET A C     1 
ATOM   1409  O  O     . MET A 1 1709 ? 191.989 232.827 263.339 1.00 69.85  ? 1709 MET A O     1 
ATOM   1410  C  CB    . MET A 1 1709 ? 191.237 230.493 261.011 1.00 67.44  ? 1709 MET A CB    1 
ATOM   1411  C  CG    . MET A 1 1709 ? 192.718 230.217 261.181 1.00 69.42  ? 1709 MET A CG    1 
ATOM   1412  S  SD    . MET A 1 1709 ? 193.397 229.306 259.782 1.00 79.68  ? 1709 MET A SD    1 
ATOM   1413  C  CE    . MET A 1 1709 ? 193.384 230.573 258.517 1.00 60.94  ? 1709 MET A CE    1 
ATOM   1414  N  N     . ARG A 1 1710 ? 191.080 233.498 261.386 1.00 68.11  ? 1710 ARG A N     1 
ATOM   1415  C  CA    . ARG A 1 1710 ? 191.712 234.812 261.472 1.00 60.85  ? 1710 ARG A CA    1 
ATOM   1416  C  C     . ARG A 1 1710 ? 191.257 235.566 262.718 1.00 63.84  ? 1710 ARG A C     1 
ATOM   1417  O  O     . ARG A 1 1710 ? 192.080 236.154 263.433 1.00 66.54  ? 1710 ARG A O     1 
ATOM   1418  C  CB    . ARG A 1 1710 ? 191.413 235.613 260.207 1.00 60.16  ? 1710 ARG A CB    1 
ATOM   1419  C  CG    . ARG A 1 1710 ? 192.112 235.072 258.971 1.00 63.12  ? 1710 ARG A CG    1 
ATOM   1420  C  CD    . ARG A 1 1710 ? 192.154 236.100 257.859 1.00 64.59  ? 1710 ARG A CD    1 
ATOM   1421  N  NE    . ARG A 1 1710 ? 191.288 235.728 256.747 1.00 68.88  ? 1710 ARG A NE    1 
ATOM   1422  C  CZ    . ARG A 1 1710 ? 190.249 236.440 256.334 1.00 70.74  ? 1710 ARG A CZ    1 
ATOM   1423  N  NH1   . ARG A 1 1710 ? 189.905 237.570 256.928 1.00 67.57  ? 1710 ARG A NH1   1 
ATOM   1424  N  NH2   . ARG A 1 1710 ? 189.535 236.005 255.299 1.00 64.53  ? 1710 ARG A NH2   1 
ATOM   1425  N  N     . VAL A 1 1711 ? 189.955 235.537 263.008 1.00 64.72  ? 1711 VAL A N     1 
ATOM   1426  C  CA    . VAL A 1 1711 ? 189.422 236.290 264.141 1.00 63.58  ? 1711 VAL A CA    1 
ATOM   1427  C  C     . VAL A 1 1711 ? 189.965 235.748 265.458 1.00 61.76  ? 1711 VAL A C     1 
ATOM   1428  O  O     . VAL A 1 1711 ? 190.381 236.516 266.333 1.00 67.50  ? 1711 VAL A O     1 
ATOM   1429  C  CB    . VAL A 1 1711 ? 187.884 236.286 264.116 1.00 65.56  ? 1711 VAL A CB    1 
ATOM   1430  C  CG1   . VAL A 1 1711 ? 187.336 236.975 265.351 1.00 69.22  ? 1711 VAL A CG1   1 
ATOM   1431  C  CG2   . VAL A 1 1711 ? 187.381 236.992 262.871 1.00 59.38  ? 1711 VAL A CG2   1 
ATOM   1432  N  N     . THR A 1 1712 ? 189.968 234.422 265.627 1.00 57.53  ? 1712 THR A N     1 
ATOM   1433  C  CA    . THR A 1 1712 ? 190.439 233.853 266.883 1.00 59.38  ? 1712 THR A CA    1 
ATOM   1434  C  C     . THR A 1 1712 ? 191.935 234.060 267.057 1.00 63.88  ? 1712 THR A C     1 
ATOM   1435  O  O     . THR A 1 1712 ? 192.397 234.279 268.181 1.00 71.04  ? 1712 THR A O     1 
ATOM   1436  C  CB    . THR A 1 1712 ? 190.076 232.367 266.983 1.00 55.98  ? 1712 THR A CB    1 
ATOM   1437  O  OG1   . THR A 1 1712 ? 190.324 231.907 268.317 1.00 65.17  ? 1712 THR A OG1   1 
ATOM   1438  C  CG2   . THR A 1 1712 ? 190.891 231.522 266.023 1.00 58.62  ? 1712 THR A CG2   1 
ATOM   1439  N  N     . LEU A 1 1713 ? 192.708 234.029 265.966 1.00 59.03  ? 1713 LEU A N     1 
ATOM   1440  C  CA    . LEU A 1 1713 ? 194.116 234.379 266.084 1.00 54.30  ? 1713 LEU A CA    1 
ATOM   1441  C  C     . LEU A 1 1713 ? 194.300 235.831 266.498 1.00 59.57  ? 1713 LEU A C     1 
ATOM   1442  O  O     . LEU A 1 1713 ? 195.181 236.128 267.311 1.00 63.71  ? 1713 LEU A O     1 
ATOM   1443  C  CB    . LEU A 1 1713 ? 194.847 234.100 264.773 1.00 57.76  ? 1713 LEU A CB    1 
ATOM   1444  C  CG    . LEU A 1 1713 ? 195.114 232.624 264.484 1.00 55.89  ? 1713 LEU A CG    1 
ATOM   1445  C  CD1   . LEU A 1 1713 ? 195.619 232.444 263.070 1.00 59.86  ? 1713 LEU A CD1   1 
ATOM   1446  C  CD2   . LEU A 1 1713 ? 196.111 232.066 265.481 1.00 55.76  ? 1713 LEU A CD2   1 
ATOM   1447  N  N     . ALA A 1 1714 ? 193.475 236.741 265.974 1.00 57.84  ? 1714 ALA A N     1 
ATOM   1448  C  CA    . ALA A 1 1714 ? 193.564 238.139 266.392 1.00 55.95  ? 1714 ALA A CA    1 
ATOM   1449  C  C     . ALA A 1 1714 ? 193.243 238.307 267.874 1.00 62.75  ? 1714 ALA A C     1 
ATOM   1450  O  O     . ALA A 1 1714 ? 193.951 239.026 268.591 1.00 61.18  ? 1714 ALA A O     1 
ATOM   1451  C  CB    . ALA A 1 1714 ? 192.630 239.000 265.547 1.00 55.83  ? 1714 ALA A CB    1 
ATOM   1452  N  N     . LYS A 1 1715 ? 192.176 237.660 268.353 1.00 59.63  ? 1715 LYS A N     1 
ATOM   1453  C  CA    . LYS A 1 1715 ? 191.820 237.784 269.767 1.00 52.70  ? 1715 LYS A CA    1 
ATOM   1454  C  C     . LYS A 1 1715 ? 192.890 237.175 270.666 1.00 55.60  ? 1715 LYS A C     1 
ATOM   1455  O  O     . LYS A 1 1715 ? 193.244 237.750 271.707 1.00 62.27  ? 1715 LYS A O     1 
ATOM   1456  C  CB    . LYS A 1 1715 ? 190.463 237.136 270.042 1.00 56.54  ? 1715 LYS A CB    1 
ATOM   1457  C  CG    . LYS A 1 1715 ? 189.403 237.412 268.994 1.00 63.28  ? 1715 LYS A CG    1 
ATOM   1458  C  CD    . LYS A 1 1715 ? 188.538 238.606 269.348 1.00 62.60  ? 1715 LYS A CD    1 
ATOM   1459  C  CE    . LYS A 1 1715 ? 187.134 238.442 268.788 1.00 60.59  ? 1715 LYS A CE    1 
ATOM   1460  N  NZ    . LYS A 1 1715 ? 186.364 239.715 268.821 1.00 63.94  ? 1715 LYS A NZ    1 
ATOM   1461  N  N     . LEU A 1 1716 ? 193.413 236.007 270.284 1.00 52.49  ? 1716 LEU A N     1 
ATOM   1462  C  CA    . LEU A 1 1716 ? 194.482 235.390 271.053 1.00 54.32  ? 1716 LEU A CA    1 
ATOM   1463  C  C     . LEU A 1 1716 ? 195.725 236.265 271.072 1.00 57.65  ? 1716 LEU A C     1 
ATOM   1464  O  O     . LEU A 1 1716 ? 196.400 236.359 272.103 1.00 62.03  ? 1716 LEU A O     1 
ATOM   1465  C  CB    . LEU A 1 1716 ? 194.805 234.012 270.480 1.00 56.57  ? 1716 LEU A CB    1 
ATOM   1466  C  CG    . LEU A 1 1716 ? 193.842 232.873 270.813 1.00 54.00  ? 1716 LEU A CG    1 
ATOM   1467  C  CD1   . LEU A 1 1716 ? 194.300 231.588 270.149 1.00 53.02  ? 1716 LEU A CD1   1 
ATOM   1468  C  CD2   . LEU A 1 1716 ? 193.735 232.693 272.314 1.00 59.49  ? 1716 LEU A CD2   1 
ATOM   1469  N  N     . LEU A 1 1717 ? 196.042 236.917 269.950 1.00 51.76  ? 1717 LEU A N     1 
ATOM   1470  C  CA    . LEU A 1 1717 ? 197.162 237.849 269.934 1.00 51.99  ? 1717 LEU A CA    1 
ATOM   1471  C  C     . LEU A 1 1717 ? 196.910 239.029 270.860 1.00 54.64  ? 1717 LEU A C     1 
ATOM   1472  O  O     . LEU A 1 1717 ? 197.829 239.491 271.539 1.00 60.79  ? 1717 LEU A O     1 
ATOM   1473  C  CB    . LEU A 1 1717 ? 197.431 238.338 268.513 1.00 55.26  ? 1717 LEU A CB    1 
ATOM   1474  C  CG    . LEU A 1 1717 ? 198.483 239.447 268.422 1.00 54.37  ? 1717 LEU A CG    1 
ATOM   1475  C  CD1   . LEU A 1 1717 ? 199.842 238.930 268.857 1.00 47.65  ? 1717 LEU A CD1   1 
ATOM   1476  C  CD2   . LEU A 1 1717 ? 198.545 240.030 267.024 1.00 53.97  ? 1717 LEU A CD2   1 
ATOM   1477  N  N     . ALA A 1 1718 ? 195.678 239.539 270.893 1.00 57.80  ? 1718 ALA A N     1 
ATOM   1478  C  CA    . ALA A 1 1718 ? 195.373 240.645 271.797 1.00 56.08  ? 1718 ALA A CA    1 
ATOM   1479  C  C     . ALA A 1 1718 ? 195.597 240.248 273.251 1.00 62.39  ? 1718 ALA A C     1 
ATOM   1480  O  O     . ALA A 1 1718 ? 196.233 240.985 274.018 1.00 62.48  ? 1718 ALA A O     1 
ATOM   1481  C  CB    . ALA A 1 1718 ? 193.937 241.118 271.583 1.00 52.78  ? 1718 ALA A CB    1 
ATOM   1482  N  N     . GLU A 1 1719 ? 195.099 239.073 273.645 1.00 62.41  ? 1719 GLU A N     1 
ATOM   1483  C  CA    . GLU A 1 1719 ? 195.300 238.615 275.019 1.00 57.88  ? 1719 GLU A CA    1 
ATOM   1484  C  C     . GLU A 1 1719 ? 196.778 238.379 275.321 1.00 60.43  ? 1719 GLU A C     1 
ATOM   1485  O  O     . GLU A 1 1719 ? 197.271 238.754 276.396 1.00 63.55  ? 1719 GLU A O     1 
ATOM   1486  C  CB    . GLU A 1 1719 ? 194.490 237.346 275.277 1.00 55.15  ? 1719 GLU A CB    1 
ATOM   1487  C  CG    . GLU A 1 1719 ? 193.036 237.439 274.850 1.00 60.58  ? 1719 GLU A CG    1 
ATOM   1488  C  CD    . GLU A 1 1719 ? 192.342 236.092 274.850 1.00 68.88  ? 1719 GLU A CD    1 
ATOM   1489  O  OE1   . GLU A 1 1719 ? 192.919 235.127 275.394 1.00 65.60  ? 1719 GLU A OE1   1 
ATOM   1490  O  OE2   . GLU A 1 1719 ? 191.223 235.998 274.303 1.00 60.66  ? 1719 GLU A OE2   1 
ATOM   1491  N  N     . SER A 1 1720 ? 197.502 237.759 274.386 1.00 57.41  ? 1720 SER A N     1 
ATOM   1492  C  CA    . SER A 1 1720 ? 198.918 237.486 274.603 1.00 54.92  ? 1720 SER A CA    1 
ATOM   1493  C  C     . SER A 1 1720 ? 199.719 238.777 274.705 1.00 54.75  ? 1720 SER A C     1 
ATOM   1494  O  O     . SER A 1 1720 ? 200.666 238.863 275.491 1.00 56.47  ? 1720 SER A O     1 
ATOM   1495  C  CB    . SER A 1 1720 ? 199.456 236.602 273.481 1.00 59.35  ? 1720 SER A CB    1 
ATOM   1496  O  OG    . SER A 1 1720 ? 200.855 236.424 273.598 1.00 62.50  ? 1720 SER A OG    1 
ATOM   1497  N  N     . VAL A 1 1721 ? 199.362 239.785 273.908 1.00 57.64  ? 1721 VAL A N     1 
ATOM   1498  C  CA    . VAL A 1 1721 ? 200.023 241.081 273.993 1.00 57.37  ? 1721 VAL A CA    1 
ATOM   1499  C  C     . VAL A 1 1721 ? 199.740 241.731 275.338 1.00 62.76  ? 1721 VAL A C     1 
ATOM   1500  O  O     . VAL A 1 1721 ? 200.638 242.305 275.964 1.00 64.12  ? 1721 VAL A O     1 
ATOM   1501  C  CB    . VAL A 1 1721 ? 199.582 241.979 272.823 1.00 56.96  ? 1721 VAL A CB    1 
ATOM   1502  C  CG1   . VAL A 1 1721 ? 199.885 243.437 273.122 1.00 60.81  ? 1721 VAL A CG1   1 
ATOM   1503  C  CG2   . VAL A 1 1721 ? 200.269 241.546 271.545 1.00 61.07  ? 1721 VAL A CG2   1 
ATOM   1504  N  N     . THR A 1 1722 ? 198.493 241.641 275.808 1.00 67.05  ? 1722 THR A N     1 
ATOM   1505  C  CA    . THR A 1 1722 ? 198.164 242.187 277.121 1.00 63.96  ? 1722 THR A CA    1 
ATOM   1506  C  C     . THR A 1 1722 ? 199.006 241.538 278.212 1.00 63.65  ? 1722 THR A C     1 
ATOM   1507  O  O     . THR A 1 1722 ? 199.493 242.220 279.121 1.00 67.84  ? 1722 THR A O     1 
ATOM   1508  C  CB    . THR A 1 1722 ? 196.674 242.003 277.407 1.00 64.85  ? 1722 THR A CB    1 
ATOM   1509  O  OG1   . THR A 1 1722 ? 195.913 242.864 276.552 1.00 66.91  ? 1722 THR A OG1   1 
ATOM   1510  C  CG2   . THR A 1 1722 ? 196.358 242.337 278.855 1.00 62.88  ? 1722 THR A CG2   1 
ATOM   1511  N  N     . GLU A 1 1723 ? 199.204 240.221 278.129 1.00 68.91  ? 1723 GLU A N     1 
ATOM   1512  C  CA    . GLU A 1 1723 ? 199.994 239.538 279.154 1.00 66.68  ? 1723 GLU A CA    1 
ATOM   1513  C  C     . GLU A 1 1723 ? 201.483 239.863 279.037 1.00 67.57  ? 1723 GLU A C     1 
ATOM   1514  O  O     . GLU A 1 1723 ? 202.152 240.122 280.048 1.00 69.68  ? 1723 GLU A O     1 
ATOM   1515  C  CB    . GLU A 1 1723 ? 199.758 238.031 279.076 1.00 65.19  ? 1723 GLU A CB    1 
ATOM   1516  C  CG    . GLU A 1 1723 ? 198.358 237.620 279.500 1.00 67.48  ? 1723 GLU A CG    1 
ATOM   1517  C  CD    . GLU A 1 1723 ? 198.152 236.121 279.475 1.00 74.81  ? 1723 GLU A CD    1 
ATOM   1518  O  OE1   . GLU A 1 1723 ? 198.990 235.396 280.050 1.00 75.79  ? 1723 GLU A OE1   1 
ATOM   1519  O  OE2   . GLU A 1 1723 ? 197.148 235.669 278.886 1.00 73.90  ? 1723 GLU A OE2   1 
ATOM   1520  N  N     . VAL A 1 1724 ? 202.027 239.856 277.818 1.00 68.45  ? 1724 VAL A N     1 
ATOM   1521  C  CA    . VAL A 1 1724 ? 203.455 240.104 277.651 1.00 65.20  ? 1724 VAL A CA    1 
ATOM   1522  C  C     . VAL A 1 1724 ? 203.795 241.553 277.975 1.00 71.94  ? 1724 VAL A C     1 
ATOM   1523  O  O     . VAL A 1 1724 ? 204.937 241.862 278.339 1.00 71.89  ? 1724 VAL A O     1 
ATOM   1524  C  CB    . VAL A 1 1724 ? 203.910 239.714 276.231 1.00 63.46  ? 1724 VAL A CB    1 
ATOM   1525  C  CG1   . VAL A 1 1724 ? 203.424 240.725 275.211 1.00 68.37  ? 1724 VAL A CG1   1 
ATOM   1526  C  CG2   . VAL A 1 1724 ? 205.422 239.569 276.174 1.00 66.03  ? 1724 VAL A CG2   1 
ATOM   1527  N  N     . GLU A 1 1725 ? 202.825 242.466 277.854 1.00 78.41  ? 1725 GLU A N     1 
ATOM   1528  C  CA    . GLU A 1 1725 ? 203.046 243.834 278.305 1.00 76.53  ? 1725 GLU A CA    1 
ATOM   1529  C  C     . GLU A 1 1725 ? 203.290 243.884 279.806 1.00 79.86  ? 1725 GLU A C     1 
ATOM   1530  O  O     . GLU A 1 1725 ? 204.135 244.657 280.272 1.00 81.24  ? 1725 GLU A O     1 
ATOM   1531  C  CB    . GLU A 1 1725 ? 201.853 244.710 277.926 1.00 75.95  ? 1725 GLU A CB    1 
ATOM   1532  C  CG    . GLU A 1 1725 ? 202.020 246.176 278.282 1.00 83.16  ? 1725 GLU A CG    1 
ATOM   1533  C  CD    . GLU A 1 1725 ? 200.839 247.021 277.846 1.00 85.49  ? 1725 GLU A CD    1 
ATOM   1534  O  OE1   . GLU A 1 1725 ? 199.878 246.457 277.283 1.00 81.47  ? 1725 GLU A OE1   1 
ATOM   1535  O  OE2   . GLU A 1 1725 ? 200.875 248.250 278.064 1.00 85.67  ? 1725 GLU A OE2   1 
ATOM   1536  N  N     . ILE A 1 1726 ? 202.558 243.075 280.572 1.00 76.16  ? 1726 ILE A N     1 
ATOM   1537  C  CA    . ILE A 1 1726 ? 202.871 242.900 281.986 1.00 73.03  ? 1726 ILE A CA    1 
ATOM   1538  C  C     . ILE A 1 1726 ? 204.254 242.285 282.144 1.00 72.50  ? 1726 ILE A C     1 
ATOM   1539  O  O     . ILE A 1 1726 ? 205.041 242.702 283.002 1.00 72.87  ? 1726 ILE A O     1 
ATOM   1540  C  CB    . ILE A 1 1726 ? 201.786 242.049 282.669 1.00 75.88  ? 1726 ILE A CB    1 
ATOM   1541  C  CG1   . ILE A 1 1726 ? 200.594 242.920 283.063 1.00 74.11  ? 1726 ILE A CG1   1 
ATOM   1542  C  CG2   . ILE A 1 1726 ? 202.349 241.329 283.884 1.00 74.41  ? 1726 ILE A CG2   1 
ATOM   1543  C  CD1   . ILE A 1 1726 ? 199.316 242.141 283.272 1.00 74.88  ? 1726 ILE A CD1   1 
ATOM   1544  N  N     . PHE A 1 1727 ? 204.576 241.286 281.316 1.00 80.83  ? 1727 PHE A N     1 
ATOM   1545  C  CA    . PHE A 1 1727 ? 205.914 240.701 281.364 1.00 79.61  ? 1727 PHE A CA    1 
ATOM   1546  C  C     . PHE A 1 1727 ? 206.985 241.707 280.969 1.00 77.18  ? 1727 PHE A C     1 
ATOM   1547  O  O     . PHE A 1 1727 ? 208.140 241.581 281.391 1.00 76.40  ? 1727 PHE A O     1 
ATOM   1548  C  CB    . PHE A 1 1727 ? 205.988 239.466 280.471 1.00 76.14  ? 1727 PHE A CB    1 
ATOM   1549  C  CG    . PHE A 1 1727 ? 205.426 238.239 281.108 1.00 72.65  ? 1727 PHE A CG    1 
ATOM   1550  C  CD1   . PHE A 1 1727 ? 205.606 238.009 282.460 1.00 74.60  ? 1727 PHE A CD1   1 
ATOM   1551  C  CD2   . PHE A 1 1727 ? 204.705 237.324 280.368 1.00 69.28  ? 1727 PHE A CD2   1 
ATOM   1552  C  CE1   . PHE A 1 1727 ? 205.086 236.885 283.059 1.00 77.63  ? 1727 PHE A CE1   1 
ATOM   1553  C  CE2   . PHE A 1 1727 ? 204.183 236.202 280.963 1.00 77.64  ? 1727 PHE A CE2   1 
ATOM   1554  C  CZ    . PHE A 1 1727 ? 204.373 235.980 282.309 1.00 79.93  ? 1727 PHE A CZ    1 
ATOM   1555  N  N     . GLY A 1 1728 ? 206.629 242.702 280.165 1.00 81.18  ? 1728 GLY A N     1 
ATOM   1556  C  CA    . GLY A 1 1728 ? 207.530 243.795 279.882 1.00 80.00  ? 1728 GLY A CA    1 
ATOM   1557  C  C     . GLY A 1 1728 ? 207.608 244.751 281.057 1.00 86.39  ? 1728 GLY A C     1 
ATOM   1558  O  O     . GLY A 1 1728 ? 207.005 244.549 282.111 1.00 86.02  ? 1728 GLY A O     1 
ATOM   1559  N  N     . LYS A 1 1729 ? 208.385 245.821 280.857 1.00 89.85  ? 1729 LYS A N     1 
ATOM   1560  C  CA    . LYS A 1 1729 ? 208.612 246.886 281.834 1.00 89.13  ? 1729 LYS A CA    1 
ATOM   1561  C  C     . LYS A 1 1729 ? 208.753 246.356 283.260 1.00 88.81  ? 1729 LYS A C     1 
ATOM   1562  O  O     . LYS A 1 1729 ? 208.214 246.942 284.205 1.00 88.51  ? 1729 LYS A O     1 
ATOM   1563  C  CB    . LYS A 1 1729 ? 207.499 247.945 281.752 1.00 85.80  ? 1729 LYS A CB    1 
ATOM   1564  C  CG    . LYS A 1 1729 ? 206.077 247.455 281.999 1.00 86.76  ? 1729 LYS A CG    1 
ATOM   1565  C  CD    . LYS A 1 1729 ? 205.083 248.601 282.023 1.00 89.52  ? 1729 LYS A CD    1 
ATOM   1566  C  CE    . LYS A 1 1729 ? 203.663 248.087 282.196 1.00 90.75  ? 1729 LYS A CE    1 
ATOM   1567  N  NZ    . LYS A 1 1729 ? 203.214 248.155 283.615 1.00 90.59  ? 1729 LYS A NZ    1 
ATOM   1568  N  N     . ALA A 1 1730 ? 209.484 245.255 283.423 1.00 83.25  ? 1730 ALA A N     1 
ATOM   1569  C  CA    . ALA A 1 1730 ? 209.677 244.621 284.719 1.00 82.90  ? 1730 ALA A CA    1 
ATOM   1570  C  C     . ALA A 1 1730 ? 211.160 244.393 284.966 1.00 85.69  ? 1730 ALA A C     1 
ATOM   1571  O  O     . ALA A 1 1730 ? 211.891 243.972 284.065 1.00 84.68  ? 1730 ALA A O     1 
ATOM   1572  C  CB    . ALA A 1 1730 ? 208.924 243.289 284.805 1.00 78.22  ? 1730 ALA A CB    1 
ATOM   1573  N  N     . THR A 1 1731 ? 211.599 244.674 286.195 1.00 85.21  ? 1731 THR A N     1 
ATOM   1574  C  CA    . THR A 1 1731 ? 213.002 244.471 286.542 1.00 84.26  ? 1731 THR A CA    1 
ATOM   1575  C  C     . THR A 1 1731 ? 213.328 242.990 286.692 1.00 83.20  ? 1731 THR A C     1 
ATOM   1576  O  O     . THR A 1 1731 ? 214.462 242.569 286.439 1.00 80.87  ? 1731 THR A O     1 
ATOM   1577  C  CB    . THR A 1 1731 ? 213.343 245.225 287.827 1.00 84.36  ? 1731 THR A CB    1 
ATOM   1578  O  OG1   . THR A 1 1731 ? 212.551 244.715 288.907 1.00 85.71  ? 1731 THR A OG1   1 
ATOM   1579  C  CG2   . THR A 1 1731 ? 213.068 246.711 287.659 1.00 81.21  ? 1731 THR A CG2   1 
ATOM   1580  N  N     . SER A 1 1732 ? 212.352 242.187 287.110 1.00 80.26  ? 1732 SER A N     1 
ATOM   1581  C  CA    . SER A 1 1732 ? 212.526 240.752 287.265 1.00 79.53  ? 1732 SER A CA    1 
ATOM   1582  C  C     . SER A 1 1732 ? 211.298 240.033 286.725 1.00 82.12  ? 1732 SER A C     1 
ATOM   1583  O  O     . SER A 1 1732 ? 210.195 240.586 286.705 1.00 81.37  ? 1732 SER A O     1 
ATOM   1584  C  CB    . SER A 1 1732 ? 212.758 240.367 288.732 1.00 79.63  ? 1732 SER A CB    1 
ATOM   1585  O  OG    . SER A 1 1732 ? 212.969 238.973 288.867 1.00 83.31  ? 1732 SER A OG    1 
ATOM   1586  N  N     . ILE A 1 1733 ? 211.500 238.795 286.284 1.00 75.43  ? 1733 ILE A N     1 
ATOM   1587  C  CA    . ILE A 1 1733 ? 210.438 237.970 285.719 1.00 76.02  ? 1733 ILE A CA    1 
ATOM   1588  C  C     . ILE A 1 1733 ? 210.389 236.652 286.477 1.00 75.34  ? 1733 ILE A C     1 
ATOM   1589  O  O     . ILE A 1 1733 ? 211.417 235.987 286.643 1.00 76.03  ? 1733 ILE A O     1 
ATOM   1590  C  CB    . ILE A 1 1733 ? 210.645 237.725 284.214 1.00 73.89  ? 1733 ILE A CB    1 
ATOM   1591  C  CG1   . ILE A 1 1733 ? 210.380 239.005 283.425 1.00 76.09  ? 1733 ILE A CG1   1 
ATOM   1592  C  CG2   . ILE A 1 1733 ? 209.748 236.601 283.721 1.00 72.44  ? 1733 ILE A CG2   1 
ATOM   1593  C  CD1   . ILE A 1 1733 ? 210.628 238.859 281.950 1.00 74.29  ? 1733 ILE A CD1   1 
ATOM   1594  N  N     . ASP A 1 1734 ? 209.199 236.281 286.933 1.00 74.28  ? 1734 ASP A N     1 
ATOM   1595  C  CA    . ASP A 1 1734 ? 209.004 234.975 287.544 1.00 76.40  ? 1734 ASP A CA    1 
ATOM   1596  C  C     . ASP A 1 1734 ? 209.039 233.911 286.454 1.00 75.51  ? 1734 ASP A C     1 
ATOM   1597  O  O     . ASP A 1 1734 ? 208.229 233.970 285.523 1.00 70.94  ? 1734 ASP A O     1 
ATOM   1598  C  CB    . ASP A 1 1734 ? 207.676 234.930 288.292 1.00 76.95  ? 1734 ASP A CB    1 
ATOM   1599  C  CG    . ASP A 1 1734 ? 207.590 233.773 289.271 1.00 78.70  ? 1734 ASP A CG    1 
ATOM   1600  O  OD1   . ASP A 1 1734 ? 208.003 232.649 288.918 1.00 76.68  ? 1734 ASP A OD1   1 
ATOM   1601  O  OD2   . ASP A 1 1734 ? 207.110 233.992 290.403 1.00 76.17  ? 1734 ASP A OD2   1 
ATOM   1602  N  N     . PRO A 1 1735 ? 209.958 232.945 286.516 1.00 78.44  ? 1735 PRO A N     1 
ATOM   1603  C  CA    . PRO A 1 1735 ? 210.022 231.938 285.444 1.00 73.41  ? 1735 PRO A CA    1 
ATOM   1604  C  C     . PRO A 1 1735 ? 208.737 231.148 285.277 1.00 72.45  ? 1735 PRO A C     1 
ATOM   1605  O  O     . PRO A 1 1735 ? 208.347 230.850 284.142 1.00 77.32  ? 1735 PRO A O     1 
ATOM   1606  C  CB    . PRO A 1 1735 ? 211.191 231.042 285.877 1.00 70.02  ? 1735 PRO A CB    1 
ATOM   1607  C  CG    . PRO A 1 1735 ? 212.011 231.898 286.786 1.00 71.86  ? 1735 PRO A CG    1 
ATOM   1608  C  CD    . PRO A 1 1735 ? 211.031 232.769 287.508 1.00 75.20  ? 1735 PRO A CD    1 
ATOM   1609  N  N     . ASN A 1 1736 ? 208.054 230.818 286.375 1.00 74.59  ? 1736 ASN A N     1 
ATOM   1610  C  CA    . ASN A 1 1736 ? 206.852 229.997 286.277 1.00 72.26  ? 1736 ASN A CA    1 
ATOM   1611  C  C     . ASN A 1 1736 ? 205.765 230.696 285.471 1.00 71.51  ? 1736 ASN A C     1 
ATOM   1612  O  O     . ASN A 1 1736 ? 205.130 230.080 284.609 1.00 74.20  ? 1736 ASN A O     1 
ATOM   1613  C  CB    . ASN A 1 1736 ? 206.340 229.647 287.674 1.00 76.97  ? 1736 ASN A CB    1 
ATOM   1614  C  CG    . ASN A 1 1736 ? 207.362 228.891 288.496 1.00 78.38  ? 1736 ASN A CG    1 
ATOM   1615  O  OD1   . ASN A 1 1736 ? 208.136 228.094 287.965 1.00 77.55  ? 1736 ASN A OD1   1 
ATOM   1616  N  ND2   . ASN A 1 1736 ? 207.370 229.137 289.800 1.00 76.13  ? 1736 ASN A ND2   1 
ATOM   1617  N  N     . THR A 1 1737 ? 205.544 231.987 285.729 1.00 70.19  ? 1737 THR A N     1 
ATOM   1618  C  CA    . THR A 1 1737 ? 204.521 232.722 284.992 1.00 72.83  ? 1737 THR A CA    1 
ATOM   1619  C  C     . THR A 1 1737 ? 204.886 232.854 283.518 1.00 73.63  ? 1737 THR A C     1 
ATOM   1620  O  O     . THR A 1 1737 ? 204.015 232.755 282.644 1.00 75.66  ? 1737 THR A O     1 
ATOM   1621  C  CB    . THR A 1 1737 ? 204.311 234.100 285.616 1.00 75.76  ? 1737 THR A CB    1 
ATOM   1622  O  OG1   . THR A 1 1737 ? 205.575 234.757 285.763 1.00 77.30  ? 1737 THR A OG1   1 
ATOM   1623  C  CG2   . THR A 1 1737 ? 203.658 233.968 286.982 1.00 73.39  ? 1737 THR A CG2   1 
ATOM   1624  N  N     . TYR A 1 1738 ? 206.167 233.083 283.223 1.00 69.37  ? 1738 TYR A N     1 
ATOM   1625  C  CA    . TYR A 1 1738 ? 206.591 233.206 281.833 1.00 67.16  ? 1738 TYR A CA    1 
ATOM   1626  C  C     . TYR A 1 1738 ? 206.387 231.901 281.075 1.00 65.17  ? 1738 TYR A C     1 
ATOM   1627  O  O     . TYR A 1 1738 ? 205.888 231.902 279.944 1.00 67.83  ? 1738 TYR A O     1 
ATOM   1628  C  CB    . TYR A 1 1738 ? 208.052 233.648 281.767 1.00 64.85  ? 1738 TYR A CB    1 
ATOM   1629  C  CG    . TYR A 1 1738 ? 208.417 234.321 280.467 1.00 67.35  ? 1738 TYR A CG    1 
ATOM   1630  C  CD1   . TYR A 1 1738 ? 207.791 235.493 280.073 1.00 67.18  ? 1738 TYR A CD1   1 
ATOM   1631  C  CD2   . TYR A 1 1738 ? 209.382 233.781 279.630 1.00 67.09  ? 1738 TYR A CD2   1 
ATOM   1632  C  CE1   . TYR A 1 1738 ? 208.118 236.112 278.885 1.00 69.07  ? 1738 TYR A CE1   1 
ATOM   1633  C  CE2   . TYR A 1 1738 ? 209.715 234.393 278.440 1.00 66.85  ? 1738 TYR A CE2   1 
ATOM   1634  C  CZ    . TYR A 1 1738 ? 209.079 235.557 278.072 1.00 69.24  ? 1738 TYR A CZ    1 
ATOM   1635  O  OH    . TYR A 1 1738 ? 209.408 236.172 276.887 1.00 68.17  ? 1738 TYR A OH    1 
ATOM   1636  N  N     . ILE A 1 1739 ? 206.763 230.773 281.684 1.00 60.22  ? 1739 ILE A N     1 
ATOM   1637  C  CA    . ILE A 1 1739 ? 206.537 229.482 281.039 1.00 59.68  ? 1739 ILE A CA    1 
ATOM   1638  C  C     . ILE A 1 1739 ? 205.049 229.176 280.922 1.00 60.19  ? 1739 ILE A C     1 
ATOM   1639  O  O     . ILE A 1 1739 ? 204.614 228.566 279.939 1.00 68.66  ? 1739 ILE A O     1 
ATOM   1640  C  CB    . ILE A 1 1739 ? 207.297 228.365 281.777 1.00 61.54  ? 1739 ILE A CB    1 
ATOM   1641  C  CG1   . ILE A 1 1739 ? 208.742 228.784 282.037 1.00 61.80  ? 1739 ILE A CG1   1 
ATOM   1642  C  CG2   . ILE A 1 1739 ? 207.258 227.084 280.992 1.00 64.20  ? 1739 ILE A CG2   1 
ATOM   1643  C  CD1   . ILE A 1 1739 ? 209.565 228.923 280.781 1.00 60.26  ? 1739 ILE A CD1   1 
ATOM   1644  N  N     . THR A 1 1740 ? 204.243 229.589 281.903 1.00 59.72  ? 1740 THR A N     1 
ATOM   1645  C  CA    . THR A 1 1740 ? 202.799 229.408 281.789 1.00 64.41  ? 1740 THR A CA    1 
ATOM   1646  C  C     . THR A 1 1740 ? 202.244 230.169 280.591 1.00 65.47  ? 1740 THR A C     1 
ATOM   1647  O  O     . THR A 1 1740 ? 201.442 229.630 279.817 1.00 68.22  ? 1740 THR A O     1 
ATOM   1648  C  CB    . THR A 1 1740 ? 202.112 229.862 283.077 1.00 64.21  ? 1740 THR A CB    1 
ATOM   1649  O  OG1   . THR A 1 1740 ? 202.405 228.935 284.129 1.00 66.26  ? 1740 THR A OG1   1 
ATOM   1650  C  CG2   . THR A 1 1740 ? 200.607 229.940 282.884 1.00 62.50  ? 1740 THR A CG2   1 
ATOM   1651  N  N     . TRP A 1 1741 ? 202.672 231.420 280.414 1.00 62.98  ? 1741 TRP A N     1 
ATOM   1652  C  CA    . TRP A 1 1741 ? 202.219 232.203 279.268 1.00 64.37  ? 1741 TRP A CA    1 
ATOM   1653  C  C     . TRP A 1 1741 ? 202.701 231.598 277.956 1.00 63.24  ? 1741 TRP A C     1 
ATOM   1654  O  O     . TRP A 1 1741 ? 201.958 231.575 276.968 1.00 62.08  ? 1741 TRP A O     1 
ATOM   1655  C  CB    . TRP A 1 1741 ? 202.695 233.646 279.395 1.00 60.06  ? 1741 TRP A CB    1 
ATOM   1656  C  CG    . TRP A 1 1741 ? 202.610 234.419 278.118 1.00 64.81  ? 1741 TRP A CG    1 
ATOM   1657  C  CD1   . TRP A 1 1741 ? 201.490 234.958 277.562 1.00 62.40  ? 1741 TRP A CD1   1 
ATOM   1658  C  CD2   . TRP A 1 1741 ? 203.691 234.738 277.235 1.00 63.12  ? 1741 TRP A CD2   1 
ATOM   1659  N  NE1   . TRP A 1 1741 ? 201.804 235.594 276.386 1.00 63.92  ? 1741 TRP A NE1   1 
ATOM   1660  C  CE2   . TRP A 1 1741 ? 203.150 235.472 276.163 1.00 61.97  ? 1741 TRP A CE2   1 
ATOM   1661  C  CE3   . TRP A 1 1741 ? 205.063 234.472 277.245 1.00 60.42  ? 1741 TRP A CE3   1 
ATOM   1662  C  CZ2   . TRP A 1 1741 ? 203.932 235.945 275.114 1.00 57.63  ? 1741 TRP A CZ2   1 
ATOM   1663  C  CZ3   . TRP A 1 1741 ? 205.836 234.940 276.204 1.00 58.49  ? 1741 TRP A CZ3   1 
ATOM   1664  C  CH2   . TRP A 1 1741 ? 205.270 235.669 275.153 1.00 58.99  ? 1741 TRP A CH2   1 
ATOM   1665  N  N     . ILE A 1 1742 ? 203.945 231.114 277.924 1.00 58.12  ? 1742 ILE A N     1 
ATOM   1666  C  CA    . ILE A 1 1742 ? 204.466 230.476 276.719 1.00 57.74  ? 1742 ILE A CA    1 
ATOM   1667  C  C     . ILE A 1 1742 ? 203.629 229.256 276.362 1.00 63.30  ? 1742 ILE A C     1 
ATOM   1668  O  O     . ILE A 1 1742 ? 203.261 229.053 275.199 1.00 69.70  ? 1742 ILE A O     1 
ATOM   1669  C  CB    . ILE A 1 1742 ? 205.949 230.107 276.912 1.00 57.67  ? 1742 ILE A CB    1 
ATOM   1670  C  CG1   . ILE A 1 1742 ? 206.827 231.353 276.828 1.00 59.47  ? 1742 ILE A CG1   1 
ATOM   1671  C  CG2   . ILE A 1 1742 ? 206.389 229.080 275.885 1.00 58.73  ? 1742 ILE A CG2   1 
ATOM   1672  C  CD1   . ILE A 1 1742 ? 208.262 231.103 277.219 1.00 61.65  ? 1742 ILE A CD1   1 
ATOM   1673  N  N     . ASP A 1 1743 ? 203.306 228.431 277.360 1.00 63.09  ? 1743 ASP A N     1 
ATOM   1674  C  CA    . ASP A 1 1743 ? 202.497 227.243 277.120 1.00 62.26  ? 1743 ASP A CA    1 
ATOM   1675  C  C     . ASP A 1 1743 ? 201.080 227.598 276.689 1.00 64.49  ? 1743 ASP A C     1 
ATOM   1676  O  O     . ASP A 1 1743 ? 200.472 226.862 275.904 1.00 64.50  ? 1743 ASP A O     1 
ATOM   1677  C  CB    . ASP A 1 1743 ? 202.464 226.378 278.378 1.00 62.94  ? 1743 ASP A CB    1 
ATOM   1678  C  CG    . ASP A 1 1743 ? 203.592 225.374 278.423 1.00 69.03  ? 1743 ASP A CG    1 
ATOM   1679  O  OD1   . ASP A 1 1743 ? 204.130 225.035 277.349 1.00 71.52  ? 1743 ASP A OD1   1 
ATOM   1680  O  OD2   . ASP A 1 1743 ? 203.943 224.924 279.534 1.00 66.16  ? 1743 ASP A OD2   1 
ATOM   1681  N  N     . LYS A 1 1744 ? 200.536 228.708 277.195 1.00 58.40  ? 1744 LYS A N     1 
ATOM   1682  C  CA    . LYS A 1 1744 ? 199.144 229.045 276.913 1.00 56.02  ? 1744 LYS A CA    1 
ATOM   1683  C  C     . LYS A 1 1744 ? 198.919 229.337 275.434 1.00 62.32  ? 1744 LYS A C     1 
ATOM   1684  O  O     . LYS A 1 1744 ? 197.893 228.940 274.869 1.00 65.09  ? 1744 LYS A O     1 
ATOM   1685  C  CB    . LYS A 1 1744 ? 198.712 230.238 277.763 1.00 61.34  ? 1744 LYS A CB    1 
ATOM   1686  C  CG    . LYS A 1 1744 ? 197.238 230.580 277.633 1.00 60.26  ? 1744 LYS A CG    1 
ATOM   1687  C  CD    . LYS A 1 1744 ? 196.883 231.810 278.445 1.00 60.90  ? 1744 LYS A CD    1 
ATOM   1688  C  CE    . LYS A 1 1744 ? 196.860 231.500 279.930 1.00 66.66  ? 1744 LYS A CE    1 
ATOM   1689  N  NZ    . LYS A 1 1744 ? 196.399 232.666 280.732 1.00 66.70  ? 1744 LYS A NZ    1 
ATOM   1690  N  N     . TYR A 1 1745 ? 199.855 230.026 274.790 1.00 68.28  ? 1745 TYR A N     1 
ATOM   1691  C  CA    . TYR A 1 1745 ? 199.660 230.531 273.439 1.00 63.34  ? 1745 TYR A CA    1 
ATOM   1692  C  C     . TYR A 1 1745 ? 200.538 229.791 272.439 1.00 58.75  ? 1745 TYR A C     1 
ATOM   1693  O  O     . TYR A 1 1745 ? 201.478 229.080 272.803 1.00 62.05  ? 1745 TYR A O     1 
ATOM   1694  C  CB    . TYR A 1 1745 ? 199.939 232.035 273.381 1.00 54.78  ? 1745 TYR A CB    1 
ATOM   1695  C  CG    . TYR A 1 1745 ? 198.977 232.836 274.224 1.00 55.93  ? 1745 TYR A CG    1 
ATOM   1696  C  CD1   . TYR A 1 1745 ? 197.674 233.056 273.803 1.00 57.44  ? 1745 TYR A CD1   1 
ATOM   1697  C  CD2   . TYR A 1 1745 ? 199.366 233.355 275.449 1.00 58.41  ? 1745 TYR A CD2   1 
ATOM   1698  C  CE1   . TYR A 1 1745 ? 196.789 233.781 274.573 1.00 59.19  ? 1745 TYR A CE1   1 
ATOM   1699  C  CE2   . TYR A 1 1745 ? 198.488 234.079 276.225 1.00 60.98  ? 1745 TYR A CE2   1 
ATOM   1700  C  CZ    . TYR A 1 1745 ? 197.202 234.289 275.783 1.00 62.60  ? 1745 TYR A CZ    1 
ATOM   1701  O  OH    . TYR A 1 1745 ? 196.326 235.012 276.557 1.00 64.36  ? 1745 TYR A OH    1 
ATOM   1702  N  N     . GLN A 1 1746 ? 200.212 229.976 271.163 1.00 58.31  ? 1746 GLN A N     1 
ATOM   1703  C  CA    . GLN A 1 1746 ? 200.857 229.245 270.084 1.00 58.50  ? 1746 GLN A CA    1 
ATOM   1704  C  C     . GLN A 1 1746 ? 202.242 229.815 269.792 1.00 56.66  ? 1746 GLN A C     1 
ATOM   1705  O  O     . GLN A 1 1746 ? 202.560 230.956 270.132 1.00 61.64  ? 1746 GLN A O     1 
ATOM   1706  C  CB    . GLN A 1 1746 ? 199.991 229.285 268.825 1.00 58.24  ? 1746 GLN A CB    1 
ATOM   1707  C  CG    . GLN A 1 1746 ? 198.723 228.455 268.927 1.00 65.96  ? 1746 GLN A CG    1 
ATOM   1708  C  CD    . GLN A 1 1746 ? 197.636 229.146 269.728 1.00 68.31  ? 1746 GLN A CD    1 
ATOM   1709  O  OE1   . GLN A 1 1746 ? 197.721 230.341 270.005 1.00 68.09  ? 1746 GLN A OE1   1 
ATOM   1710  N  NE2   . GLN A 1 1746 ? 196.619 228.392 270.123 1.00 62.64  ? 1746 GLN A NE2   1 
ATOM   1711  N  N     . ALA A 1 1747 ? 203.072 228.992 269.141 1.00 51.97  ? 1747 ALA A N     1 
ATOM   1712  C  CA    . ALA A 1 1747 ? 204.456 229.377 268.875 1.00 53.21  ? 1747 ALA A CA    1 
ATOM   1713  C  C     . ALA A 1 1747 ? 204.541 230.622 268.004 1.00 57.55  ? 1747 ALA A C     1 
ATOM   1714  O  O     . ALA A 1 1747 ? 205.480 231.414 268.140 1.00 57.09  ? 1747 ALA A O     1 
ATOM   1715  C  CB    . ALA A 1 1747 ? 205.202 228.218 268.217 1.00 48.08  ? 1747 ALA A CB    1 
ATOM   1716  N  N     . GLN A 1 1748 ? 203.581 230.803 267.098 1.00 49.92  ? 1748 GLN A N     1 
ATOM   1717  C  CA    . GLN A 1 1748 ? 203.507 232.030 266.314 1.00 45.30  ? 1748 GLN A CA    1 
ATOM   1718  C  C     . GLN A 1 1748 ? 203.211 233.234 267.198 1.00 50.59  ? 1748 GLN A C     1 
ATOM   1719  O  O     . GLN A 1 1748 ? 203.908 234.258 267.131 1.00 51.61  ? 1748 GLN A O     1 
ATOM   1720  C  CB    . GLN A 1 1748 ? 202.424 231.876 265.248 1.00 38.62  ? 1748 GLN A CB    1 
ATOM   1721  C  CG    . GLN A 1 1748 ? 202.240 233.059 264.332 1.00 46.80  ? 1748 GLN A CG    1 
ATOM   1722  C  CD    . GLN A 1 1748 ? 201.127 232.831 263.332 1.00 48.44  ? 1748 GLN A CD    1 
ATOM   1723  O  OE1   . GLN A 1 1748 ? 200.462 231.797 263.356 1.00 49.65  ? 1748 GLN A OE1   1 
ATOM   1724  N  NE2   . GLN A 1 1748 ? 200.909 233.802 262.456 1.00 51.62  ? 1748 GLN A NE2   1 
ATOM   1725  N  N     . LEU A 1 1749 ? 202.194 233.116 268.051 1.00 51.37  ? 1749 LEU A N     1 
ATOM   1726  C  CA    . LEU A 1 1749 ? 201.684 234.262 268.788 1.00 42.63  ? 1749 LEU A CA    1 
ATOM   1727  C  C     . LEU A 1 1749 ? 202.616 234.705 269.903 1.00 43.20  ? 1749 LEU A C     1 
ATOM   1728  O  O     . LEU A 1 1749 ? 202.666 235.896 270.208 1.00 52.81  ? 1749 LEU A O     1 
ATOM   1729  C  CB    . LEU A 1 1749 ? 200.302 233.943 269.351 1.00 43.98  ? 1749 LEU A CB    1 
ATOM   1730  C  CG    . LEU A 1 1749 ? 199.241 233.727 268.274 1.00 49.78  ? 1749 LEU A CG    1 
ATOM   1731  C  CD1   . LEU A 1 1749 ? 197.904 233.427 268.906 1.00 48.94  ? 1749 LEU A CD1   1 
ATOM   1732  C  CD2   . LEU A 1 1749 ? 199.147 234.935 267.358 1.00 46.96  ? 1749 LEU A CD2   1 
ATOM   1733  N  N     . VAL A 1 1750 ? 203.359 233.785 270.521 1.00 44.05  ? 1750 VAL A N     1 
ATOM   1734  C  CA    . VAL A 1 1750 ? 204.288 234.199 271.569 1.00 44.26  ? 1750 VAL A CA    1 
ATOM   1735  C  C     . VAL A 1 1750 ? 205.389 235.081 270.988 1.00 46.01  ? 1750 VAL A C     1 
ATOM   1736  O  O     . VAL A 1 1750 ? 205.719 236.135 271.547 1.00 55.02  ? 1750 VAL A O     1 
ATOM   1737  C  CB    . VAL A 1 1750 ? 204.860 232.972 272.306 1.00 43.43  ? 1750 VAL A CB    1 
ATOM   1738  C  CG1   . VAL A 1 1750 ? 203.793 232.342 273.181 1.00 45.61  ? 1750 VAL A CG1   1 
ATOM   1739  C  CG2   . VAL A 1 1750 ? 205.405 231.951 271.330 1.00 45.01  ? 1750 VAL A CG2   1 
ATOM   1740  N  N     . VAL A 1 1751 ? 205.952 234.685 269.845 1.00 39.32  ? 1751 VAL A N     1 
ATOM   1741  C  CA    . VAL A 1 1751 ? 206.984 235.492 269.203 1.00 38.70  ? 1751 VAL A CA    1 
ATOM   1742  C  C     . VAL A 1 1751 ? 206.400 236.804 268.700 1.00 38.24  ? 1751 VAL A C     1 
ATOM   1743  O  O     . VAL A 1 1751 ? 207.026 237.865 268.825 1.00 54.70  ? 1751 VAL A O     1 
ATOM   1744  C  CB    . VAL A 1 1751 ? 207.655 234.699 268.069 1.00 39.01  ? 1751 VAL A CB    1 
ATOM   1745  C  CG1   . VAL A 1 1751 ? 208.800 235.493 267.474 1.00 36.84  ? 1751 VAL A CG1   1 
ATOM   1746  C  CG2   . VAL A 1 1751 ? 208.143 233.365 268.584 1.00 39.11  ? 1751 VAL A CG2   1 
ATOM   1747  N  N     . LEU A 1 1752 ? 205.196 236.760 268.123 1.00 35.77  ? 1752 LEU A N     1 
ATOM   1748  C  CA    . LEU A 1 1752 ? 204.568 237.990 267.653 1.00 29.32  ? 1752 LEU A CA    1 
ATOM   1749  C  C     . LEU A 1 1752 ? 204.337 238.965 268.802 1.00 38.17  ? 1752 LEU A C     1 
ATOM   1750  O  O     . LEU A 1 1752 ? 204.591 240.168 268.668 1.00 45.99  ? 1752 LEU A O     1 
ATOM   1751  C  CB    . LEU A 1 1752 ? 203.255 237.664 266.945 1.00 35.32  ? 1752 LEU A CB    1 
ATOM   1752  C  CG    . LEU A 1 1752 ? 202.573 238.783 266.162 1.00 40.50  ? 1752 LEU A CG    1 
ATOM   1753  C  CD1   . LEU A 1 1752 ? 203.522 239.393 265.146 1.00 37.29  ? 1752 LEU A CD1   1 
ATOM   1754  C  CD2   . LEU A 1 1752 ? 201.334 238.247 265.478 1.00 42.43  ? 1752 LEU A CD2   1 
ATOM   1755  N  N     . SER A 1 1753 ? 203.868 238.461 269.945 1.00 43.67  ? 1753 SER A N     1 
ATOM   1756  C  CA    . SER A 1 1753 ? 203.615 239.312 271.101 1.00 39.27  ? 1753 SER A CA    1 
ATOM   1757  C  C     . SER A 1 1753 ? 204.908 239.876 271.670 1.00 33.80  ? 1753 SER A C     1 
ATOM   1758  O  O     . SER A 1 1753 ? 204.951 241.038 272.091 1.00 48.38  ? 1753 SER A O     1 
ATOM   1759  C  CB    . SER A 1 1753 ? 202.863 238.522 272.169 1.00 46.71  ? 1753 SER A CB    1 
ATOM   1760  O  OG    . SER A 1 1753 ? 201.776 237.816 271.601 1.00 47.41  ? 1753 SER A OG    1 
ATOM   1761  N  N     . ALA A 1 1754 ? 205.966 239.063 271.719 1.00 28.42  ? 1754 ALA A N     1 
ATOM   1762  C  CA    . ALA A 1 1754 ? 207.252 239.568 272.185 1.00 30.14  ? 1754 ALA A CA    1 
ATOM   1763  C  C     . ALA A 1 1754 ? 207.755 240.691 271.289 1.00 34.10  ? 1754 ALA A C     1 
ATOM   1764  O  O     . ALA A 1 1754 ? 208.197 241.740 271.780 1.00 39.39  ? 1754 ALA A O     1 
ATOM   1765  C  CB    . ALA A 1 1754 ? 208.272 238.433 272.244 1.00 36.02  ? 1754 ALA A CB    1 
ATOM   1766  N  N     . GLN A 1 1755 ? 207.675 240.496 269.969 1.00 41.72  ? 1755 GLN A N     1 
ATOM   1767  C  CA    . GLN A 1 1755 ? 208.092 241.537 269.037 1.00 31.38  ? 1755 GLN A CA    1 
ATOM   1768  C  C     . GLN A 1 1755 ? 207.267 242.802 269.218 1.00 29.65  ? 1755 GLN A C     1 
ATOM   1769  O  O     . GLN A 1 1755 ? 207.818 243.909 269.248 1.00 38.67  ? 1755 GLN A O     1 
ATOM   1770  C  CB    . GLN A 1 1755 ? 207.970 241.038 267.601 1.00 25.24  ? 1755 GLN A CB    1 
ATOM   1771  C  CG    . GLN A 1 1755 ? 208.925 239.948 267.213 1.00 29.53  ? 1755 GLN A CG    1 
ATOM   1772  C  CD    . GLN A 1 1755 ? 208.591 239.338 265.871 1.00 31.61  ? 1755 GLN A CD    1 
ATOM   1773  O  OE1   . GLN A 1 1755 ? 207.498 238.815 265.668 1.00 34.05  ? 1755 GLN A OE1   1 
ATOM   1774  N  NE2   . GLN A 1 1755 ? 209.532 239.408 264.941 1.00 41.71  ? 1755 GLN A NE2   1 
ATOM   1775  N  N     . ILE A 1 1756 ? 205.946 242.657 269.344 1.00 35.70  ? 1756 ILE A N     1 
ATOM   1776  C  CA    . ILE A 1 1756 ? 205.086 243.813 269.573 1.00 38.46  ? 1756 ILE A CA    1 
ATOM   1777  C  C     . ILE A 1 1756 ? 205.537 244.560 270.820 1.00 42.84  ? 1756 ILE A C     1 
ATOM   1778  O  O     . ILE A 1 1756 ? 206.016 245.698 270.740 1.00 54.31  ? 1756 ILE A O     1 
ATOM   1779  C  CB    . ILE A 1 1756 ? 203.614 243.372 269.673 1.00 38.36  ? 1756 ILE A CB    1 
ATOM   1780  C  CG1   . ILE A 1 1756 ? 203.058 243.045 268.288 1.00 39.92  ? 1756 ILE A CG1   1 
ATOM   1781  C  CG2   . ILE A 1 1756 ? 202.765 244.450 270.309 1.00 36.57  ? 1756 ILE A CG2   1 
ATOM   1782  C  CD1   . ILE A 1 1756 ? 201.663 242.480 268.313 1.00 35.02  ? 1756 ILE A CD1   1 
ATOM   1783  N  N     . ALA A 1 1757 ? 205.482 243.890 271.976 1.00 39.81  ? 1757 ALA A N     1 
ATOM   1784  C  CA    . ALA A 1 1757 ? 205.804 244.537 273.243 1.00 36.93  ? 1757 ALA A CA    1 
ATOM   1785  C  C     . ALA A 1 1757 ? 207.155 245.234 273.188 1.00 43.30  ? 1757 ALA A C     1 
ATOM   1786  O  O     . ALA A 1 1757 ? 207.296 246.362 273.676 1.00 50.91  ? 1757 ALA A O     1 
ATOM   1787  C  CB    . ALA A 1 1757 ? 205.777 243.513 274.375 1.00 39.39  ? 1757 ALA A CB    1 
ATOM   1788  N  N     . TRP A 1 1758 ? 208.157 244.598 272.574 1.00 40.40  ? 1758 TRP A N     1 
ATOM   1789  C  CA    . TRP A 1 1758 ? 209.448 245.263 272.435 1.00 36.21  ? 1758 TRP A CA    1 
ATOM   1790  C  C     . TRP A 1 1758 ? 209.335 246.504 271.557 1.00 43.06  ? 1758 TRP A C     1 
ATOM   1791  O  O     . TRP A 1 1758 ? 209.995 247.516 271.818 1.00 50.38  ? 1758 TRP A O     1 
ATOM   1792  C  CB    . TRP A 1 1758 ? 210.482 244.293 271.870 1.00 41.25  ? 1758 TRP A CB    1 
ATOM   1793  C  CG    . TRP A 1 1758 ? 211.780 244.945 271.509 1.00 45.17  ? 1758 TRP A CG    1 
ATOM   1794  C  CD1   . TRP A 1 1758 ? 212.800 245.260 272.357 1.00 46.60  ? 1758 TRP A CD1   1 
ATOM   1795  C  CD2   . TRP A 1 1758 ? 212.202 245.356 270.205 1.00 42.00  ? 1758 TRP A CD2   1 
ATOM   1796  N  NE1   . TRP A 1 1758 ? 213.829 245.842 271.664 1.00 36.76  ? 1758 TRP A NE1   1 
ATOM   1797  C  CE2   . TRP A 1 1758 ? 213.487 245.914 270.340 1.00 36.61  ? 1758 TRP A CE2   1 
ATOM   1798  C  CE3   . TRP A 1 1758 ? 211.618 245.309 268.937 1.00 43.00  ? 1758 TRP A CE3   1 
ATOM   1799  C  CZ2   . TRP A 1 1758 ? 214.195 246.422 269.257 1.00 39.08  ? 1758 TRP A CZ2   1 
ATOM   1800  C  CZ3   . TRP A 1 1758 ? 212.324 245.811 267.865 1.00 43.70  ? 1758 TRP A CZ3   1 
ATOM   1801  C  CH2   . TRP A 1 1758 ? 213.598 246.361 268.031 1.00 41.26  ? 1758 TRP A CH2   1 
ATOM   1802  N  N     . SER A 1 1759 ? 208.504 246.449 270.512 1.00 43.75  ? 1759 SER A N     1 
ATOM   1803  C  CA    . SER A 1 1759 ? 208.362 247.603 269.631 1.00 35.11  ? 1759 SER A CA    1 
ATOM   1804  C  C     . SER A 1 1759 ? 207.750 248.794 270.357 1.00 45.53  ? 1759 SER A C     1 
ATOM   1805  O  O     . SER A 1 1759 ? 208.264 249.913 270.255 1.00 60.07  ? 1759 SER A O     1 
ATOM   1806  C  CB    . SER A 1 1759 ? 207.532 247.233 268.404 1.00 47.68  ? 1759 SER A CB    1 
ATOM   1807  O  OG    . SER A 1 1759 ? 208.230 246.313 267.585 1.00 53.96  ? 1759 SER A OG    1 
ATOM   1808  N  N     . GLU A 1 1760 ? 206.654 248.583 271.097 1.00 45.29  ? 1760 GLU A N     1 
ATOM   1809  C  CA    . GLU A 1 1760 ? 206.116 249.709 271.868 1.00 43.01  ? 1760 GLU A CA    1 
ATOM   1810  C  C     . GLU A 1 1760 ? 207.069 250.154 272.971 1.00 46.42  ? 1760 GLU A C     1 
ATOM   1811  O  O     . GLU A 1 1760 ? 207.135 251.347 273.281 1.00 54.89  ? 1760 GLU A O     1 
ATOM   1812  C  CB    . GLU A 1 1760 ? 204.719 249.462 272.457 1.00 43.85  ? 1760 GLU A CB    1 
ATOM   1813  C  CG    . GLU A 1 1760 ? 203.547 249.352 271.472 1.00 49.30  ? 1760 GLU A CG    1 
ATOM   1814  C  CD    . GLU A 1 1760 ? 203.366 248.003 270.869 1.00 58.75  ? 1760 GLU A CD    1 
ATOM   1815  O  OE1   . GLU A 1 1760 ? 204.109 247.104 271.261 1.00 62.93  ? 1760 GLU A OE1   1 
ATOM   1816  O  OE2   . GLU A 1 1760 ? 202.477 247.840 270.008 1.00 59.25  ? 1760 GLU A OE2   1 
ATOM   1817  N  N     . ASN A 1 1761 ? 207.824 249.230 273.572 1.00 48.06  ? 1761 ASN A N     1 
ATOM   1818  C  CA    . ASN A 1 1761 ? 208.787 249.650 274.587 1.00 44.26  ? 1761 ASN A CA    1 
ATOM   1819  C  C     . ASN A 1 1761 ? 209.834 250.587 273.999 1.00 48.66  ? 1761 ASN A C     1 
ATOM   1820  O  O     . ASN A 1 1761 ? 210.109 251.656 274.559 1.00 57.42  ? 1761 ASN A O     1 
ATOM   1821  C  CB    . ASN A 1 1761 ? 209.459 248.432 275.218 1.00 43.12  ? 1761 ASN A CB    1 
ATOM   1822  C  CG    . ASN A 1 1761 ? 208.548 247.692 276.172 1.00 51.21  ? 1761 ASN A CG    1 
ATOM   1823  O  OD1   . ASN A 1 1761 ? 207.364 248.005 276.289 1.00 56.75  ? 1761 ASN A OD1   1 
ATOM   1824  N  ND2   . ASN A 1 1761 ? 209.098 246.702 276.863 1.00 51.06  ? 1761 ASN A ND2   1 
ATOM   1825  N  N     . VAL A 1 1762 ? 210.412 250.215 272.856 1.00 50.82  ? 1762 VAL A N     1 
ATOM   1826  C  CA    . VAL A 1 1762 ? 211.444 251.046 272.246 1.00 48.85  ? 1762 VAL A CA    1 
ATOM   1827  C  C     . VAL A 1 1762 ? 210.847 252.349 271.726 1.00 48.72  ? 1762 VAL A C     1 
ATOM   1828  O  O     . VAL A 1 1762 ? 211.476 253.409 271.813 1.00 55.03  ? 1762 VAL A O     1 
ATOM   1829  C  CB    . VAL A 1 1762 ? 212.176 250.269 271.138 1.00 48.07  ? 1762 VAL A CB    1 
ATOM   1830  C  CG1   . VAL A 1 1762 ? 213.236 251.142 270.494 1.00 51.98  ? 1762 VAL A CG1   1 
ATOM   1831  C  CG2   . VAL A 1 1762 ? 212.812 249.023 271.714 1.00 49.96  ? 1762 VAL A CG2   1 
ATOM   1832  N  N     . GLU A 1 1763 ? 209.628 252.297 271.183 1.00 50.31  ? 1763 GLU A N     1 
ATOM   1833  C  CA    . GLU A 1 1763 ? 208.983 253.516 270.706 1.00 47.51  ? 1763 GLU A CA    1 
ATOM   1834  C  C     . GLU A 1 1763 ? 208.723 254.489 271.848 1.00 57.72  ? 1763 GLU A C     1 
ATOM   1835  O  O     . GLU A 1 1763 ? 208.960 255.694 271.711 1.00 64.56  ? 1763 GLU A O     1 
ATOM   1836  C  CB    . GLU A 1 1763 ? 207.681 253.170 269.987 1.00 44.69  ? 1763 GLU A CB    1 
ATOM   1837  C  CG    . GLU A 1 1763 ? 207.098 254.311 269.179 1.00 58.90  ? 1763 GLU A CG    1 
ATOM   1838  C  CD    . GLU A 1 1763 ? 207.591 254.321 267.747 1.00 65.22  ? 1763 GLU A CD    1 
ATOM   1839  O  OE1   . GLU A 1 1763 ? 208.392 253.433 267.387 1.00 64.15  ? 1763 GLU A OE1   1 
ATOM   1840  O  OE2   . GLU A 1 1763 ? 207.176 255.214 266.981 1.00 61.86  ? 1763 GLU A OE2   1 
ATOM   1841  N  N     . THR A 1 1764 ? 208.240 253.986 272.986 1.00 52.22  ? 1764 THR A N     1 
ATOM   1842  C  CA    . THR A 1 1764 ? 208.018 254.844 274.145 1.00 50.25  ? 1764 THR A CA    1 
ATOM   1843  C  C     . THR A 1 1764 ? 209.331 255.409 274.671 1.00 55.16  ? 1764 THR A C     1 
ATOM   1844  O  O     . THR A 1 1764 ? 209.408 256.590 275.029 1.00 58.40  ? 1764 THR A O     1 
ATOM   1845  C  CB    . THR A 1 1764 ? 207.292 254.062 275.240 1.00 54.52  ? 1764 THR A CB    1 
ATOM   1846  O  OG1   . THR A 1 1764 ? 205.987 253.691 274.779 1.00 58.68  ? 1764 THR A OG1   1 
ATOM   1847  C  CG2   . THR A 1 1764 ? 207.157 254.901 276.497 1.00 56.32  ? 1764 THR A CG2   1 
ATOM   1848  N  N     . ALA A 1 1765 ? 210.378 254.581 274.719 1.00 59.41  ? 1765 ALA A N     1 
ATOM   1849  C  CA    . ALA A 1 1765 ? 211.673 255.057 275.194 1.00 57.48  ? 1765 ALA A CA    1 
ATOM   1850  C  C     . ALA A 1 1765 ? 212.222 256.153 274.289 1.00 59.89  ? 1765 ALA A C     1 
ATOM   1851  O  O     . ALA A 1 1765 ? 212.789 257.141 274.769 1.00 61.68  ? 1765 ALA A O     1 
ATOM   1852  C  CB    . ALA A 1 1765 ? 212.655 253.891 275.292 1.00 55.35  ? 1765 ALA A CB    1 
ATOM   1853  N  N     . LEU A 1 1766 ? 212.072 255.991 272.973 1.00 61.46  ? 1766 LEU A N     1 
ATOM   1854  C  CA    . LEU A 1 1766 ? 212.537 257.016 272.045 1.00 58.83  ? 1766 LEU A CA    1 
ATOM   1855  C  C     . LEU A 1 1766 ? 211.685 258.276 272.127 1.00 60.68  ? 1766 LEU A C     1 
ATOM   1856  O  O     . LEU A 1 1766 ? 212.206 259.386 271.974 1.00 68.17  ? 1766 LEU A O     1 
ATOM   1857  C  CB    . LEU A 1 1766 ? 212.546 256.467 270.620 1.00 61.61  ? 1766 LEU A CB    1 
ATOM   1858  C  CG    . LEU A 1 1766 ? 213.635 255.437 270.317 1.00 60.65  ? 1766 LEU A CG    1 
ATOM   1859  C  CD1   . LEU A 1 1766 ? 213.700 255.146 268.831 1.00 57.49  ? 1766 LEU A CD1   1 
ATOM   1860  C  CD2   . LEU A 1 1766 ? 214.981 255.914 270.829 1.00 59.76  ? 1766 LEU A CD2   1 
ATOM   1861  N  N     . SER A 1 1767 ? 210.379 258.127 272.360 1.00 65.67  ? 1767 SER A N     1 
ATOM   1862  C  CA    . SER A 1 1767 ? 209.526 259.295 272.559 1.00 67.05  ? 1767 SER A CA    1 
ATOM   1863  C  C     . SER A 1 1767 ? 209.936 260.065 273.808 1.00 66.69  ? 1767 SER A C     1 
ATOM   1864  O  O     . SER A 1 1767 ? 209.884 261.300 273.830 1.00 69.51  ? 1767 SER A O     1 
ATOM   1865  C  CB    . SER A 1 1767 ? 208.061 258.869 272.646 1.00 65.17  ? 1767 SER A CB    1 
ATOM   1866  O  OG    . SER A 1 1767 ? 207.662 258.170 271.479 1.00 69.70  ? 1767 SER A OG    1 
ATOM   1867  N  N     . SER A 1 1768 ? 210.335 259.350 274.862 1.00 71.92  ? 1768 SER A N     1 
ATOM   1868  C  CA    . SER A 1 1768 ? 210.840 260.014 276.060 1.00 70.79  ? 1768 SER A CA    1 
ATOM   1869  C  C     . SER A 1 1768 ? 212.106 260.804 275.753 1.00 72.69  ? 1768 SER A C     1 
ATOM   1870  O  O     . SER A 1 1768 ? 212.277 261.936 276.219 1.00 73.89  ? 1768 SER A O     1 
ATOM   1871  C  CB    . SER A 1 1768 ? 211.099 258.985 277.160 1.00 71.67  ? 1768 SER A CB    1 
ATOM   1872  O  OG    . SER A 1 1768 ? 211.766 259.575 278.261 1.00 70.23  ? 1768 SER A OG    1 
ATOM   1873  N  N     . MET A 1 1769 ? 213.010 260.218 274.965 1.00 74.75  ? 1769 MET A N     1 
ATOM   1874  C  CA    . MET A 1 1769 ? 214.232 260.900 274.558 1.00 72.47  ? 1769 MET A CA    1 
ATOM   1875  C  C     . MET A 1 1769 ? 213.991 261.957 273.490 1.00 76.44  ? 1769 MET A C     1 
ATOM   1876  O  O     . MET A 1 1769 ? 214.915 262.715 273.178 1.00 75.72  ? 1769 MET A O     1 
ATOM   1877  C  CB    . MET A 1 1769 ? 215.254 259.884 274.045 1.00 77.60  ? 1769 MET A CB    1 
ATOM   1878  C  CG    . MET A 1 1769 ? 215.776 258.935 275.104 1.00 77.78  ? 1769 MET A CG    1 
ATOM   1879  S  SD    . MET A 1 1769 ? 216.912 257.705 274.439 1.00 86.77  ? 1769 MET A SD    1 
ATOM   1880  C  CE    . MET A 1 1769 ? 218.335 258.724 274.066 1.00 77.35  ? 1769 MET A CE    1 
ATOM   1881  N  N     . GLY A 1 1770 ? 212.783 262.024 272.926 1.00 82.67  ? 1770 GLY A N     1 
ATOM   1882  C  CA    . GLY A 1 1770 ? 212.521 262.970 271.854 1.00 81.82  ? 1770 GLY A CA    1 
ATOM   1883  C  C     . GLY A 1 1770 ? 212.640 264.419 272.281 1.00 84.79  ? 1770 GLY A C     1 
ATOM   1884  O  O     . GLY A 1 1770 ? 212.721 265.314 271.436 1.00 82.05  ? 1770 GLY A O     1 
ATOM   1885  N  N     . GLY A 1 1771 ? 212.647 264.674 273.591 1.00 87.03  ? 1771 GLY A N     1 
ATOM   1886  C  CA    . GLY A 1 1771 ? 212.824 266.033 274.069 1.00 85.86  ? 1771 GLY A CA    1 
ATOM   1887  C  C     . GLY A 1 1771 ? 214.202 266.592 273.778 1.00 89.00  ? 1771 GLY A C     1 
ATOM   1888  O  O     . GLY A 1 1771 ? 214.384 267.812 273.733 1.00 88.85  ? 1771 GLY A O     1 
ATOM   1889  N  N     . GLY A 1 1772 ? 215.186 265.719 273.579 1.00 86.63  ? 1772 GLY A N     1 
ATOM   1890  C  CA    . GLY A 1 1772 ? 216.536 266.153 273.275 1.00 83.74  ? 1772 GLY A CA    1 
ATOM   1891  C  C     . GLY A 1 1772 ? 217.414 266.255 274.505 1.00 87.36  ? 1772 GLY A C     1 
ATOM   1892  O  O     . GLY A 1 1772 ? 217.181 267.102 275.373 1.00 83.48  ? 1772 GLY A O     1 
ATOM   1893  N  N     . GLY A 1 1773 ? 218.428 265.397 274.590 1.00 90.14  ? 1773 GLY A N     1 
ATOM   1894  C  CA    . GLY A 1 1773 ? 219.314 265.395 275.736 1.00 86.38  ? 1773 GLY A CA    1 
ATOM   1895  C  C     . GLY A 1 1773 ? 218.770 264.709 276.966 1.00 88.33  ? 1773 GLY A C     1 
ATOM   1896  O  O     . GLY A 1 1773 ? 219.406 264.768 278.022 1.00 88.74  ? 1773 GLY A O     1 
ATOM   1897  N  N     . ASP A 1 1774 ? 217.612 264.063 276.864 1.00 92.04  ? 1774 ASP A N     1 
ATOM   1898  C  CA    . ASP A 1 1774 ? 217.017 263.390 278.009 1.00 90.77  ? 1774 ASP A CA    1 
ATOM   1899  C  C     . ASP A 1 1774 ? 217.809 262.139 278.373 1.00 90.04  ? 1774 ASP A C     1 
ATOM   1900  O  O     . ASP A 1 1774 ? 218.418 261.490 277.518 1.00 88.19  ? 1774 ASP A O     1 
ATOM   1901  C  CB    . ASP A 1 1774 ? 215.563 263.024 277.708 1.00 91.75  ? 1774 ASP A CB    1 
ATOM   1902  C  CG    . ASP A 1 1774 ? 214.841 262.453 278.913 1.00 93.61  ? 1774 ASP A CG    1 
ATOM   1903  O  OD1   . ASP A 1 1774 ? 214.535 263.225 279.846 1.00 92.48  ? 1774 ASP A OD1   1 
ATOM   1904  O  OD2   . ASP A 1 1774 ? 214.571 261.234 278.923 1.00 91.82  ? 1774 ASP A OD2   1 
ATOM   1905  N  N     . ALA A 1 1775 ? 217.806 261.812 279.665 1.00 90.14  ? 1775 ALA A N     1 
ATOM   1906  C  CA    . ALA A 1 1775 ? 218.428 260.578 280.127 1.00 90.92  ? 1775 ALA A CA    1 
ATOM   1907  C  C     . ALA A 1 1775 ? 217.766 259.382 279.459 1.00 93.48  ? 1775 ALA A C     1 
ATOM   1908  O  O     . ALA A 1 1775 ? 216.542 259.330 279.316 1.00 93.78  ? 1775 ALA A O     1 
ATOM   1909  C  CB    . ALA A 1 1775 ? 218.322 260.463 281.648 1.00 87.06  ? 1775 ALA A CB    1 
ATOM   1910  N  N     . ALA A 1 1776 ? 218.583 258.415 279.052 1.00 81.54  ? 1776 ALA A N     1 
ATOM   1911  C  CA    . ALA A 1 1776 ? 218.104 257.324 278.213 1.00 77.93  ? 1776 ALA A CA    1 
ATOM   1912  C  C     . ALA A 1 1776 ? 217.336 256.277 279.011 1.00 78.57  ? 1776 ALA A C     1 
ATOM   1913  O  O     . ALA A 1 1776 ? 217.889 255.666 279.935 1.00 72.54  ? 1776 ALA A O     1 
ATOM   1914  C  CB    . ALA A 1 1776 ? 219.277 256.667 277.485 1.00 73.49  ? 1776 ALA A CB    1 
ATOM   1915  N  N     . PRO A 1 1777 ? 216.059 256.047 278.691 1.00 75.43  ? 1777 PRO A N     1 
ATOM   1916  C  CA    . PRO A 1 1777 ? 215.374 254.852 279.197 1.00 72.15  ? 1777 PRO A CA    1 
ATOM   1917  C  C     . PRO A 1 1777 ? 215.521 253.650 278.282 1.00 73.98  ? 1777 PRO A C     1 
ATOM   1918  O  O     . PRO A 1 1777 ? 214.963 252.588 278.588 1.00 76.25  ? 1777 PRO A O     1 
ATOM   1919  C  CB    . PRO A 1 1777 ? 213.915 255.307 279.277 1.00 67.28  ? 1777 PRO A CB    1 
ATOM   1920  C  CG    . PRO A 1 1777 ? 213.785 256.262 278.139 1.00 72.88  ? 1777 PRO A CG    1 
ATOM   1921  C  CD    . PRO A 1 1777 ? 215.137 256.928 277.954 1.00 71.79  ? 1777 PRO A CD    1 
ATOM   1922  N  N     . LEU A 1 1778 ? 216.240 253.793 277.166 1.00 67.00  ? 1778 LEU A N     1 
ATOM   1923  C  CA    . LEU A 1 1778 ? 216.502 252.657 276.292 1.00 62.37  ? 1778 LEU A CA    1 
ATOM   1924  C  C     . LEU A 1 1778 ? 217.364 251.615 276.989 1.00 64.42  ? 1778 LEU A C     1 
ATOM   1925  O  O     . LEU A 1 1778 ? 217.278 250.421 276.676 1.00 69.77  ? 1778 LEU A O     1 
ATOM   1926  C  CB    . LEU A 1 1778 ? 217.172 253.142 275.007 1.00 60.84  ? 1778 LEU A CB    1 
ATOM   1927  C  CG    . LEU A 1 1778 ? 216.926 252.355 273.721 1.00 66.23  ? 1778 LEU A CG    1 
ATOM   1928  C  CD1   . LEU A 1 1778 ? 215.456 252.393 273.344 1.00 63.96  ? 1778 LEU A CD1   1 
ATOM   1929  C  CD2   . LEU A 1 1778 ? 217.775 252.924 272.602 1.00 66.43  ? 1778 LEU A CD2   1 
ATOM   1930  N  N     . HIS A 1 1779 ? 218.200 252.049 277.935 1.00 61.29  ? 1779 HIS A N     1 
ATOM   1931  C  CA    . HIS A 1 1779 ? 218.958 251.104 278.747 1.00 61.28  ? 1779 HIS A CA    1 
ATOM   1932  C  C     . HIS A 1 1779 ? 218.026 250.203 279.543 1.00 59.74  ? 1779 HIS A C     1 
ATOM   1933  O  O     . HIS A 1 1779 ? 218.319 249.021 279.748 1.00 63.99  ? 1779 HIS A O     1 
ATOM   1934  C  CB    . HIS A 1 1779 ? 219.905 251.858 279.678 1.00 63.74  ? 1779 HIS A CB    1 
ATOM   1935  C  CG    . HIS A 1 1779 ? 220.990 252.602 278.965 1.00 66.67  ? 1779 HIS A CG    1 
ATOM   1936  N  ND1   . HIS A 1 1779 ? 221.083 253.977 278.979 1.00 69.91  ? 1779 HIS A ND1   1 
ATOM   1937  C  CD2   . HIS A 1 1779 ? 222.037 252.162 278.228 1.00 64.89  ? 1779 HIS A CD2   1 
ATOM   1938  C  CE1   . HIS A 1 1779 ? 222.135 254.353 278.274 1.00 67.22  ? 1779 HIS A CE1   1 
ATOM   1939  N  NE2   . HIS A 1 1779 ? 222.731 253.271 277.808 1.00 66.92  ? 1779 HIS A NE2   1 
ATOM   1940  N  N     . SER A 1 1780 ? 216.895 250.744 280.000 1.00 61.43  ? 1780 SER A N     1 
ATOM   1941  C  CA    . SER A 1 1780 ? 215.907 249.923 280.692 1.00 64.02  ? 1780 SER A CA    1 
ATOM   1942  C  C     . SER A 1 1780 ? 215.316 248.869 279.764 1.00 65.44  ? 1780 SER A C     1 
ATOM   1943  O  O     . SER A 1 1780 ? 215.105 247.722 280.175 1.00 67.31  ? 1780 SER A O     1 
ATOM   1944  C  CB    . SER A 1 1780 ? 214.804 250.806 281.272 1.00 65.39  ? 1780 SER A CB    1 
ATOM   1945  O  OG    . SER A 1 1780 ? 213.961 251.302 280.248 1.00 69.03  ? 1780 SER A OG    1 
ATOM   1946  N  N     . VAL A 1 1781 ? 215.038 249.239 278.512 1.00 59.51  ? 1781 VAL A N     1 
ATOM   1947  C  CA    . VAL A 1 1781 ? 214.524 248.271 277.546 1.00 59.45  ? 1781 VAL A CA    1 
ATOM   1948  C  C     . VAL A 1 1781 ? 215.552 247.177 277.294 1.00 57.76  ? 1781 VAL A C     1 
ATOM   1949  O  O     . VAL A 1 1781 ? 215.216 245.986 277.235 1.00 61.75  ? 1781 VAL A O     1 
ATOM   1950  C  CB    . VAL A 1 1781 ? 214.122 248.983 276.241 1.00 57.56  ? 1781 VAL A CB    1 
ATOM   1951  C  CG1   . VAL A 1 1781 ? 213.522 247.994 275.258 1.00 58.63  ? 1781 VAL A CG1   1 
ATOM   1952  C  CG2   . VAL A 1 1781 ? 213.147 250.110 276.530 1.00 58.81  ? 1781 VAL A CG2   1 
ATOM   1953  N  N     . LEU A 1 1782 ? 216.820 247.562 277.145 1.00 56.18  ? 1782 LEU A N     1 
ATOM   1954  C  CA    . LEU A 1 1782 ? 217.874 246.573 276.940 1.00 56.07  ? 1782 LEU A CA    1 
ATOM   1955  C  C     . LEU A 1 1782 ? 218.001 245.644 278.142 1.00 61.58  ? 1782 LEU A C     1 
ATOM   1956  O  O     . LEU A 1 1782 ? 218.187 244.433 277.985 1.00 67.70  ? 1782 LEU A O     1 
ATOM   1957  C  CB    . LEU A 1 1782 ? 219.202 247.273 276.655 1.00 57.17  ? 1782 LEU A CB    1 
ATOM   1958  C  CG    . LEU A 1 1782 ? 220.400 246.349 276.448 1.00 59.23  ? 1782 LEU A CG    1 
ATOM   1959  C  CD1   . LEU A 1 1782 ? 220.201 245.492 275.213 1.00 55.93  ? 1782 LEU A CD1   1 
ATOM   1960  C  CD2   . LEU A 1 1782 ? 221.682 247.153 276.343 1.00 59.85  ? 1782 LEU A CD2   1 
ATOM   1961  N  N     . SER A 1 1783 ? 217.906 246.194 279.355 1.00 60.45  ? 1783 SER A N     1 
ATOM   1962  C  CA    . SER A 1 1783 ? 218.000 245.367 280.553 1.00 57.95  ? 1783 SER A CA    1 
ATOM   1963  C  C     . SER A 1 1783 ? 216.821 244.408 280.660 1.00 63.77  ? 1783 SER A C     1 
ATOM   1964  O  O     . SER A 1 1783 ? 216.986 243.254 281.073 1.00 69.19  ? 1783 SER A O     1 
ATOM   1965  C  CB    . SER A 1 1783 ? 218.089 246.253 281.794 1.00 59.62  ? 1783 SER A CB    1 
ATOM   1966  O  OG    . SER A 1 1783 ? 219.248 247.065 281.752 1.00 64.35  ? 1783 SER A OG    1 
ATOM   1967  N  N     . ASN A 1 1784 ? 215.621 244.871 280.307 1.00 57.15  ? 1784 ASN A N     1 
ATOM   1968  C  CA    . ASN A 1 1784 ? 214.463 243.983 280.287 1.00 53.73  ? 1784 ASN A CA    1 
ATOM   1969  C  C     . ASN A 1 1784 ? 214.667 242.848 279.293 1.00 57.61  ? 1784 ASN A C     1 
ATOM   1970  O  O     . ASN A 1 1784 ? 214.382 241.680 279.597 1.00 61.99  ? 1784 ASN A O     1 
ATOM   1971  C  CB    . ASN A 1 1784 ? 213.207 244.780 279.938 1.00 61.16  ? 1784 ASN A CB    1 
ATOM   1972  C  CG    . ASN A 1 1784 ? 211.933 243.974 280.099 1.00 68.30  ? 1784 ASN A CG    1 
ATOM   1973  O  OD1   . ASN A 1 1784 ? 210.830 244.473 279.882 1.00 67.36  ? 1784 ASN A OD1   1 
ATOM   1974  N  ND2   . ASN A 1 1784 ? 212.081 242.719 280.498 1.00 69.64  ? 1784 ASN A ND2   1 
ATOM   1975  N  N     . VAL A 1 1785 ? 215.167 243.173 278.100 1.00 59.66  ? 1785 VAL A N     1 
ATOM   1976  C  CA    . VAL A 1 1785 ? 215.435 242.141 277.105 1.00 56.89  ? 1785 VAL A CA    1 
ATOM   1977  C  C     . VAL A 1 1785 ? 216.461 241.150 277.633 1.00 55.14  ? 1785 VAL A C     1 
ATOM   1978  O  O     . VAL A 1 1785 ? 216.320 239.937 277.453 1.00 60.63  ? 1785 VAL A O     1 
ATOM   1979  C  CB    . VAL A 1 1785 ? 215.889 242.780 275.780 1.00 51.57  ? 1785 VAL A CB    1 
ATOM   1980  C  CG1   . VAL A 1 1785 ? 216.421 241.721 274.837 1.00 54.19  ? 1785 VAL A CG1   1 
ATOM   1981  C  CG2   . VAL A 1 1785 ? 214.739 243.529 275.133 1.00 50.49  ? 1785 VAL A CG2   1 
ATOM   1982  N  N     . GLU A 1 1786 ? 217.499 241.646 278.309 1.00 53.02  ? 1786 GLU A N     1 
ATOM   1983  C  CA    . GLU A 1 1786 ? 218.549 240.763 278.808 1.00 53.06  ? 1786 GLU A CA    1 
ATOM   1984  C  C     . GLU A 1 1786 ? 218.041 239.847 279.917 1.00 58.88  ? 1786 GLU A C     1 
ATOM   1985  O  O     . GLU A 1 1786 ? 218.404 238.668 279.960 1.00 60.90  ? 1786 GLU A O     1 
ATOM   1986  C  CB    . GLU A 1 1786 ? 219.742 241.587 279.287 1.00 54.65  ? 1786 GLU A CB    1 
ATOM   1987  C  CG    . GLU A 1 1786 ? 220.504 242.269 278.162 1.00 58.50  ? 1786 GLU A CG    1 
ATOM   1988  C  CD    . GLU A 1 1786 ? 221.995 242.344 278.423 1.00 67.94  ? 1786 GLU A CD    1 
ATOM   1989  O  OE1   . GLU A 1 1786 ? 222.560 241.363 278.951 1.00 67.02  ? 1786 GLU A OE1   1 
ATOM   1990  O  OE2   . GLU A 1 1786 ? 222.605 243.385 278.098 1.00 65.87  ? 1786 GLU A OE2   1 
ATOM   1991  N  N     . VAL A 1 1787 ? 217.201 240.357 280.822 1.00 59.72  ? 1787 VAL A N     1 
ATOM   1992  C  CA    . VAL A 1 1787 ? 216.691 239.485 281.880 1.00 58.80  ? 1787 VAL A CA    1 
ATOM   1993  C  C     . VAL A 1 1787 ? 215.711 238.456 281.318 1.00 58.30  ? 1787 VAL A C     1 
ATOM   1994  O  O     . VAL A 1 1787 ? 215.718 237.288 281.737 1.00 60.84  ? 1787 VAL A O     1 
ATOM   1995  C  CB    . VAL A 1 1787 ? 216.075 240.299 283.038 1.00 58.15  ? 1787 VAL A CB    1 
ATOM   1996  C  CG1   . VAL A 1 1787 ? 217.059 241.342 283.541 1.00 57.14  ? 1787 VAL A CG1   1 
ATOM   1997  C  CG2   . VAL A 1 1787 ? 214.761 240.951 282.637 1.00 56.20  ? 1787 VAL A CG2   1 
ATOM   1998  N  N     . THR A 1 1788 ? 214.869 238.849 280.356 1.00 54.57  ? 1788 THR A N     1 
ATOM   1999  C  CA    . THR A 1 1788 ? 213.983 237.868 279.739 1.00 51.43  ? 1788 THR A CA    1 
ATOM   2000  C  C     . THR A 1 1788 ? 214.777 236.818 278.973 1.00 48.80  ? 1788 THR A C     1 
ATOM   2001  O  O     . THR A 1 1788 ? 214.426 235.631 278.991 1.00 56.95  ? 1788 THR A O     1 
ATOM   2002  C  CB    . THR A 1 1788 ? 212.989 238.562 278.811 1.00 53.88  ? 1788 THR A CB    1 
ATOM   2003  O  OG1   . THR A 1 1788 ? 212.407 239.681 279.486 1.00 61.92  ? 1788 THR A OG1   1 
ATOM   2004  C  CG2   . THR A 1 1788 ? 211.882 237.603 278.427 1.00 53.50  ? 1788 THR A CG2   1 
ATOM   2005  N  N     . LEU A 1 1789 ? 215.857 237.235 278.311 1.00 52.09  ? 1789 LEU A N     1 
ATOM   2006  C  CA    . LEU A 1 1789 ? 216.721 236.295 277.610 1.00 49.30  ? 1789 LEU A CA    1 
ATOM   2007  C  C     . LEU A 1 1789 ? 217.426 235.365 278.585 1.00 46.67  ? 1789 LEU A C     1 
ATOM   2008  O  O     . LEU A 1 1789 ? 217.647 234.192 278.276 1.00 48.09  ? 1789 LEU A O     1 
ATOM   2009  C  CB    . LEU A 1 1789 ? 217.731 237.066 276.762 1.00 45.08  ? 1789 LEU A CB    1 
ATOM   2010  C  CG    . LEU A 1 1789 ? 218.444 236.318 275.641 1.00 47.45  ? 1789 LEU A CG    1 
ATOM   2011  C  CD1   . LEU A 1 1789 ? 217.445 235.793 274.634 1.00 47.43  ? 1789 LEU A CD1   1 
ATOM   2012  C  CD2   . LEU A 1 1789 ? 219.435 237.246 274.971 1.00 50.01  ? 1789 LEU A CD2   1 
ATOM   2013  N  N     . ASN A 1 1790 ? 217.793 235.869 279.764 1.00 54.95  ? 1790 ASN A N     1 
ATOM   2014  C  CA    . ASN A 1 1790 ? 218.368 235.008 280.793 1.00 51.28  ? 1790 ASN A CA    1 
ATOM   2015  C  C     . ASN A 1 1790 ? 217.368 233.956 281.249 1.00 53.60  ? 1790 ASN A C     1 
ATOM   2016  O  O     . ASN A 1 1790 ? 217.725 232.786 281.430 1.00 58.72  ? 1790 ASN A O     1 
ATOM   2017  C  CB    . ASN A 1 1790 ? 218.834 235.845 281.982 1.00 52.08  ? 1790 ASN A CB    1 
ATOM   2018  C  CG    . ASN A 1 1790 ? 220.308 236.166 281.922 1.00 62.11  ? 1790 ASN A CG    1 
ATOM   2019  O  OD1   . ASN A 1 1790 ? 220.867 236.372 280.846 1.00 64.49  ? 1790 ASN A OD1   1 
ATOM   2020  N  ND2   . ASN A 1 1790 ? 220.950 236.210 283.083 1.00 62.31  ? 1790 ASN A ND2   1 
ATOM   2021  N  N     . VAL A 1 1791 ? 216.111 234.356 281.446 1.00 59.56  ? 1791 VAL A N     1 
ATOM   2022  C  CA    . VAL A 1 1791 ? 215.082 233.388 281.824 1.00 53.69  ? 1791 VAL A CA    1 
ATOM   2023  C  C     . VAL A 1 1791 ? 214.925 232.328 280.740 1.00 55.96  ? 1791 VAL A C     1 
ATOM   2024  O  O     . VAL A 1 1791 ? 214.888 231.122 281.025 1.00 57.45  ? 1791 VAL A O     1 
ATOM   2025  C  CB    . VAL A 1 1791 ? 213.752 234.109 282.114 1.00 52.51  ? 1791 VAL A CB    1 
ATOM   2026  C  CG1   . VAL A 1 1791 ? 212.646 233.103 282.373 1.00 58.30  ? 1791 VAL A CG1   1 
ATOM   2027  C  CG2   . VAL A 1 1791 ? 213.907 235.047 283.297 1.00 55.08  ? 1791 VAL A CG2   1 
ATOM   2028  N  N     . LEU A 1 1792 ? 214.856 232.758 279.477 1.00 55.88  ? 1792 LEU A N     1 
ATOM   2029  C  CA    . LEU A 1 1792 ? 214.703 231.812 278.374 1.00 47.33  ? 1792 LEU A CA    1 
ATOM   2030  C  C     . LEU A 1 1792 ? 215.903 230.877 278.264 1.00 51.86  ? 1792 LEU A C     1 
ATOM   2031  O  O     . LEU A 1 1792 ? 215.741 229.681 277.995 1.00 57.05  ? 1792 LEU A O     1 
ATOM   2032  C  CB    . LEU A 1 1792 ? 214.494 232.565 277.062 1.00 50.57  ? 1792 LEU A CB    1 
ATOM   2033  C  CG    . LEU A 1 1792 ? 213.171 233.309 276.898 1.00 52.10  ? 1792 LEU A CG    1 
ATOM   2034  C  CD1   . LEU A 1 1792 ? 213.284 234.347 275.799 1.00 54.87  ? 1792 LEU A CD1   1 
ATOM   2035  C  CD2   . LEU A 1 1792 ? 212.052 232.336 276.602 1.00 53.06  ? 1792 LEU A CD2   1 
ATOM   2036  N  N     . ALA A 1 1793 ? 217.115 231.404 278.455 1.00 52.41  ? 1793 ALA A N     1 
ATOM   2037  C  CA    . ALA A 1 1793 ? 218.316 230.584 278.345 1.00 54.34  ? 1793 ALA A CA    1 
ATOM   2038  C  C     . ALA A 1 1793 ? 218.422 229.594 279.495 1.00 57.43  ? 1793 ALA A C     1 
ATOM   2039  O  O     . ALA A 1 1793 ? 218.927 228.481 279.317 1.00 66.34  ? 1793 ALA A O     1 
ATOM   2040  C  CB    . ALA A 1 1793 ? 219.555 231.475 278.288 1.00 52.20  ? 1793 ALA A CB    1 
ATOM   2041  N  N     . ASP A 1 1794 ? 217.979 229.986 280.691 1.00 58.80  ? 1794 ASP A N     1 
ATOM   2042  C  CA    . ASP A 1 1794 ? 217.911 229.023 281.784 1.00 56.77  ? 1794 ASP A CA    1 
ATOM   2043  C  C     . ASP A 1 1794 ? 216.840 227.972 281.531 1.00 57.12  ? 1794 ASP A C     1 
ATOM   2044  O  O     . ASP A 1 1794 ? 216.954 226.844 282.021 1.00 59.73  ? 1794 ASP A O     1 
ATOM   2045  C  CB    . ASP A 1 1794 ? 217.651 229.737 283.110 1.00 60.07  ? 1794 ASP A CB    1 
ATOM   2046  C  CG    . ASP A 1 1794 ? 218.888 230.420 283.660 1.00 67.04  ? 1794 ASP A CG    1 
ATOM   2047  O  OD1   . ASP A 1 1794 ? 219.968 230.290 283.047 1.00 65.71  ? 1794 ASP A OD1   1 
ATOM   2048  O  OD2   . ASP A 1 1794 ? 218.780 231.085 284.712 1.00 66.79  ? 1794 ASP A OD2   1 
ATOM   2049  N  N     . SER A 1 1795 ? 215.799 228.319 280.770 1.00 62.33  ? 1795 SER A N     1 
ATOM   2050  C  CA    . SER A 1 1795 ? 214.732 227.358 280.503 1.00 60.63  ? 1795 SER A CA    1 
ATOM   2051  C  C     . SER A 1 1795 ? 215.205 226.212 279.615 1.00 63.59  ? 1795 SER A C     1 
ATOM   2052  O  O     . SER A 1 1795 ? 214.760 225.071 279.784 1.00 67.59  ? 1795 SER A O     1 
ATOM   2053  C  CB    . SER A 1 1795 ? 213.536 228.063 279.864 1.00 61.39  ? 1795 SER A CB    1 
ATOM   2054  O  OG    . SER A 1 1795 ? 213.027 229.079 280.708 1.00 63.41  ? 1795 SER A OG    1 
ATOM   2055  N  N     . VAL A 1 1796 ? 216.109 226.483 278.668 1.00 61.95  ? 1796 VAL A N     1 
ATOM   2056  C  CA    . VAL A 1 1796 ? 216.449 225.464 277.679 1.00 59.70  ? 1796 VAL A CA    1 
ATOM   2057  C  C     . VAL A 1 1796 ? 217.427 224.430 278.217 1.00 65.70  ? 1796 VAL A C     1 
ATOM   2058  O  O     . VAL A 1 1796 ? 217.593 223.371 277.601 1.00 67.40  ? 1796 VAL A O     1 
ATOM   2059  C  CB    . VAL A 1 1796 ? 217.022 226.093 276.395 1.00 51.76  ? 1796 VAL A CB    1 
ATOM   2060  C  CG1   . VAL A 1 1796 ? 215.965 226.909 275.680 1.00 53.92  ? 1796 VAL A CG1   1 
ATOM   2061  C  CG2   . VAL A 1 1796 ? 218.225 226.942 276.717 1.00 54.28  ? 1796 VAL A CG2   1 
ATOM   2062  N  N     . LEU A 1 1797 ? 218.101 224.707 279.336 1.00 64.44  ? 1797 LEU A N     1 
ATOM   2063  C  CA    . LEU A 1 1797 ? 218.969 223.692 279.926 1.00 63.31  ? 1797 LEU A CA    1 
ATOM   2064  C  C     . LEU A 1 1797 ? 218.161 222.508 280.439 1.00 65.65  ? 1797 LEU A C     1 
ATOM   2065  O  O     . LEU A 1 1797 ? 218.486 221.351 280.148 1.00 68.67  ? 1797 LEU A O     1 
ATOM   2066  C  CB    . LEU A 1 1797 ? 219.799 224.288 281.062 1.00 64.05  ? 1797 LEU A CB    1 
ATOM   2067  C  CG    . LEU A 1 1797 ? 220.383 225.691 280.923 1.00 66.84  ? 1797 LEU A CG    1 
ATOM   2068  C  CD1   . LEU A 1 1797 ? 220.917 226.136 282.270 1.00 66.78  ? 1797 LEU A CD1   1 
ATOM   2069  C  CD2   . LEU A 1 1797 ? 221.482 225.712 279.880 1.00 62.33  ? 1797 LEU A CD2   1 
ATOM   2070  N  N     . MET A 1 1798 ? 217.099 222.777 281.193 1.00 74.27  ? 1798 MET A N     1 
ATOM   2071  C  CA    . MET A 1 1798 ? 216.279 221.735 281.783 1.00 77.46  ? 1798 MET A CA    1 
ATOM   2072  C  C     . MET A 1 1798 ? 215.354 221.139 280.723 1.00 78.27  ? 1798 MET A C     1 
ATOM   2073  O  O     . MET A 1 1798 ? 215.089 221.747 279.684 1.00 80.66  ? 1798 MET A O     1 
ATOM   2074  C  CB    . MET A 1 1798 ? 215.503 222.294 282.975 1.00 78.45  ? 1798 MET A CB    1 
ATOM   2075  C  CG    . MET A 1 1798 ? 214.478 223.353 282.619 1.00 83.08  ? 1798 MET A CG    1 
ATOM   2076  S  SD    . MET A 1 1798 ? 213.638 224.006 284.075 1.00 96.18  ? 1798 MET A SD    1 
ATOM   2077  C  CE    . MET A 1 1798 ? 212.541 225.208 283.329 1.00 77.44  ? 1798 MET A CE    1 
ATOM   2078  N  N     . GLU A 1 1799 ? 214.862 219.928 280.978 1.00 83.74  ? 1799 GLU A N     1 
ATOM   2079  C  CA    . GLU A 1 1799 ? 214.064 219.217 279.987 1.00 84.60  ? 1799 GLU A CA    1 
ATOM   2080  C  C     . GLU A 1 1799 ? 212.704 219.873 279.799 1.00 88.07  ? 1799 GLU A C     1 
ATOM   2081  O  O     . GLU A 1 1799 ? 212.050 220.272 280.768 1.00 88.02  ? 1799 GLU A O     1 
ATOM   2082  C  CB    . GLU A 1 1799 ? 213.890 217.749 280.371 1.00 85.23  ? 1799 GLU A CB    1 
ATOM   2083  C  CG    . GLU A 1 1799 ? 215.112 216.889 280.102 1.00 90.15  ? 1799 GLU A CG    1 
ATOM   2084  C  CD    . GLU A 1 1799 ? 214.736 215.482 279.672 1.00 92.84  ? 1799 GLU A CD    1 
ATOM   2085  O  OE1   . GLU A 1 1799 ? 213.777 215.339 278.883 1.00 88.04  ? 1799 GLU A OE1   1 
ATOM   2086  O  OE2   . GLU A 1 1799 ? 215.400 214.520 280.111 1.00 92.24  ? 1799 GLU A OE2   1 
ATOM   2087  N  N     . GLN A 1 1800 ? 212.281 219.969 278.548 1.00 74.79  ? 1800 GLN A N     1 
ATOM   2088  C  CA    . GLN A 1 1800 ? 211.052 220.628 278.147 1.00 72.00  ? 1800 GLN A CA    1 
ATOM   2089  C  C     . GLN A 1 1800 ? 210.291 219.750 277.169 1.00 73.35  ? 1800 GLN A C     1 
ATOM   2090  O  O     . GLN A 1 1800 ? 210.885 218.930 276.460 1.00 70.52  ? 1800 GLN A O     1 
ATOM   2091  C  CB    . GLN A 1 1800 ? 211.353 221.989 277.500 1.00 71.42  ? 1800 GLN A CB    1 
ATOM   2092  C  CG    . GLN A 1 1800 ? 212.358 222.843 278.263 1.00 69.99  ? 1800 GLN A CG    1 
ATOM   2093  C  CD    . GLN A 1 1800 ? 211.703 223.707 279.318 1.00 71.24  ? 1800 GLN A CD    1 
ATOM   2094  O  OE1   . GLN A 1 1800 ? 210.484 223.679 279.485 1.00 70.62  ? 1800 GLN A OE1   1 
ATOM   2095  N  NE2   . GLN A 1 1800 ? 212.510 224.471 280.047 1.00 72.53  ? 1800 GLN A NE2   1 
ATOM   2096  N  N     . PRO A 1 1801 ? 208.968 219.886 277.121 1.00 71.37  ? 1801 PRO A N     1 
ATOM   2097  C  CA    . PRO A 1 1801 ? 208.216 219.271 276.035 1.00 70.48  ? 1801 PRO A CA    1 
ATOM   2098  C  C     . PRO A 1 1801 ? 208.666 219.826 274.703 1.00 70.27  ? 1801 PRO A C     1 
ATOM   2099  O  O     . PRO A 1 1801 ? 209.056 221.005 274.600 1.00 73.50  ? 1801 PRO A O     1 
ATOM   2100  C  CB    . PRO A 1 1801 ? 206.764 219.659 276.348 1.00 68.40  ? 1801 PRO A CB    1 
ATOM   2101  C  CG    . PRO A 1 1801 ? 206.754 219.920 277.812 1.00 66.98  ? 1801 PRO A CG    1 
ATOM   2102  C  CD    . PRO A 1 1801 ? 208.094 220.501 278.132 1.00 65.87  ? 1801 PRO A CD    1 
ATOM   2103  N  N     . PRO A 1 1802 ? 208.641 219.010 273.644 1.00 70.21  ? 1802 PRO A N     1 
ATOM   2104  C  CA    . PRO A 1 1802 ? 209.198 219.467 272.358 1.00 71.10  ? 1802 PRO A CA    1 
ATOM   2105  C  C     . PRO A 1 1802 ? 208.570 220.749 271.836 1.00 68.26  ? 1802 PRO A C     1 
ATOM   2106  O  O     . PRO A 1 1802 ? 209.285 221.607 271.305 1.00 69.28  ? 1802 PRO A O     1 
ATOM   2107  C  CB    . PRO A 1 1802 ? 208.934 218.276 271.425 1.00 70.30  ? 1802 PRO A CB    1 
ATOM   2108  C  CG    . PRO A 1 1802 ? 208.780 217.099 272.342 1.00 71.85  ? 1802 PRO A CG    1 
ATOM   2109  C  CD    . PRO A 1 1802 ? 208.126 217.634 273.573 1.00 69.54  ? 1802 PRO A CD    1 
ATOM   2110  N  N     . LEU A 1 1803 ? 207.254 220.913 271.984 1.00 65.78  ? 1803 LEU A N     1 
ATOM   2111  C  CA    . LEU A 1 1803 ? 206.620 222.157 271.562 1.00 63.04  ? 1803 LEU A CA    1 
ATOM   2112  C  C     . LEU A 1 1803 ? 207.082 223.334 272.408 1.00 61.59  ? 1803 LEU A C     1 
ATOM   2113  O  O     . LEU A 1 1803 ? 207.364 224.415 271.877 1.00 70.31  ? 1803 LEU A O     1 
ATOM   2114  C  CB    . LEU A 1 1803 ? 205.100 222.020 271.618 1.00 62.03  ? 1803 LEU A CB    1 
ATOM   2115  C  CG    . LEU A 1 1803 ? 204.331 223.245 271.124 1.00 66.63  ? 1803 LEU A CG    1 
ATOM   2116  C  CD1   . LEU A 1 1803 ? 204.673 223.540 269.675 1.00 63.23  ? 1803 LEU A CD1   1 
ATOM   2117  C  CD2   . LEU A 1 1803 ? 202.833 223.036 271.294 1.00 65.58  ? 1803 LEU A CD2   1 
ATOM   2118  N  N     . ARG A 1 1804 ? 207.161 223.153 273.727 1.00 59.80  ? 1804 ARG A N     1 
ATOM   2119  C  CA    . ARG A 1 1804 ? 207.628 224.244 274.571 1.00 61.07  ? 1804 ARG A CA    1 
ATOM   2120  C  C     . ARG A 1 1804 ? 209.109 224.519 274.341 1.00 59.80  ? 1804 ARG A C     1 
ATOM   2121  O  O     . ARG A 1 1804 ? 209.537 225.676 274.398 1.00 66.25  ? 1804 ARG A O     1 
ATOM   2122  C  CB    . ARG A 1 1804 ? 207.299 223.949 276.039 1.00 63.97  ? 1804 ARG A CB    1 
ATOM   2123  C  CG    . ARG A 1 1804 ? 207.643 225.080 276.991 1.00 63.50  ? 1804 ARG A CG    1 
ATOM   2124  C  CD    . ARG A 1 1804 ? 207.276 224.786 278.448 1.00 63.46  ? 1804 ARG A CD    1 
ATOM   2125  N  NE    . ARG A 1 1804 ? 208.022 223.725 279.113 1.00 70.79  ? 1804 ARG A NE    1 
ATOM   2126  C  CZ    . ARG A 1 1804 ? 207.706 223.243 280.309 1.00 71.40  ? 1804 ARG A CZ    1 
ATOM   2127  N  NH1   . ARG A 1 1804 ? 206.681 223.719 280.997 1.00 64.22  ? 1804 ARG A NH1   1 
ATOM   2128  N  NH2   . ARG A 1 1804 ? 208.447 222.273 280.836 1.00 73.23  ? 1804 ARG A NH2   1 
ATOM   2129  N  N     . ARG A 1 1805 ? 209.894 223.482 274.032 1.00 55.13  ? 1805 ARG A N     1 
ATOM   2130  C  CA    . ARG A 1 1805 ? 211.283 223.692 273.633 1.00 51.89  ? 1805 ARG A CA    1 
ATOM   2131  C  C     . ARG A 1 1805 ? 211.382 224.525 272.359 1.00 58.38  ? 1805 ARG A C     1 
ATOM   2132  O  O     . ARG A 1 1805 ? 212.211 225.439 272.269 1.00 65.74  ? 1805 ARG A O     1 
ATOM   2133  C  CB    . ARG A 1 1805 ? 211.982 222.348 273.436 1.00 54.10  ? 1805 ARG A CB    1 
ATOM   2134  C  CG    . ARG A 1 1805 ? 213.422 222.317 273.914 1.00 55.03  ? 1805 ARG A CG    1 
ATOM   2135  C  CD    . ARG A 1 1805 ? 214.211 221.219 273.218 1.00 58.77  ? 1805 ARG A CD    1 
ATOM   2136  N  NE    . ARG A 1 1805 ? 214.157 221.331 271.765 1.00 68.60  ? 1805 ARG A NE    1 
ATOM   2137  C  CZ    . ARG A 1 1805 ? 213.695 220.385 270.957 1.00 65.79  ? 1805 ARG A CZ    1 
ATOM   2138  N  NH1   . ARG A 1 1805 ? 213.237 219.238 271.428 1.00 60.31  ? 1805 ARG A NH1   1 
ATOM   2139  N  NH2   . ARG A 1 1805 ? 213.697 220.596 269.644 1.00 59.24  ? 1805 ARG A NH2   1 
ATOM   2140  N  N     . ARG A 1 1806 ? 210.556 224.216 271.356 1.00 57.36  ? 1806 ARG A N     1 
ATOM   2141  C  CA    . ARG A 1 1806 ? 210.590 224.979 270.112 1.00 52.40  ? 1806 ARG A CA    1 
ATOM   2142  C  C     . ARG A 1 1806 ? 210.154 226.421 270.335 1.00 59.18  ? 1806 ARG A C     1 
ATOM   2143  O  O     . ARG A 1 1806 ? 210.724 227.348 269.744 1.00 69.08  ? 1806 ARG A O     1 
ATOM   2144  C  CB    . ARG A 1 1806 ? 209.716 224.307 269.053 1.00 53.59  ? 1806 ARG A CB    1 
ATOM   2145  C  CG    . ARG A 1 1806 ? 210.241 222.960 268.577 1.00 56.91  ? 1806 ARG A CG    1 
ATOM   2146  C  CD    . ARG A 1 1806 ? 209.421 222.417 267.415 1.00 57.81  ? 1806 ARG A CD    1 
ATOM   2147  N  NE    . ARG A 1 1806 ? 209.741 223.073 266.153 1.00 63.34  ? 1806 ARG A NE    1 
ATOM   2148  C  CZ    . ARG A 1 1806 ? 209.174 222.776 264.992 1.00 60.79  ? 1806 ARG A CZ    1 
ATOM   2149  N  NH1   . ARG A 1 1806 ? 208.250 221.835 264.894 1.00 56.07  ? 1806 ARG A NH1   1 
ATOM   2150  N  NH2   . ARG A 1 1806 ? 209.543 223.441 263.901 1.00 56.77  ? 1806 ARG A NH2   1 
ATOM   2151  N  N     . LYS A 1 1807 ? 209.142 226.632 271.180 1.00 50.49  ? 1807 LYS A N     1 
ATOM   2152  C  CA    . LYS A 1 1807 ? 208.733 227.993 271.511 1.00 43.07  ? 1807 LYS A CA    1 
ATOM   2153  C  C     . LYS A 1 1807 ? 209.859 228.752 272.202 1.00 46.89  ? 1807 LYS A C     1 
ATOM   2154  O  O     . LYS A 1 1807 ? 210.092 229.932 271.912 1.00 57.41  ? 1807 LYS A O     1 
ATOM   2155  C  CB    . LYS A 1 1807 ? 207.487 227.972 272.392 1.00 50.16  ? 1807 LYS A CB    1 
ATOM   2156  C  CG    . LYS A 1 1807 ? 206.230 227.522 271.681 1.00 54.70  ? 1807 LYS A CG    1 
ATOM   2157  C  CD    . LYS A 1 1807 ? 205.046 227.511 272.628 1.00 50.52  ? 1807 LYS A CD    1 
ATOM   2158  C  CE    . LYS A 1 1807 ? 203.826 226.895 271.975 1.00 51.58  ? 1807 LYS A CE    1 
ATOM   2159  N  NZ    . LYS A 1 1807 ? 202.684 226.828 272.921 1.00 57.91  ? 1807 LYS A NZ    1 
ATOM   2160  N  N     . LEU A 1 1808 ? 210.570 228.091 273.120 1.00 47.09  ? 1808 LEU A N     1 
ATOM   2161  C  CA    . LEU A 1 1808 ? 211.697 228.739 273.782 1.00 49.12  ? 1808 LEU A CA    1 
ATOM   2162  C  C     . LEU A 1 1808 ? 212.798 229.081 272.789 1.00 49.11  ? 1808 LEU A C     1 
ATOM   2163  O  O     . LEU A 1 1808 ? 213.429 230.136 272.895 1.00 54.26  ? 1808 LEU A O     1 
ATOM   2164  C  CB    . LEU A 1 1808 ? 212.244 227.849 274.897 1.00 49.27  ? 1808 LEU A CB    1 
ATOM   2165  C  CG    . LEU A 1 1808 ? 211.336 227.599 276.102 1.00 50.55  ? 1808 LEU A CG    1 
ATOM   2166  C  CD1   . LEU A 1 1808 ? 211.857 226.433 276.918 1.00 48.68  ? 1808 LEU A CD1   1 
ATOM   2167  C  CD2   . LEU A 1 1808 ? 211.211 228.841 276.958 1.00 52.09  ? 1808 LEU A CD2   1 
ATOM   2168  N  N     . GLU A 1 1809 ? 213.052 228.196 271.823 1.00 46.75  ? 1809 GLU A N     1 
ATOM   2169  C  CA    . GLU A 1 1809 ? 214.065 228.480 270.809 1.00 48.37  ? 1809 GLU A CA    1 
ATOM   2170  C  C     . GLU A 1 1809 ? 213.673 229.681 269.953 1.00 50.95  ? 1809 GLU A C     1 
ATOM   2171  O  O     . GLU A 1 1809 ? 214.507 230.551 269.664 1.00 50.08  ? 1809 GLU A O     1 
ATOM   2172  C  CB    . GLU A 1 1809 ? 214.286 227.249 269.931 1.00 45.55  ? 1809 GLU A CB    1 
ATOM   2173  C  CG    . GLU A 1 1809 ? 215.007 226.111 270.626 1.00 48.48  ? 1809 GLU A CG    1 
ATOM   2174  C  CD    . GLU A 1 1809 ? 214.941 224.817 269.838 1.00 61.66  ? 1809 GLU A CD    1 
ATOM   2175  O  OE1   . GLU A 1 1809 ? 214.162 224.752 268.863 1.00 58.79  ? 1809 GLU A OE1   1 
ATOM   2176  O  OE2   . GLU A 1 1809 ? 215.667 223.865 270.192 1.00 62.52  ? 1809 GLU A OE2   1 
ATOM   2177  N  N     . HIS A 1 1810 ? 212.404 229.743 269.539 1.00 42.89  ? 1810 HIS A N     1 
ATOM   2178  C  CA    . HIS A 1 1810 ? 211.938 230.888 268.762 1.00 36.23  ? 1810 HIS A CA    1 
ATOM   2179  C  C     . HIS A 1 1810 ? 212.071 232.179 269.557 1.00 44.59  ? 1810 HIS A C     1 
ATOM   2180  O  O     . HIS A 1 1810 ? 212.526 233.201 269.025 1.00 49.82  ? 1810 HIS A O     1 
ATOM   2181  C  CB    . HIS A 1 1810 ? 210.486 230.688 268.331 1.00 33.61  ? 1810 HIS A CB    1 
ATOM   2182  C  CG    . HIS A 1 1810 ? 210.268 229.500 267.449 1.00 44.47  ? 1810 HIS A CG    1 
ATOM   2183  N  ND1   . HIS A 1 1810 ? 211.304 228.766 266.915 1.00 53.29  ? 1810 HIS A ND1   1 
ATOM   2184  C  CD2   . HIS A 1 1810 ? 209.128 228.930 266.991 1.00 41.99  ? 1810 HIS A CD2   1 
ATOM   2185  C  CE1   . HIS A 1 1810 ? 210.812 227.787 266.179 1.00 52.73  ? 1810 HIS A CE1   1 
ATOM   2186  N  NE2   . HIS A 1 1810 ? 209.495 227.866 266.206 1.00 46.89  ? 1810 HIS A NE2   1 
ATOM   2187  N  N     . LEU A 1 1811 ? 211.682 232.150 270.833 1.00 47.20  ? 1811 LEU A N     1 
ATOM   2188  C  CA    . LEU A 1 1811 ? 211.783 233.343 271.662 1.00 41.66  ? 1811 LEU A CA    1 
ATOM   2189  C  C     . LEU A 1 1811 ? 213.232 233.745 271.896 1.00 39.58  ? 1811 LEU A C     1 
ATOM   2190  O  O     . LEU A 1 1811 ? 213.537 234.939 271.944 1.00 42.56  ? 1811 LEU A O     1 
ATOM   2191  C  CB    . LEU A 1 1811 ? 211.066 233.120 272.991 1.00 39.41  ? 1811 LEU A CB    1 
ATOM   2192  C  CG    . LEU A 1 1811 ? 209.580 233.472 272.969 1.00 44.42  ? 1811 LEU A CG    1 
ATOM   2193  C  CD1   . LEU A 1 1811 ? 208.949 233.203 274.318 1.00 49.15  ? 1811 LEU A CD1   1 
ATOM   2194  C  CD2   . LEU A 1 1811 ? 209.388 234.921 272.562 1.00 43.70  ? 1811 LEU A CD2   1 
ATOM   2195  N  N     . ILE A 1 1812 ? 214.136 232.774 272.034 1.00 39.53  ? 1812 ILE A N     1 
ATOM   2196  C  CA    . ILE A 1 1812 ? 215.548 233.098 272.198 1.00 36.91  ? 1812 ILE A CA    1 
ATOM   2197  C  C     . ILE A 1 1812 ? 216.085 233.783 270.950 1.00 40.93  ? 1812 ILE A C     1 
ATOM   2198  O  O     . ILE A 1 1812 ? 216.786 234.796 271.039 1.00 53.36  ? 1812 ILE A O     1 
ATOM   2199  C  CB    . ILE A 1 1812 ? 216.357 231.835 272.539 1.00 40.02  ? 1812 ILE A CB    1 
ATOM   2200  C  CG1   . ILE A 1 1812 ? 216.174 231.464 274.008 1.00 39.54  ? 1812 ILE A CG1   1 
ATOM   2201  C  CG2   . ILE A 1 1812 ? 217.826 232.053 272.244 1.00 46.08  ? 1812 ILE A CG2   1 
ATOM   2202  C  CD1   . ILE A 1 1812 ? 216.951 230.245 274.421 1.00 39.93  ? 1812 ILE A CD1   1 
ATOM   2203  N  N     . THR A 1 1813 ? 215.760 233.252 269.769 1.00 38.77  ? 1813 THR A N     1 
ATOM   2204  C  CA    . THR A 1 1813 ? 216.206 233.895 268.535 1.00 34.11  ? 1813 THR A CA    1 
ATOM   2205  C  C     . THR A 1 1813 ? 215.664 235.316 268.428 1.00 36.89  ? 1813 THR A C     1 
ATOM   2206  O  O     . THR A 1 1813 ? 216.415 236.266 268.147 1.00 47.75  ? 1813 THR A O     1 
ATOM   2207  C  CB    . THR A 1 1813 ? 215.771 233.067 267.326 1.00 40.80  ? 1813 THR A CB    1 
ATOM   2208  O  OG1   . THR A 1 1813 ? 216.127 231.695 267.529 1.00 46.39  ? 1813 THR A OG1   1 
ATOM   2209  C  CG2   . THR A 1 1813 ? 216.439 233.575 266.064 1.00 40.58  ? 1813 THR A CG2   1 
ATOM   2210  N  N     . GLU A 1 1814 ? 214.364 235.484 268.678 1.00 46.17  ? 1814 GLU A N     1 
ATOM   2211  C  CA    . GLU A 1 1814 ? 213.746 236.799 268.552 1.00 40.55  ? 1814 GLU A CA    1 
ATOM   2212  C  C     . GLU A 1 1814 ? 214.344 237.791 269.541 1.00 35.39  ? 1814 GLU A C     1 
ATOM   2213  O  O     . GLU A 1 1814 ? 214.619 238.943 269.190 1.00 46.78  ? 1814 GLU A O     1 
ATOM   2214  C  CB    . GLU A 1 1814 ? 212.237 236.686 268.751 1.00 40.67  ? 1814 GLU A CB    1 
ATOM   2215  C  CG    . GLU A 1 1814 ? 211.504 237.980 268.501 1.00 37.60  ? 1814 GLU A CG    1 
ATOM   2216  C  CD    . GLU A 1 1814 ? 212.035 238.723 267.291 1.00 53.68  ? 1814 GLU A CD    1 
ATOM   2217  O  OE1   . GLU A 1 1814 ? 212.033 238.144 266.184 1.00 49.29  ? 1814 GLU A OE1   1 
ATOM   2218  O  OE2   . GLU A 1 1814 ? 212.452 239.890 267.444 1.00 54.77  ? 1814 GLU A OE2   1 
ATOM   2219  N  N     . LEU A 1 1815 ? 214.561 237.364 270.785 1.00 35.60  ? 1815 LEU A N     1 
ATOM   2220  C  CA    . LEU A 1 1815 ? 215.073 238.287 271.788 1.00 38.96  ? 1815 LEU A CA    1 
ATOM   2221  C  C     . LEU A 1 1815 ? 216.555 238.571 271.598 1.00 38.84  ? 1815 LEU A C     1 
ATOM   2222  O  O     . LEU A 1 1815 ? 217.020 239.649 271.972 1.00 49.00  ? 1815 LEU A O     1 
ATOM   2223  C  CB    . LEU A 1 1815 ? 214.803 237.750 273.189 1.00 40.37  ? 1815 LEU A CB    1 
ATOM   2224  C  CG    . LEU A 1 1815 ? 213.525 238.288 273.829 1.00 37.56  ? 1815 LEU A CG    1 
ATOM   2225  C  CD1   . LEU A 1 1815 ? 212.291 237.679 273.193 1.00 41.58  ? 1815 LEU A CD1   1 
ATOM   2226  C  CD2   . LEU A 1 1815 ? 213.551 238.020 275.308 1.00 43.01  ? 1815 LEU A CD2   1 
ATOM   2227  N  N     . VAL A 1 1816 ? 217.312 237.640 271.015 1.00 34.40  ? 1816 VAL A N     1 
ATOM   2228  C  CA    . VAL A 1 1816 ? 218.684 237.960 270.632 1.00 37.27  ? 1816 VAL A CA    1 
ATOM   2229  C  C     . VAL A 1 1816 ? 218.689 239.045 269.566 1.00 38.51  ? 1816 VAL A C     1 
ATOM   2230  O  O     . VAL A 1 1816 ? 219.478 239.999 269.629 1.00 43.13  ? 1816 VAL A O     1 
ATOM   2231  C  CB    . VAL A 1 1816 ? 219.423 236.694 270.164 1.00 34.12  ? 1816 VAL A CB    1 
ATOM   2232  C  CG1   . VAL A 1 1816 ? 220.695 237.068 269.431 1.00 45.11  ? 1816 VAL A CG1   1 
ATOM   2233  C  CG2   . VAL A 1 1816 ? 219.751 235.812 271.352 1.00 38.15  ? 1816 VAL A CG2   1 
ATOM   2234  N  N     . HIS A 1 1817 ? 217.794 238.931 268.579 1.00 33.53  ? 1817 HIS A N     1 
ATOM   2235  C  CA    . HIS A 1 1817 ? 217.684 239.990 267.578 1.00 32.81  ? 1817 HIS A CA    1 
ATOM   2236  C  C     . HIS A 1 1817 ? 217.292 241.320 268.214 1.00 46.47  ? 1817 HIS A C     1 
ATOM   2237  O  O     . HIS A 1 1817 ? 217.853 242.371 267.875 1.00 50.69  ? 1817 HIS A O     1 
ATOM   2238  C  CB    . HIS A 1 1817 ? 216.672 239.600 266.503 1.00 36.14  ? 1817 HIS A CB    1 
ATOM   2239  C  CG    . HIS A 1 1817 ? 216.397 240.691 265.517 1.00 38.18  ? 1817 HIS A CG    1 
ATOM   2240  N  ND1   . HIS A 1 1817 ? 217.398 241.352 264.840 1.00 44.54  ? 1817 HIS A ND1   1 
ATOM   2241  C  CD2   . HIS A 1 1817 ? 215.233 241.239 265.094 1.00 41.28  ? 1817 HIS A CD2   1 
ATOM   2242  C  CE1   . HIS A 1 1817 ? 216.864 242.260 264.043 1.00 40.94  ? 1817 HIS A CE1   1 
ATOM   2243  N  NE2   . HIS A 1 1817 ? 215.552 242.211 264.178 1.00 45.95  ? 1817 HIS A NE2   1 
ATOM   2244  N  N     . GLN A 1 1818 ? 216.325 241.293 269.133 1.00 46.53  ? 1818 GLN A N     1 
ATOM   2245  C  CA    . GLN A 1 1818 ? 215.882 242.519 269.791 1.00 33.40  ? 1818 GLN A CA    1 
ATOM   2246  C  C     . GLN A 1 1818 ? 217.000 243.144 270.614 1.00 36.74  ? 1818 GLN A C     1 
ATOM   2247  O  O     . GLN A 1 1818 ? 217.167 244.368 270.621 1.00 41.96  ? 1818 GLN A O     1 
ATOM   2248  C  CB    . GLN A 1 1818 ? 214.672 242.230 270.675 1.00 34.20  ? 1818 GLN A CB    1 
ATOM   2249  C  CG    . GLN A 1 1818 ? 213.416 241.882 269.908 1.00 37.30  ? 1818 GLN A CG    1 
ATOM   2250  C  CD    . GLN A 1 1818 ? 212.293 241.442 270.816 1.00 43.84  ? 1818 GLN A CD    1 
ATOM   2251  O  OE1   . GLN A 1 1818 ? 212.420 241.475 272.038 1.00 47.99  ? 1818 GLN A OE1   1 
ATOM   2252  N  NE2   . GLN A 1 1818 ? 211.187 241.020 270.223 1.00 42.67  ? 1818 GLN A NE2   1 
ATOM   2253  N  N     . ARG A 1 1819 ? 217.767 242.318 271.325 1.00 36.82  ? 1819 ARG A N     1 
ATOM   2254  C  CA    . ARG A 1 1819 ? 218.890 242.821 272.105 1.00 37.56  ? 1819 ARG A CA    1 
ATOM   2255  C  C     . ARG A 1 1819 ? 219.943 243.452 271.208 1.00 46.22  ? 1819 ARG A C     1 
ATOM   2256  O  O     . ARG A 1 1819 ? 220.490 244.511 271.535 1.00 54.25  ? 1819 ARG A O     1 
ATOM   2257  C  CB    . ARG A 1 1819 ? 219.492 241.685 272.930 1.00 42.06  ? 1819 ARG A CB    1 
ATOM   2258  C  CG    . ARG A 1 1819 ? 220.629 242.096 273.839 1.00 44.05  ? 1819 ARG A CG    1 
ATOM   2259  C  CD    . ARG A 1 1819 ? 221.423 240.882 274.272 1.00 47.08  ? 1819 ARG A CD    1 
ATOM   2260  N  NE    . ARG A 1 1819 ? 221.948 240.149 273.127 1.00 49.02  ? 1819 ARG A NE    1 
ATOM   2261  C  CZ    . ARG A 1 1819 ? 222.460 238.929 273.190 1.00 54.82  ? 1819 ARG A CZ    1 
ATOM   2262  N  NH1   . ARG A 1 1819 ? 222.539 238.271 274.334 1.00 50.33  ? 1819 ARG A NH1   1 
ATOM   2263  N  NH2   . ARG A 1 1819 ? 222.908 238.355 272.077 1.00 51.38  ? 1819 ARG A NH2   1 
ATOM   2264  N  N     . ASP A 1 1820 ? 220.244 242.818 270.073 1.00 48.98  ? 1820 ASP A N     1 
ATOM   2265  C  CA    . ASP A 1 1820 ? 221.218 243.396 269.151 1.00 40.98  ? 1820 ASP A CA    1 
ATOM   2266  C  C     . ASP A 1 1820 ? 220.734 244.732 268.596 1.00 40.43  ? 1820 ASP A C     1 
ATOM   2267  O  O     . ASP A 1 1820 ? 221.511 245.692 268.503 1.00 43.77  ? 1820 ASP A O     1 
ATOM   2268  C  CB    . ASP A 1 1820 ? 221.513 242.416 268.018 1.00 46.27  ? 1820 ASP A CB    1 
ATOM   2269  C  CG    . ASP A 1 1820 ? 222.465 241.315 268.438 1.00 57.92  ? 1820 ASP A CG    1 
ATOM   2270  O  OD1   . ASP A 1 1820 ? 222.953 241.358 269.587 1.00 57.03  ? 1820 ASP A OD1   1 
ATOM   2271  O  OD2   . ASP A 1 1820 ? 222.729 240.409 267.620 1.00 58.31  ? 1820 ASP A OD2   1 
ATOM   2272  N  N     . VAL A 1 1821 ? 219.453 244.816 268.232 1.00 42.93  ? 1821 VAL A N     1 
ATOM   2273  C  CA    . VAL A 1 1821 ? 218.913 246.069 267.709 1.00 38.12  ? 1821 VAL A CA    1 
ATOM   2274  C  C     . VAL A 1 1821 ? 218.951 247.159 268.774 1.00 44.35  ? 1821 VAL A C     1 
ATOM   2275  O  O     . VAL A 1 1821 ? 219.302 248.310 268.490 1.00 48.23  ? 1821 VAL A O     1 
ATOM   2276  C  CB    . VAL A 1 1821 ? 217.490 245.855 267.168 1.00 34.24  ? 1821 VAL A CB    1 
ATOM   2277  C  CG1   . VAL A 1 1821 ? 216.827 247.189 266.880 1.00 38.14  ? 1821 VAL A CG1   1 
ATOM   2278  C  CG2   . VAL A 1 1821 ? 217.532 245.010 265.918 1.00 38.62  ? 1821 VAL A CG2   1 
ATOM   2279  N  N     . THR A 1 1822 ? 218.587 246.819 270.012 1.00 50.64  ? 1822 THR A N     1 
ATOM   2280  C  CA    . THR A 1 1822 ? 218.599 247.811 271.082 1.00 41.32  ? 1822 THR A CA    1 
ATOM   2281  C  C     . THR A 1 1822 ? 220.019 248.273 271.387 1.00 42.48  ? 1822 THR A C     1 
ATOM   2282  O  O     . THR A 1 1822 ? 220.250 249.458 271.651 1.00 51.14  ? 1822 THR A O     1 
ATOM   2283  C  CB    . THR A 1 1822 ? 217.933 247.241 272.333 1.00 46.73  ? 1822 THR A CB    1 
ATOM   2284  O  OG1   . THR A 1 1822 ? 216.671 246.664 271.979 1.00 45.39  ? 1822 THR A OG1   1 
ATOM   2285  C  CG2   . THR A 1 1822 ? 217.698 248.339 273.352 1.00 45.96  ? 1822 THR A CG2   1 
ATOM   2286  N  N     . ARG A 1 1823 ? 220.984 247.352 271.353 1.00 48.00  ? 1823 ARG A N     1 
ATOM   2287  C  CA    . ARG A 1 1823 ? 222.380 247.731 271.545 1.00 49.69  ? 1823 ARG A CA    1 
ATOM   2288  C  C     . ARG A 1 1823 ? 222.850 248.673 270.445 1.00 53.24  ? 1823 ARG A C     1 
ATOM   2289  O  O     . ARG A 1 1823 ? 223.559 249.651 270.714 1.00 56.28  ? 1823 ARG A O     1 
ATOM   2290  C  CB    . ARG A 1 1823 ? 223.260 246.483 271.588 1.00 47.89  ? 1823 ARG A CB    1 
ATOM   2291  C  CG    . ARG A 1 1823 ? 223.259 245.756 272.918 1.00 46.73  ? 1823 ARG A CG    1 
ATOM   2292  C  CD    . ARG A 1 1823 ? 224.140 244.521 272.857 1.00 49.67  ? 1823 ARG A CD    1 
ATOM   2293  N  NE    . ARG A 1 1823 ? 224.125 243.770 274.107 1.00 57.10  ? 1823 ARG A NE    1 
ATOM   2294  C  CZ    . ARG A 1 1823 ? 224.590 242.537 274.243 1.00 58.71  ? 1823 ARG A CZ    1 
ATOM   2295  N  NH1   . ARG A 1 1823 ? 225.121 241.882 273.223 1.00 53.70  ? 1823 ARG A NH1   1 
ATOM   2296  N  NH2   . ARG A 1 1823 ? 224.523 241.945 275.432 1.00 52.24  ? 1823 ARG A NH2   1 
ATOM   2297  N  N     . SER A 1 1824 ? 222.474 248.390 269.195 1.00 55.25  ? 1824 SER A N     1 
ATOM   2298  C  CA    . SER A 1 1824 ? 222.844 249.277 268.095 1.00 50.61  ? 1824 SER A CA    1 
ATOM   2299  C  C     . SER A 1 1824 ? 222.211 250.654 268.265 1.00 51.94  ? 1824 SER A C     1 
ATOM   2300  O  O     . SER A 1 1824 ? 222.850 251.678 268.002 1.00 57.84  ? 1824 SER A O     1 
ATOM   2301  C  CB    . SER A 1 1824 ? 222.436 248.661 266.758 1.00 51.03  ? 1824 SER A CB    1 
ATOM   2302  O  OG    . SER A 1 1824 ? 221.027 248.570 266.647 1.00 55.36  ? 1824 SER A OG    1 
ATOM   2303  N  N     . LEU A 1 1825 ? 220.949 250.696 268.696 1.00 49.82  ? 1825 LEU A N     1 
ATOM   2304  C  CA    . LEU A 1 1825 ? 220.285 251.976 268.928 1.00 50.52  ? 1825 LEU A CA    1 
ATOM   2305  C  C     . LEU A 1 1825 ? 220.980 252.763 270.032 1.00 55.63  ? 1825 LEU A C     1 
ATOM   2306  O  O     . LEU A 1 1825 ? 221.156 253.981 269.927 1.00 61.50  ? 1825 LEU A O     1 
ATOM   2307  C  CB    . LEU A 1 1825 ? 218.814 251.751 269.275 1.00 52.92  ? 1825 LEU A CB    1 
ATOM   2308  C  CG    . LEU A 1 1825 ? 217.876 251.345 268.139 1.00 56.05  ? 1825 LEU A CG    1 
ATOM   2309  C  CD1   . LEU A 1 1825 ? 216.433 251.439 268.594 1.00 48.15  ? 1825 LEU A CD1   1 
ATOM   2310  C  CD2   . LEU A 1 1825 ? 218.109 252.211 266.914 1.00 55.93  ? 1825 LEU A CD2   1 
ATOM   2311  N  N     . ILE A 1 1826 ? 221.373 252.080 271.109 1.00 62.61  ? 1826 ILE A N     1 
ATOM   2312  C  CA    . ILE A 1 1826 ? 222.056 252.752 272.213 1.00 57.64  ? 1826 ILE A CA    1 
ATOM   2313  C  C     . ILE A 1 1826 ? 223.403 253.297 271.753 1.00 58.63  ? 1826 ILE A C     1 
ATOM   2314  O  O     . ILE A 1 1826 ? 223.766 254.439 272.059 1.00 61.23  ? 1826 ILE A O     1 
ATOM   2315  C  CB    . ILE A 1 1826 ? 222.211 251.796 273.409 1.00 54.34  ? 1826 ILE A CB    1 
ATOM   2316  C  CG1   . ILE A 1 1826 ? 220.853 251.519 274.051 1.00 51.11  ? 1826 ILE A CG1   1 
ATOM   2317  C  CG2   . ILE A 1 1826 ? 223.174 252.369 274.431 1.00 55.90  ? 1826 ILE A CG2   1 
ATOM   2318  C  CD1   . ILE A 1 1826 ? 220.929 250.648 275.282 1.00 56.35  ? 1826 ILE A CD1   1 
ATOM   2319  N  N     . LYS A 1 1827 ? 224.164 252.489 271.011 1.00 56.38  ? 1827 LYS A N     1 
ATOM   2320  C  CA    . LYS A 1 1827 ? 225.479 252.931 270.554 1.00 60.52  ? 1827 LYS A CA    1 
ATOM   2321  C  C     . LYS A 1 1827 ? 225.370 254.127 269.616 1.00 64.39  ? 1827 LYS A C     1 
ATOM   2322  O  O     . LYS A 1 1827 ? 226.170 255.065 269.699 1.00 64.38  ? 1827 LYS A O     1 
ATOM   2323  C  CB    . LYS A 1 1827 ? 226.215 251.782 269.867 1.00 61.79  ? 1827 LYS A CB    1 
ATOM   2324  C  CG    . LYS A 1 1827 ? 227.641 252.127 269.477 1.00 63.67  ? 1827 LYS A CG    1 
ATOM   2325  C  CD    . LYS A 1 1827 ? 228.316 250.986 268.741 1.00 63.37  ? 1827 LYS A CD    1 
ATOM   2326  C  CE    . LYS A 1 1827 ? 228.672 249.852 269.684 1.00 66.27  ? 1827 LYS A CE    1 
ATOM   2327  N  NZ    . LYS A 1 1827 ? 229.439 248.782 268.989 1.00 64.81  ? 1827 LYS A NZ    1 
ATOM   2328  N  N     . SER A 1 1828 ? 224.386 254.112 268.716 1.00 65.23  ? 1828 SER A N     1 
ATOM   2329  C  CA    . SER A 1 1828 ? 224.211 255.205 267.769 1.00 60.46  ? 1828 SER A CA    1 
ATOM   2330  C  C     . SER A 1 1828 ? 223.623 256.454 268.410 1.00 66.06  ? 1828 SER A C     1 
ATOM   2331  O  O     . SER A 1 1828 ? 223.542 257.488 267.739 1.00 68.59  ? 1828 SER A O     1 
ATOM   2332  C  CB    . SER A 1 1828 ? 223.322 254.754 266.609 1.00 61.91  ? 1828 SER A CB    1 
ATOM   2333  O  OG    . SER A 1 1828 ? 223.844 253.592 265.990 1.00 65.18  ? 1828 SER A OG    1 
ATOM   2334  N  N     . LYS A 1 1829 ? 223.209 256.379 269.676 1.00 67.64  ? 1829 LYS A N     1 
ATOM   2335  C  CA    . LYS A 1 1829 ? 222.641 257.518 270.398 1.00 65.85  ? 1829 LYS A CA    1 
ATOM   2336  C  C     . LYS A 1 1829 ? 221.400 258.060 269.695 1.00 69.57  ? 1829 LYS A C     1 
ATOM   2337  O  O     . LYS A 1 1829 ? 221.266 259.263 269.465 1.00 70.97  ? 1829 LYS A O     1 
ATOM   2338  C  CB    . LYS A 1 1829 ? 223.681 258.622 270.599 1.00 66.28  ? 1829 LYS A CB    1 
ATOM   2339  C  CG    . LYS A 1 1829 ? 224.851 258.206 271.470 1.00 67.32  ? 1829 LYS A CG    1 
ATOM   2340  C  CD    . LYS A 1 1829 ? 225.801 259.361 271.711 1.00 69.49  ? 1829 LYS A CD    1 
ATOM   2341  C  CE    . LYS A 1 1829 ? 227.011 258.910 272.506 1.00 70.50  ? 1829 LYS A CE    1 
ATOM   2342  N  NZ    . LYS A 1 1829 ? 226.635 258.466 273.875 1.00 68.15  ? 1829 LYS A NZ    1 
ATOM   2343  N  N     . ILE A 1 1830 ? 220.482 257.159 269.348 1.00 69.08  ? 1830 ILE A N     1 
ATOM   2344  C  CA    . ILE A 1 1830 ? 219.232 257.563 268.718 1.00 66.08  ? 1830 ILE A CA    1 
ATOM   2345  C  C     . ILE A 1 1830 ? 218.268 258.053 269.788 1.00 69.07  ? 1830 ILE A C     1 
ATOM   2346  O  O     . ILE A 1 1830 ? 218.003 257.355 270.775 1.00 73.05  ? 1830 ILE A O     1 
ATOM   2347  C  CB    . ILE A 1 1830 ? 218.632 256.398 267.917 1.00 63.90  ? 1830 ILE A CB    1 
ATOM   2348  C  CG1   . ILE A 1 1830 ? 219.684 255.794 266.985 1.00 65.42  ? 1830 ILE A CG1   1 
ATOM   2349  C  CG2   . ILE A 1 1830 ? 217.421 256.863 267.129 1.00 65.95  ? 1830 ILE A CG2   1 
ATOM   2350  C  CD1   . ILE A 1 1830 ? 220.323 256.798 266.053 1.00 65.35  ? 1830 ILE A CD1   1 
ATOM   2351  N  N     . ASP A 1 1831 ? 217.739 259.261 269.600 1.00 69.42  ? 1831 ASP A N     1 
ATOM   2352  C  CA    . ASP A 1 1831 ? 216.784 259.838 270.533 1.00 69.28  ? 1831 ASP A CA    1 
ATOM   2353  C  C     . ASP A 1 1831 ? 215.461 260.222 269.885 1.00 68.12  ? 1831 ASP A C     1 
ATOM   2354  O  O     . ASP A 1 1831 ? 214.615 260.825 270.554 1.00 67.51  ? 1831 ASP A O     1 
ATOM   2355  C  CB    . ASP A 1 1831 ? 217.393 261.063 271.232 1.00 71.20  ? 1831 ASP A CB    1 
ATOM   2356  C  CG    . ASP A 1 1831 ? 217.732 262.187 270.269 1.00 75.72  ? 1831 ASP A CG    1 
ATOM   2357  O  OD1   . ASP A 1 1831 ? 217.542 262.021 269.046 1.00 77.55  ? 1831 ASP A OD1   1 
ATOM   2358  O  OD2   . ASP A 1 1831 ? 218.192 263.247 270.741 1.00 75.35  ? 1831 ASP A OD2   1 
ATOM   2359  N  N     . ASN A 1 1832 ? 215.257 259.895 268.613 1.00 62.94  ? 1832 ASN A N     1 
ATOM   2360  C  CA    . ASN A 1 1832 ? 214.036 260.232 267.898 1.00 64.38  ? 1832 ASN A CA    1 
ATOM   2361  C  C     . ASN A 1 1832 ? 213.395 258.969 267.345 1.00 62.47  ? 1832 ASN A C     1 
ATOM   2362  O  O     . ASN A 1 1832 ? 214.090 258.062 266.879 1.00 63.20  ? 1832 ASN A O     1 
ATOM   2363  C  CB    . ASN A 1 1832 ? 214.318 261.215 266.759 1.00 63.36  ? 1832 ASN A CB    1 
ATOM   2364  C  CG    . ASN A 1 1832 ? 213.129 262.098 266.446 1.00 66.72  ? 1832 ASN A CG    1 
ATOM   2365  O  OD1   . ASN A 1 1832 ? 212.177 262.175 267.221 1.00 65.31  ? 1832 ASN A OD1   1 
ATOM   2366  N  ND2   . ASN A 1 1832 ? 213.177 262.770 265.303 1.00 64.56  ? 1832 ASN A ND2   1 
ATOM   2367  N  N     . ALA A 1 1833 ? 212.066 258.914 267.404 1.00 52.91  ? 1833 ALA A N     1 
ATOM   2368  C  CA    . ALA A 1 1833 ? 211.330 257.802 266.821 1.00 55.03  ? 1833 ALA A CA    1 
ATOM   2369  C  C     . ALA A 1 1833 ? 211.209 257.907 265.308 1.00 62.04  ? 1833 ALA A C     1 
ATOM   2370  O  O     . ALA A 1 1833 ? 210.873 256.911 264.660 1.00 60.43  ? 1833 ALA A O     1 
ATOM   2371  C  CB    . ALA A 1 1833 ? 209.935 257.705 267.441 1.00 55.84  ? 1833 ALA A CB    1 
ATOM   2372  N  N     . LYS A 1 1834 ? 211.466 259.082 264.735 1.00 58.14  ? 1834 LYS A N     1 
ATOM   2373  C  CA    . LYS A 1 1834 ? 211.458 259.266 263.292 1.00 50.14  ? 1834 LYS A CA    1 
ATOM   2374  C  C     . LYS A 1 1834 ? 212.839 259.129 262.669 1.00 54.39  ? 1834 LYS A C     1 
ATOM   2375  O  O     . LYS A 1 1834 ? 212.970 259.289 261.452 1.00 59.09  ? 1834 LYS A O     1 
ATOM   2376  C  CB    . LYS A 1 1834 ? 210.872 260.637 262.936 1.00 51.10  ? 1834 LYS A CB    1 
ATOM   2377  C  CG    . LYS A 1 1834 ? 209.356 260.707 263.018 1.00 51.22  ? 1834 LYS A CG    1 
ATOM   2378  C  CD    . LYS A 1 1834 ? 208.705 259.559 262.266 1.00 60.15  ? 1834 LYS A CD    1 
ATOM   2379  C  CE    . LYS A 1 1834 ? 207.257 259.367 262.690 1.00 58.67  ? 1834 LYS A CE    1 
ATOM   2380  N  NZ    . LYS A 1 1834 ? 207.136 258.469 263.872 1.00 58.12  ? 1834 LYS A NZ    1 
ATOM   2381  N  N     . SER A 1 1835 ? 213.866 258.848 263.468 1.00 49.32  ? 1835 SER A N     1 
ATOM   2382  C  CA    . SER A 1 1835 ? 215.196 258.619 262.924 1.00 41.26  ? 1835 SER A CA    1 
ATOM   2383  C  C     . SER A 1 1835 ? 215.213 257.336 262.105 1.00 48.56  ? 1835 SER A C     1 
ATOM   2384  O  O     . SER A 1 1835 ? 214.575 256.344 262.465 1.00 63.75  ? 1835 SER A O     1 
ATOM   2385  C  CB    . SER A 1 1835 ? 216.221 258.539 264.052 1.00 49.16  ? 1835 SER A CB    1 
ATOM   2386  O  OG    . SER A 1 1835 ? 217.472 258.085 263.571 1.00 55.93  ? 1835 SER A OG    1 
ATOM   2387  N  N     . PHE A 1 1836 ? 215.948 257.358 260.991 1.00 49.29  ? 1836 PHE A N     1 
ATOM   2388  C  CA    . PHE A 1 1836 ? 215.963 256.199 260.106 1.00 43.83  ? 1836 PHE A CA    1 
ATOM   2389  C  C     . PHE A 1 1836 ? 216.636 254.997 260.754 1.00 42.51  ? 1836 PHE A C     1 
ATOM   2390  O  O     . PHE A 1 1836 ? 216.363 253.857 260.365 1.00 47.82  ? 1836 PHE A O     1 
ATOM   2391  C  CB    . PHE A 1 1836 ? 216.651 256.537 258.786 1.00 39.34  ? 1836 PHE A CB    1 
ATOM   2392  C  CG    . PHE A 1 1836 ? 216.409 255.522 257.710 1.00 42.22  ? 1836 PHE A CG    1 
ATOM   2393  C  CD1   . PHE A 1 1836 ? 215.191 255.463 257.058 1.00 43.18  ? 1836 PHE A CD1   1 
ATOM   2394  C  CD2   . PHE A 1 1836 ? 217.391 254.613 257.362 1.00 39.25  ? 1836 PHE A CD2   1 
ATOM   2395  C  CE1   . PHE A 1 1836 ? 214.962 254.526 256.073 1.00 42.94  ? 1836 PHE A CE1   1 
ATOM   2396  C  CE2   . PHE A 1 1836 ? 217.164 253.673 256.379 1.00 35.07  ? 1836 PHE A CE2   1 
ATOM   2397  C  CZ    . PHE A 1 1836 ? 215.951 253.630 255.735 1.00 38.51  ? 1836 PHE A CZ    1 
ATOM   2398  N  N     . GLU A 1 1837 ? 217.514 255.221 261.732 1.00 41.59  ? 1837 GLU A N     1 
ATOM   2399  C  CA    . GLU A 1 1837 ? 218.107 254.099 262.451 1.00 49.39  ? 1837 GLU A CA    1 
ATOM   2400  C  C     . GLU A 1 1837 ? 217.058 253.294 263.203 1.00 50.87  ? 1837 GLU A C     1 
ATOM   2401  O  O     . GLU A 1 1837 ? 217.301 252.127 263.528 1.00 51.18  ? 1837 GLU A O     1 
ATOM   2402  C  CB    . GLU A 1 1837 ? 219.183 254.598 263.414 1.00 51.60  ? 1837 GLU A CB    1 
ATOM   2403  C  CG    . GLU A 1 1837 ? 220.496 254.949 262.738 1.00 52.58  ? 1837 GLU A CG    1 
ATOM   2404  C  CD    . GLU A 1 1837 ? 220.559 256.401 262.307 1.00 60.91  ? 1837 GLU A CD    1 
ATOM   2405  O  OE1   . GLU A 1 1837 ? 219.572 257.133 262.534 1.00 60.98  ? 1837 GLU A OE1   1 
ATOM   2406  O  OE2   . GLU A 1 1837 ? 221.593 256.811 261.740 1.00 57.15  ? 1837 GLU A OE2   1 
ATOM   2407  N  N     . TRP A 1 1838 ? 215.905 253.893 263.488 1.00 49.74  ? 1838 TRP A N     1 
ATOM   2408  C  CA    . TRP A 1 1838 ? 214.755 253.186 264.032 1.00 40.29  ? 1838 TRP A CA    1 
ATOM   2409  C  C     . TRP A 1 1838 ? 213.702 252.878 262.981 1.00 41.93  ? 1838 TRP A C     1 
ATOM   2410  O  O     . TRP A 1 1838 ? 213.057 251.828 263.055 1.00 54.37  ? 1838 TRP A O     1 
ATOM   2411  C  CB    . TRP A 1 1838 ? 214.119 254.003 265.161 1.00 45.45  ? 1838 TRP A CB    1 
ATOM   2412  C  CG    . TRP A 1 1838 ? 212.850 253.423 265.704 1.00 42.95  ? 1838 TRP A CG    1 
ATOM   2413  C  CD1   . TRP A 1 1838 ? 211.628 254.025 265.743 1.00 42.99  ? 1838 TRP A CD1   1 
ATOM   2414  C  CD2   . TRP A 1 1838 ? 212.676 252.128 266.290 1.00 44.50  ? 1838 TRP A CD2   1 
ATOM   2415  N  NE1   . TRP A 1 1838 ? 210.704 253.188 266.314 1.00 42.44  ? 1838 TRP A NE1   1 
ATOM   2416  C  CE2   . TRP A 1 1838 ? 211.323 252.016 266.660 1.00 45.55  ? 1838 TRP A CE2   1 
ATOM   2417  C  CE3   . TRP A 1 1838 ? 213.533 251.052 266.537 1.00 44.71  ? 1838 TRP A CE3   1 
ATOM   2418  C  CZ2   . TRP A 1 1838 ? 210.807 250.873 267.262 1.00 43.96  ? 1838 TRP A CZ2   1 
ATOM   2419  C  CZ3   . TRP A 1 1838 ? 213.018 249.920 267.135 1.00 38.47  ? 1838 TRP A CZ3   1 
ATOM   2420  C  CH2   . TRP A 1 1838 ? 211.670 249.838 267.489 1.00 42.32  ? 1838 TRP A CH2   1 
ATOM   2421  N  N     . LEU A 1 1839 ? 213.518 253.764 262.000 1.00 36.14  ? 1839 LEU A N     1 
ATOM   2422  C  CA    . LEU A 1 1839 ? 212.521 253.527 260.964 1.00 38.59  ? 1839 LEU A CA    1 
ATOM   2423  C  C     . LEU A 1 1839 ? 212.900 252.354 260.069 1.00 45.29  ? 1839 LEU A C     1 
ATOM   2424  O  O     . LEU A 1 1839 ? 212.015 251.655 259.563 1.00 48.51  ? 1839 LEU A O     1 
ATOM   2425  C  CB    . LEU A 1 1839 ? 212.320 254.788 260.126 1.00 32.60  ? 1839 LEU A CB    1 
ATOM   2426  C  CG    . LEU A 1 1839 ? 211.593 255.953 260.796 1.00 43.15  ? 1839 LEU A CG    1 
ATOM   2427  C  CD1   . LEU A 1 1839 ? 211.174 256.981 259.762 1.00 46.57  ? 1839 LEU A CD1   1 
ATOM   2428  C  CD2   . LEU A 1 1839 ? 210.389 255.469 261.581 1.00 44.63  ? 1839 LEU A CD2   1 
ATOM   2429  N  N     . SER A 1 1840 ? 214.197 252.122 259.857 1.00 40.22  ? 1840 SER A N     1 
ATOM   2430  C  CA    . SER A 1 1840 ? 214.621 251.016 259.007 1.00 28.84  ? 1840 SER A CA    1 
ATOM   2431  C  C     . SER A 1 1840 ? 214.298 249.656 259.610 1.00 40.37  ? 1840 SER A C     1 
ATOM   2432  O  O     . SER A 1 1840 ? 214.165 248.680 258.866 1.00 48.51  ? 1840 SER A O     1 
ATOM   2433  C  CB    . SER A 1 1840 ? 216.119 251.112 258.727 1.00 33.19  ? 1840 SER A CB    1 
ATOM   2434  O  OG    . SER A 1 1840 ? 216.853 251.228 259.930 1.00 45.24  ? 1840 SER A OG    1 
ATOM   2435  N  N     . GLN A 1 1841 ? 214.172 249.567 260.931 1.00 41.52  ? 1841 GLN A N     1 
ATOM   2436  C  CA    . GLN A 1 1841 ? 213.866 248.303 261.579 1.00 40.73  ? 1841 GLN A CA    1 
ATOM   2437  C  C     . GLN A 1 1841 ? 212.412 247.912 261.338 1.00 43.90  ? 1841 GLN A C     1 
ATOM   2438  O  O     . GLN A 1 1841 ? 211.576 248.730 260.949 1.00 47.67  ? 1841 GLN A O     1 
ATOM   2439  C  CB    . GLN A 1 1841 ? 214.133 248.386 263.082 1.00 34.61  ? 1841 GLN A CB    1 
ATOM   2440  C  CG    . GLN A 1 1841 ? 215.486 248.957 263.456 1.00 36.90  ? 1841 GLN A CG    1 
ATOM   2441  C  CD    . GLN A 1 1841 ? 216.638 248.146 262.904 1.00 47.61  ? 1841 GLN A CD    1 
ATOM   2442  O  OE1   . GLN A 1 1841 ? 216.554 246.924 262.789 1.00 51.16  ? 1841 GLN A OE1   1 
ATOM   2443  N  NE2   . GLN A 1 1841 ? 217.727 248.823 262.566 1.00 46.70  ? 1841 GLN A NE2   1 
ATOM   2444  N  N     . MET A 1 1842 ? 212.118 246.636 261.572 1.00 39.22  ? 1842 MET A N     1 
ATOM   2445  C  CA    . MET A 1 1842 ? 210.743 246.157 261.535 1.00 35.78  ? 1842 MET A CA    1 
ATOM   2446  C  C     . MET A 1 1842 ? 210.081 246.464 262.870 1.00 43.26  ? 1842 MET A C     1 
ATOM   2447  O  O     . MET A 1 1842 ? 210.560 246.028 263.922 1.00 48.66  ? 1842 MET A O     1 
ATOM   2448  C  CB    . MET A 1 1842 ? 210.699 244.661 261.238 1.00 37.49  ? 1842 MET A CB    1 
ATOM   2449  C  CG    . MET A 1 1842 ? 209.356 244.177 260.717 1.00 37.44  ? 1842 MET A CG    1 
ATOM   2450  S  SD    . MET A 1 1842 ? 209.489 242.698 259.701 1.00 54.36  ? 1842 MET A SD    1 
ATOM   2451  C  CE    . MET A 1 1842 ? 209.399 243.403 258.059 1.00 47.36  ? 1842 MET A CE    1 
ATOM   2452  N  N     . ARG A 1 1843 ? 208.985 247.215 262.830 1.00 44.01  ? 1843 ARG A N     1 
ATOM   2453  C  CA    . ARG A 1 1843 ? 208.313 247.696 264.027 1.00 41.42  ? 1843 ARG A CA    1 
ATOM   2454  C  C     . ARG A 1 1843 ? 206.855 247.269 263.987 1.00 42.71  ? 1843 ARG A C     1 
ATOM   2455  O  O     . ARG A 1 1843 ? 206.200 247.391 262.947 1.00 42.85  ? 1843 ARG A O     1 
ATOM   2456  C  CB    . ARG A 1 1843 ? 208.426 249.218 264.134 1.00 43.47  ? 1843 ARG A CB    1 
ATOM   2457  C  CG    . ARG A 1 1843 ? 209.803 249.746 263.767 1.00 36.78  ? 1843 ARG A CG    1 
ATOM   2458  C  CD    . ARG A 1 1843 ? 209.834 251.259 263.701 1.00 35.95  ? 1843 ARG A CD    1 
ATOM   2459  N  NE    . ARG A 1 1843 ? 208.918 251.804 262.707 1.00 38.92  ? 1843 ARG A NE    1 
ATOM   2460  C  CZ    . ARG A 1 1843 ? 209.105 251.741 261.396 1.00 40.54  ? 1843 ARG A CZ    1 
ATOM   2461  N  NH1   . ARG A 1 1843 ? 210.161 251.142 260.876 1.00 43.44  ? 1843 ARG A NH1   1 
ATOM   2462  N  NH2   . ARG A 1 1843 ? 208.208 252.297 260.587 1.00 39.95  ? 1843 ARG A NH2   1 
ATOM   2463  N  N     . PHE A 1 1844 ? 206.353 246.770 265.112 1.00 45.52  ? 1844 PHE A N     1 
ATOM   2464  C  CA    . PHE A 1 1844 ? 204.986 246.279 265.211 1.00 42.68  ? 1844 PHE A CA    1 
ATOM   2465  C  C     . PHE A 1 1844 ? 204.157 247.248 266.039 1.00 46.76  ? 1844 PHE A C     1 
ATOM   2466  O  O     . PHE A 1 1844 ? 204.561 247.635 267.139 1.00 46.47  ? 1844 PHE A O     1 
ATOM   2467  C  CB    . PHE A 1 1844 ? 204.938 244.889 265.843 1.00 42.90  ? 1844 PHE A CB    1 
ATOM   2468  C  CG    . PHE A 1 1844 ? 205.539 243.816 264.992 1.00 36.54  ? 1844 PHE A CG    1 
ATOM   2469  C  CD1   . PHE A 1 1844 ? 205.805 244.036 263.659 1.00 50.75  ? 1844 PHE A CD1   1 
ATOM   2470  C  CD2   . PHE A 1 1844 ? 205.800 242.573 265.514 1.00 52.74  ? 1844 PHE A CD2   1 
ATOM   2471  C  CE1   . PHE A 1 1844 ? 206.357 243.046 262.882 1.00 52.38  ? 1844 PHE A CE1   1 
ATOM   2472  C  CE2   . PHE A 1 1844 ? 206.341 241.582 264.730 1.00 55.65  ? 1844 PHE A CE2   1 
ATOM   2473  C  CZ    . PHE A 1 1844 ? 206.620 241.821 263.416 1.00 47.11  ? 1844 PHE A CZ    1 
ATOM   2474  N  N     . TYR A 1 1845 ? 202.996 247.625 265.512 1.00 44.94  ? 1845 TYR A N     1 
ATOM   2475  C  CA    . TYR A 1 1845 ? 202.089 248.557 266.168 1.00 54.83  ? 1845 TYR A CA    1 
ATOM   2476  C  C     . TYR A 1 1845 ? 200.722 247.902 266.280 1.00 54.24  ? 1845 TYR A C     1 
ATOM   2477  O  O     . TYR A 1 1845 ? 200.062 247.659 265.264 1.00 57.24  ? 1845 TYR A O     1 
ATOM   2478  C  CB    . TYR A 1 1845 ? 202.010 249.871 265.391 1.00 50.98  ? 1845 TYR A CB    1 
ATOM   2479  C  CG    . TYR A 1 1845 ? 203.350 250.551 265.235 1.00 53.36  ? 1845 TYR A CG    1 
ATOM   2480  C  CD1   . TYR A 1 1845 ? 204.254 250.587 266.287 1.00 58.63  ? 1845 TYR A CD1   1 
ATOM   2481  C  CD2   . TYR A 1 1845 ? 203.717 251.141 264.036 1.00 50.23  ? 1845 TYR A CD2   1 
ATOM   2482  C  CE1   . TYR A 1 1845 ? 205.482 251.199 266.153 1.00 55.17  ? 1845 TYR A CE1   1 
ATOM   2483  C  CE2   . TYR A 1 1845 ? 204.945 251.756 263.893 1.00 50.94  ? 1845 TYR A CE2   1 
ATOM   2484  C  CZ    . TYR A 1 1845 ? 205.822 251.782 264.956 1.00 55.41  ? 1845 TYR A CZ    1 
ATOM   2485  O  OH    . TYR A 1 1845 ? 207.044 252.394 264.822 1.00 59.00  ? 1845 TYR A OH    1 
ATOM   2486  N  N     . PHE A 1 1846 ? 200.297 247.627 267.509 1.00 59.72  ? 1846 PHE A N     1 
ATOM   2487  C  CA    . PHE A 1 1846 ? 199.083 246.869 267.777 1.00 63.67  ? 1846 PHE A CA    1 
ATOM   2488  C  C     . PHE A 1 1846 ? 197.991 247.815 268.256 1.00 69.99  ? 1846 PHE A C     1 
ATOM   2489  O  O     . PHE A 1 1846 ? 198.193 248.571 269.212 1.00 67.70  ? 1846 PHE A O     1 
ATOM   2490  C  CB    . PHE A 1 1846 ? 199.346 245.777 268.814 1.00 64.09  ? 1846 PHE A CB    1 
ATOM   2491  C  CG    . PHE A 1 1846 ? 198.224 244.793 268.953 1.00 65.07  ? 1846 PHE A CG    1 
ATOM   2492  C  CD1   . PHE A 1 1846 ? 197.492 244.720 270.122 1.00 64.31  ? 1846 PHE A CD1   1 
ATOM   2493  C  CD2   . PHE A 1 1846 ? 197.898 243.943 267.912 1.00 67.55  ? 1846 PHE A CD2   1 
ATOM   2494  C  CE1   . PHE A 1 1846 ? 196.460 243.819 270.251 1.00 67.00  ? 1846 PHE A CE1   1 
ATOM   2495  C  CE2   . PHE A 1 1846 ? 196.867 243.040 268.037 1.00 62.27  ? 1846 PHE A CE2   1 
ATOM   2496  C  CZ    . PHE A 1 1846 ? 196.148 242.978 269.206 1.00 67.69  ? 1846 PHE A CZ    1 
ATOM   2497  N  N     . ASP A 1 1847 ? 196.840 247.772 267.587 1.00 85.72  ? 1847 ASP A N     1 
ATOM   2498  C  CA    . ASP A 1 1847 ? 195.683 248.602 267.921 1.00 80.13  ? 1847 ASP A CA    1 
ATOM   2499  C  C     . ASP A 1 1847 ? 194.467 247.689 268.004 1.00 86.13  ? 1847 ASP A C     1 
ATOM   2500  O  O     . ASP A 1 1847 ? 193.704 247.560 267.037 1.00 85.20  ? 1847 ASP A O     1 
ATOM   2501  C  CB    . ASP A 1 1847 ? 195.482 249.711 266.887 1.00 81.03  ? 1847 ASP A CB    1 
ATOM   2502  C  CG    . ASP A 1 1847 ? 194.457 250.742 267.322 1.00 85.38  ? 1847 ASP A CG    1 
ATOM   2503  O  OD1   . ASP A 1 1847 ? 193.747 250.506 268.321 1.00 86.41  ? 1847 ASP A OD1   1 
ATOM   2504  O  OD2   . ASP A 1 1847 ? 194.363 251.796 266.660 1.00 85.15  ? 1847 ASP A OD2   1 
ATOM   2505  N  N     . PRO A 1 1848 ? 194.259 247.030 269.148 1.00 92.88  ? 1848 PRO A N     1 
ATOM   2506  C  CA    . PRO A 1 1848 ? 193.112 246.115 269.269 1.00 87.05  ? 1848 PRO A CA    1 
ATOM   2507  C  C     . PRO A 1 1848 ? 191.767 246.812 269.199 1.00 91.19  ? 1848 PRO A C     1 
ATOM   2508  O  O     . PRO A 1 1848 ? 190.754 246.146 268.953 1.00 87.33  ? 1848 PRO A O     1 
ATOM   2509  C  CB    . PRO A 1 1848 ? 193.331 245.461 270.639 1.00 86.92  ? 1848 PRO A CB    1 
ATOM   2510  C  CG    . PRO A 1 1848 ? 194.112 246.474 271.407 1.00 88.01  ? 1848 PRO A CG    1 
ATOM   2511  C  CD    . PRO A 1 1848 ? 195.004 247.159 270.411 1.00 88.49  ? 1848 PRO A CD    1 
ATOM   2512  N  N     . LYS A 1 1849 ? 191.725 248.129 269.416 1.00 94.78  ? 1849 LYS A N     1 
ATOM   2513  C  CA    . LYS A 1 1849 ? 190.455 248.847 269.433 1.00 91.30  ? 1849 LYS A CA    1 
ATOM   2514  C  C     . LYS A 1 1849 ? 189.759 248.791 268.079 1.00 91.74  ? 1849 LYS A C     1 
ATOM   2515  O  O     . LYS A 1 1849 ? 188.525 248.752 268.008 1.00 93.19  ? 1849 LYS A O     1 
ATOM   2516  C  CB    . LYS A 1 1849 ? 190.684 250.299 269.856 1.00 87.83  ? 1849 LYS A CB    1 
ATOM   2517  C  CG    . LYS A 1 1849 ? 191.785 250.475 270.888 1.00 89.53  ? 1849 LYS A CG    1 
ATOM   2518  C  CD    . LYS A 1 1849 ? 192.083 251.945 271.132 1.00 91.70  ? 1849 LYS A CD    1 
ATOM   2519  C  CE    . LYS A 1 1849 ? 193.297 252.121 272.032 1.00 92.04  ? 1849 LYS A CE    1 
ATOM   2520  N  NZ    . LYS A 1 1849 ? 193.106 251.479 273.362 1.00 90.69  ? 1849 LYS A NZ    1 
ATOM   2521  N  N     . GLN A 1 1850 ? 190.530 248.791 266.995 1.00 86.29  ? 1850 GLN A N     1 
ATOM   2522  C  CA    . GLN A 1 1850 ? 189.942 248.772 265.662 1.00 87.79  ? 1850 GLN A CA    1 
ATOM   2523  C  C     . GLN A 1 1850 ? 189.211 247.454 265.429 1.00 88.15  ? 1850 GLN A C     1 
ATOM   2524  O  O     . GLN A 1 1850 ? 189.677 246.389 265.842 1.00 85.60  ? 1850 GLN A O     1 
ATOM   2525  C  CB    . GLN A 1 1850 ? 191.027 248.989 264.608 1.00 85.81  ? 1850 GLN A CB    1 
ATOM   2526  C  CG    . GLN A 1 1850 ? 190.566 248.779 263.178 1.00 88.35  ? 1850 GLN A CG    1 
ATOM   2527  C  CD    . GLN A 1 1850 ? 191.325 249.647 262.197 1.00 86.75  ? 1850 GLN A CD    1 
ATOM   2528  O  OE1   . GLN A 1 1850 ? 192.165 250.456 262.589 1.00 83.45  ? 1850 GLN A OE1   1 
ATOM   2529  N  NE2   . GLN A 1 1850 ? 191.024 249.493 260.914 1.00 86.26  ? 1850 GLN A NE2   1 
ATOM   2530  N  N     . THR A 1 1851 ? 188.054 247.534 264.767 1.00 90.89  ? 1851 THR A N     1 
ATOM   2531  C  CA    . THR A 1 1851 ? 187.167 246.377 264.681 1.00 92.20  ? 1851 THR A CA    1 
ATOM   2532  C  C     . THR A 1 1851 ? 187.673 245.345 263.680 1.00 89.94  ? 1851 THR A C     1 
ATOM   2533  O  O     . THR A 1 1851 ? 187.495 244.138 263.883 1.00 89.11  ? 1851 THR A O     1 
ATOM   2534  C  CB    . THR A 1 1851 ? 185.755 246.828 264.310 1.00 92.39  ? 1851 THR A CB    1 
ATOM   2535  O  OG1   . THR A 1 1851 ? 185.758 247.377 262.986 1.00 91.01  ? 1851 THR A OG1   1 
ATOM   2536  C  CG2   . THR A 1 1851 ? 185.259 247.882 265.289 1.00 87.22  ? 1851 THR A CG2   1 
ATOM   2537  N  N     . ASP A 1 1852 ? 188.294 245.793 262.591 1.00 85.56  ? 1852 ASP A N     1 
ATOM   2538  C  CA    . ASP A 1 1852 ? 188.683 244.873 261.532 1.00 86.04  ? 1852 ASP A CA    1 
ATOM   2539  C  C     . ASP A 1 1852 ? 189.763 243.916 262.024 1.00 88.57  ? 1852 ASP A C     1 
ATOM   2540  O  O     . ASP A 1 1852 ? 190.699 244.305 262.726 1.00 92.36  ? 1852 ASP A O     1 
ATOM   2541  C  CB    . ASP A 1 1852 ? 189.174 245.645 260.307 1.00 87.31  ? 1852 ASP A CB    1 
ATOM   2542  C  CG    . ASP A 1 1852 ? 189.428 244.746 259.108 1.00 90.71  ? 1852 ASP A CG    1 
ATOM   2543  O  OD1   . ASP A 1 1852 ? 190.374 243.931 259.152 1.00 88.79  ? 1852 ASP A OD1   1 
ATOM   2544  O  OD2   . ASP A 1 1852 ? 188.675 244.853 258.118 1.00 91.45  ? 1852 ASP A OD2   1 
ATOM   2545  N  N     . VAL A 1 1853 ? 189.622 242.645 261.643 1.00 82.18  ? 1853 VAL A N     1 
ATOM   2546  C  CA    . VAL A 1 1853 ? 190.528 241.607 262.131 1.00 81.24  ? 1853 VAL A CA    1 
ATOM   2547  C  C     . VAL A 1 1853 ? 191.921 241.768 261.529 1.00 81.98  ? 1853 VAL A C     1 
ATOM   2548  O  O     . VAL A 1 1853 ? 192.934 241.589 262.213 1.00 81.46  ? 1853 VAL A O     1 
ATOM   2549  C  CB    . VAL A 1 1853 ? 189.938 240.209 261.871 1.00 81.87  ? 1853 VAL A CB    1 
ATOM   2550  C  CG1   . VAL A 1 1853 ? 189.808 239.926 260.392 1.00 79.73  ? 1853 VAL A CG1   1 
ATOM   2551  C  CG2   . VAL A 1 1853 ? 190.813 239.155 262.509 1.00 81.48  ? 1853 VAL A CG2   1 
ATOM   2552  N  N     . LEU A 1 1854 ? 191.998 242.108 260.241 1.00 84.73  ? 1854 LEU A N     1 
ATOM   2553  C  CA    . LEU A 1 1854 ? 193.307 242.265 259.615 1.00 85.93  ? 1854 LEU A CA    1 
ATOM   2554  C  C     . LEU A 1 1854 ? 194.028 243.511 260.112 1.00 83.58  ? 1854 LEU A C     1 
ATOM   2555  O  O     . LEU A 1 1854 ? 195.252 243.612 259.974 1.00 86.27  ? 1854 LEU A O     1 
ATOM   2556  C  CB    . LEU A 1 1854 ? 193.177 242.318 258.090 1.00 82.35  ? 1854 LEU A CB    1 
ATOM   2557  C  CG    . LEU A 1 1854 ? 193.092 241.030 257.261 1.00 82.79  ? 1854 LEU A CG    1 
ATOM   2558  C  CD1   . LEU A 1 1854 ? 194.370 240.220 257.393 1.00 80.46  ? 1854 LEU A CD1   1 
ATOM   2559  C  CD2   . LEU A 1 1854 ? 191.886 240.184 257.606 1.00 77.94  ? 1854 LEU A CD2   1 
ATOM   2560  N  N     . GLN A 1 1855 ? 193.297 244.463 260.695 1.00 72.22  ? 1855 GLN A N     1 
ATOM   2561  C  CA    . GLN A 1 1855 ? 193.852 245.796 260.895 1.00 71.05  ? 1855 GLN A CA    1 
ATOM   2562  C  C     . GLN A 1 1855 ? 194.204 246.113 262.343 1.00 73.78  ? 1855 GLN A C     1 
ATOM   2563  O  O     . GLN A 1 1855 ? 194.585 247.255 262.621 1.00 75.10  ? 1855 GLN A O     1 
ATOM   2564  C  CB    . GLN A 1 1855 ? 192.871 246.837 260.362 1.00 73.68  ? 1855 GLN A CB    1 
ATOM   2565  C  CG    . GLN A 1 1855 ? 192.405 246.560 258.943 1.00 77.11  ? 1855 GLN A CG    1 
ATOM   2566  C  CD    . GLN A 1 1855 ? 192.205 247.825 258.135 1.00 80.70  ? 1855 GLN A CD    1 
ATOM   2567  O  OE1   . GLN A 1 1855 ? 191.100 248.364 258.073 1.00 77.92  ? 1855 GLN A OE1   1 
ATOM   2568  N  NE2   . GLN A 1 1855 ? 193.274 248.307 257.513 1.00 77.30  ? 1855 GLN A NE2   1 
ATOM   2569  N  N     . GLN A 1 1856 ? 194.089 245.161 263.271 1.00 74.39  ? 1856 GLN A N     1 
ATOM   2570  C  CA    . GLN A 1 1856 ? 194.535 245.430 264.636 1.00 76.28  ? 1856 GLN A CA    1 
ATOM   2571  C  C     . GLN A 1 1856 ? 196.045 245.632 264.691 1.00 71.39  ? 1856 GLN A C     1 
ATOM   2572  O  O     . GLN A 1 1856 ? 196.537 246.543 265.365 1.00 67.20  ? 1856 GLN A O     1 
ATOM   2573  C  CB    . GLN A 1 1856 ? 194.114 244.307 265.587 1.00 77.94  ? 1856 GLN A CB    1 
ATOM   2574  C  CG    . GLN A 1 1856 ? 192.640 244.304 265.964 1.00 76.73  ? 1856 GLN A CG    1 
ATOM   2575  C  CD    . GLN A 1 1856 ? 191.847 243.253 265.224 1.00 78.13  ? 1856 GLN A CD    1 
ATOM   2576  O  OE1   . GLN A 1 1856 ? 192.395 242.247 264.783 1.00 79.15  ? 1856 GLN A OE1   1 
ATOM   2577  N  NE2   . GLN A 1 1856 ? 190.547 243.482 265.081 1.00 73.26  ? 1856 GLN A NE2   1 
ATOM   2578  N  N     . LEU A 1 1857 ? 196.797 244.792 263.986 1.00 57.78  ? 1857 LEU A N     1 
ATOM   2579  C  CA    . LEU A 1 1857 ? 198.252 244.826 264.010 1.00 56.68  ? 1857 LEU A CA    1 
ATOM   2580  C  C     . LEU A 1 1857 ? 198.776 245.320 262.670 1.00 57.82  ? 1857 LEU A C     1 
ATOM   2581  O  O     . LEU A 1 1857 ? 198.337 244.852 261.615 1.00 50.97  ? 1857 LEU A O     1 
ATOM   2582  C  CB    . LEU A 1 1857 ? 198.826 243.443 264.327 1.00 50.19  ? 1857 LEU A CB    1 
ATOM   2583  C  CG    . LEU A 1 1857 ? 200.329 243.250 264.123 1.00 46.44  ? 1857 LEU A CG    1 
ATOM   2584  C  CD1   . LEU A 1 1857 ? 201.122 244.173 265.029 1.00 48.97  ? 1857 LEU A CD1   1 
ATOM   2585  C  CD2   . LEU A 1 1857 ? 200.708 241.805 264.375 1.00 51.41  ? 1857 LEU A CD2   1 
ATOM   2586  N  N     . SER A 1 1858 ? 199.713 246.265 262.716 1.00 49.52  ? 1858 SER A N     1 
ATOM   2587  C  CA    . SER A 1 1858 ? 200.326 246.830 261.521 1.00 42.17  ? 1858 SER A CA    1 
ATOM   2588  C  C     . SER A 1 1858 ? 201.831 246.638 261.607 1.00 50.75  ? 1858 SER A C     1 
ATOM   2589  O  O     . SER A 1 1858 ? 202.442 246.960 262.630 1.00 55.65  ? 1858 SER A O     1 
ATOM   2590  C  CB    . SER A 1 1858 ? 199.981 248.312 261.370 1.00 48.35  ? 1858 SER A CB    1 
ATOM   2591  O  OG    . SER A 1 1858 ? 200.551 248.849 260.190 1.00 50.15  ? 1858 SER A OG    1 
ATOM   2592  N  N     . ILE A 1 1859 ? 202.421 246.116 260.540 1.00 47.85  ? 1859 ILE A N     1 
ATOM   2593  C  CA    . ILE A 1 1859 ? 203.859 245.893 260.466 1.00 37.39  ? 1859 ILE A CA    1 
ATOM   2594  C  C     . ILE A 1 1859 ? 204.466 246.926 259.530 1.00 43.86  ? 1859 ILE A C     1 
ATOM   2595  O  O     . ILE A 1 1859 ? 204.019 247.081 258.388 1.00 50.51  ? 1859 ILE A O     1 
ATOM   2596  C  CB    . ILE A 1 1859 ? 204.165 244.466 259.989 1.00 43.33  ? 1859 ILE A CB    1 
ATOM   2597  C  CG1   . ILE A 1 1859 ? 203.520 243.448 260.931 1.00 35.32  ? 1859 ILE A CG1   1 
ATOM   2598  C  CG2   . ILE A 1 1859 ? 205.664 244.260 259.843 1.00 43.33  ? 1859 ILE A CG2   1 
ATOM   2599  C  CD1   . ILE A 1 1859 ? 203.662 242.022 260.479 1.00 47.07  ? 1859 ILE A CD1   1 
ATOM   2600  N  N     . GLN A 1 1860 ? 205.484 247.636 260.009 1.00 42.19  ? 1860 GLN A N     1 
ATOM   2601  C  CA    . GLN A 1 1860 ? 206.087 248.727 259.257 1.00 45.34  ? 1860 GLN A CA    1 
ATOM   2602  C  C     . GLN A 1 1860 ? 207.599 248.572 259.225 1.00 45.24  ? 1860 GLN A C     1 
ATOM   2603  O  O     . GLN A 1 1860 ? 208.223 248.308 260.256 1.00 47.07  ? 1860 GLN A O     1 
ATOM   2604  C  CB    . GLN A 1 1860 ? 205.701 250.083 259.856 1.00 43.04  ? 1860 GLN A CB    1 
ATOM   2605  C  CG    . GLN A 1 1860 ? 204.202 250.276 259.997 1.00 44.86  ? 1860 GLN A CG    1 
ATOM   2606  C  CD    . GLN A 1 1860 ? 203.833 251.649 260.508 1.00 53.96  ? 1860 GLN A CD    1 
ATOM   2607  O  OE1   . GLN A 1 1860 ? 204.697 252.493 260.735 1.00 58.38  ? 1860 GLN A OE1   1 
ATOM   2608  N  NE2   . GLN A 1 1860 ? 202.540 251.880 260.691 1.00 54.68  ? 1860 GLN A NE2   1 
ATOM   2609  N  N     . MET A 1 1861 ? 208.175 248.729 258.036 1.00 40.92  ? 1861 MET A N     1 
ATOM   2610  C  CA    . MET A 1 1861 ? 209.619 248.734 257.835 1.00 32.93  ? 1861 MET A CA    1 
ATOM   2611  C  C     . MET A 1 1861 ? 209.947 249.850 256.858 1.00 43.35  ? 1861 MET A C     1 
ATOM   2612  O  O     . MET A 1 1861 ? 209.516 249.806 255.701 1.00 51.48  ? 1861 MET A O     1 
ATOM   2613  C  CB    . MET A 1 1861 ? 210.111 247.387 257.301 1.00 37.29  ? 1861 MET A CB    1 
ATOM   2614  C  CG    . MET A 1 1861 ? 211.622 247.250 257.244 1.00 36.96  ? 1861 MET A CG    1 
ATOM   2615  S  SD    . MET A 1 1861 ? 212.146 245.558 256.928 1.00 50.34  ? 1861 MET A SD    1 
ATOM   2616  C  CE    . MET A 1 1861 ? 213.468 245.380 258.117 1.00 41.21  ? 1861 MET A CE    1 
ATOM   2617  N  N     . ALA A 1 1862 ? 210.706 250.844 257.321 1.00 41.64  ? 1862 ALA A N     1 
ATOM   2618  C  CA    . ALA A 1 1862 ? 211.007 252.059 256.556 1.00 43.38  ? 1862 ALA A CA    1 
ATOM   2619  C  C     . ALA A 1 1862 ? 209.678 252.712 256.197 1.00 44.98  ? 1862 ALA A C     1 
ATOM   2620  O  O     . ALA A 1 1862 ? 208.928 253.082 257.117 1.00 42.70  ? 1862 ALA A O     1 
ATOM   2621  C  CB    . ALA A 1 1862 ? 211.925 251.714 255.382 1.00 42.27  ? 1862 ALA A CB    1 
ATOM   2622  N  N     . ASN A 1 1863 ? 209.341 252.881 254.922 1.00 43.13  ? 1863 ASN A N     1 
ATOM   2623  C  CA    . ASN A 1 1863 ? 208.067 253.462 254.527 1.00 44.22  ? 1863 ASN A CA    1 
ATOM   2624  C  C     . ASN A 1 1863 ? 207.036 252.418 254.124 1.00 49.59  ? 1863 ASN A C     1 
ATOM   2625  O  O     . ASN A 1 1863 ? 205.955 252.785 253.655 1.00 55.69  ? 1863 ASN A O     1 
ATOM   2626  C  CB    . ASN A 1 1863 ? 208.271 254.452 253.377 1.00 44.65  ? 1863 ASN A CB    1 
ATOM   2627  C  CG    . ASN A 1 1863 ? 208.555 253.763 252.061 1.00 51.19  ? 1863 ASN A CG    1 
ATOM   2628  O  OD1   . ASN A 1 1863 ? 209.589 253.119 251.894 1.00 51.23  ? 1863 ASN A OD1   1 
ATOM   2629  N  ND2   . ASN A 1 1863 ? 207.633 253.893 251.116 1.00 49.88  ? 1863 ASN A ND2   1 
ATOM   2630  N  N     . ALA A 1 1864 ? 207.338 251.134 254.295 1.00 41.12  ? 1864 ALA A N     1 
ATOM   2631  C  CA    . ALA A 1 1864 ? 206.430 250.067 253.902 1.00 39.58  ? 1864 ALA A CA    1 
ATOM   2632  C  C     . ALA A 1 1864 ? 205.567 249.663 255.088 1.00 44.23  ? 1864 ALA A C     1 
ATOM   2633  O  O     . ALA A 1 1864 ? 206.086 249.375 256.169 1.00 46.09  ? 1864 ALA A O     1 
ATOM   2634  C  CB    . ALA A 1 1864 ? 207.209 248.861 253.380 1.00 43.65  ? 1864 ALA A CB    1 
ATOM   2635  N  N     . LYS A 1 1865 ? 204.254 249.638 254.881 1.00 51.35  ? 1865 LYS A N     1 
ATOM   2636  C  CA    . LYS A 1 1865 ? 203.296 249.280 255.916 1.00 45.46  ? 1865 LYS A CA    1 
ATOM   2637  C  C     . LYS A 1 1865 ? 202.528 248.041 255.486 1.00 51.34  ? 1865 LYS A C     1 
ATOM   2638  O  O     . LYS A 1 1865 ? 201.996 247.991 254.373 1.00 55.65  ? 1865 LYS A O     1 
ATOM   2639  C  CB    . LYS A 1 1865 ? 202.327 250.431 256.194 1.00 42.39  ? 1865 LYS A CB    1 
ATOM   2640  C  CG    . LYS A 1 1865 ? 202.978 251.666 256.790 1.00 49.15  ? 1865 LYS A CG    1 
ATOM   2641  C  CD    . LYS A 1 1865 ? 201.979 252.805 256.917 1.00 52.93  ? 1865 LYS A CD    1 
ATOM   2642  C  CE    . LYS A 1 1865 ? 202.653 254.087 257.376 1.00 53.96  ? 1865 LYS A CE    1 
ATOM   2643  N  NZ    . LYS A 1 1865 ? 203.888 254.381 256.595 1.00 54.47  ? 1865 LYS A NZ    1 
ATOM   2644  N  N     . PHE A 1 1866 ? 202.468 247.047 256.368 1.00 45.27  ? 1866 PHE A N     1 
ATOM   2645  C  CA    . PHE A 1 1866 ? 201.740 245.816 256.113 1.00 43.00  ? 1866 PHE A CA    1 
ATOM   2646  C  C     . PHE A 1 1866 ? 200.838 245.499 257.294 1.00 49.41  ? 1866 PHE A C     1 
ATOM   2647  O  O     . PHE A 1 1866 ? 201.151 245.825 258.441 1.00 56.52  ? 1866 PHE A O     1 
ATOM   2648  C  CB    . PHE A 1 1866 ? 202.683 244.631 255.865 1.00 42.99  ? 1866 PHE A CB    1 
ATOM   2649  C  CG    . PHE A 1 1866 ? 203.716 244.888 254.811 1.00 46.90  ? 1866 PHE A CG    1 
ATOM   2650  C  CD1   . PHE A 1 1866 ? 203.437 244.651 253.478 1.00 43.45  ? 1866 PHE A CD1   1 
ATOM   2651  C  CD2   . PHE A 1 1866 ? 204.969 245.355 255.154 1.00 43.30  ? 1866 PHE A CD2   1 
ATOM   2652  C  CE1   . PHE A 1 1866 ? 204.384 244.886 252.507 1.00 40.87  ? 1866 PHE A CE1   1 
ATOM   2653  C  CE2   . PHE A 1 1866 ? 205.919 245.591 254.187 1.00 49.71  ? 1866 PHE A CE2   1 
ATOM   2654  C  CZ    . PHE A 1 1866 ? 205.626 245.355 252.862 1.00 50.91  ? 1866 PHE A CZ    1 
ATOM   2655  N  N     . ASN A 1 1867 ? 199.713 244.858 257.000 1.00 51.59  ? 1867 ASN A N     1 
ATOM   2656  C  CA    . ASN A 1 1867 ? 198.802 244.353 258.014 1.00 45.56  ? 1867 ASN A CA    1 
ATOM   2657  C  C     . ASN A 1 1867 ? 199.000 242.851 258.152 1.00 49.63  ? 1867 ASN A C     1 
ATOM   2658  O  O     . ASN A 1 1867 ? 199.108 242.138 257.150 1.00 52.03  ? 1867 ASN A O     1 
ATOM   2659  C  CB    . ASN A 1 1867 ? 197.346 244.659 257.653 1.00 47.92  ? 1867 ASN A CB    1 
ATOM   2660  C  CG    . ASN A 1 1867 ? 196.951 246.088 257.975 1.00 54.24  ? 1867 ASN A CG    1 
ATOM   2661  O  OD1   . ASN A 1 1867 ? 196.812 246.459 259.140 1.00 57.61  ? 1867 ASN A OD1   1 
ATOM   2662  N  ND2   . ASN A 1 1867 ? 196.764 246.896 256.940 1.00 53.18  ? 1867 ASN A ND2   1 
ATOM   2663  N  N     . TYR A 1 1868 ? 199.061 242.377 259.395 1.00 47.33  ? 1868 TYR A N     1 
ATOM   2664  C  CA    . TYR A 1 1868 ? 199.260 240.956 259.641 1.00 39.75  ? 1868 TYR A CA    1 
ATOM   2665  C  C     . TYR A 1 1868 ? 198.122 240.151 259.029 1.00 41.73  ? 1868 TYR A C     1 
ATOM   2666  O  O     . TYR A 1 1868 ? 196.946 240.455 259.241 1.00 51.87  ? 1868 TYR A O     1 
ATOM   2667  C  CB    . TYR A 1 1868 ? 199.346 240.689 261.142 1.00 40.66  ? 1868 TYR A CB    1 
ATOM   2668  C  CG    . TYR A 1 1868 ? 200.076 239.416 261.503 1.00 40.60  ? 1868 TYR A CG    1 
ATOM   2669  C  CD1   . TYR A 1 1868 ? 201.459 239.376 261.548 1.00 44.45  ? 1868 TYR A CD1   1 
ATOM   2670  C  CD2   . TYR A 1 1868 ? 199.380 238.255 261.798 1.00 41.20  ? 1868 TYR A CD2   1 
ATOM   2671  C  CE1   . TYR A 1 1868 ? 202.127 238.218 261.877 1.00 44.26  ? 1868 TYR A CE1   1 
ATOM   2672  C  CE2   . TYR A 1 1868 ? 200.041 237.091 262.128 1.00 39.27  ? 1868 TYR A CE2   1 
ATOM   2673  C  CZ    . TYR A 1 1868 ? 201.414 237.079 262.166 1.00 43.34  ? 1868 TYR A CZ    1 
ATOM   2674  O  OH    . TYR A 1 1868 ? 202.081 235.923 262.495 1.00 46.60  ? 1868 TYR A OH    1 
ATOM   2675  N  N     . GLY A 1 1869 ? 198.478 239.116 258.265 1.00 44.90  ? 1869 GLY A N     1 
ATOM   2676  C  CA    . GLY A 1 1869 ? 197.474 238.305 257.602 1.00 44.41  ? 1869 GLY A CA    1 
ATOM   2677  C  C     . GLY A 1 1869 ? 196.723 237.364 258.514 1.00 49.28  ? 1869 GLY A C     1 
ATOM   2678  O  O     . GLY A 1 1869 ? 195.640 236.899 258.146 1.00 53.99  ? 1869 GLY A O     1 
ATOM   2679  N  N     . PHE A 1 1870 ? 197.275 237.076 259.693 1.00 56.57  ? 1870 PHE A N     1 
ATOM   2680  C  CA    . PHE A 1 1870 ? 196.654 236.192 260.679 1.00 53.74  ? 1870 PHE A CA    1 
ATOM   2681  C  C     . PHE A 1 1870 ? 196.330 234.823 260.092 1.00 56.48  ? 1870 PHE A C     1 
ATOM   2682  O  O     . PHE A 1 1870 ? 195.292 234.233 260.395 1.00 60.52  ? 1870 PHE A O     1 
ATOM   2683  C  CB    . PHE A 1 1870 ? 195.403 236.829 261.288 1.00 44.10  ? 1870 PHE A CB    1 
ATOM   2684  C  CG    . PHE A 1 1870 ? 195.707 237.892 262.300 1.00 50.67  ? 1870 PHE A CG    1 
ATOM   2685  C  CD1   . PHE A 1 1870 ? 196.419 237.585 263.446 1.00 55.27  ? 1870 PHE A CD1   1 
ATOM   2686  C  CD2   . PHE A 1 1870 ? 195.299 239.196 262.101 1.00 54.56  ? 1870 PHE A CD2   1 
ATOM   2687  C  CE1   . PHE A 1 1870 ? 196.709 238.557 264.376 1.00 49.40  ? 1870 PHE A CE1   1 
ATOM   2688  C  CE2   . PHE A 1 1870 ? 195.588 240.173 263.030 1.00 56.18  ? 1870 PHE A CE2   1 
ATOM   2689  C  CZ    . PHE A 1 1870 ? 196.292 239.852 264.169 1.00 51.05  ? 1870 PHE A CZ    1 
ATOM   2690  N  N     . GLU A 1 1871 ? 197.217 234.318 259.243 1.00 56.99  ? 1871 GLU A N     1 
ATOM   2691  C  CA    . GLU A 1 1871 ? 197.109 232.956 258.746 1.00 51.01  ? 1871 GLU A CA    1 
ATOM   2692  C  C     . GLU A 1 1871 ? 197.781 232.014 259.733 1.00 56.68  ? 1871 GLU A C     1 
ATOM   2693  O  O     . GLU A 1 1871 ? 198.922 232.248 260.144 1.00 58.22  ? 1871 GLU A O     1 
ATOM   2694  C  CB    . GLU A 1 1871 ? 197.756 232.840 257.366 1.00 47.95  ? 1871 GLU A CB    1 
ATOM   2695  C  CG    . GLU A 1 1871 ? 197.947 231.416 256.879 1.00 56.53  ? 1871 GLU A CG    1 
ATOM   2696  C  CD    . GLU A 1 1871 ? 196.818 230.949 255.983 1.00 61.73  ? 1871 GLU A CD    1 
ATOM   2697  O  OE1   . GLU A 1 1871 ? 195.984 231.789 255.587 1.00 60.11  ? 1871 GLU A OE1   1 
ATOM   2698  O  OE2   . GLU A 1 1871 ? 196.764 229.740 255.677 1.00 59.14  ? 1871 GLU A OE2   1 
ATOM   2699  N  N     . TYR A 1 1872 ? 197.072 230.960 260.130 1.00 60.57  ? 1872 TYR A N     1 
ATOM   2700  C  CA    . TYR A 1 1872 ? 197.630 229.998 261.074 1.00 58.96  ? 1872 TYR A CA    1 
ATOM   2701  C  C     . TYR A 1 1872 ? 198.787 229.265 260.410 1.00 59.67  ? 1872 TYR A C     1 
ATOM   2702  O  O     . TYR A 1 1872 ? 198.582 228.449 259.506 1.00 63.61  ? 1872 TYR A O     1 
ATOM   2703  C  CB    . TYR A 1 1872 ? 196.563 229.019 261.548 1.00 60.22  ? 1872 TYR A CB    1 
ATOM   2704  C  CG    . TYR A 1 1872 ? 197.082 228.046 262.580 1.00 59.11  ? 1872 TYR A CG    1 
ATOM   2705  C  CD1   . TYR A 1 1872 ? 197.768 228.497 263.697 1.00 59.16  ? 1872 TYR A CD1   1 
ATOM   2706  C  CD2   . TYR A 1 1872 ? 196.905 226.680 262.429 1.00 58.02  ? 1872 TYR A CD2   1 
ATOM   2707  C  CE1   . TYR A 1 1872 ? 198.252 227.618 264.639 1.00 57.99  ? 1872 TYR A CE1   1 
ATOM   2708  C  CE2   . TYR A 1 1872 ? 197.387 225.792 263.367 1.00 58.68  ? 1872 TYR A CE2   1 
ATOM   2709  C  CZ    . TYR A 1 1872 ? 198.060 226.268 264.469 1.00 60.31  ? 1872 TYR A CZ    1 
ATOM   2710  O  OH    . TYR A 1 1872 ? 198.545 225.391 265.409 1.00 67.77  ? 1872 TYR A OH    1 
ATOM   2711  N  N     . LEU A 1 1873 ? 200.003 229.558 260.857 1.00 45.51  ? 1873 LEU A N     1 
ATOM   2712  C  CA    . LEU A 1 1873 ? 201.214 229.034 260.246 1.00 49.91  ? 1873 LEU A CA    1 
ATOM   2713  C  C     . LEU A 1 1873 ? 201.723 227.770 260.922 1.00 56.67  ? 1873 LEU A C     1 
ATOM   2714  O  O     . LEU A 1 1873 ? 202.739 227.221 260.486 1.00 65.35  ? 1873 LEU A O     1 
ATOM   2715  C  CB    . LEU A 1 1873 ? 202.307 230.104 260.274 1.00 54.76  ? 1873 LEU A CB    1 
ATOM   2716  C  CG    . LEU A 1 1873 ? 202.008 231.362 259.459 1.00 56.63  ? 1873 LEU A CG    1 
ATOM   2717  C  CD1   . LEU A 1 1873 ? 203.067 232.407 259.713 1.00 52.31  ? 1873 LEU A CD1   1 
ATOM   2718  C  CD2   . LEU A 1 1873 ? 201.914 231.040 257.980 1.00 54.63  ? 1873 LEU A CD2   1 
ATOM   2719  N  N     . GLY A 1 1874 ? 201.048 227.294 261.964 1.00 56.78  ? 1874 GLY A N     1 
ATOM   2720  C  CA    . GLY A 1 1874 ? 201.551 226.137 262.683 1.00 56.01  ? 1874 GLY A CA    1 
ATOM   2721  C  C     . GLY A 1 1874 ? 202.796 226.489 263.473 1.00 59.96  ? 1874 GLY A C     1 
ATOM   2722  O  O     . GLY A 1 1874 ? 202.919 227.585 264.031 1.00 59.71  ? 1874 GLY A O     1 
ATOM   2723  N  N     . VAL A 1 1875 ? 203.733 225.549 263.525 1.00 61.54  ? 1875 VAL A N     1 
ATOM   2724  C  CA    . VAL A 1 1875 ? 205.006 225.732 264.214 1.00 63.85  ? 1875 VAL A CA    1 
ATOM   2725  C  C     . VAL A 1 1875 ? 206.101 225.636 263.160 1.00 61.83  ? 1875 VAL A C     1 
ATOM   2726  O  O     . VAL A 1 1875 ? 206.444 224.542 262.699 1.00 63.84  ? 1875 VAL A O     1 
ATOM   2727  C  CB    . VAL A 1 1875 ? 205.208 224.704 265.331 1.00 61.61  ? 1875 VAL A CB    1 
ATOM   2728  C  CG1   . VAL A 1 1875 ? 206.408 225.082 266.186 1.00 59.41  ? 1875 VAL A CG1   1 
ATOM   2729  C  CG2   . VAL A 1 1875 ? 203.957 224.594 266.181 1.00 63.29  ? 1875 VAL A CG2   1 
ATOM   2730  N  N     . GLN A 1 1876 ? 206.657 226.780 262.776 1.00 58.47  ? 1876 GLN A N     1 
ATOM   2731  C  CA    . GLN A 1 1876 ? 207.715 226.828 261.780 1.00 58.92  ? 1876 GLN A CA    1 
ATOM   2732  C  C     . GLN A 1 1876 ? 209.075 227.000 262.450 1.00 60.18  ? 1876 GLN A C     1 
ATOM   2733  O  O     . GLN A 1 1876 ? 209.181 227.363 263.623 1.00 66.48  ? 1876 GLN A O     1 
ATOM   2734  C  CB    . GLN A 1 1876 ? 207.461 227.962 260.787 1.00 58.88  ? 1876 GLN A CB    1 
ATOM   2735  C  CG    . GLN A 1 1876 ? 206.016 228.081 260.340 1.00 57.78  ? 1876 GLN A CG    1 
ATOM   2736  C  CD    . GLN A 1 1876 ? 205.747 227.338 259.050 1.00 59.58  ? 1876 GLN A CD    1 
ATOM   2737  O  OE1   . GLN A 1 1876 ? 206.647 226.731 258.471 1.00 60.67  ? 1876 GLN A OE1   1 
ATOM   2738  N  NE2   . GLN A 1 1876 ? 204.502 227.381 258.591 1.00 59.92  ? 1876 GLN A NE2   1 
ATOM   2739  N  N     . ASP A 1 1877 ? 210.128 226.736 261.683 1.00 62.16  ? 1877 ASP A N     1 
ATOM   2740  C  CA    . ASP A 1 1877 ? 211.496 226.885 262.163 1.00 61.93  ? 1877 ASP A CA    1 
ATOM   2741  C  C     . ASP A 1 1877 ? 211.977 228.297 261.854 1.00 62.65  ? 1877 ASP A C     1 
ATOM   2742  O  O     . ASP A 1 1877 ? 212.162 228.653 260.685 1.00 61.61  ? 1877 ASP A O     1 
ATOM   2743  C  CB    . ASP A 1 1877 ? 212.410 225.846 261.515 1.00 65.22  ? 1877 ASP A CB    1 
ATOM   2744  C  CG    . ASP A 1 1877 ? 213.709 225.658 262.274 1.00 70.56  ? 1877 ASP A CG    1 
ATOM   2745  O  OD1   . ASP A 1 1877 ? 213.659 225.488 263.510 1.00 72.06  ? 1877 ASP A OD1   1 
ATOM   2746  O  OD2   . ASP A 1 1877 ? 214.781 225.679 261.633 1.00 69.43  ? 1877 ASP A OD2   1 
ATOM   2747  N  N     . LYS A 1 1878 ? 212.386 229.018 262.895 1.00 55.65  ? 1878 LYS A N     1 
ATOM   2748  C  CA    . LYS A 1 1878 ? 212.753 230.445 262.763 1.00 58.21  ? 1878 LYS A CA    1 
ATOM   2749  C  C     . LYS A 1 1878 ? 214.198 230.660 262.361 1.00 56.22  ? 1878 LYS A C     1 
ATOM   2750  O  O     . LYS A 1 1878 ? 215.061 229.903 262.802 1.00 53.44  ? 1878 LYS A O     1 
ATOM   2751  C  CB    . LYS A 1 1878 ? 212.535 231.171 264.087 1.00 52.09  ? 1878 LYS A CB    1 
ATOM   2752  C  CG    . LYS A 1 1878 ? 211.064 231.433 264.361 1.00 51.22  ? 1878 LYS A CG    1 
ATOM   2753  C  CD    . LYS A 1 1878 ? 210.776 232.861 264.796 1.00 57.05  ? 1878 LYS A CD    1 
ATOM   2754  C  CE    . LYS A 1 1878 ? 212.021 233.578 265.195 1.00 54.73  ? 1878 LYS A CE    1 
ATOM   2755  N  NZ    . LYS A 1 1878 ? 211.853 235.025 265.057 1.00 60.21  ? 1878 LYS A NZ    1 
ATOM   2756  N  N     . LEU A 1 1879 ? 214.427 231.709 261.582 1.00 43.42  ? 1879 LEU A N     1 
ATOM   2757  C  CA    . LEU A 1 1879 ? 215.760 232.003 261.049 1.00 41.51  ? 1879 LEU A CA    1 
ATOM   2758  C  C     . LEU A 1 1879 ? 216.433 233.080 261.889 1.00 43.78  ? 1879 LEU A C     1 
ATOM   2759  O  O     . LEU A 1 1879 ? 215.807 234.087 262.136 1.00 48.86  ? 1879 LEU A O     1 
ATOM   2760  C  CB    . LEU A 1 1879 ? 215.383 232.538 259.669 1.00 43.60  ? 1879 LEU A CB    1 
ATOM   2761  C  CG    . LEU A 1 1879 ? 215.064 231.544 258.555 1.00 40.33  ? 1879 LEU A CG    1 
ATOM   2762  C  CD1   . LEU A 1 1879 ? 215.709 232.093 257.309 1.00 42.17  ? 1879 LEU A CD1   1 
ATOM   2763  C  CD2   . LEU A 1 1879 ? 215.500 230.126 258.828 1.00 44.02  ? 1879 LEU A CD2   1 
ATOM   2764  N  N     . VAL A 1 1880 ? 217.657 232.877 262.336 1.00 40.37  ? 1880 VAL A N     1 
ATOM   2765  C  CA    . VAL A 1 1880 ? 218.387 233.971 263.013 1.00 38.42  ? 1880 VAL A CA    1 
ATOM   2766  C  C     . VAL A 1 1880 ? 218.302 235.182 262.082 1.00 41.87  ? 1880 VAL A C     1 
ATOM   2767  O  O     . VAL A 1 1880 ? 218.742 235.046 260.954 1.00 40.15  ? 1880 VAL A O     1 
ATOM   2768  C  CB    . VAL A 1 1880 ? 219.836 233.525 263.282 1.00 37.13  ? 1880 VAL A CB    1 
ATOM   2769  C  CG1   . VAL A 1 1880 ? 220.649 234.576 264.014 1.00 33.32  ? 1880 VAL A CG1   1 
ATOM   2770  C  CG2   . VAL A 1 1880 ? 219.901 232.177 263.977 1.00 38.65  ? 1880 VAL A CG2   1 
ATOM   2771  N  N     . GLN A 1 1881 ? 217.744 236.306 262.527 1.00 43.00  ? 1881 GLN A N     1 
ATOM   2772  C  CA    . GLN A 1 1881 ? 217.705 237.525 261.692 1.00 39.33  ? 1881 GLN A CA    1 
ATOM   2773  C  C     . GLN A 1 1881 ? 219.086 238.128 261.782 1.00 45.18  ? 1881 GLN A C     1 
ATOM   2774  O  O     . GLN A 1 1881 ? 219.439 238.553 262.878 1.00 45.05  ? 1881 GLN A O     1 
ATOM   2775  C  CB    . GLN A 1 1881 ? 216.624 238.489 262.149 1.00 42.08  ? 1881 GLN A CB    1 
ATOM   2776  C  CG    . GLN A 1 1881 ? 216.557 239.776 261.343 1.00 38.29  ? 1881 GLN A CG    1 
ATOM   2777  C  CD    . GLN A 1 1881 ? 215.260 239.898 260.583 1.00 45.20  ? 1881 GLN A CD    1 
ATOM   2778  O  OE1   . GLN A 1 1881 ? 214.600 238.899 260.294 1.00 49.18  ? 1881 GLN A OE1   1 
ATOM   2779  N  NE2   . GLN A 1 1881 ? 214.877 241.124 260.263 1.00 40.61  ? 1881 GLN A NE2   1 
ATOM   2780  N  N     . THR A 1 1882 ? 219.840 238.109 260.688 1.00 40.87  ? 1882 THR A N     1 
ATOM   2781  C  CA    . THR A 1 1882 ? 221.237 238.533 260.703 1.00 40.00  ? 1882 THR A CA    1 
ATOM   2782  C  C     . THR A 1 1882 ? 221.328 239.779 259.882 1.00 42.45  ? 1882 THR A C     1 
ATOM   2783  O  O     . THR A 1 1882 ? 220.312 240.163 259.315 1.00 44.97  ? 1882 THR A O     1 
ATOM   2784  C  CB    . THR A 1 1882 ? 222.067 237.381 260.139 1.00 38.60  ? 1882 THR A CB    1 
ATOM   2785  O  OG1   . THR A 1 1882 ? 221.523 237.136 258.851 1.00 37.03  ? 1882 THR A OG1   1 
ATOM   2786  C  CG2   . THR A 1 1882 ? 221.976 236.103 260.947 1.00 34.54  ? 1882 THR A CG2   1 
ATOM   2787  N  N     . PRO A 1 1883 ? 222.471 240.478 259.795 1.00 42.64  ? 1883 PRO A N     1 
ATOM   2788  C  CA    . PRO A 1 1883 ? 222.561 241.616 258.906 1.00 39.96  ? 1883 PRO A CA    1 
ATOM   2789  C  C     . PRO A 1 1883 ? 222.174 241.404 257.442 1.00 41.00  ? 1883 PRO A C     1 
ATOM   2790  O  O     . PRO A 1 1883 ? 222.118 242.391 256.734 1.00 46.11  ? 1883 PRO A O     1 
ATOM   2791  C  CB    . PRO A 1 1883 ? 224.033 241.856 259.107 1.00 31.81  ? 1883 PRO A CB    1 
ATOM   2792  C  CG    . PRO A 1 1883 ? 224.237 241.634 260.564 1.00 33.48  ? 1883 PRO A CG    1 
ATOM   2793  C  CD    . PRO A 1 1883 ? 223.638 240.262 260.619 1.00 36.19  ? 1883 PRO A CD    1 
ATOM   2794  N  N     . LEU A 1 1884 ? 221.859 240.186 257.018 1.00 32.45  ? 1884 LEU A N     1 
ATOM   2795  C  CA    . LEU A 1 1884 ? 221.458 239.873 255.623 1.00 26.22  ? 1884 LEU A CA    1 
ATOM   2796  C  C     . LEU A 1 1884 ? 219.979 239.523 255.541 1.00 31.59  ? 1884 LEU A C     1 
ATOM   2797  O  O     . LEU A 1 1884 ? 219.449 239.638 254.449 1.00 45.23  ? 1884 LEU A O     1 
ATOM   2798  C  CB    . LEU A 1 1884 ? 222.303 238.730 255.073 1.00 36.44  ? 1884 LEU A CB    1 
ATOM   2799  C  CG    . LEU A 1 1884 ? 222.064 238.302 253.623 1.00 36.21  ? 1884 LEU A CG    1 
ATOM   2800  C  CD1   . LEU A 1 1884 ? 222.311 239.430 252.648 1.00 38.35  ? 1884 LEU A CD1   1 
ATOM   2801  C  CD2   . LEU A 1 1884 ? 222.948 237.124 253.299 1.00 28.10  ? 1884 LEU A CD2   1 
ATOM   2802  N  N     . THR A 1 1885 ? 219.360 239.045 256.609 1.00 32.05  ? 1885 THR A N     1 
ATOM   2803  C  CA    . THR A 1 1885 ? 217.930 238.752 256.628 1.00 27.25  ? 1885 THR A CA    1 
ATOM   2804  C  C     . THR A 1 1885 ? 217.275 240.039 256.943 1.00 35.26  ? 1885 THR A C     1 
ATOM   2805  O  O     . THR A 1 1885 ? 216.080 240.094 256.842 1.00 44.43  ? 1885 THR A O     1 
ATOM   2806  C  CB    . THR A 1 1885 ? 217.665 237.691 257.677 1.00 39.36  ? 1885 THR A CB    1 
ATOM   2807  O  OG1   . THR A 1 1885 ? 218.512 236.641 257.230 1.00 50.85  ? 1885 THR A OG1   1 
ATOM   2808  C  CG2   . THR A 1 1885 ? 216.222 237.232 257.731 1.00 35.33  ? 1885 THR A CG2   1 
ATOM   2809  N  N     . ASP A 1 1886 ? 218.034 241.067 257.270 1.00 29.40  ? 1886 ASP A N     1 
ATOM   2810  C  CA    . ASP A 1 1886 ? 217.515 242.391 257.644 1.00 19.97  ? 1886 ASP A CA    1 
ATOM   2811  C  C     . ASP A 1 1886 ? 217.640 243.214 256.403 1.00 34.38  ? 1886 ASP A C     1 
ATOM   2812  O  O     . ASP A 1 1886 ? 216.859 244.132 256.225 1.00 50.73  ? 1886 ASP A O     1 
ATOM   2813  C  CB    . ASP A 1 1886 ? 218.435 243.045 258.634 1.00 32.34  ? 1886 ASP A CB    1 
ATOM   2814  C  CG    . ASP A 1 1886 ? 218.095 242.828 260.098 1.00 54.32  ? 1886 ASP A CG    1 
ATOM   2815  O  OD1   . ASP A 1 1886 ? 219.031 242.813 260.924 1.00 48.46  ? 1886 ASP A OD1   1 
ATOM   2816  O  OD2   . ASP A 1 1886 ? 216.895 242.693 260.398 1.00 56.73  ? 1886 ASP A OD2   1 
ATOM   2817  N  N     . ARG A 1 1887 ? 218.709 242.990 255.668 1.00 34.87  ? 1887 ARG A N     1 
ATOM   2818  C  CA    . ARG A 1 1887 ? 218.800 243.603 254.348 1.00 27.06  ? 1887 ARG A CA    1 
ATOM   2819  C  C     . ARG A 1 1887 ? 217.784 242.997 253.390 1.00 32.25  ? 1887 ARG A C     1 
ATOM   2820  O  O     . ARG A 1 1887 ? 217.173 243.712 252.587 1.00 40.69  ? 1887 ARG A O     1 
ATOM   2821  C  CB    . ARG A 1 1887 ? 220.218 243.443 253.805 1.00 28.59  ? 1887 ARG A CB    1 
ATOM   2822  C  CG    . ARG A 1 1887 ? 220.496 244.188 252.521 1.00 31.09  ? 1887 ARG A CG    1 
ATOM   2823  C  CD    . ARG A 1 1887 ? 221.960 244.061 252.157 1.00 32.37  ? 1887 ARG A CD    1 
ATOM   2824  N  NE    . ARG A 1 1887 ? 222.266 244.662 250.867 1.00 40.85  ? 1887 ARG A NE    1 
ATOM   2825  C  CZ    . ARG A 1 1887 ? 223.434 245.206 250.557 1.00 42.14  ? 1887 ARG A CZ    1 
ATOM   2826  N  NH1   . ARG A 1 1887 ? 224.426 245.256 251.431 1.00 33.95  ? 1887 ARG A NH1   1 
ATOM   2827  N  NH2   . ARG A 1 1887 ? 223.613 245.711 249.341 1.00 44.00  ? 1887 ARG A NH2   1 
ATOM   2828  N  N     . CYS A 1 1888 ? 217.600 241.677 253.452 1.00 31.58  ? 1888 CYS A N     1 
ATOM   2829  C  CA    . CYS A 1 1888 ? 216.598 241.028 252.615 1.00 29.48  ? 1888 CYS A CA    1 
ATOM   2830  C  C     . CYS A 1 1888 ? 215.201 241.518 252.957 1.00 32.37  ? 1888 CYS A C     1 
ATOM   2831  O  O     . CYS A 1 1888 ? 214.399 241.798 252.061 1.00 38.23  ? 1888 CYS A O     1 
ATOM   2832  C  CB    . CYS A 1 1888 ? 216.688 239.510 252.765 1.00 29.32  ? 1888 CYS A CB    1 
ATOM   2833  S  SG    . CYS A 1 1888 ? 215.471 238.587 251.798 1.00 56.89  ? 1888 CYS A SG    1 
ATOM   2834  N  N     . TYR A 1 1889 ? 214.895 241.632 254.250 1.00 33.31  ? 1889 TYR A N     1 
ATOM   2835  C  CA    . TYR A 1 1889 ? 213.597 242.152 254.659 1.00 25.08  ? 1889 TYR A CA    1 
ATOM   2836  C  C     . TYR A 1 1889 ? 213.381 243.558 254.123 1.00 28.05  ? 1889 TYR A C     1 
ATOM   2837  O  O     . TYR A 1 1889 ? 212.322 243.859 253.562 1.00 41.12  ? 1889 TYR A O     1 
ATOM   2838  C  CB    . TYR A 1 1889 ? 213.485 242.145 256.183 1.00 21.15  ? 1889 TYR A CB    1 
ATOM   2839  C  CG    . TYR A 1 1889 ? 213.042 240.831 256.782 1.00 29.89  ? 1889 TYR A CG    1 
ATOM   2840  C  CD1   . TYR A 1 1889 ? 213.382 239.623 256.192 1.00 36.45  ? 1889 TYR A CD1   1 
ATOM   2841  C  CD2   . TYR A 1 1889 ? 212.293 240.802 257.948 1.00 32.14  ? 1889 TYR A CD2   1 
ATOM   2842  C  CE1   . TYR A 1 1889 ? 212.982 238.424 256.744 1.00 35.72  ? 1889 TYR A CE1   1 
ATOM   2843  C  CE2   . TYR A 1 1889 ? 211.888 239.610 258.505 1.00 37.00  ? 1889 TYR A CE2   1 
ATOM   2844  C  CZ    . TYR A 1 1889 ? 212.235 238.425 257.901 1.00 41.93  ? 1889 TYR A CZ    1 
ATOM   2845  O  OH    . TYR A 1 1889 ? 211.832 237.236 258.459 1.00 47.81  ? 1889 TYR A OH    1 
ATOM   2846  N  N     . LEU A 1 1890 ? 214.384 244.426 254.264 1.00 27.96  ? 1890 LEU A N     1 
ATOM   2847  C  CA    . LEU A 1 1890 ? 214.245 245.803 253.799 1.00 26.59  ? 1890 LEU A CA    1 
ATOM   2848  C  C     . LEU A 1 1890 ? 214.035 245.862 252.292 1.00 29.93  ? 1890 LEU A C     1 
ATOM   2849  O  O     . LEU A 1 1890 ? 213.116 246.533 251.810 1.00 39.65  ? 1890 LEU A O     1 
ATOM   2850  C  CB    . LEU A 1 1890 ? 215.471 246.621 254.202 1.00 27.27  ? 1890 LEU A CB    1 
ATOM   2851  C  CG    . LEU A 1 1890 ? 215.433 248.104 253.833 1.00 28.56  ? 1890 LEU A CG    1 
ATOM   2852  C  CD1   . LEU A 1 1890 ? 214.361 248.827 254.627 1.00 32.42  ? 1890 LEU A CD1   1 
ATOM   2853  C  CD2   . LEU A 1 1890 ? 216.790 248.748 254.056 1.00 27.31  ? 1890 LEU A CD2   1 
ATOM   2854  N  N     . THR A 1 1891 ? 214.874 245.157 251.529 1.00 37.28  ? 1891 THR A N     1 
ATOM   2855  C  CA    . THR A 1 1891 ? 214.761 245.195 250.074 1.00 34.49  ? 1891 THR A CA    1 
ATOM   2856  C  C     . THR A 1 1891 ? 213.434 244.616 249.601 1.00 29.74  ? 1891 THR A C     1 
ATOM   2857  O  O     . THR A 1 1891 ? 212.778 245.185 248.720 1.00 40.60  ? 1891 THR A O     1 
ATOM   2858  C  CB    . THR A 1 1891 ? 215.928 244.442 249.439 1.00 32.86  ? 1891 THR A CB    1 
ATOM   2859  O  OG1   . THR A 1 1891 ? 217.163 244.977 249.927 1.00 24.23  ? 1891 THR A OG1   1 
ATOM   2860  C  CG2   . THR A 1 1891 ? 215.887 244.576 247.929 1.00 31.83  ? 1891 THR A CG2   1 
ATOM   2861  N  N     . MET A 1 1892 ? 213.012 243.493 250.183 1.00 29.02  ? 1892 MET A N     1 
ATOM   2862  C  CA    . MET A 1 1892 ? 211.783 242.850 249.737 1.00 27.53  ? 1892 MET A CA    1 
ATOM   2863  C  C     . MET A 1 1892 ? 210.558 243.666 250.125 1.00 25.38  ? 1892 MET A C     1 
ATOM   2864  O  O     . MET A 1 1892 ? 209.584 243.724 249.368 1.00 42.17  ? 1892 MET A O     1 
ATOM   2865  C  CB    . MET A 1 1892 ? 211.701 241.436 250.305 1.00 30.88  ? 1892 MET A CB    1 
ATOM   2866  C  CG    . MET A 1 1892 ? 212.695 240.463 249.689 1.00 30.94  ? 1892 MET A CG    1 
ATOM   2867  S  SD    . MET A 1 1892 ? 212.928 240.725 247.923 1.00 55.41  ? 1892 MET A SD    1 
ATOM   2868  C  CE    . MET A 1 1892 ? 214.712 240.725 247.803 1.00 28.62  ? 1892 MET A CE    1 
ATOM   2869  N  N     . THR A 1 1893 ? 210.584 244.318 251.290 1.00 26.50  ? 1893 THR A N     1 
ATOM   2870  C  CA    . THR A 1 1893 ? 209.468 245.179 251.662 1.00 26.46  ? 1893 THR A CA    1 
ATOM   2871  C  C     . THR A 1 1893 ? 209.428 246.441 250.813 1.00 32.49  ? 1893 THR A C     1 
ATOM   2872  O  O     . THR A 1 1893 ? 208.341 246.946 250.509 1.00 41.23  ? 1893 THR A O     1 
ATOM   2873  C  CB    . THR A 1 1893 ? 209.547 245.537 253.143 1.00 35.77  ? 1893 THR A CB    1 
ATOM   2874  O  OG1   . THR A 1 1893 ? 210.875 245.973 253.456 1.00 40.61  ? 1893 THR A OG1   1 
ATOM   2875  C  CG2   . THR A 1 1893 ? 209.201 244.331 253.997 1.00 29.70  ? 1893 THR A CG2   1 
ATOM   2876  N  N     . GLN A 1 1894 ? 210.592 246.966 250.421 1.00 33.34  ? 1894 GLN A N     1 
ATOM   2877  C  CA    . GLN A 1 1894 ? 210.614 248.086 249.487 1.00 25.98  ? 1894 GLN A CA    1 
ATOM   2878  C  C     . GLN A 1 1894 ? 210.048 247.676 248.135 1.00 30.20  ? 1894 GLN A C     1 
ATOM   2879  O  O     . GLN A 1 1894 ? 209.352 248.459 247.480 1.00 39.52  ? 1894 GLN A O     1 
ATOM   2880  C  CB    . GLN A 1 1894 ? 212.037 248.617 249.335 1.00 29.63  ? 1894 GLN A CB    1 
ATOM   2881  C  CG    . GLN A 1 1894 ? 212.547 249.392 250.536 1.00 36.35  ? 1894 GLN A CG    1 
ATOM   2882  C  CD    . GLN A 1 1894 ? 211.716 250.618 250.832 1.00 38.79  ? 1894 GLN A CD    1 
ATOM   2883  O  OE1   . GLN A 1 1894 ? 211.792 251.618 250.122 1.00 39.34  ? 1894 GLN A OE1   1 
ATOM   2884  N  NE2   . GLN A 1 1894 ? 210.913 250.547 251.885 1.00 40.30  ? 1894 GLN A NE2   1 
ATOM   2885  N  N     . ALA A 1 1895 ? 210.352 246.454 247.695 1.00 33.02  ? 1895 ALA A N     1 
ATOM   2886  C  CA    . ALA A 1 1895 ? 209.746 245.936 246.473 1.00 22.90  ? 1895 ALA A CA    1 
ATOM   2887  C  C     . ALA A 1 1895 ? 208.235 245.803 246.617 1.00 21.45  ? 1895 ALA A C     1 
ATOM   2888  O  O     . ALA A 1 1895 ? 207.486 246.164 245.704 1.00 36.05  ? 1895 ALA A O     1 
ATOM   2889  C  CB    . ALA A 1 1895 ? 210.369 244.590 246.111 1.00 20.89  ? 1895 ALA A CB    1 
ATOM   2890  N  N     . LEU A 1 1896 ? 207.773 245.290 247.759 1.00 31.85  ? 1896 LEU A N     1 
ATOM   2891  C  CA    . LEU A 1 1896 ? 206.340 245.119 247.983 1.00 28.23  ? 1896 LEU A CA    1 
ATOM   2892  C  C     . LEU A 1 1896 ? 205.612 246.456 247.981 1.00 34.90  ? 1896 LEU A C     1 
ATOM   2893  O  O     . LEU A 1 1896 ? 204.522 246.575 247.413 1.00 38.32  ? 1896 LEU A O     1 
ATOM   2894  C  CB    . LEU A 1 1896 ? 206.099 244.393 249.304 1.00 35.12  ? 1896 LEU A CB    1 
ATOM   2895  C  CG    . LEU A 1 1896 ? 206.427 242.904 249.364 1.00 34.39  ? 1896 LEU A CG    1 
ATOM   2896  C  CD1   . LEU A 1 1896 ? 206.574 242.455 250.804 1.00 36.26  ? 1896 LEU A CD1   1 
ATOM   2897  C  CD2   . LEU A 1 1896 ? 205.344 242.115 248.675 1.00 31.79  ? 1896 LEU A CD2   1 
ATOM   2898  N  N     . GLU A 1 1897 ? 206.191 247.470 248.628 1.00 39.01  ? 1897 GLU A N     1 
ATOM   2899  C  CA    . GLU A 1 1897 ? 205.562 248.785 248.643 1.00 37.13  ? 1897 GLU A CA    1 
ATOM   2900  C  C     . GLU A 1 1897 ? 205.537 249.407 247.253 1.00 43.03  ? 1897 GLU A C     1 
ATOM   2901  O  O     . GLU A 1 1897 ? 204.653 250.216 246.952 1.00 47.01  ? 1897 GLU A O     1 
ATOM   2902  C  CB    . GLU A 1 1897 ? 206.283 249.698 249.635 1.00 39.60  ? 1897 GLU A CB    1 
ATOM   2903  C  CG    . GLU A 1 1897 ? 205.620 251.050 249.844 1.00 44.92  ? 1897 GLU A CG    1 
ATOM   2904  C  CD    . GLU A 1 1897 ? 204.369 250.972 250.701 1.00 55.67  ? 1897 GLU A CD    1 
ATOM   2905  O  OE1   . GLU A 1 1897 ? 204.063 249.880 251.225 1.00 60.15  ? 1897 GLU A OE1   1 
ATOM   2906  O  OE2   . GLU A 1 1897 ? 203.686 252.006 250.850 1.00 52.46  ? 1897 GLU A OE2   1 
ATOM   2907  N  N     . ALA A 1 1898 ? 206.481 249.033 246.393 1.00 40.26  ? 1898 ALA A N     1 
ATOM   2908  C  CA    . ALA A 1 1898 ? 206.494 249.486 245.010 1.00 29.73  ? 1898 ALA A CA    1 
ATOM   2909  C  C     . ALA A 1 1898 ? 205.589 248.657 244.113 1.00 36.34  ? 1898 ALA A C     1 
ATOM   2910  O  O     . ALA A 1 1898 ? 205.533 248.919 242.908 1.00 46.83  ? 1898 ALA A O     1 
ATOM   2911  C  CB    . ALA A 1 1898 ? 207.922 249.463 244.461 1.00 37.36  ? 1898 ALA A CB    1 
ATOM   2912  N  N     . ARG A 1 1899 ? 204.894 247.665 244.673 1.00 46.30  ? 1899 ARG A N     1 
ATOM   2913  C  CA    . ARG A 1 1899 ? 203.972 246.806 243.930 1.00 41.97  ? 1899 ARG A CA    1 
ATOM   2914  C  C     . ARG A 1 1899 ? 204.679 246.077 242.791 1.00 36.92  ? 1899 ARG A C     1 
ATOM   2915  O  O     . ARG A 1 1899 ? 204.129 245.906 241.703 1.00 54.02  ? 1899 ARG A O     1 
ATOM   2916  C  CB    . ARG A 1 1899 ? 202.772 247.598 243.407 1.00 44.01  ? 1899 ARG A CB    1 
ATOM   2917  C  CG    . ARG A 1 1899 ? 201.601 247.641 244.368 1.00 42.39  ? 1899 ARG A CG    1 
ATOM   2918  C  CD    . ARG A 1 1899 ? 201.756 248.768 245.369 1.00 43.94  ? 1899 ARG A CD    1 
ATOM   2919  N  NE    . ARG A 1 1899 ? 201.039 248.499 246.609 1.00 53.97  ? 1899 ARG A NE    1 
ATOM   2920  C  CZ    . ARG A 1 1899 ? 201.061 249.290 247.673 1.00 58.90  ? 1899 ARG A CZ    1 
ATOM   2921  N  NH1   . ARG A 1 1899 ? 201.759 250.413 247.684 1.00 53.55  ? 1899 ARG A NH1   1 
ATOM   2922  N  NH2   . ARG A 1 1899 ? 200.369 248.943 248.754 1.00 49.67  ? 1899 ARG A NH2   1 
ATOM   2923  N  N     . LEU A 1 1900 ? 205.911 245.645 243.043 1.00 24.09  ? 1900 LEU A N     1 
ATOM   2924  C  CA    . LEU A 1 1900 ? 206.643 244.809 242.106 1.00 36.41  ? 1900 LEU A CA    1 
ATOM   2925  C  C     . LEU A 1 1900 ? 207.422 243.763 242.890 1.00 34.83  ? 1900 LEU A C     1 
ATOM   2926  O  O     . LEU A 1 1900 ? 207.811 243.982 244.038 1.00 47.29  ? 1900 LEU A O     1 
ATOM   2927  C  CB    . LEU A 1 1900 ? 207.565 245.641 241.202 1.00 36.66  ? 1900 LEU A CB    1 
ATOM   2928  C  CG    . LEU A 1 1900 ? 208.685 246.486 241.803 1.00 32.48  ? 1900 LEU A CG    1 
ATOM   2929  C  CD1   . LEU A 1 1900 ? 209.962 245.696 241.842 1.00 39.52  ? 1900 LEU A CD1   1 
ATOM   2930  C  CD2   . LEU A 1 1900 ? 208.877 247.749 240.990 1.00 37.91  ? 1900 LEU A CD2   1 
ATOM   2931  N  N     . GLY A 1 1901 ? 207.649 242.621 242.252 1.00 29.03  ? 1901 GLY A N     1 
ATOM   2932  C  CA    . GLY A 1 1901 ? 208.199 241.476 242.945 1.00 26.28  ? 1901 GLY A CA    1 
ATOM   2933  C  C     . GLY A 1 1901 ? 209.629 241.680 243.402 1.00 35.62  ? 1901 GLY A C     1 
ATOM   2934  O  O     . GLY A 1 1901 ? 210.298 242.658 243.073 1.00 44.91  ? 1901 GLY A O     1 
ATOM   2935  N  N     . GLY A 1 1902 ? 210.098 240.728 244.198 1.00 21.42  ? 1902 GLY A N     1 
ATOM   2936  C  CA    . GLY A 1 1902 ? 211.462 240.721 244.704 1.00 21.19  ? 1902 GLY A CA    1 
ATOM   2937  C  C     . GLY A 1 1902 ? 212.198 239.494 244.198 1.00 28.22  ? 1902 GLY A C     1 
ATOM   2938  O  O     . GLY A 1 1902 ? 211.614 238.416 244.084 1.00 36.92  ? 1902 GLY A O     1 
ATOM   2939  N  N     . SER A 1 1903 ? 213.484 239.665 243.901 1.00 26.13  ? 1903 SER A N     1 
ATOM   2940  C  CA    . SER A 1 1903 ? 214.295 238.625 243.269 1.00 17.35  ? 1903 SER A CA    1 
ATOM   2941  C  C     . SER A 1 1903 ? 215.614 238.453 244.008 1.00 28.51  ? 1903 SER A C     1 
ATOM   2942  O  O     . SER A 1 1903 ? 216.664 238.907 243.536 1.00 40.21  ? 1903 SER A O     1 
ATOM   2943  C  CB    . SER A 1 1903 ? 214.546 238.953 241.798 1.00 24.31  ? 1903 SER A CB    1 
ATOM   2944  O  OG    . SER A 1 1903 ? 215.671 238.247 241.310 1.00 40.80  ? 1903 SER A OG    1 
ATOM   2945  N  N     . PRO A 1 1904 ? 215.605 237.791 245.164 1.00 31.55  ? 1904 PRO A N     1 
ATOM   2946  C  CA    . PRO A 1 1904 ? 216.873 237.490 245.840 1.00 22.67  ? 1904 PRO A CA    1 
ATOM   2947  C  C     . PRO A 1 1904 ? 217.666 236.459 245.049 1.00 28.23  ? 1904 PRO A C     1 
ATOM   2948  O  O     . PRO A 1 1904 ? 217.156 235.390 244.711 1.00 39.79  ? 1904 PRO A O     1 
ATOM   2949  C  CB    . PRO A 1 1904 ? 216.432 236.946 247.202 1.00 15.73  ? 1904 PRO A CB    1 
ATOM   2950  C  CG    . PRO A 1 1904 ? 215.066 236.420 246.970 1.00 31.23  ? 1904 PRO A CG    1 
ATOM   2951  C  CD    . PRO A 1 1904 ? 214.444 237.276 245.909 1.00 29.13  ? 1904 PRO A CD    1 
ATOM   2952  N  N     . PHE A 1 1905 ? 218.919 236.789 244.751 1.00 25.43  ? 1905 PHE A N     1 
ATOM   2953  C  CA    . PHE A 1 1905 ? 219.764 235.941 243.926 1.00 23.93  ? 1905 PHE A CA    1 
ATOM   2954  C  C     . PHE A 1 1905 ? 221.126 235.773 244.581 1.00 29.47  ? 1905 PHE A C     1 
ATOM   2955  O  O     . PHE A 1 1905 ? 221.539 236.574 245.421 1.00 36.02  ? 1905 PHE A O     1 
ATOM   2956  C  CB    . PHE A 1 1905 ? 219.923 236.512 242.509 1.00 35.05  ? 1905 PHE A CB    1 
ATOM   2957  C  CG    . PHE A 1 1905 ? 220.822 237.713 242.434 1.00 33.31  ? 1905 PHE A CG    1 
ATOM   2958  C  CD1   . PHE A 1 1905 ? 220.345 238.971 242.748 1.00 29.73  ? 1905 PHE A CD1   1 
ATOM   2959  C  CD2   . PHE A 1 1905 ? 222.141 237.584 242.038 1.00 34.41  ? 1905 PHE A CD2   1 
ATOM   2960  C  CE1   . PHE A 1 1905 ? 221.166 240.073 242.679 1.00 27.06  ? 1905 PHE A CE1   1 
ATOM   2961  C  CE2   . PHE A 1 1905 ? 222.965 238.683 241.968 1.00 36.87  ? 1905 PHE A CE2   1 
ATOM   2962  C  CZ    . PHE A 1 1905 ? 222.477 239.929 242.288 1.00 32.84  ? 1905 PHE A CZ    1 
ATOM   2963  N  N     . GLY A 1 1906 ? 221.816 234.720 244.174 1.00 29.00  ? 1906 GLY A N     1 
ATOM   2964  C  CA    . GLY A 1 1906 ? 223.157 234.487 244.683 1.00 26.12  ? 1906 GLY A CA    1 
ATOM   2965  C  C     . GLY A 1 1906 ? 223.604 233.080 244.487 1.00 26.92  ? 1906 GLY A C     1 
ATOM   2966  O  O     . GLY A 1 1906 ? 223.062 232.406 243.643 1.00 36.42  ? 1906 GLY A O     1 
ATOM   2967  N  N     . PRO A 1 1907 ? 224.637 232.626 245.223 1.00 30.87  ? 1907 PRO A N     1 
ATOM   2968  C  CA    . PRO A 1 1907 ? 225.068 231.248 245.138 1.00 32.45  ? 1907 PRO A CA    1 
ATOM   2969  C  C     . PRO A 1 1907 ? 224.138 230.305 245.891 1.00 39.64  ? 1907 PRO A C     1 
ATOM   2970  O  O     . PRO A 1 1907 ? 222.999 230.701 246.147 1.00 45.79  ? 1907 PRO A O     1 
ATOM   2971  C  CB    . PRO A 1 1907 ? 226.442 231.408 245.702 1.00 32.36  ? 1907 PRO A CB    1 
ATOM   2972  C  CG    . PRO A 1 1907 ? 226.284 232.424 246.781 1.00 29.30  ? 1907 PRO A CG    1 
ATOM   2973  C  CD    . PRO A 1 1907 ? 225.415 233.446 246.109 1.00 35.11  ? 1907 PRO A CD    1 
ATOM   2974  N  N     . ALA A 1 1908 ? 224.551 229.092 246.231 1.00 37.78  ? 1908 ALA A N     1 
ATOM   2975  C  CA    . ALA A 1 1908 ? 223.636 228.099 246.821 1.00 30.26  ? 1908 ALA A CA    1 
ATOM   2976  C  C     . ALA A 1 1908 ? 223.785 228.035 248.324 1.00 38.60  ? 1908 ALA A C     1 
ATOM   2977  O  O     . ALA A 1 1908 ? 224.932 227.925 248.740 1.00 45.77  ? 1908 ALA A O     1 
ATOM   2978  C  CB    . ALA A 1 1908 ? 224.032 226.791 246.282 1.00 29.12  ? 1908 ALA A CB    1 
ATOM   2979  N  N     . GLY A 1 1909 ? 222.696 228.032 249.089 1.00 42.01  ? 1909 GLY A N     1 
ATOM   2980  C  CA    . GLY A 1 1909 ? 222.745 227.886 250.540 1.00 27.40  ? 1909 GLY A CA    1 
ATOM   2981  C  C     . GLY A 1 1909 ? 222.999 229.203 251.166 1.00 35.18  ? 1909 GLY A C     1 
ATOM   2982  O  O     . GLY A 1 1909 ? 223.864 229.252 252.027 1.00 42.54  ? 1909 GLY A O     1 
ATOM   2983  N  N     . THR A 1 1910 ? 222.246 230.224 250.784 1.00 41.27  ? 1910 THR A N     1 
ATOM   2984  C  CA    . THR A 1 1910 ? 222.531 231.573 251.280 1.00 37.59  ? 1910 THR A CA    1 
ATOM   2985  C  C     . THR A 1 1910 ? 221.320 232.102 251.995 1.00 36.65  ? 1910 THR A C     1 
ATOM   2986  O  O     . THR A 1 1910 ? 221.408 233.175 252.540 1.00 44.94  ? 1910 THR A O     1 
ATOM   2987  C  CB    . THR A 1 1910 ? 223.068 232.485 250.174 1.00 27.77  ? 1910 THR A CB    1 
ATOM   2988  O  OG1   . THR A 1 1910 ? 222.205 232.394 249.051 1.00 41.99  ? 1910 THR A OG1   1 
ATOM   2989  C  CG2   . THR A 1 1910 ? 224.472 232.096 249.757 1.00 29.12  ? 1910 THR A CG2   1 
ATOM   2990  N  N     . GLY A 1 1911 ? 220.240 231.369 252.030 1.00 31.85  ? 1911 GLY A N     1 
ATOM   2991  C  CA    . GLY A 1 1911 ? 219.053 231.783 252.770 1.00 35.40  ? 1911 GLY A CA    1 
ATOM   2992  C  C     . GLY A 1 1911 ? 218.047 232.519 251.940 1.00 38.78  ? 1911 GLY A C     1 
ATOM   2993  O  O     . GLY A 1 1911 ? 217.217 233.176 252.527 1.00 43.63  ? 1911 GLY A O     1 
ATOM   2994  N  N     . LYS A 1 1912 ? 218.060 232.344 250.639 1.00 31.66  ? 1912 LYS A N     1 
ATOM   2995  C  CA    . LYS A 1 1912 ? 217.156 233.028 249.714 1.00 18.63  ? 1912 LYS A CA    1 
ATOM   2996  C  C     . LYS A 1 1912 ? 215.719 232.577 249.873 1.00 19.66  ? 1912 LYS A C     1 
ATOM   2997  O  O     . LYS A 1 1912 ? 214.894 233.453 249.994 1.00 41.17  ? 1912 LYS A O     1 
ATOM   2998  C  CB    . LYS A 1 1912 ? 217.788 232.744 248.359 1.00 24.90  ? 1912 LYS A CB    1 
ATOM   2999  C  CG    . LYS A 1 1912 ? 218.830 233.736 247.921 1.00 30.41  ? 1912 LYS A CG    1 
ATOM   3000  C  CD    . LYS A 1 1912 ? 219.267 233.363 246.520 1.00 27.60  ? 1912 LYS A CD    1 
ATOM   3001  C  CE    . LYS A 1 1912 ? 220.070 232.129 246.549 1.00 18.88  ? 1912 LYS A CE    1 
ATOM   3002  N  NZ    . LYS A 1 1912 ? 219.798 231.390 245.322 1.00 35.44  ? 1912 LYS A NZ    1 
ATOM   3003  N  N     . THR A 1 1913 ? 215.426 231.289 249.850 1.00 27.46  ? 1913 THR A N     1 
ATOM   3004  C  CA    . THR A 1 1913 ? 214.049 230.777 249.899 1.00 28.46  ? 1913 THR A CA    1 
ATOM   3005  C  C     . THR A 1 1913 ? 213.590 230.879 251.286 1.00 31.98  ? 1913 THR A C     1 
ATOM   3006  O  O     . THR A 1 1913 ? 212.469 231.295 251.479 1.00 34.15  ? 1913 THR A O     1 
ATOM   3007  C  CB    . THR A 1 1913 ? 213.999 229.316 249.488 1.00 37.40  ? 1913 THR A CB    1 
ATOM   3008  O  OG1   . THR A 1 1913 ? 214.645 229.208 248.223 1.00 45.44  ? 1913 THR A OG1   1 
ATOM   3009  C  CG2   . THR A 1 1913 ? 212.579 228.792 249.407 1.00 37.31  ? 1913 THR A CG2   1 
ATOM   3010  N  N     . GLU A 1 1914 ? 214.436 230.519 252.218 1.00 42.35  ? 1914 GLU A N     1 
ATOM   3011  C  CA    . GLU A 1 1914 ? 214.100 230.545 253.651 1.00 31.29  ? 1914 GLU A CA    1 
ATOM   3012  C  C     . GLU A 1 1914 ? 213.869 231.958 254.158 1.00 36.21  ? 1914 GLU A C     1 
ATOM   3013  O  O     . GLU A 1 1914 ? 213.093 232.071 255.089 1.00 43.50  ? 1914 GLU A O     1 
ATOM   3014  C  CB    . GLU A 1 1914 ? 215.273 229.918 254.387 1.00 34.83  ? 1914 GLU A CB    1 
ATOM   3015  C  CG    . GLU A 1 1914 ? 215.435 228.431 254.097 1.00 43.37  ? 1914 GLU A CG    1 
ATOM   3016  C  CD    . GLU A 1 1914 ? 214.181 227.589 254.221 1.00 49.75  ? 1914 GLU A CD    1 
ATOM   3017  O  OE1   . GLU A 1 1914 ? 213.508 227.719 255.254 1.00 49.94  ? 1914 GLU A OE1   1 
ATOM   3018  O  OE2   . GLU A 1 1914 ? 213.878 226.802 253.302 1.00 44.52  ? 1914 GLU A OE2   1 
ATOM   3019  N  N     . SER A 1 1915 ? 214.446 232.984 253.540 1.00 34.01  ? 1915 SER A N     1 
ATOM   3020  C  CA    . SER A 1 1915 ? 214.345 234.391 253.978 1.00 18.66  ? 1915 SER A CA    1 
ATOM   3021  C  C     . SER A 1 1915 ? 213.088 234.946 253.357 1.00 22.97  ? 1915 SER A C     1 
ATOM   3022  O  O     . SER A 1 1915 ? 212.477 235.806 253.932 1.00 42.40  ? 1915 SER A O     1 
ATOM   3023  C  CB    . SER A 1 1915 ? 215.510 235.120 253.532 1.00 24.13  ? 1915 SER A CB    1 
ATOM   3024  O  OG    . SER A 1 1915 ? 216.602 234.916 254.411 1.00 38.74  ? 1915 SER A OG    1 
ATOM   3025  N  N     . VAL A 1 1916 ? 212.784 234.511 252.162 1.00 30.91  ? 1916 VAL A N     1 
ATOM   3026  C  CA    . VAL A 1 1916 ? 211.485 234.894 251.612 1.00 24.85  ? 1916 VAL A CA    1 
ATOM   3027  C  C     . VAL A 1 1916 ? 210.357 234.259 252.415 1.00 30.70  ? 1916 VAL A C     1 
ATOM   3028  O  O     . VAL A 1 1916 ? 209.366 234.919 252.755 1.00 35.47  ? 1916 VAL A O     1 
ATOM   3029  C  CB    . VAL A 1 1916 ? 211.401 234.519 250.122 1.00 24.26  ? 1916 VAL A CB    1 
ATOM   3030  C  CG1   . VAL A 1 1916 ? 209.986 234.701 249.613 1.00 23.13  ? 1916 VAL A CG1   1 
ATOM   3031  C  CG2   . VAL A 1 1916 ? 212.369 235.358 249.313 1.00 30.75  ? 1916 VAL A CG2   1 
ATOM   3032  N  N     . LYS A 1 1917 ? 210.495 232.971 252.743 1.00 29.41  ? 1917 LYS A N     1 
ATOM   3033  C  CA    . LYS A 1 1917 ? 209.477 232.297 253.544 1.00 16.67  ? 1917 LYS A CA    1 
ATOM   3034  C  C     . LYS A 1 1917 ? 209.363 232.915 254.932 1.00 32.03  ? 1917 LYS A C     1 
ATOM   3035  O  O     . LYS A 1 1917 ? 208.257 233.066 255.461 1.00 44.69  ? 1917 LYS A O     1 
ATOM   3036  C  CB    . LYS A 1 1917 ? 209.796 230.808 253.651 1.00 21.74  ? 1917 LYS A CB    1 
ATOM   3037  C  CG    . LYS A 1 1917 ? 209.477 230.007 252.405 1.00 30.10  ? 1917 LYS A CG    1 
ATOM   3038  C  CD    . LYS A 1 1917 ? 209.350 228.531 252.728 1.00 23.21  ? 1917 LYS A CD    1 
ATOM   3039  C  CE    . LYS A 1 1917 ? 210.577 228.021 253.458 1.00 31.32  ? 1917 LYS A CE    1 
ATOM   3040  N  NZ    . LYS A 1 1917 ? 210.448 226.585 253.822 1.00 28.91  ? 1917 LYS A NZ    1 
ATOM   3041  N  N     . ALA A 1 1918 ? 210.495 233.272 255.541 1.00 31.03  ? 1918 ALA A N     1 
ATOM   3042  C  CA    . ALA A 1 1918 ? 210.479 233.853 256.877 1.00 13.18  ? 1918 ALA A CA    1 
ATOM   3043  C  C     . ALA A 1 1918 ? 209.843 235.233 256.872 1.00 24.02  ? 1918 ALA A C     1 
ATOM   3044  O  O     . ALA A 1 1918 ? 209.129 235.595 257.811 1.00 45.16  ? 1918 ALA A O     1 
ATOM   3045  C  CB    . ALA A 1 1918 ? 211.899 233.917 257.435 1.00 22.80  ? 1918 ALA A CB    1 
ATOM   3046  N  N     . LEU A 1 1919 ? 210.103 236.028 255.833 1.00 21.91  ? 1919 LEU A N     1 
ATOM   3047  C  CA    . LEU A 1 1919 ? 209.437 237.321 255.717 1.00 18.58  ? 1919 LEU A CA    1 
ATOM   3048  C  C     . LEU A 1 1919 ? 207.939 237.149 255.511 1.00 32.42  ? 1919 LEU A C     1 
ATOM   3049  O  O     . LEU A 1 1919 ? 207.137 237.895 256.083 1.00 31.52  ? 1919 LEU A O     1 
ATOM   3050  C  CB    . LEU A 1 1919 ? 210.043 238.131 254.574 1.00 23.59  ? 1919 LEU A CB    1 
ATOM   3051  C  CG    . LEU A 1 1919 ? 209.341 239.458 254.286 1.00 26.48  ? 1919 LEU A CG    1 
ATOM   3052  C  CD1   . LEU A 1 1919 ? 209.477 240.415 255.455 1.00 26.88  ? 1919 LEU A CD1   1 
ATOM   3053  C  CD2   . LEU A 1 1919 ? 209.875 240.083 253.019 1.00 22.85  ? 1919 LEU A CD2   1 
ATOM   3054  N  N     . GLY A 1 1920 ? 207.540 236.175 254.692 1.00 36.77  ? 1920 GLY A N     1 
ATOM   3055  C  CA    . GLY A 1 1920 ? 206.121 235.921 254.508 1.00 24.33  ? 1920 GLY A CA    1 
ATOM   3056  C  C     . GLY A 1 1920 ? 205.439 235.481 255.787 1.00 29.89  ? 1920 GLY A C     1 
ATOM   3057  O  O     . GLY A 1 1920 ? 204.305 235.875 256.065 1.00 43.24  ? 1920 GLY A O     1 
ATOM   3058  N  N     . HIS A 1 1921 ? 206.117 234.649 256.578 1.00 31.41  ? 1921 HIS A N     1 
ATOM   3059  C  CA    . HIS A 1 1921 ? 205.572 234.236 257.865 1.00 28.35  ? 1921 HIS A CA    1 
ATOM   3060  C  C     . HIS A 1 1921 ? 205.588 235.378 258.872 1.00 36.98  ? 1921 HIS A C     1 
ATOM   3061  O  O     . HIS A 1 1921 ? 204.770 235.400 259.797 1.00 46.55  ? 1921 HIS A O     1 
ATOM   3062  C  CB    . HIS A 1 1921 ? 206.354 233.041 258.406 1.00 24.96  ? 1921 HIS A CB    1 
ATOM   3063  C  CG    . HIS A 1 1921 ? 206.339 231.848 257.501 1.00 43.93  ? 1921 HIS A CG    1 
ATOM   3064  N  ND1   . HIS A 1 1921 ? 205.376 231.660 256.533 1.00 45.56  ? 1921 HIS A ND1   1 
ATOM   3065  C  CD2   . HIS A 1 1921 ? 207.170 230.783 257.415 1.00 42.49  ? 1921 HIS A CD2   1 
ATOM   3066  C  CE1   . HIS A 1 1921 ? 205.615 230.531 255.890 1.00 41.19  ? 1921 HIS A CE1   1 
ATOM   3067  N  NE2   . HIS A 1 1921 ? 206.698 229.980 256.406 1.00 40.17  ? 1921 HIS A NE2   1 
ATOM   3068  N  N     . GLN A 1 1922 ? 206.512 236.327 258.710 1.00 37.16  ? 1922 GLN A N     1 
ATOM   3069  C  CA    . GLN A 1 1922 ? 206.578 237.471 259.610 1.00 29.19  ? 1922 GLN A CA    1 
ATOM   3070  C  C     . GLN A 1 1922 ? 205.331 238.334 259.489 1.00 28.64  ? 1922 GLN A C     1 
ATOM   3071  O  O     . GLN A 1 1922 ? 204.834 238.866 260.487 1.00 39.41  ? 1922 GLN A O     1 
ATOM   3072  C  CB    . GLN A 1 1922 ? 207.829 238.295 259.311 1.00 31.28  ? 1922 GLN A CB    1 
ATOM   3073  C  CG    . GLN A 1 1922 ? 208.063 239.434 260.276 1.00 33.71  ? 1922 GLN A CG    1 
ATOM   3074  C  CD    . GLN A 1 1922 ? 208.321 238.946 261.681 1.00 46.36  ? 1922 GLN A CD    1 
ATOM   3075  O  OE1   . GLN A 1 1922 ? 207.450 239.016 262.545 1.00 47.22  ? 1922 GLN A OE1   1 
ATOM   3076  N  NE2   . GLN A 1 1922 ? 209.524 238.439 261.917 1.00 47.86  ? 1922 GLN A NE2   1 
ATOM   3077  N  N     . LEU A 1 1923 ? 204.819 238.489 258.273 1.00 37.84  ? 1923 LEU A N     1 
ATOM   3078  C  CA    . LEU A 1 1923 ? 203.593 239.232 258.026 1.00 31.60  ? 1923 LEU A CA    1 
ATOM   3079  C  C     . LEU A 1 1923 ? 202.355 238.350 258.085 1.00 34.91  ? 1923 LEU A C     1 
ATOM   3080  O  O     . LEU A 1 1923 ? 201.253 238.834 257.813 1.00 43.52  ? 1923 LEU A O     1 
ATOM   3081  C  CB    . LEU A 1 1923 ? 203.662 239.929 256.665 1.00 29.54  ? 1923 LEU A CB    1 
ATOM   3082  C  CG    . LEU A 1 1923 ? 204.993 240.581 256.284 1.00 33.92  ? 1923 LEU A CG    1 
ATOM   3083  C  CD1   . LEU A 1 1923 ? 204.919 241.153 254.887 1.00 32.77  ? 1923 LEU A CD1   1 
ATOM   3084  C  CD2   . LEU A 1 1923 ? 205.380 241.659 257.273 1.00 34.39  ? 1923 LEU A CD2   1 
ATOM   3085  N  N     . GLY A 1 1924 ? 202.508 237.078 258.434 1.00 34.93  ? 1924 GLY A N     1 
ATOM   3086  C  CA    . GLY A 1 1924 ? 201.376 236.172 258.500 1.00 30.32  ? 1924 GLY A CA    1 
ATOM   3087  C  C     . GLY A 1 1924 ? 200.746 235.891 257.156 1.00 42.69  ? 1924 GLY A C     1 
ATOM   3088  O  O     . GLY A 1 1924 ? 199.515 235.849 257.049 1.00 49.59  ? 1924 GLY A O     1 
ATOM   3089  N  N     . ARG A 1 1925 ? 201.559 235.698 256.127 1.00 47.09  ? 1925 ARG A N     1 
ATOM   3090  C  CA    . ARG A 1 1925 ? 201.077 235.440 254.781 1.00 34.82  ? 1925 ARG A CA    1 
ATOM   3091  C  C     . ARG A 1 1925 ? 201.165 233.954 254.459 1.00 41.84  ? 1925 ARG A C     1 
ATOM   3092  O  O     . ARG A 1 1925 ? 201.981 233.217 255.017 1.00 51.33  ? 1925 ARG A O     1 
ATOM   3093  C  CB    . ARG A 1 1925 ? 201.882 236.240 253.754 1.00 30.81  ? 1925 ARG A CB    1 
ATOM   3094  C  CG    . ARG A 1 1925 ? 201.723 237.743 253.864 1.00 37.99  ? 1925 ARG A CG    1 
ATOM   3095  C  CD    . ARG A 1 1925 ? 200.304 238.180 253.556 1.00 42.14  ? 1925 ARG A CD    1 
ATOM   3096  N  NE    . ARG A 1 1925 ? 200.245 239.593 253.202 1.00 41.81  ? 1925 ARG A NE    1 
ATOM   3097  C  CZ    . ARG A 1 1925 ? 200.219 240.585 254.079 1.00 43.53  ? 1925 ARG A CZ    1 
ATOM   3098  N  NH1   . ARG A 1 1925 ? 200.219 240.357 255.381 1.00 43.13  ? 1925 ARG A NH1   1 
ATOM   3099  N  NH2   . ARG A 1 1925 ? 200.192 241.839 253.639 1.00 41.63  ? 1925 ARG A NH2   1 
ATOM   3100  N  N     . PHE A 1 1926 ? 200.304 233.522 253.544 1.00 43.46  ? 1926 PHE A N     1 
ATOM   3101  C  CA    . PHE A 1 1926 ? 200.359 232.171 253.000 1.00 44.46  ? 1926 PHE A CA    1 
ATOM   3102  C  C     . PHE A 1 1926 ? 201.409 232.165 251.895 1.00 41.07  ? 1926 PHE A C     1 
ATOM   3103  O  O     . PHE A 1 1926 ? 201.208 232.767 250.837 1.00 45.68  ? 1926 PHE A O     1 
ATOM   3104  C  CB    . PHE A 1 1926 ? 198.986 231.746 252.484 1.00 42.76  ? 1926 PHE A CB    1 
ATOM   3105  C  CG    . PHE A 1 1926 ? 198.900 230.301 252.070 1.00 45.22  ? 1926 PHE A CG    1 
ATOM   3106  C  CD1   . PHE A 1 1926 ? 199.895 229.400 252.404 1.00 43.66  ? 1926 PHE A CD1   1 
ATOM   3107  C  CD2   . PHE A 1 1926 ? 197.806 229.843 251.359 1.00 44.00  ? 1926 PHE A CD2   1 
ATOM   3108  C  CE1   . PHE A 1 1926 ? 199.808 228.078 252.023 1.00 42.52  ? 1926 PHE A CE1   1 
ATOM   3109  C  CE2   . PHE A 1 1926 ? 197.713 228.522 250.980 1.00 44.66  ? 1926 PHE A CE2   1 
ATOM   3110  C  CZ    . PHE A 1 1926 ? 198.715 227.640 251.311 1.00 45.34  ? 1926 PHE A CZ    1 
ATOM   3111  N  N     . VAL A 1 1927 ? 202.533 231.501 252.143 1.00 29.96  ? 1927 VAL A N     1 
ATOM   3112  C  CA    . VAL A 1 1927 ? 203.651 231.465 251.208 1.00 36.26  ? 1927 VAL A CA    1 
ATOM   3113  C  C     . VAL A 1 1927 ? 203.690 230.086 250.570 1.00 40.97  ? 1927 VAL A C     1 
ATOM   3114  O  O     . VAL A 1 1927 ? 203.870 229.078 251.263 1.00 44.87  ? 1927 VAL A O     1 
ATOM   3115  C  CB    . VAL A 1 1927 ? 204.982 231.788 251.900 1.00 34.85  ? 1927 VAL A CB    1 
ATOM   3116  C  CG1   . VAL A 1 1927 ? 206.117 231.784 250.893 1.00 25.47  ? 1927 VAL A CG1   1 
ATOM   3117  C  CG2   . VAL A 1 1927 ? 204.896 233.127 252.596 1.00 39.69  ? 1927 VAL A CG2   1 
ATOM   3118  N  N     . LEU A 1 1928 ? 203.527 230.042 249.252 1.00 30.65  ? 1928 LEU A N     1 
ATOM   3119  C  CA    . LEU A 1 1928 ? 203.597 228.805 248.491 1.00 28.26  ? 1928 LEU A CA    1 
ATOM   3120  C  C     . LEU A 1 1928 ? 204.908 228.772 247.724 1.00 25.86  ? 1928 LEU A C     1 
ATOM   3121  O  O     . LEU A 1 1928 ? 205.228 229.713 246.991 1.00 38.19  ? 1928 LEU A O     1 
ATOM   3122  C  CB    . LEU A 1 1928 ? 202.416 228.672 247.528 1.00 30.80  ? 1928 LEU A CB    1 
ATOM   3123  C  CG    . LEU A 1 1928 ? 201.071 228.263 248.125 1.00 27.54  ? 1928 LEU A CG    1 
ATOM   3124  C  CD1   . LEU A 1 1928 ? 200.339 229.475 248.668 1.00 40.15  ? 1928 LEU A CD1   1 
ATOM   3125  C  CD2   . LEU A 1 1928 ? 200.223 227.540 247.098 1.00 29.40  ? 1928 LEU A CD2   1 
ATOM   3126  N  N     . VAL A 1 1929 ? 205.659 227.692 247.896 1.00 24.73  ? 1929 VAL A N     1 
ATOM   3127  C  CA    . VAL A 1 1929 ? 206.956 227.516 247.259 1.00 31.30  ? 1929 VAL A CA    1 
ATOM   3128  C  C     . VAL A 1 1929 ? 206.783 226.607 246.054 1.00 33.92  ? 1929 VAL A C     1 
ATOM   3129  O  O     . VAL A 1 1929 ? 206.238 225.503 246.172 1.00 53.22  ? 1929 VAL A O     1 
ATOM   3130  C  CB    . VAL A 1 1929 ? 207.981 226.937 248.247 1.00 39.28  ? 1929 VAL A CB    1 
ATOM   3131  C  CG1   . VAL A 1 1929 ? 209.192 226.411 247.507 1.00 34.67  ? 1929 VAL A CG1   1 
ATOM   3132  C  CG2   . VAL A 1 1929 ? 208.392 227.995 249.253 1.00 35.64  ? 1929 VAL A CG2   1 
ATOM   3133  N  N     . PHE A 1 1930 ? 207.235 227.071 244.893 1.00 22.40  ? 1930 PHE A N     1 
ATOM   3134  C  CA    . PHE A 1 1930 ? 207.186 226.302 243.660 1.00 31.32  ? 1930 PHE A CA    1 
ATOM   3135  C  C     . PHE A 1 1930 ? 208.604 226.088 243.158 1.00 31.48  ? 1930 PHE A C     1 
ATOM   3136  O  O     . PHE A 1 1930 ? 209.373 227.047 243.039 1.00 38.49  ? 1930 PHE A O     1 
ATOM   3137  C  CB    . PHE A 1 1930 ? 206.351 227.015 242.592 1.00 24.31  ? 1930 PHE A CB    1 
ATOM   3138  C  CG    . PHE A 1 1930 ? 204.974 227.393 243.049 1.00 29.69  ? 1930 PHE A CG    1 
ATOM   3139  C  CD1   . PHE A 1 1930 ? 203.930 226.491 242.963 1.00 28.06  ? 1930 PHE A CD1   1 
ATOM   3140  C  CD2   . PHE A 1 1930 ? 204.723 228.651 243.565 1.00 37.28  ? 1930 PHE A CD2   1 
ATOM   3141  C  CE1   . PHE A 1 1930 ? 202.663 226.837 243.385 1.00 24.40  ? 1930 PHE A CE1   1 
ATOM   3142  C  CE2   . PHE A 1 1930 ? 203.459 229.001 243.990 1.00 34.30  ? 1930 PHE A CE2   1 
ATOM   3143  C  CZ    . PHE A 1 1930 ? 202.428 228.093 243.899 1.00 27.12  ? 1930 PHE A CZ    1 
ATOM   3144  N  N     . ASN A 1 1931 ? 208.953 224.837 242.875 1.00 35.77  ? 1931 ASN A N     1 
ATOM   3145  C  CA    . ASN A 1 1931 ? 210.246 224.517 242.277 1.00 32.77  ? 1931 ASN A CA    1 
ATOM   3146  C  C     . ASN A 1 1931 ? 210.065 224.534 240.767 1.00 37.73  ? 1931 ASN A C     1 
ATOM   3147  O  O     . ASN A 1 1931 ? 209.479 223.617 240.187 1.00 42.49  ? 1931 ASN A O     1 
ATOM   3148  C  CB    . ASN A 1 1931 ? 210.763 223.172 242.769 1.00 38.18  ? 1931 ASN A CB    1 
ATOM   3149  C  CG    . ASN A 1 1931 ? 212.241 222.992 242.504 1.00 41.39  ? 1931 ASN A CG    1 
ATOM   3150  O  OD1   . ASN A 1 1931 ? 213.077 223.560 243.201 1.00 49.12  ? 1931 ASN A OD1   1 
ATOM   3151  N  ND2   . ASN A 1 1931 ? 212.571 222.208 241.489 1.00 42.79  ? 1931 ASN A ND2   1 
ATOM   3152  N  N     . CYS A 1 1932 ? 210.569 225.583 240.130 1.00 38.92  ? 1932 CYS A N     1 
ATOM   3153  C  CA    . CYS A 1 1932 ? 210.323 225.810 238.717 1.00 40.25  ? 1932 CYS A CA    1 
ATOM   3154  C  C     . CYS A 1 1932 ? 211.263 224.981 237.852 1.00 48.28  ? 1932 CYS A C     1 
ATOM   3155  O  O     . CYS A 1 1932 ? 212.424 224.752 238.197 1.00 54.46  ? 1932 CYS A O     1 
ATOM   3156  C  CB    . CYS A 1 1932 ? 210.480 227.293 238.390 1.00 36.26  ? 1932 CYS A CB    1 
ATOM   3157  S  SG    . CYS A 1 1932 ? 209.269 228.352 239.201 1.00 56.70  ? 1932 CYS A SG    1 
ATOM   3158  N  N     . ASP A 1 1933 ? 210.741 224.527 236.716 1.00 47.30  ? 1933 ASP A N     1 
ATOM   3159  C  CA    . ASP A 1 1933 ? 211.532 223.821 235.720 1.00 43.83  ? 1933 ASP A CA    1 
ATOM   3160  C  C     . ASP A 1 1933 ? 210.972 224.158 234.345 1.00 49.06  ? 1933 ASP A C     1 
ATOM   3161  O  O     . ASP A 1 1933 ? 210.021 224.932 234.215 1.00 49.11  ? 1933 ASP A O     1 
ATOM   3162  C  CB    . ASP A 1 1933 ? 211.544 222.312 235.984 1.00 50.59  ? 1933 ASP A CB    1 
ATOM   3163  C  CG    . ASP A 1 1933 ? 210.203 221.662 235.731 1.00 57.96  ? 1933 ASP A CG    1 
ATOM   3164  O  OD1   . ASP A 1 1933 ? 209.315 221.765 236.602 1.00 59.53  ? 1933 ASP A OD1   1 
ATOM   3165  O  OD2   . ASP A 1 1933 ? 210.038 221.038 234.664 1.00 58.24  ? 1933 ASP A OD2   1 
ATOM   3166  N  N     . GLU A 1 1934 ? 211.570 223.565 233.309 1.00 51.35  ? 1934 GLU A N     1 
ATOM   3167  C  CA    . GLU A 1 1934 ? 211.206 223.918 231.941 1.00 50.36  ? 1934 GLU A CA    1 
ATOM   3168  C  C     . GLU A 1 1934 ? 209.773 223.536 231.592 1.00 55.86  ? 1934 GLU A C     1 
ATOM   3169  O  O     . GLU A 1 1934 ? 209.239 224.043 230.600 1.00 60.02  ? 1934 GLU A O     1 
ATOM   3170  C  CB    . GLU A 1 1934 ? 212.172 223.268 230.952 1.00 47.07  ? 1934 GLU A CB    1 
ATOM   3171  C  CG    . GLU A 1 1934 ? 212.055 221.760 230.864 1.00 57.80  ? 1934 GLU A CG    1 
ATOM   3172  C  CD    . GLU A 1 1934 ? 212.998 221.047 231.812 1.00 64.47  ? 1934 GLU A CD    1 
ATOM   3173  O  OE1   . GLU A 1 1934 ? 213.543 221.707 232.722 1.00 61.73  ? 1934 GLU A OE1   1 
ATOM   3174  O  OE2   . GLU A 1 1934 ? 213.196 219.827 231.645 1.00 61.75  ? 1934 GLU A OE2   1 
ATOM   3175  N  N     . THR A 1 1935 ? 209.137 222.664 232.374 1.00 49.52  ? 1935 THR A N     1 
ATOM   3176  C  CA    . THR A 1 1935 ? 207.747 222.310 232.122 1.00 51.17  ? 1935 THR A CA    1 
ATOM   3177  C  C     . THR A 1 1935 ? 206.764 223.315 232.704 1.00 52.45  ? 1935 THR A C     1 
ATOM   3178  O  O     . THR A 1 1935 ? 205.558 223.179 232.476 1.00 49.45  ? 1935 THR A O     1 
ATOM   3179  C  CB    . THR A 1 1935 ? 207.443 220.918 232.677 1.00 51.82  ? 1935 THR A CB    1 
ATOM   3180  O  OG1   . THR A 1 1935 ? 207.600 220.924 234.101 1.00 54.46  ? 1935 THR A OG1   1 
ATOM   3181  C  CG2   . THR A 1 1935 ? 208.385 219.892 232.072 1.00 52.57  ? 1935 THR A CG2   1 
ATOM   3182  N  N     . PHE A 1 1936 ? 207.242 224.311 233.452 1.00 50.68  ? 1936 PHE A N     1 
ATOM   3183  C  CA    . PHE A 1 1936 ? 206.393 225.401 233.931 1.00 47.24  ? 1936 PHE A CA    1 
ATOM   3184  C  C     . PHE A 1 1936 ? 206.187 226.370 232.772 1.00 53.19  ? 1936 PHE A C     1 
ATOM   3185  O  O     . PHE A 1 1936 ? 206.814 227.427 232.675 1.00 55.30  ? 1936 PHE A O     1 
ATOM   3186  C  CB    . PHE A 1 1936 ? 207.019 226.090 235.136 1.00 47.09  ? 1936 PHE A CB    1 
ATOM   3187  C  CG    . PHE A 1 1936 ? 206.741 225.408 236.441 1.00 47.34  ? 1936 PHE A CG    1 
ATOM   3188  C  CD1   . PHE A 1 1936 ? 207.285 224.169 236.721 1.00 47.30  ? 1936 PHE A CD1   1 
ATOM   3189  C  CD2   . PHE A 1 1936 ? 205.940 226.011 237.393 1.00 50.85  ? 1936 PHE A CD2   1 
ATOM   3190  C  CE1   . PHE A 1 1936 ? 207.033 223.542 237.923 1.00 46.03  ? 1936 PHE A CE1   1 
ATOM   3191  C  CE2   . PHE A 1 1936 ? 205.684 225.389 238.597 1.00 49.69  ? 1936 PHE A CE2   1 
ATOM   3192  C  CZ    . PHE A 1 1936 ? 206.230 224.154 238.862 1.00 46.77  ? 1936 PHE A CZ    1 
ATOM   3193  N  N     . ASP A 1 1937 ? 205.290 225.990 231.871 1.00 49.45  ? 1937 ASP A N     1 
ATOM   3194  C  CA    . ASP A 1 1937 ? 205.064 226.754 230.654 1.00 41.25  ? 1937 ASP A CA    1 
ATOM   3195  C  C     . ASP A 1 1937 ? 204.160 227.948 230.953 1.00 50.76  ? 1937 ASP A C     1 
ATOM   3196  O  O     . ASP A 1 1937 ? 203.893 228.291 232.107 1.00 55.37  ? 1937 ASP A O     1 
ATOM   3197  C  CB    . ASP A 1 1937 ? 204.492 225.850 229.565 1.00 42.71  ? 1937 ASP A CB    1 
ATOM   3198  C  CG    . ASP A 1 1937 ? 203.111 225.333 229.902 1.00 53.95  ? 1937 ASP A CG    1 
ATOM   3199  O  OD1   . ASP A 1 1937 ? 202.945 224.740 230.987 1.00 56.03  ? 1937 ASP A OD1   1 
ATOM   3200  O  OD2   . ASP A 1 1937 ? 202.192 225.512 229.078 1.00 54.80  ? 1937 ASP A OD2   1 
ATOM   3201  N  N     . PHE A 1 1938 ? 203.689 228.603 229.891 1.00 53.29  ? 1938 PHE A N     1 
ATOM   3202  C  CA    . PHE A 1 1938 ? 202.843 229.780 230.045 1.00 42.19  ? 1938 PHE A CA    1 
ATOM   3203  C  C     . PHE A 1 1938 ? 201.537 229.436 230.750 1.00 51.21  ? 1938 PHE A C     1 
ATOM   3204  O  O     . PHE A 1 1938 ? 201.081 230.179 231.626 1.00 55.93  ? 1938 PHE A O     1 
ATOM   3205  C  CB    . PHE A 1 1938 ? 202.581 230.390 228.668 1.00 46.04  ? 1938 PHE A CB    1 
ATOM   3206  C  CG    . PHE A 1 1938 ? 201.785 231.661 228.695 1.00 52.40  ? 1938 PHE A CG    1 
ATOM   3207  C  CD1   . PHE A 1 1938 ? 202.349 232.836 229.152 1.00 51.01  ? 1938 PHE A CD1   1 
ATOM   3208  C  CD2   . PHE A 1 1938 ? 200.481 231.685 228.234 1.00 49.38  ? 1938 PHE A CD2   1 
ATOM   3209  C  CE1   . PHE A 1 1938 ? 201.623 234.008 229.163 1.00 49.12  ? 1938 PHE A CE1   1 
ATOM   3210  C  CE2   . PHE A 1 1938 ? 199.750 232.853 228.245 1.00 48.24  ? 1938 PHE A CE2   1 
ATOM   3211  C  CZ    . PHE A 1 1938 ? 200.321 234.016 228.711 1.00 50.99  ? 1938 PHE A CZ    1 
ATOM   3212  N  N     . GLN A 1 1939 ? 200.930 228.302 230.395 1.00 48.01  ? 1939 GLN A N     1 
ATOM   3213  C  CA    . GLN A 1 1939 ? 199.627 227.952 230.953 1.00 41.82  ? 1939 GLN A CA    1 
ATOM   3214  C  C     . GLN A 1 1939 ? 199.725 227.559 232.423 1.00 47.68  ? 1939 GLN A C     1 
ATOM   3215  O  O     . GLN A 1 1939 ? 198.886 227.965 233.235 1.00 51.43  ? 1939 GLN A O     1 
ATOM   3216  C  CB    . GLN A 1 1939 ? 199.000 226.824 230.137 1.00 46.24  ? 1939 GLN A CB    1 
ATOM   3217  C  CG    . GLN A 1 1939 ? 198.854 227.143 228.661 1.00 45.65  ? 1939 GLN A CG    1 
ATOM   3218  C  CD    . GLN A 1 1939 ? 197.614 227.959 228.366 1.00 58.91  ? 1939 GLN A CD    1 
ATOM   3219  O  OE1   . GLN A 1 1939 ? 196.510 227.602 228.775 1.00 60.19  ? 1939 GLN A OE1   1 
ATOM   3220  N  NE2   . GLN A 1 1939 ? 197.789 229.066 227.657 1.00 55.44  ? 1939 GLN A NE2   1 
ATOM   3221  N  N     . ALA A 1 1940 ? 200.732 226.760 232.784 1.00 45.34  ? 1940 ALA A N     1 
ATOM   3222  C  CA    . ALA A 1 1940 ? 200.881 226.352 234.178 1.00 38.30  ? 1940 ALA A CA    1 
ATOM   3223  C  C     . ALA A 1 1940 ? 201.153 227.549 235.077 1.00 46.34  ? 1940 ALA A C     1 
ATOM   3224  O  O     . ALA A 1 1940 ? 200.539 227.691 236.145 1.00 57.61  ? 1940 ALA A O     1 
ATOM   3225  C  CB    . ALA A 1 1940 ? 202.000 225.321 234.305 1.00 39.27  ? 1940 ALA A CB    1 
ATOM   3226  N  N     . MET A 1 1941 ? 202.064 228.427 234.655 1.00 42.80  ? 1941 MET A N     1 
ATOM   3227  C  CA    . MET A 1 1941 ? 202.326 229.642 235.411 1.00 37.35  ? 1941 MET A CA    1 
ATOM   3228  C  C     . MET A 1 1941 ? 201.095 230.534 235.462 1.00 34.90  ? 1941 MET A C     1 
ATOM   3229  O  O     . MET A 1 1941 ? 200.865 231.209 236.469 1.00 43.71  ? 1941 MET A O     1 
ATOM   3230  C  CB    . MET A 1 1941 ? 203.510 230.390 234.802 1.00 38.51  ? 1941 MET A CB    1 
ATOM   3231  C  CG    . MET A 1 1941 ? 204.857 229.947 235.340 1.00 37.87  ? 1941 MET A CG    1 
ATOM   3232  S  SD    . MET A 1 1941 ? 205.017 230.168 237.118 1.00 63.35  ? 1941 MET A SD    1 
ATOM   3233  C  CE    . MET A 1 1941 ? 206.014 231.650 237.186 1.00 44.45  ? 1941 MET A CE    1 
ATOM   3234  N  N     . GLY A 1 1942 ? 200.289 230.541 234.399 1.00 33.11  ? 1942 GLY A N     1 
ATOM   3235  C  CA    . GLY A 1 1942 ? 199.054 231.307 234.425 1.00 39.07  ? 1942 GLY A CA    1 
ATOM   3236  C  C     . GLY A 1 1942 ? 198.065 230.801 235.458 1.00 44.26  ? 1942 GLY A C     1 
ATOM   3237  O  O     . GLY A 1 1942 ? 197.464 231.591 236.190 1.00 51.39  ? 1942 GLY A O     1 
ATOM   3238  N  N     . ARG A 1 1943 ? 197.876 229.480 235.531 1.00 39.14  ? 1943 ARG A N     1 
ATOM   3239  C  CA    . ARG A 1 1943 ? 197.008 228.924 236.569 1.00 39.78  ? 1943 ARG A CA    1 
ATOM   3240  C  C     . ARG A 1 1943 ? 197.544 229.211 237.966 1.00 44.14  ? 1943 ARG A C     1 
ATOM   3241  O  O     . ARG A 1 1943 ? 196.764 229.525 238.878 1.00 49.53  ? 1943 ARG A O     1 
ATOM   3242  C  CB    . ARG A 1 1943 ? 196.829 227.413 236.398 1.00 45.57  ? 1943 ARG A CB    1 
ATOM   3243  C  CG    . ARG A 1 1943 ? 195.733 226.943 235.437 1.00 50.80  ? 1943 ARG A CG    1 
ATOM   3244  C  CD    . ARG A 1 1943 ? 196.019 227.217 233.975 1.00 51.31  ? 1943 ARG A CD    1 
ATOM   3245  N  NE    . ARG A 1 1943 ? 195.010 226.606 233.116 1.00 49.07  ? 1943 ARG A NE    1 
ATOM   3246  C  CZ    . ARG A 1 1943 ? 194.939 226.763 231.801 1.00 53.77  ? 1943 ARG A CZ    1 
ATOM   3247  N  NH1   . ARG A 1 1943 ? 195.816 227.502 231.143 1.00 55.20  ? 1943 ARG A NH1   1 
ATOM   3248  N  NH2   . ARG A 1 1943 ? 193.967 226.156 231.127 1.00 50.46  ? 1943 ARG A NH2   1 
ATOM   3249  N  N     . ILE A 1 1944 ? 198.860 229.099 238.159 1.00 44.92  ? 1944 ILE A N     1 
ATOM   3250  C  CA    . ILE A 1 1944 ? 199.439 229.393 239.467 1.00 39.31  ? 1944 ILE A CA    1 
ATOM   3251  C  C     . ILE A 1 1944 ? 199.199 230.850 239.843 1.00 40.15  ? 1944 ILE A C     1 
ATOM   3252  O  O     . ILE A 1 1944 ? 198.834 231.161 240.986 1.00 46.87  ? 1944 ILE A O     1 
ATOM   3253  C  CB    . ILE A 1 1944 ? 200.938 229.043 239.476 1.00 30.55  ? 1944 ILE A CB    1 
ATOM   3254  C  CG1   . ILE A 1 1944 ? 201.130 227.528 239.489 1.00 30.50  ? 1944 ILE A CG1   1 
ATOM   3255  C  CG2   . ILE A 1 1944 ? 201.626 229.669 240.673 1.00 37.45  ? 1944 ILE A CG2   1 
ATOM   3256  C  CD1   . ILE A 1 1944 ? 202.547 227.100 239.215 1.00 31.39  ? 1944 ILE A CD1   1 
ATOM   3257  N  N     . PHE A 1 1945 ? 199.400 231.766 238.892 1.00 38.47  ? 1945 PHE A N     1 
ATOM   3258  C  CA    . PHE A 1 1945 ? 199.142 233.177 239.150 1.00 33.87  ? 1945 PHE A CA    1 
ATOM   3259  C  C     . PHE A 1 1945 ? 197.675 233.434 239.448 1.00 33.50  ? 1945 PHE A C     1 
ATOM   3260  O  O     . PHE A 1 1945 ? 197.359 234.277 240.288 1.00 34.55  ? 1945 PHE A O     1 
ATOM   3261  C  CB    . PHE A 1 1945 ? 199.589 234.029 237.964 1.00 36.14  ? 1945 PHE A CB    1 
ATOM   3262  C  CG    . PHE A 1 1945 ? 201.076 234.133 237.816 1.00 37.42  ? 1945 PHE A CG    1 
ATOM   3263  C  CD1   . PHE A 1 1945 ? 201.909 233.932 238.900 1.00 38.57  ? 1945 PHE A CD1   1 
ATOM   3264  C  CD2   . PHE A 1 1945 ? 201.640 234.456 236.596 1.00 42.00  ? 1945 PHE A CD2   1 
ATOM   3265  C  CE1   . PHE A 1 1945 ? 203.275 234.034 238.765 1.00 42.48  ? 1945 PHE A CE1   1 
ATOM   3266  C  CE2   . PHE A 1 1945 ? 203.005 234.560 236.458 1.00 41.72  ? 1945 PHE A CE2   1 
ATOM   3267  C  CZ    . PHE A 1 1945 ? 203.823 234.351 237.544 1.00 38.34  ? 1945 PHE A CZ    1 
ATOM   3268  N  N     . VAL A 1 1946 ? 196.766 232.740 238.761 1.00 39.53  ? 1946 VAL A N     1 
ATOM   3269  C  CA    . VAL A 1 1946 ? 195.343 232.902 239.046 1.00 40.12  ? 1946 VAL A CA    1 
ATOM   3270  C  C     . VAL A 1 1946 ? 195.042 232.493 240.481 1.00 34.91  ? 1946 VAL A C     1 
ATOM   3271  O  O     . VAL A 1 1946 ? 194.328 233.196 241.211 1.00 45.95  ? 1946 VAL A O     1 
ATOM   3272  C  CB    . VAL A 1 1946 ? 194.502 232.096 238.038 1.00 39.38  ? 1946 VAL A CB    1 
ATOM   3273  C  CG1   . VAL A 1 1946 ? 193.083 231.919 238.547 1.00 43.10  ? 1946 VAL A CG1   1 
ATOM   3274  C  CG2   . VAL A 1 1946 ? 194.503 232.777 236.684 1.00 37.25  ? 1946 VAL A CG2   1 
ATOM   3275  N  N     . GLY A 1 1947 ? 195.590 231.355 240.909 1.00 37.97  ? 1947 GLY A N     1 
ATOM   3276  C  CA    . GLY A 1 1947 ? 195.389 230.923 242.282 1.00 41.36  ? 1947 GLY A CA    1 
ATOM   3277  C  C     . GLY A 1 1947 ? 195.936 231.911 243.295 1.00 41.99  ? 1947 GLY A C     1 
ATOM   3278  O  O     . GLY A 1 1947 ? 195.267 232.237 244.281 1.00 40.23  ? 1947 GLY A O     1 
ATOM   3279  N  N     . LEU A 1 1948 ? 197.155 232.407 243.065 1.00 47.35  ? 1948 LEU A N     1 
ATOM   3280  C  CA    . LEU A 1 1948 ? 197.744 233.373 243.990 1.00 36.18  ? 1948 LEU A CA    1 
ATOM   3281  C  C     . LEU A 1 1948 ? 196.950 234.674 244.018 1.00 38.53  ? 1948 LEU A C     1 
ATOM   3282  O  O     . LEU A 1 1948 ? 196.751 235.262 245.087 1.00 40.61  ? 1948 LEU A O     1 
ATOM   3283  C  CB    . LEU A 1 1948 ? 199.200 233.647 243.615 1.00 34.01  ? 1948 LEU A CB    1 
ATOM   3284  C  CG    . LEU A 1 1948 ? 200.172 232.469 243.655 1.00 36.01  ? 1948 LEU A CG    1 
ATOM   3285  C  CD1   . LEU A 1 1948 ? 201.554 232.919 243.224 1.00 33.17  ? 1948 LEU A CD1   1 
ATOM   3286  C  CD2   . LEU A 1 1948 ? 200.216 231.845 245.036 1.00 36.95  ? 1948 LEU A CD2   1 
ATOM   3287  N  N     . CYS A 1 1949 ? 196.495 235.143 242.853 1.00 48.72  ? 1949 CYS A N     1 
ATOM   3288  C  CA    . CYS A 1 1949 ? 195.699 236.362 242.789 1.00 33.64  ? 1949 CYS A CA    1 
ATOM   3289  C  C     . CYS A 1 1949 ? 194.407 236.219 243.576 1.00 44.24  ? 1949 CYS A C     1 
ATOM   3290  O  O     . CYS A 1 1949 ? 194.041 237.111 244.348 1.00 51.58  ? 1949 CYS A O     1 
ATOM   3291  C  CB    . CYS A 1 1949 ? 195.378 236.708 241.335 1.00 41.04  ? 1949 CYS A CB    1 
ATOM   3292  S  SG    . CYS A 1 1949 ? 196.731 237.367 240.350 1.00 52.31  ? 1949 CYS A SG    1 
ATOM   3293  N  N     . GLN A 1 1950 ? 193.699 235.104 243.391 1.00 51.37  ? 1950 GLN A N     1 
ATOM   3294  C  CA    . GLN A 1 1950 ? 192.391 234.968 244.021 1.00 43.99  ? 1950 GLN A CA    1 
ATOM   3295  C  C     . GLN A 1 1950 ? 192.512 234.707 245.517 1.00 51.22  ? 1950 GLN A C     1 
ATOM   3296  O  O     . GLN A 1 1950 ? 191.768 235.291 246.313 1.00 54.69  ? 1950 GLN A O     1 
ATOM   3297  C  CB    . GLN A 1 1950 ? 191.598 233.862 243.333 1.00 49.27  ? 1950 GLN A CB    1 
ATOM   3298  C  CG    . GLN A 1 1950 ? 191.204 234.209 241.909 1.00 53.79  ? 1950 GLN A CG    1 
ATOM   3299  C  CD    . GLN A 1 1950 ? 189.824 234.826 241.822 1.00 62.75  ? 1950 GLN A CD    1 
ATOM   3300  O  OE1   . GLN A 1 1950 ? 189.115 234.930 242.822 1.00 66.56  ? 1950 GLN A OE1   1 
ATOM   3301  N  NE2   . GLN A 1 1950 ? 189.433 235.236 240.622 1.00 57.19  ? 1950 GLN A NE2   1 
ATOM   3302  N  N     . VAL A 1 1951 ? 193.438 233.837 245.925 1.00 48.47  ? 1951 VAL A N     1 
ATOM   3303  C  CA    . VAL A 1 1951 ? 193.589 233.551 247.348 1.00 44.45  ? 1951 VAL A CA    1 
ATOM   3304  C  C     . VAL A 1 1951 ? 194.187 234.747 248.077 1.00 43.88  ? 1951 VAL A C     1 
ATOM   3305  O  O     . VAL A 1 1951 ? 193.736 235.116 249.168 1.00 48.98  ? 1951 VAL A O     1 
ATOM   3306  C  CB    . VAL A 1 1951 ? 194.435 232.283 247.556 1.00 47.69  ? 1951 VAL A CB    1 
ATOM   3307  C  CG1   . VAL A 1 1951 ? 194.693 232.055 249.033 1.00 45.69  ? 1951 VAL A CG1   1 
ATOM   3308  C  CG2   . VAL A 1 1951 ? 193.739 231.085 246.951 1.00 48.81  ? 1951 VAL A CG2   1 
ATOM   3309  N  N     . GLY A 1 1952 ? 195.201 235.374 247.490 1.00 43.16  ? 1952 GLY A N     1 
ATOM   3310  C  CA    . GLY A 1 1952 ? 195.915 236.439 248.163 1.00 37.40  ? 1952 GLY A CA    1 
ATOM   3311  C  C     . GLY A 1 1952 ? 197.120 235.907 248.906 1.00 43.44  ? 1952 GLY A C     1 
ATOM   3312  O  O     . GLY A 1 1952 ? 197.325 236.214 250.083 1.00 48.38  ? 1952 GLY A O     1 
ATOM   3313  N  N     . ALA A 1 1953 ? 197.923 235.101 248.223 1.00 34.05  ? 1953 ALA A N     1 
ATOM   3314  C  CA    . ALA A 1 1953 ? 199.061 234.421 248.816 1.00 32.28  ? 1953 ALA A CA    1 
ATOM   3315  C  C     . ALA A 1 1953 ? 200.356 234.878 248.159 1.00 31.88  ? 1953 ALA A C     1 
ATOM   3316  O  O     . ALA A 1 1953 ? 200.360 235.503 247.096 1.00 41.72  ? 1953 ALA A O     1 
ATOM   3317  C  CB    . ALA A 1 1953 ? 198.903 232.903 248.689 1.00 36.87  ? 1953 ALA A CB    1 
ATOM   3318  N  N     . TRP A 1 1954 ? 201.466 234.554 248.812 1.00 29.47  ? 1954 TRP A N     1 
ATOM   3319  C  CA    . TRP A 1 1954 ? 202.797 234.843 248.298 1.00 26.08  ? 1954 TRP A CA    1 
ATOM   3320  C  C     . TRP A 1 1954 ? 203.299 233.644 247.509 1.00 25.20  ? 1954 TRP A C     1 
ATOM   3321  O  O     . TRP A 1 1954 ? 203.131 232.499 247.938 1.00 42.66  ? 1954 TRP A O     1 
ATOM   3322  C  CB    . TRP A 1 1954 ? 203.769 235.162 249.434 1.00 25.05  ? 1954 TRP A CB    1 
ATOM   3323  C  CG    . TRP A 1 1954 ? 203.600 236.524 250.017 1.00 28.34  ? 1954 TRP A CG    1 
ATOM   3324  C  CD1   . TRP A 1 1954 ? 202.480 237.298 249.982 1.00 30.87  ? 1954 TRP A CD1   1 
ATOM   3325  C  CD2   . TRP A 1 1954 ? 204.585 237.274 250.734 1.00 32.31  ? 1954 TRP A CD2   1 
ATOM   3326  N  NE1   . TRP A 1 1954 ? 202.706 238.487 250.628 1.00 31.29  ? 1954 TRP A NE1   1 
ATOM   3327  C  CE2   . TRP A 1 1954 ? 203.992 238.496 251.101 1.00 30.27  ? 1954 TRP A CE2   1 
ATOM   3328  C  CE3   . TRP A 1 1954 ? 205.910 237.032 251.100 1.00 26.24  ? 1954 TRP A CE3   1 
ATOM   3329  C  CZ2   . TRP A 1 1954 ? 204.678 239.471 251.813 1.00 27.92  ? 1954 TRP A CZ2   1 
ATOM   3330  C  CZ3   . TRP A 1 1954 ? 206.590 238.002 251.805 1.00 28.81  ? 1954 TRP A CZ3   1 
ATOM   3331  C  CH2   . TRP A 1 1954 ? 205.973 239.205 252.158 1.00 31.16  ? 1954 TRP A CH2   1 
ATOM   3332  N  N     . GLY A 1 1955 ? 203.909 233.907 246.359 1.00 23.48  ? 1955 GLY A N     1 
ATOM   3333  C  CA    . GLY A 1 1955 ? 204.454 232.841 245.546 1.00 25.50  ? 1955 GLY A CA    1 
ATOM   3334  C  C     . GLY A 1 1955 ? 205.958 232.915 245.416 1.00 32.63  ? 1955 GLY A C     1 
ATOM   3335  O  O     . GLY A 1 1955 ? 206.487 233.831 244.782 1.00 46.64  ? 1955 GLY A O     1 
ATOM   3336  N  N     . CYS A 1 1956 ? 206.661 231.960 246.016 1.00 28.58  ? 1956 CYS A N     1 
ATOM   3337  C  CA    . CYS A 1 1956 ? 208.115 231.885 245.939 1.00 25.63  ? 1956 CYS A CA    1 
ATOM   3338  C  C     . CYS A 1 1956 ? 208.479 230.897 244.839 1.00 26.39  ? 1956 CYS A C     1 
ATOM   3339  O  O     . CYS A 1 1956 ? 208.320 229.685 245.007 1.00 43.50  ? 1956 CYS A O     1 
ATOM   3340  C  CB    . CYS A 1 1956 ? 208.712 231.466 247.280 1.00 32.46  ? 1956 CYS A CB    1 
ATOM   3341  S  SG    . CYS A 1 1956 ? 210.513 231.502 247.331 1.00 54.56  ? 1956 CYS A SG    1 
ATOM   3342  N  N     . PHE A 1 1957 ? 208.965 231.416 243.717 1.00 26.83  ? 1957 PHE A N     1 
ATOM   3343  C  CA    . PHE A 1 1957 ? 209.295 230.604 242.548 1.00 27.44  ? 1957 PHE A CA    1 
ATOM   3344  C  C     . PHE A 1 1957 ? 210.801 230.367 242.545 1.00 29.16  ? 1957 PHE A C     1 
ATOM   3345  O  O     . PHE A 1 1957 ? 211.559 231.074 241.883 1.00 34.57  ? 1957 PHE A O     1 
ATOM   3346  C  CB    . PHE A 1 1957 ? 208.822 231.288 241.272 1.00 24.19  ? 1957 PHE A CB    1 
ATOM   3347  C  CG    . PHE A 1 1957 ? 207.334 231.442 241.190 1.00 36.73  ? 1957 PHE A CG    1 
ATOM   3348  C  CD1   . PHE A 1 1957 ? 206.544 230.409 240.721 1.00 34.84  ? 1957 PHE A CD1   1 
ATOM   3349  C  CD2   . PHE A 1 1957 ? 206.722 232.612 241.598 1.00 33.10  ? 1957 PHE A CD2   1 
ATOM   3350  C  CE1   . PHE A 1 1957 ? 205.176 230.545 240.651 1.00 25.97  ? 1957 PHE A CE1   1 
ATOM   3351  C  CE2   . PHE A 1 1957 ? 205.354 232.752 241.531 1.00 33.88  ? 1957 PHE A CE2   1 
ATOM   3352  C  CZ    . PHE A 1 1957 ? 204.580 231.717 241.056 1.00 28.62  ? 1957 PHE A CZ    1 
ATOM   3353  N  N     . ASP A 1 1958 ? 211.234 229.307 243.192 1.00 25.44  ? 1958 ASP A N     1 
ATOM   3354  C  CA    . ASP A 1 1958 ? 212.661 228.993 243.297 1.00 24.60  ? 1958 ASP A CA    1 
ATOM   3355  C  C     . ASP A 1 1958 ? 213.127 228.338 242.020 1.00 34.69  ? 1958 ASP A C     1 
ATOM   3356  O  O     . ASP A 1 1958 ? 212.323 227.731 241.355 1.00 49.70  ? 1958 ASP A O     1 
ATOM   3357  C  CB    . ASP A 1 1958 ? 212.873 227.991 244.397 1.00 38.63  ? 1958 ASP A CB    1 
ATOM   3358  C  CG    . ASP A 1 1958 ? 212.331 228.401 245.755 1.00 52.33  ? 1958 ASP A CG    1 
ATOM   3359  O  OD1   . ASP A 1 1958 ? 212.597 229.546 246.168 1.00 53.71  ? 1958 ASP A OD1   1 
ATOM   3360  O  OD2   . ASP A 1 1958 ? 211.657 227.568 246.385 1.00 43.37  ? 1958 ASP A OD2   1 
ATOM   3361  N  N     . GLU A 1 1959 ? 214.407 228.452 241.729 1.00 29.43  ? 1959 GLU A N     1 
ATOM   3362  C  CA    . GLU A 1 1959 ? 214.952 227.882 240.492 1.00 37.93  ? 1959 GLU A CA    1 
ATOM   3363  C  C     . GLU A 1 1959 ? 214.027 228.369 239.393 1.00 43.92  ? 1959 GLU A C     1 
ATOM   3364  O  O     . GLU A 1 1959 ? 213.407 227.543 238.766 1.00 44.67  ? 1959 GLU A O     1 
ATOM   3365  C  CB    . GLU A 1 1959 ? 215.028 226.368 240.679 1.00 37.93  ? 1959 GLU A CB    1 
ATOM   3366  C  CG    . GLU A 1 1959 ? 216.376 225.878 241.191 1.00 45.37  ? 1959 GLU A CG    1 
ATOM   3367  C  CD    . GLU A 1 1959 ? 216.624 226.288 242.627 1.00 52.81  ? 1959 GLU A CD    1 
ATOM   3368  O  OE1   . GLU A 1 1959 ? 216.037 225.652 243.527 1.00 56.68  ? 1959 GLU A OE1   1 
ATOM   3369  O  OE2   . GLU A 1 1959 ? 217.395 227.247 242.840 1.00 45.78  ? 1959 GLU A OE2   1 
ATOM   3370  N  N     . PHE A 1 1960 ? 213.944 229.669 239.179 1.00 34.27  ? 1960 PHE A N     1 
ATOM   3371  C  CA    . PHE A 1 1960 ? 213.001 230.242 238.186 1.00 26.35  ? 1960 PHE A CA    1 
ATOM   3372  C  C     . PHE A 1 1960 ? 213.692 230.416 236.886 1.00 35.00  ? 1960 PHE A C     1 
ATOM   3373  O  O     . PHE A 1 1960 ? 213.061 230.327 235.854 1.00 44.96  ? 1960 PHE A O     1 
ATOM   3374  C  CB    . PHE A 1 1960 ? 212.600 231.648 238.591 1.00 30.44  ? 1960 PHE A CB    1 
ATOM   3375  C  CG    . PHE A 1 1960 ? 211.556 232.365 237.750 1.00 37.70  ? 1960 PHE A CG    1 
ATOM   3376  C  CD1   . PHE A 1 1960 ? 210.247 231.910 237.694 1.00 37.03  ? 1960 PHE A CD1   1 
ATOM   3377  C  CD2   . PHE A 1 1960 ? 211.878 233.521 237.054 1.00 37.75  ? 1960 PHE A CD2   1 
ATOM   3378  C  CE1   . PHE A 1 1960 ? 209.302 232.579 236.943 1.00 37.54  ? 1960 PHE A CE1   1 
ATOM   3379  C  CE2   . PHE A 1 1960 ? 210.927 234.183 236.301 1.00 35.13  ? 1960 PHE A CE2   1 
ATOM   3380  C  CZ    . PHE A 1 1960 ? 209.643 233.710 236.246 1.00 37.65  ? 1960 PHE A CZ    1 
ATOM   3381  N  N     . ASN A 1 1961 ? 214.986 230.683 236.921 1.00 35.39  ? 1961 ASN A N     1 
ATOM   3382  C  CA    . ASN A 1 1961 ? 215.711 230.756 235.659 1.00 30.11  ? 1961 ASN A CA    1 
ATOM   3383  C  C     . ASN A 1 1961 ? 215.904 229.376 235.045 1.00 38.90  ? 1961 ASN A C     1 
ATOM   3384  O  O     . ASN A 1 1961 ? 216.596 229.235 234.032 1.00 43.94  ? 1961 ASN A O     1 
ATOM   3385  C  CB    . ASN A 1 1961 ? 217.061 231.451 235.850 1.00 29.32  ? 1961 ASN A CB    1 
ATOM   3386  C  CG    . ASN A 1 1961 ? 217.821 230.933 237.048 1.00 41.19  ? 1961 ASN A CG    1 
ATOM   3387  O  OD1   . ASN A 1 1961 ? 217.349 230.057 237.768 1.00 42.46  ? 1961 ASN A OD1   1 
ATOM   3388  N  ND2   . ASN A 1 1961 ? 219.016 231.467 237.261 1.00 40.15  ? 1961 ASN A ND2   1 
ATOM   3389  N  N     . ARG A 1 1962 ? 215.306 228.349 235.651 1.00 40.42  ? 1962 ARG A N     1 
ATOM   3390  C  CA    . ARG A 1 1962 ? 215.276 227.034 235.027 1.00 36.58  ? 1962 ARG A CA    1 
ATOM   3391  C  C     . ARG A 1 1962 ? 214.209 226.933 233.948 1.00 40.75  ? 1962 ARG A C     1 
ATOM   3392  O  O     . ARG A 1 1962 ? 214.174 225.932 233.226 1.00 48.83  ? 1962 ARG A O     1 
ATOM   3393  C  CB    . ARG A 1 1962 ? 215.058 225.951 236.083 1.00 32.55  ? 1962 ARG A CB    1 
ATOM   3394  C  CG    . ARG A 1 1962 ? 216.301 225.628 236.893 1.00 31.53  ? 1962 ARG A CG    1 
ATOM   3395  C  CD    . ARG A 1 1962 ? 216.109 224.380 237.733 1.00 41.55  ? 1962 ARG A CD    1 
ATOM   3396  N  NE    . ARG A 1 1962 ? 216.105 223.165 236.928 1.00 41.70  ? 1962 ARG A NE    1 
ATOM   3397  C  CZ    . ARG A 1 1962 ? 215.193 222.208 237.027 1.00 44.54  ? 1962 ARG A CZ    1 
ATOM   3398  N  NH1   . ARG A 1 1962 ? 214.193 222.294 237.887 1.00 49.50  ? 1962 ARG A NH1   1 
ATOM   3399  N  NH2   . ARG A 1 1962 ? 215.286 221.139 236.241 1.00 31.40  ? 1962 ARG A NH2   1 
ATOM   3400  N  N     . LEU A 1 1963 ? 213.348 227.938 233.825 1.00 38.12  ? 1963 LEU A N     1 
ATOM   3401  C  CA    . LEU A 1 1963 ? 212.383 227.994 232.741 1.00 36.07  ? 1963 LEU A CA    1 
ATOM   3402  C  C     . LEU A 1 1963 ? 213.092 228.243 231.415 1.00 38.33  ? 1963 LEU A C     1 
ATOM   3403  O  O     . LEU A 1 1963 ? 214.239 228.694 231.365 1.00 44.93  ? 1963 LEU A O     1 
ATOM   3404  C  CB    . LEU A 1 1963 ? 211.362 229.104 232.989 1.00 33.79  ? 1963 LEU A CB    1 
ATOM   3405  C  CG    . LEU A 1 1963 ? 210.017 228.751 233.617 1.00 39.23  ? 1963 LEU A CG    1 
ATOM   3406  C  CD1   . LEU A 1 1963 ? 210.225 228.104 234.962 1.00 41.30  ? 1963 LEU A CD1   1 
ATOM   3407  C  CD2   . LEU A 1 1963 ? 209.156 229.994 233.756 1.00 35.78  ? 1963 LEU A CD2   1 
ATOM   3408  N  N     . GLU A 1 1964 ? 212.395 227.935 230.327 1.00 39.60  ? 1964 GLU A N     1 
ATOM   3409  C  CA    . GLU A 1 1964 ? 212.882 228.313 229.011 1.00 38.04  ? 1964 GLU A CA    1 
ATOM   3410  C  C     . GLU A 1 1964 ? 212.855 229.830 228.867 1.00 45.27  ? 1964 GLU A C     1 
ATOM   3411  O  O     . GLU A 1 1964 ? 212.014 230.515 229.453 1.00 53.17  ? 1964 GLU A O     1 
ATOM   3412  C  CB    . GLU A 1 1964 ? 212.034 227.668 227.917 1.00 43.19  ? 1964 GLU A CB    1 
ATOM   3413  C  CG    . GLU A 1 1964 ? 211.921 226.161 228.021 1.00 49.63  ? 1964 GLU A CG    1 
ATOM   3414  C  CD    . GLU A 1 1964 ? 211.113 225.563 226.888 1.00 57.76  ? 1964 GLU A CD    1 
ATOM   3415  O  OE1   . GLU A 1 1964 ? 210.639 226.332 226.027 1.00 51.15  ? 1964 GLU A OE1   1 
ATOM   3416  O  OE2   . GLU A 1 1964 ? 210.951 224.325 226.858 1.00 54.91  ? 1964 GLU A OE2   1 
ATOM   3417  N  N     . GLU A 1 1965 ? 213.792 230.355 228.076 1.00 38.81  ? 1965 GLU A N     1 
ATOM   3418  C  CA    . GLU A 1 1965 ? 213.872 231.802 227.897 1.00 40.83  ? 1965 GLU A CA    1 
ATOM   3419  C  C     . GLU A 1 1965 ? 212.596 232.351 227.273 1.00 44.92  ? 1965 GLU A C     1 
ATOM   3420  O  O     . GLU A 1 1965 ? 212.096 233.405 227.685 1.00 58.60  ? 1965 GLU A O     1 
ATOM   3421  C  CB    . GLU A 1 1965 ? 215.085 232.159 227.042 1.00 41.97  ? 1965 GLU A CB    1 
ATOM   3422  C  CG    . GLU A 1 1965 ? 215.350 233.648 226.943 1.00 47.53  ? 1965 GLU A CG    1 
ATOM   3423  C  CD    . GLU A 1 1965 ? 216.827 233.972 226.887 1.00 58.60  ? 1965 GLU A CD    1 
ATOM   3424  O  OE1   . GLU A 1 1965 ? 217.641 233.027 226.837 1.00 53.92  ? 1965 GLU A OE1   1 
ATOM   3425  O  OE2   . GLU A 1 1965 ? 217.174 235.171 226.891 1.00 56.75  ? 1965 GLU A OE2   1 
ATOM   3426  N  N     . ARG A 1 1966 ? 212.050 231.645 226.282 1.00 34.76  ? 1966 ARG A N     1 
ATOM   3427  C  CA    . ARG A 1 1966 ? 210.791 232.067 225.680 1.00 38.05  ? 1966 ARG A CA    1 
ATOM   3428  C  C     . ARG A 1 1966 ? 209.655 232.027 226.694 1.00 43.16  ? 1966 ARG A C     1 
ATOM   3429  O  O     . ARG A 1 1966 ? 208.779 232.899 226.690 1.00 48.02  ? 1966 ARG A O     1 
ATOM   3430  C  CB    . ARG A 1 1966 ? 210.473 231.191 224.470 1.00 38.48  ? 1966 ARG A CB    1 
ATOM   3431  C  CG    . ARG A 1 1966 ? 210.586 229.702 224.731 1.00 39.04  ? 1966 ARG A CG    1 
ATOM   3432  C  CD    . ARG A 1 1966 ? 210.590 228.917 223.432 1.00 52.08  ? 1966 ARG A CD    1 
ATOM   3433  N  NE    . ARG A 1 1966 ? 210.023 227.584 223.596 1.00 53.84  ? 1966 ARG A NE    1 
ATOM   3434  C  CZ    . ARG A 1 1966 ? 208.724 227.317 223.591 1.00 48.40  ? 1966 ARG A CZ    1 
ATOM   3435  N  NH1   . ARG A 1 1966 ? 207.823 228.271 223.426 1.00 43.23  ? 1966 ARG A NH1   1 
ATOM   3436  N  NH2   . ARG A 1 1966 ? 208.320 226.061 223.753 1.00 48.02  ? 1966 ARG A NH2   1 
ATOM   3437  N  N     . MET A 1 1967 ? 209.657 231.032 227.581 1.00 43.23  ? 1967 MET A N     1 
ATOM   3438  C  CA    . MET A 1 1967 ? 208.615 230.962 228.598 1.00 36.03  ? 1967 MET A CA    1 
ATOM   3439  C  C     . MET A 1 1967 ? 208.783 232.044 229.655 1.00 37.57  ? 1967 MET A C     1 
ATOM   3440  O  O     . MET A 1 1967 ? 207.786 232.566 230.160 1.00 42.69  ? 1967 MET A O     1 
ATOM   3441  C  CB    . MET A 1 1967 ? 208.595 229.578 229.237 1.00 37.40  ? 1967 MET A CB    1 
ATOM   3442  C  CG    . MET A 1 1967 ? 207.900 228.548 228.374 1.00 46.71  ? 1967 MET A CG    1 
ATOM   3443  S  SD    . MET A 1 1967 ? 206.286 229.135 227.831 1.00 62.97  ? 1967 MET A SD    1 
ATOM   3444  C  CE    . MET A 1 1967 ? 205.936 227.982 226.511 1.00 37.55  ? 1967 MET A CE    1 
ATOM   3445  N  N     . LEU A 1 1968 ? 210.022 232.402 230.000 1.00 35.40  ? 1968 LEU A N     1 
ATOM   3446  C  CA    . LEU A 1 1968 ? 210.233 233.554 230.871 1.00 36.55  ? 1968 LEU A CA    1 
ATOM   3447  C  C     . LEU A 1 1968 ? 209.700 234.824 230.224 1.00 33.91  ? 1968 LEU A C     1 
ATOM   3448  O  O     . LEU A 1 1968 ? 209.034 235.639 230.879 1.00 46.97  ? 1968 LEU A O     1 
ATOM   3449  C  CB    . LEU A 1 1968 ? 211.720 233.707 231.192 1.00 34.55  ? 1968 LEU A CB    1 
ATOM   3450  C  CG    . LEU A 1 1968 ? 212.380 232.597 232.007 1.00 35.07  ? 1968 LEU A CG    1 
ATOM   3451  C  CD1   . LEU A 1 1968 ? 213.891 232.697 231.930 1.00 31.36  ? 1968 LEU A CD1   1 
ATOM   3452  C  CD2   . LEU A 1 1968 ? 211.916 232.653 233.443 1.00 34.12  ? 1968 LEU A CD2   1 
ATOM   3453  N  N     . SER A 1 1969 ? 209.972 234.998 228.929 1.00 33.94  ? 1969 SER A N     1 
ATOM   3454  C  CA    . SER A 1 1969 ? 209.467 236.161 228.209 1.00 27.68  ? 1969 SER A CA    1 
ATOM   3455  C  C     . SER A 1 1969 ? 207.944 236.193 228.214 1.00 33.35  ? 1969 SER A C     1 
ATOM   3456  O  O     . SER A 1 1969 ? 207.339 237.251 228.421 1.00 36.62  ? 1969 SER A O     1 
ATOM   3457  C  CB    . SER A 1 1969 ? 210.002 236.153 226.779 1.00 29.39  ? 1969 SER A CB    1 
ATOM   3458  O  OG    . SER A 1 1969 ? 209.470 237.225 226.024 1.00 49.70  ? 1969 SER A OG    1 
ATOM   3459  N  N     . ALA A 1 1970 ? 207.307 235.043 227.995 1.00 29.28  ? 1970 ALA A N     1 
ATOM   3460  C  CA    . ALA A 1 1970 ? 205.849 234.988 228.001 1.00 20.25  ? 1970 ALA A CA    1 
ATOM   3461  C  C     . ALA A 1 1970 ? 205.281 235.271 229.389 1.00 33.81  ? 1970 ALA A C     1 
ATOM   3462  O  O     . ALA A 1 1970 ? 204.274 235.975 229.520 1.00 38.63  ? 1970 ALA A O     1 
ATOM   3463  C  CB    . ALA A 1 1970 ? 205.377 233.628 227.495 1.00 32.42  ? 1970 ALA A CB    1 
ATOM   3464  N  N     . VAL A 1 1971 ? 205.910 234.728 230.434 1.00 44.84  ? 1971 VAL A N     1 
ATOM   3465  C  CA    . VAL A 1 1971 ? 205.419 234.902 231.798 1.00 32.48  ? 1971 VAL A CA    1 
ATOM   3466  C  C     . VAL A 1 1971 ? 205.580 236.348 232.255 1.00 32.49  ? 1971 VAL A C     1 
ATOM   3467  O  O     . VAL A 1 1971 ? 204.821 236.825 233.115 1.00 37.86  ? 1971 VAL A O     1 
ATOM   3468  C  CB    . VAL A 1 1971 ? 206.143 233.907 232.729 1.00 28.72  ? 1971 VAL A CB    1 
ATOM   3469  C  CG1   . VAL A 1 1971 ? 206.024 234.312 234.189 1.00 38.15  ? 1971 VAL A CG1   1 
ATOM   3470  C  CG2   . VAL A 1 1971 ? 205.596 232.505 232.526 1.00 36.67  ? 1971 VAL A CG2   1 
ATOM   3471  N  N     . SER A 1 1972 ? 206.562 237.064 231.699 1.00 40.21  ? 1972 SER A N     1 
ATOM   3472  C  CA    . SER A 1 1972 ? 206.730 238.472 232.042 1.00 31.85  ? 1972 SER A CA    1 
ATOM   3473  C  C     . SER A 1 1972 ? 205.462 239.273 231.774 1.00 28.79  ? 1972 SER A C     1 
ATOM   3474  O  O     . SER A 1 1972 ? 205.161 240.219 232.508 1.00 41.08  ? 1972 SER A O     1 
ATOM   3475  C  CB    . SER A 1 1972 ? 207.902 239.070 231.266 1.00 27.27  ? 1972 SER A CB    1 
ATOM   3476  O  OG    . SER A 1 1972 ? 207.583 239.224 229.896 1.00 33.12  ? 1972 SER A OG    1 
ATOM   3477  N  N     . GLN A 1 1973 ? 204.701 238.904 230.742 1.00 30.51  ? 1973 GLN A N     1 
ATOM   3478  C  CA    . GLN A 1 1973 ? 203.461 239.614 230.443 1.00 39.73  ? 1973 GLN A CA    1 
ATOM   3479  C  C     . GLN A 1 1973 ? 202.438 239.444 231.561 1.00 41.23  ? 1973 GLN A C     1 
ATOM   3480  O  O     . GLN A 1 1973 ? 201.798 240.418 231.979 1.00 42.08  ? 1973 GLN A O     1 
ATOM   3481  C  CB    . GLN A 1 1973 ? 202.900 239.122 229.110 1.00 35.15  ? 1973 GLN A CB    1 
ATOM   3482  C  CG    . GLN A 1 1973 ? 201.657 239.847 228.641 1.00 42.01  ? 1973 GLN A CG    1 
ATOM   3483  C  CD    . GLN A 1 1973 ? 201.182 239.357 227.289 1.00 55.42  ? 1973 GLN A CD    1 
ATOM   3484  O  OE1   . GLN A 1 1973 ? 201.764 238.441 226.709 1.00 47.30  ? 1973 GLN A OE1   1 
ATOM   3485  N  NE2   . GLN A 1 1973 ? 200.119 239.966 226.779 1.00 53.53  ? 1973 GLN A NE2   1 
ATOM   3486  N  N     . GLN A 1 1974 ? 202.277 238.217 232.064 1.00 39.08  ? 1974 GLN A N     1 
ATOM   3487  C  CA    . GLN A 1 1974 ? 201.358 237.981 233.173 1.00 32.10  ? 1974 GLN A CA    1 
ATOM   3488  C  C     . GLN A 1 1974 ? 201.815 238.699 234.433 1.00 37.98  ? 1974 GLN A C     1 
ATOM   3489  O  O     . GLN A 1 1974 ? 200.996 239.272 235.163 1.00 49.20  ? 1974 GLN A O     1 
ATOM   3490  C  CB    . GLN A 1 1974 ? 201.230 236.483 233.438 1.00 30.70  ? 1974 GLN A CB    1 
ATOM   3491  C  CG    . GLN A 1 1974 ? 200.981 235.655 232.200 1.00 37.21  ? 1974 GLN A CG    1 
ATOM   3492  C  CD    . GLN A 1 1974 ? 201.039 234.170 232.477 1.00 43.75  ? 1974 GLN A CD    1 
ATOM   3493  O  OE1   . GLN A 1 1974 ? 200.076 233.446 232.235 1.00 50.42  ? 1974 GLN A OE1   1 
ATOM   3494  N  NE2   . GLN A 1 1974 ? 202.172 233.707 232.983 1.00 44.25  ? 1974 GLN A NE2   1 
ATOM   3495  N  N     . VAL A 1 1975 ? 203.121 238.670 234.709 1.00 40.54  ? 1975 VAL A N     1 
ATOM   3496  C  CA    . VAL A 1 1975 ? 203.642 239.364 235.885 1.00 31.94  ? 1975 VAL A CA    1 
ATOM   3497  C  C     . VAL A 1 1975 ? 203.366 240.858 235.783 1.00 36.45  ? 1975 VAL A C     1 
ATOM   3498  O  O     . VAL A 1 1975 ? 202.942 241.495 236.756 1.00 38.12  ? 1975 VAL A O     1 
ATOM   3499  C  CB    . VAL A 1 1975 ? 205.144 239.076 236.059 1.00 30.03  ? 1975 VAL A CB    1 
ATOM   3500  C  CG1   . VAL A 1 1975 ? 205.681 239.801 237.276 1.00 38.57  ? 1975 VAL A CG1   1 
ATOM   3501  C  CG2   . VAL A 1 1975 ? 205.385 237.585 236.182 1.00 36.99  ? 1975 VAL A CG2   1 
ATOM   3502  N  N     . GLN A 1 1976 ? 203.598 241.438 234.604 1.00 37.56  ? 1976 GLN A N     1 
ATOM   3503  C  CA    . GLN A 1 1976 ? 203.354 242.861 234.405 1.00 34.16  ? 1976 GLN A CA    1 
ATOM   3504  C  C     . GLN A 1 1976 ? 201.879 243.202 234.566 1.00 41.33  ? 1976 GLN A C     1 
ATOM   3505  O  O     . GLN A 1 1976 ? 201.539 244.231 235.160 1.00 50.54  ? 1976 GLN A O     1 
ATOM   3506  C  CB    . GLN A 1 1976 ? 203.857 243.283 233.027 1.00 34.05  ? 1976 GLN A CB    1 
ATOM   3507  C  CG    . GLN A 1 1976 ? 203.580 244.729 232.676 1.00 43.34  ? 1976 GLN A CG    1 
ATOM   3508  C  CD    . GLN A 1 1976 ? 204.525 245.254 231.621 1.00 50.31  ? 1976 GLN A CD    1 
ATOM   3509  O  OE1   . GLN A 1 1976 ? 205.527 244.618 231.301 1.00 48.01  ? 1976 GLN A OE1   1 
ATOM   3510  N  NE2   . GLN A 1 1976 ? 204.210 246.420 231.073 1.00 49.89  ? 1976 GLN A NE2   1 
ATOM   3511  N  N     . CYS A 1 1977 ? 200.986 242.360 234.039 1.00 44.91  ? 1977 CYS A N     1 
ATOM   3512  C  CA    . CYS A 1 1977 ? 199.556 242.612 234.201 1.00 42.06  ? 1977 CYS A CA    1 
ATOM   3513  C  C     . CYS A 1 1977 ? 199.144 242.563 235.668 1.00 37.68  ? 1977 CYS A C     1 
ATOM   3514  O  O     . CYS A 1 1977 ? 198.383 243.420 236.137 1.00 43.23  ? 1977 CYS A O     1 
ATOM   3515  C  CB    . CYS A 1 1977 ? 198.750 241.605 233.384 1.00 46.36  ? 1977 CYS A CB    1 
ATOM   3516  S  SG    . CYS A 1 1977 ? 197.068 242.140 232.995 1.00 73.48  ? 1977 CYS A SG    1 
ATOM   3517  N  N     . ILE A 1 1978 ? 199.644 241.573 236.411 1.00 45.30  ? 1978 ILE A N     1 
ATOM   3518  C  CA    . ILE A 1 1978 ? 199.313 241.465 237.831 1.00 41.47  ? 1978 ILE A CA    1 
ATOM   3519  C  C     . ILE A 1 1978 ? 199.825 242.682 238.591 1.00 38.72  ? 1978 ILE A C     1 
ATOM   3520  O  O     . ILE A 1 1978 ? 199.133 243.240 239.453 1.00 43.08  ? 1978 ILE A O     1 
ATOM   3521  C  CB    . ILE A 1 1978 ? 199.877 240.158 238.415 1.00 37.96  ? 1978 ILE A CB    1 
ATOM   3522  C  CG1   . ILE A 1 1978 ? 199.119 238.956 237.857 1.00 36.39  ? 1978 ILE A CG1   1 
ATOM   3523  C  CG2   . ILE A 1 1978 ? 199.798 240.171 239.927 1.00 40.61  ? 1978 ILE A CG2   1 
ATOM   3524  C  CD1   . ILE A 1 1978 ? 199.763 237.641 238.190 1.00 40.20  ? 1978 ILE A CD1   1 
ATOM   3525  N  N     . GLN A 1 1979 ? 201.054 243.107 238.291 1.00 38.65  ? 1979 GLN A N     1 
ATOM   3526  C  CA    . GLN A 1 1979 ? 201.628 244.253 238.986 1.00 35.06  ? 1979 GLN A CA    1 
ATOM   3527  C  C     . GLN A 1 1979 ? 200.889 245.541 238.646 1.00 44.95  ? 1979 GLN A C     1 
ATOM   3528  O  O     . GLN A 1 1979 ? 200.730 246.413 239.506 1.00 53.81  ? 1979 GLN A O     1 
ATOM   3529  C  CB    . GLN A 1 1979 ? 203.114 244.372 238.658 1.00 35.28  ? 1979 GLN A CB    1 
ATOM   3530  C  CG    . GLN A 1 1979 ? 203.966 243.328 239.352 1.00 38.40  ? 1979 GLN A CG    1 
ATOM   3531  C  CD    . GLN A 1 1979 ? 205.418 243.401 238.948 1.00 39.85  ? 1979 GLN A CD    1 
ATOM   3532  O  OE1   . GLN A 1 1979 ? 205.829 244.311 238.233 1.00 43.86  ? 1979 GLN A OE1   1 
ATOM   3533  N  NE2   . GLN A 1 1979 ? 206.208 242.439 239.407 1.00 37.84  ? 1979 GLN A NE2   1 
ATOM   3534  N  N     . GLU A 1 1980 ? 200.433 245.685 237.401 1.00 48.36  ? 1980 GLU A N     1 
ATOM   3535  C  CA    . GLU A 1 1980 ? 199.623 246.847 237.048 1.00 40.95  ? 1980 GLU A CA    1 
ATOM   3536  C  C     . GLU A 1 1980 ? 198.291 246.832 237.785 1.00 43.02  ? 1980 GLU A C     1 
ATOM   3537  O  O     . GLU A 1 1980 ? 197.790 247.884 238.202 1.00 49.45  ? 1980 GLU A O     1 
ATOM   3538  C  CB    . GLU A 1 1980 ? 199.408 246.899 235.537 1.00 43.61  ? 1980 GLU A CB    1 
ATOM   3539  C  CG    . GLU A 1 1980 ? 200.526 247.605 234.790 1.00 46.39  ? 1980 GLU A CG    1 
ATOM   3540  C  CD    . GLU A 1 1980 ? 200.478 247.366 233.295 1.00 56.56  ? 1980 GLU A CD    1 
ATOM   3541  O  OE1   . GLU A 1 1980 ? 199.643 246.554 232.844 1.00 54.44  ? 1980 GLU A OE1   1 
ATOM   3542  O  OE2   . GLU A 1 1980 ? 201.280 247.990 232.569 1.00 59.47  ? 1980 GLU A OE2   1 
ATOM   3543  N  N     . ALA A 1 1981 ? 197.694 245.648 237.946 1.00 43.52  ? 1981 ALA A N     1 
ATOM   3544  C  CA    . ALA A 1 1981 ? 196.473 245.548 238.740 1.00 43.42  ? 1981 ALA A CA    1 
ATOM   3545  C  C     . ALA A 1 1981 ? 196.725 245.961 240.184 1.00 51.38  ? 1981 ALA A C     1 
ATOM   3546  O  O     . ALA A 1 1981 ? 195.917 246.676 240.787 1.00 55.13  ? 1981 ALA A O     1 
ATOM   3547  C  CB    . ALA A 1 1981 ? 195.919 244.126 238.676 1.00 49.43  ? 1981 ALA A CB    1 
ATOM   3548  N  N     . LEU A 1 1982 ? 197.851 245.527 240.752 1.00 55.05  ? 1982 LEU A N     1 
ATOM   3549  C  CA    . LEU A 1 1982 ? 198.200 245.926 242.113 1.00 49.11  ? 1982 LEU A CA    1 
ATOM   3550  C  C     . LEU A 1 1982 ? 198.401 247.434 242.215 1.00 52.47  ? 1982 LEU A C     1 
ATOM   3551  O  O     . LEU A 1 1982 ? 197.955 248.066 243.182 1.00 54.42  ? 1982 LEU A O     1 
ATOM   3552  C  CB    . LEU A 1 1982 ? 199.459 245.186 242.561 1.00 49.00  ? 1982 LEU A CB    1 
ATOM   3553  C  CG    . LEU A 1 1982 ? 199.277 243.707 242.903 1.00 48.83  ? 1982 LEU A CG    1 
ATOM   3554  C  CD1   . LEU A 1 1982 ? 200.621 243.018 243.070 1.00 50.15  ? 1982 LEU A CD1   1 
ATOM   3555  C  CD2   . LEU A 1 1982 ? 198.428 243.545 244.149 1.00 47.84  ? 1982 LEU A CD2   1 
ATOM   3556  N  N     . ARG A 1 1983 ? 199.079 248.028 241.230 1.00 49.46  ? 1983 ARG A N     1 
ATOM   3557  C  CA    . ARG A 1 1983 ? 199.313 249.467 241.253 1.00 46.01  ? 1983 ARG A CA    1 
ATOM   3558  C  C     . ARG A 1 1983 ? 198.008 250.245 241.170 1.00 55.33  ? 1983 ARG A C     1 
ATOM   3559  O  O     . ARG A 1 1983 ? 197.810 251.213 241.913 1.00 60.17  ? 1983 ARG A O     1 
ATOM   3560  C  CB    . ARG A 1 1983 ? 200.243 249.874 240.112 1.00 52.50  ? 1983 ARG A CB    1 
ATOM   3561  C  CG    . ARG A 1 1983 ? 201.712 249.873 240.472 1.00 52.87  ? 1983 ARG A CG    1 
ATOM   3562  C  CD    . ARG A 1 1983 ? 202.553 249.461 239.284 1.00 52.76  ? 1983 ARG A CD    1 
ATOM   3563  N  NE    . ARG A 1 1983 ? 203.843 248.926 239.696 1.00 53.00  ? 1983 ARG A NE    1 
ATOM   3564  C  CZ    . ARG A 1 1983 ? 204.663 248.257 238.899 1.00 60.51  ? 1983 ARG A CZ    1 
ATOM   3565  N  NH1   . ARG A 1 1983 ? 204.356 248.020 237.635 1.00 59.39  ? 1983 ARG A NH1   1 
ATOM   3566  N  NH2   . ARG A 1 1983 ? 205.818 247.811 239.383 1.00 58.72  ? 1983 ARG A NH2   1 
ATOM   3567  N  N     . GLU A 1 1984 ? 197.101 249.844 240.273 1.00 71.34  ? 1984 GLU A N     1 
ATOM   3568  C  CA    . GLU A 1 1984 ? 195.817 250.535 240.210 1.00 66.96  ? 1984 GLU A CA    1 
ATOM   3569  C  C     . GLU A 1 1984 ? 194.990 250.298 241.469 1.00 64.23  ? 1984 GLU A C     1 
ATOM   3570  O  O     . GLU A 1 1984 ? 194.188 251.162 241.837 1.00 71.67  ? 1984 GLU A O     1 
ATOM   3571  C  CB    . GLU A 1 1984 ? 195.020 250.136 238.959 1.00 63.74  ? 1984 GLU A CB    1 
ATOM   3572  C  CG    . GLU A 1 1984 ? 194.558 248.691 238.889 1.00 67.59  ? 1984 GLU A CG    1 
ATOM   3573  C  CD    . GLU A 1 1984 ? 193.830 248.362 237.590 1.00 72.28  ? 1984 GLU A CD    1 
ATOM   3574  O  OE1   . GLU A 1 1984 ? 193.706 249.256 236.725 1.00 68.29  ? 1984 GLU A OE1   1 
ATOM   3575  O  OE2   . GLU A 1 1984 ? 193.361 247.213 237.448 1.00 71.89  ? 1984 GLU A OE2   1 
ATOM   3576  N  N     . HIS A 1 1985 ? 195.166 249.154 242.136 1.00 69.78  ? 1985 HIS A N     1 
ATOM   3577  C  CA    . HIS A 1 1985 ? 194.535 248.955 243.438 1.00 74.00  ? 1985 HIS A CA    1 
ATOM   3578  C  C     . HIS A 1 1985 ? 195.071 249.936 244.475 1.00 75.44  ? 1985 HIS A C     1 
ATOM   3579  O  O     . HIS A 1 1985 ? 194.304 250.482 245.277 1.00 72.54  ? 1985 HIS A O     1 
ATOM   3580  C  CB    . HIS A 1 1985 ? 194.744 247.516 243.911 1.00 74.50  ? 1985 HIS A CB    1 
ATOM   3581  C  CG    . HIS A 1 1985 ? 193.952 247.158 245.129 1.00 76.83  ? 1985 HIS A CG    1 
ATOM   3582  N  ND1   . HIS A 1 1985 ? 194.313 247.564 246.396 1.00 80.82  ? 1985 HIS A ND1   1 
ATOM   3583  C  CD2   . HIS A 1 1985 ? 192.822 246.427 245.277 1.00 75.00  ? 1985 HIS A CD2   1 
ATOM   3584  C  CE1   . HIS A 1 1985 ? 193.438 247.102 247.271 1.00 80.04  ? 1985 HIS A CE1   1 
ATOM   3585  N  NE2   . HIS A 1 1985 ? 192.523 246.409 246.618 1.00 78.90  ? 1985 HIS A NE2   1 
ATOM   3586  N  N     . SER A 1 1986 ? 196.383 250.173 244.475 1.00 82.80  ? 1986 SER A N     1 
ATOM   3587  C  CA    . SER A 1 1986 ? 197.015 250.985 245.509 1.00 79.39  ? 1986 SER A CA    1 
ATOM   3588  C  C     . SER A 1 1986 ? 196.627 252.457 245.451 1.00 80.36  ? 1986 SER A C     1 
ATOM   3589  O  O     . SER A 1 1986 ? 196.891 253.181 246.416 1.00 83.36  ? 1986 SER A O     1 
ATOM   3590  C  CB    . SER A 1 1986 ? 198.538 250.866 245.417 1.00 76.73  ? 1986 SER A CB    1 
ATOM   3591  O  OG    . SER A 1 1986 ? 199.028 251.475 244.235 1.00 80.63  ? 1986 SER A OG    1 
ATOM   3592  N  N     . ASN A 1 1987 ? 196.023 252.917 244.360 1.00 86.85  ? 1987 ASN A N     1 
ATOM   3593  C  CA    . ASN A 1 1987 ? 195.698 254.332 244.237 1.00 88.54  ? 1987 ASN A CA    1 
ATOM   3594  C  C     . ASN A 1 1987 ? 194.636 254.729 245.261 1.00 94.73  ? 1987 ASN A C     1 
ATOM   3595  O  O     . ASN A 1 1987 ? 193.702 253.963 245.520 1.00 95.03  ? 1987 ASN A O     1 
ATOM   3596  C  CB    . ASN A 1 1987 ? 195.207 254.650 242.827 1.00 90.22  ? 1987 ASN A CB    1 
ATOM   3597  C  CG    . ASN A 1 1987 ? 196.325 254.636 241.805 1.00 92.07  ? 1987 ASN A CG    1 
ATOM   3598  O  OD1   . ASN A 1 1987 ? 197.423 255.128 242.063 1.00 93.87  ? 1987 ASN A OD1   1 
ATOM   3599  N  ND2   . ASN A 1 1987 ? 196.051 254.071 240.635 1.00 89.80  ? 1987 ASN A ND2   1 
ATOM   3600  N  N     . PRO A 1 1988 ? 194.753 255.916 245.864 1.00 101.68 ? 1988 PRO A N     1 
ATOM   3601  C  CA    . PRO A 1 1988 ? 193.742 256.348 246.843 1.00 100.19 ? 1988 PRO A CA    1 
ATOM   3602  C  C     . PRO A 1 1988 ? 192.367 256.576 246.242 1.00 100.93 ? 1988 PRO A C     1 
ATOM   3603  O  O     . PRO A 1 1988 ? 191.374 256.549 246.980 1.00 98.86  ? 1988 PRO A O     1 
ATOM   3604  C  CB    . PRO A 1 1988 ? 194.330 257.649 247.402 1.00 98.78  ? 1988 PRO A CB    1 
ATOM   3605  C  CG    . PRO A 1 1988 ? 195.204 258.161 246.308 1.00 100.01 ? 1988 PRO A CG    1 
ATOM   3606  C  CD    . PRO A 1 1988 ? 195.783 256.945 245.640 1.00 97.91  ? 1988 PRO A CD    1 
ATOM   3607  N  N     . ASN A 1 1989 ? 192.274 256.809 244.931 1.00 103.32 ? 1989 ASN A N     1 
ATOM   3608  C  CA    . ASN A 1 1989 ? 190.973 257.042 244.313 1.00 102.90 ? 1989 ASN A CA    1 
ATOM   3609  C  C     . ASN A 1 1989 ? 190.102 255.793 244.342 1.00 103.79 ? 1989 ASN A C     1 
ATOM   3610  O  O     . ASN A 1 1989 ? 188.870 255.898 244.355 1.00 101.08 ? 1989 ASN A O     1 
ATOM   3611  C  CB    . ASN A 1 1989 ? 191.153 257.530 242.875 1.00 103.30 ? 1989 ASN A CB    1 
ATOM   3612  C  CG    . ASN A 1 1989 ? 192.225 256.762 242.128 1.00 105.10 ? 1989 ASN A CG    1 
ATOM   3613  O  OD1   . ASN A 1 1989 ? 192.115 255.551 241.931 1.00 102.15 ? 1989 ASN A OD1   1 
ATOM   3614  N  ND2   . ASN A 1 1989 ? 193.270 257.464 241.706 1.00 103.39 ? 1989 ASN A ND2   1 
ATOM   3615  N  N     . TYR A 1 1990 ? 190.715 254.612 244.347 1.00 101.20 ? 1990 TYR A N     1 
ATOM   3616  C  CA    . TYR A 1 1990 ? 189.954 253.372 244.372 1.00 100.93 ? 1990 TYR A CA    1 
ATOM   3617  C  C     . TYR A 1 1990 ? 189.254 253.194 245.714 1.00 100.20 ? 1990 TYR A C     1 
ATOM   3618  O  O     . TYR A 1 1990 ? 189.814 253.495 246.772 1.00 97.02  ? 1990 TYR A O     1 
ATOM   3619  C  CB    . TYR A 1 1990 ? 190.870 252.180 244.096 1.00 99.74  ? 1990 TYR A CB    1 
ATOM   3620  C  CG    . TYR A 1 1990 ? 190.212 250.838 244.328 1.00 99.89  ? 1990 TYR A CG    1 
ATOM   3621  C  CD1   . TYR A 1 1990 ? 189.308 250.320 243.412 1.00 98.53  ? 1990 TYR A CD1   1 
ATOM   3622  C  CD2   . TYR A 1 1990 ? 190.492 250.092 245.465 1.00 98.24  ? 1990 TYR A CD2   1 
ATOM   3623  C  CE1   . TYR A 1 1990 ? 188.701 249.096 243.620 1.00 99.45  ? 1990 TYR A CE1   1 
ATOM   3624  C  CE2   . TYR A 1 1990 ? 189.890 248.867 245.682 1.00 99.15  ? 1990 TYR A CE2   1 
ATOM   3625  C  CZ    . TYR A 1 1990 ? 188.996 248.374 244.756 1.00 99.82  ? 1990 TYR A CZ    1 
ATOM   3626  O  OH    . TYR A 1 1990 ? 188.393 247.155 244.966 1.00 95.75  ? 1990 TYR A OH    1 
ATOM   3627  N  N     . ASP A 1 1991 ? 188.020 252.698 245.664 1.00 103.51 ? 1991 ASP A N     1 
ATOM   3628  C  CA    . ASP A 1 1991 ? 187.252 252.373 246.856 1.00 102.09 ? 1991 ASP A CA    1 
ATOM   3629  C  C     . ASP A 1 1991 ? 186.781 250.929 246.772 1.00 98.96  ? 1991 ASP A C     1 
ATOM   3630  O  O     . ASP A 1 1991 ? 186.460 250.427 245.692 1.00 96.62  ? 1991 ASP A O     1 
ATOM   3631  C  CB    . ASP A 1 1991 ? 186.047 253.310 247.031 1.00 99.19  ? 1991 ASP A CB    1 
ATOM   3632  C  CG    . ASP A 1 1991 ? 185.210 253.425 245.772 1.00 101.61 ? 1991 ASP A CG    1 
ATOM   3633  O  OD1   . ASP A 1 1991 ? 185.729 253.930 244.756 1.00 100.95 ? 1991 ASP A OD1   1 
ATOM   3634  O  OD2   . ASP A 1 1991 ? 184.033 253.006 245.797 1.00 99.35  ? 1991 ASP A OD2   1 
ATOM   3635  N  N     . LYS A 1 1992 ? 186.744 250.264 247.930 1.00 97.92  ? 1992 LYS A N     1 
ATOM   3636  C  CA    . LYS A 1 1992 ? 186.325 248.868 247.973 1.00 99.79  ? 1992 LYS A CA    1 
ATOM   3637  C  C     . LYS A 1 1992 ? 184.873 248.686 247.551 1.00 98.49  ? 1992 LYS A C     1 
ATOM   3638  O  O     . LYS A 1 1992 ? 184.488 247.579 247.157 1.00 94.74  ? 1992 LYS A O     1 
ATOM   3639  C  CB    . LYS A 1 1992 ? 186.537 248.297 249.375 1.00 98.93  ? 1992 LYS A CB    1 
ATOM   3640  C  CG    . LYS A 1 1992 ? 187.998 248.148 249.766 1.00 97.39  ? 1992 LYS A CG    1 
ATOM   3641  C  CD    . LYS A 1 1992 ? 188.150 247.438 251.101 1.00 99.12  ? 1992 LYS A CD    1 
ATOM   3642  C  CE    . LYS A 1 1992 ? 187.402 248.169 252.204 1.00 98.90  ? 1992 LYS A CE    1 
ATOM   3643  N  NZ    . LYS A 1 1992 ? 187.509 247.462 253.510 1.00 95.97  ? 1992 LYS A NZ    1 
ATOM   3644  N  N     . THR A 1 1993 ? 184.060 249.739 247.624 1.00 98.70  ? 1993 THR A N     1 
ATOM   3645  C  CA    . THR A 1 1993 ? 182.680 249.667 247.162 1.00 99.13  ? 1993 THR A CA    1 
ATOM   3646  C  C     . THR A 1 1993 ? 182.559 249.780 245.649 1.00 98.07  ? 1993 THR A C     1 
ATOM   3647  O  O     . THR A 1 1993 ? 181.474 249.530 245.111 1.00 95.41  ? 1993 THR A O     1 
ATOM   3648  C  CB    . THR A 1 1993 ? 181.841 250.766 247.819 1.00 96.95  ? 1993 THR A CB    1 
ATOM   3649  O  OG1   . THR A 1 1993 ? 182.282 252.048 247.356 1.00 92.59  ? 1993 THR A OG1   1 
ATOM   3650  C  CG2   . THR A 1 1993 ? 181.981 250.707 249.333 1.00 94.36  ? 1993 THR A CG2   1 
ATOM   3651  N  N     . SER A 1 1994 ? 183.634 250.145 244.955 1.00 97.99  ? 1994 SER A N     1 
ATOM   3652  C  CA    . SER A 1 1994 ? 183.617 250.258 243.504 1.00 98.00  ? 1994 SER A CA    1 
ATOM   3653  C  C     . SER A 1 1994 ? 183.873 248.884 242.886 1.00 96.77  ? 1994 SER A C     1 
ATOM   3654  O  O     . SER A 1 1994 ? 183.821 247.852 243.560 1.00 93.73  ? 1994 SER A O     1 
ATOM   3655  C  CB    . SER A 1 1994 ? 184.636 251.295 243.040 1.00 95.61  ? 1994 SER A CB    1 
ATOM   3656  O  OG    . SER A 1 1994 ? 185.947 250.938 243.440 1.00 97.53  ? 1994 SER A OG    1 
ATOM   3657  N  N     . ALA A 1 1995 ? 184.146 248.862 241.585 1.00 91.54  ? 1995 ALA A N     1 
ATOM   3658  C  CA    . ALA A 1 1995 ? 184.376 247.604 240.894 1.00 93.21  ? 1995 ALA A CA    1 
ATOM   3659  C  C     . ALA A 1 1995 ? 185.622 246.917 241.449 1.00 92.39  ? 1995 ALA A C     1 
ATOM   3660  O  O     . ALA A 1 1995 ? 186.623 247.583 241.738 1.00 89.18  ? 1995 ALA A O     1 
ATOM   3661  C  CB    . ALA A 1 1995 ? 184.530 247.838 239.390 1.00 88.44  ? 1995 ALA A CB    1 
ATOM   3662  N  N     . PRO A 1 1996 ? 185.596 245.597 241.617 1.00 87.12  ? 1996 PRO A N     1 
ATOM   3663  C  CA    . PRO A 1 1996 ? 186.773 244.900 242.141 1.00 84.49  ? 1996 PRO A CA    1 
ATOM   3664  C  C     . PRO A 1 1996 ? 187.934 244.955 241.163 1.00 83.19  ? 1996 PRO A C     1 
ATOM   3665  O  O     . PRO A 1 1996 ? 187.752 245.017 239.944 1.00 82.11  ? 1996 PRO A O     1 
ATOM   3666  C  CB    . PRO A 1 1996 ? 186.267 243.462 242.338 1.00 82.44  ? 1996 PRO A CB    1 
ATOM   3667  C  CG    . PRO A 1 1996 ? 184.742 243.610 242.290 1.00 83.35  ? 1996 PRO A CG    1 
ATOM   3668  C  CD    . PRO A 1 1996 ? 184.580 244.619 241.212 1.00 83.03  ? 1996 PRO A CD    1 
ATOM   3669  N  N     . ILE A 1 1997 ? 189.141 244.934 241.718 1.00 72.66  ? 1997 ILE A N     1 
ATOM   3670  C  CA    . ILE A 1 1997 ? 190.355 245.130 240.934 1.00 72.72  ? 1997 ILE A CA    1 
ATOM   3671  C  C     . ILE A 1 1997 ? 190.699 243.815 240.244 1.00 69.05  ? 1997 ILE A C     1 
ATOM   3672  O  O     . ILE A 1 1997 ? 190.924 242.796 240.905 1.00 71.17  ? 1997 ILE A O     1 
ATOM   3673  C  CB    . ILE A 1 1997 ? 191.504 245.618 241.828 1.00 74.92  ? 1997 ILE A CB    1 
ATOM   3674  C  CG1   . ILE A 1 1997 ? 191.377 247.125 242.056 1.00 73.88  ? 1997 ILE A CG1   1 
ATOM   3675  C  CG2   . ILE A 1 1997 ? 192.857 245.296 241.213 1.00 70.75  ? 1997 ILE A CG2   1 
ATOM   3676  C  CD1   . ILE A 1 1997 ? 191.715 247.965 240.855 1.00 71.37  ? 1997 ILE A CD1   1 
ATOM   3677  N  N     . THR A 1 1998 ? 190.732 243.832 238.912 1.00 62.81  ? 1998 THR A N     1 
ATOM   3678  C  CA    . THR A 1 1998 ? 190.899 242.624 238.119 1.00 63.96  ? 1998 THR A CA    1 
ATOM   3679  C  C     . THR A 1 1998 ? 191.986 242.828 237.073 1.00 64.86  ? 1998 THR A C     1 
ATOM   3680  O  O     . THR A 1 1998 ? 192.280 243.951 236.657 1.00 64.98  ? 1998 THR A O     1 
ATOM   3681  C  CB    . THR A 1 1998 ? 189.592 242.206 237.419 1.00 67.94  ? 1998 THR A CB    1 
ATOM   3682  O  OG1   . THR A 1 1998 ? 189.147 243.256 236.553 1.00 66.50  ? 1998 THR A OG1   1 
ATOM   3683  C  CG2   . THR A 1 1998 ? 188.507 241.910 238.437 1.00 65.82  ? 1998 THR A CG2   1 
ATOM   3684  N  N     . CYS A 1 1999 ? 192.582 241.714 236.657 1.00 58.90  ? 1999 CYS A N     1 
ATOM   3685  C  CA    . CYS A 1 1999 ? 193.581 241.690 235.602 1.00 56.08  ? 1999 CYS A CA    1 
ATOM   3686  C  C     . CYS A 1 1999 ? 193.278 240.533 234.663 1.00 59.70  ? 1999 CYS A C     1 
ATOM   3687  O  O     . CYS A 1 1999 ? 192.627 239.556 235.039 1.00 62.90  ? 1999 CYS A O     1 
ATOM   3688  C  CB    . CYS A 1 1999 ? 195.000 241.555 236.168 1.00 54.98  ? 1999 CYS A CB    1 
ATOM   3689  S  SG    . CYS A 1 1999 ? 195.463 239.872 236.627 1.00 69.05  ? 1999 CYS A SG    1 
ATOM   3690  N  N     . GLU A 1 2000 ? 193.758 240.653 233.428 1.00 58.28  ? 2000 GLU A N     1 
ATOM   3691  C  CA    . GLU A 1 2000 ? 193.525 239.638 232.403 1.00 53.52  ? 2000 GLU A CA    1 
ATOM   3692  C  C     . GLU A 1 2000 ? 194.600 238.564 232.506 1.00 54.78  ? 2000 GLU A C     1 
ATOM   3693  O  O     . GLU A 1 2000 ? 195.733 238.757 232.061 1.00 60.19  ? 2000 GLU A O     1 
ATOM   3694  C  CB    . GLU A 1 2000 ? 193.517 240.270 231.016 1.00 57.30  ? 2000 GLU A CB    1 
ATOM   3695  C  CG    . GLU A 1 2000 ? 192.982 239.364 229.921 1.00 59.90  ? 2000 GLU A CG    1 
ATOM   3696  C  CD    . GLU A 1 2000 ? 194.076 238.838 229.010 1.00 64.22  ? 2000 GLU A CD    1 
ATOM   3697  O  OE1   . GLU A 1 2000 ? 195.248 239.228 229.193 1.00 66.77  ? 2000 GLU A OE1   1 
ATOM   3698  O  OE2   . GLU A 1 2000 ? 193.766 238.028 228.113 1.00 61.53  ? 2000 GLU A OE2   1 
ATOM   3699  N  N     . LEU A 1 2001 ? 194.245 237.422 233.090 1.00 52.11  ? 2001 LEU A N     1 
ATOM   3700  C  CA    . LEU A 1 2001 ? 195.107 236.247 233.117 1.00 50.47  ? 2001 LEU A CA    1 
ATOM   3701  C  C     . LEU A 1 2001 ? 194.437 235.132 232.331 1.00 51.10  ? 2001 LEU A C     1 
ATOM   3702  O  O     . LEU A 1 2001 ? 193.341 234.688 232.691 1.00 51.49  ? 2001 LEU A O     1 
ATOM   3703  C  CB    . LEU A 1 2001 ? 195.397 235.788 234.548 1.00 53.56  ? 2001 LEU A CB    1 
ATOM   3704  C  CG    . LEU A 1 2001 ? 196.378 236.606 235.387 1.00 49.56  ? 2001 LEU A CG    1 
ATOM   3705  C  CD1   . LEU A 1 2001 ? 196.370 236.118 236.820 1.00 50.05  ? 2001 LEU A CD1   1 
ATOM   3706  C  CD2   . LEU A 1 2001 ? 197.774 236.505 234.805 1.00 49.24  ? 2001 LEU A CD2   1 
ATOM   3707  N  N     . LEU A 1 2002 ? 195.100 234.684 231.265 1.00 50.15  ? 2002 LEU A N     1 
ATOM   3708  C  CA    . LEU A 1 2002 ? 194.651 233.544 230.467 1.00 50.73  ? 2002 LEU A CA    1 
ATOM   3709  C  C     . LEU A 1 2002 ? 193.264 233.795 229.876 1.00 50.83  ? 2002 LEU A C     1 
ATOM   3710  O  O     . LEU A 1 2002 ? 192.353 232.973 229.989 1.00 54.85  ? 2002 LEU A O     1 
ATOM   3711  C  CB    . LEU A 1 2002 ? 194.676 232.261 231.299 1.00 52.73  ? 2002 LEU A CB    1 
ATOM   3712  C  CG    . LEU A 1 2002 ? 196.072 231.832 231.751 1.00 51.63  ? 2002 LEU A CG    1 
ATOM   3713  C  CD1   . LEU A 1 2002 ? 196.025 230.468 232.397 1.00 47.31  ? 2002 LEU A CD1   1 
ATOM   3714  C  CD2   . LEU A 1 2002 ? 197.051 231.850 230.589 1.00 50.99  ? 2002 LEU A CD2   1 
ATOM   3715  N  N     . ASN A 1 2003 ? 193.118 234.960 229.242 1.00 53.52  ? 2003 ASN A N     1 
ATOM   3716  C  CA    . ASN A 1 2003 ? 191.890 235.358 228.551 1.00 54.67  ? 2003 ASN A CA    1 
ATOM   3717  C  C     . ASN A 1 2003 ? 190.690 235.390 229.494 1.00 58.12  ? 2003 ASN A C     1 
ATOM   3718  O  O     . ASN A 1 2003 ? 189.555 235.127 229.092 1.00 62.41  ? 2003 ASN A O     1 
ATOM   3719  C  CB    . ASN A 1 2003 ? 191.612 234.454 227.349 1.00 57.93  ? 2003 ASN A CB    1 
ATOM   3720  C  CG    . ASN A 1 2003 ? 192.304 234.932 226.092 1.00 60.56  ? 2003 ASN A CG    1 
ATOM   3721  O  OD1   . ASN A 1 2003 ? 192.028 236.023 225.595 1.00 62.23  ? 2003 ASN A OD1   1 
ATOM   3722  N  ND2   . ASN A 1 2003 ? 193.207 234.114 225.566 1.00 57.08  ? 2003 ASN A ND2   1 
ATOM   3723  N  N     . LYS A 1 2004 ? 190.937 235.725 230.758 1.00 61.01  ? 2004 LYS A N     1 
ATOM   3724  C  CA    . LYS A 1 2004 ? 189.872 235.840 231.743 1.00 55.87  ? 2004 LYS A CA    1 
ATOM   3725  C  C     . LYS A 1 2004 ? 190.198 236.976 232.697 1.00 60.25  ? 2004 LYS A C     1 
ATOM   3726  O  O     . LYS A 1 2004 ? 191.366 237.307 232.914 1.00 66.39  ? 2004 LYS A O     1 
ATOM   3727  C  CB    . LYS A 1 2004 ? 189.677 234.539 232.530 1.00 54.51  ? 2004 LYS A CB    1 
ATOM   3728  C  CG    . LYS A 1 2004 ? 189.112 233.389 231.717 1.00 63.14  ? 2004 LYS A CG    1 
ATOM   3729  C  CD    . LYS A 1 2004 ? 188.871 232.168 232.582 1.00 68.32  ? 2004 LYS A CD    1 
ATOM   3730  C  CE    . LYS A 1 2004 ? 188.423 230.984 231.745 1.00 66.69  ? 2004 LYS A CE    1 
ATOM   3731  N  NZ    . LYS A 1 2004 ? 187.103 231.230 231.105 1.00 67.10  ? 2004 LYS A NZ    1 
ATOM   3732  N  N     . GLN A 1 2005 ? 189.154 237.566 233.272 1.00 61.33  ? 2005 GLN A N     1 
ATOM   3733  C  CA    . GLN A 1 2005 ? 189.305 238.622 234.266 1.00 59.32  ? 2005 GLN A CA    1 
ATOM   3734  C  C     . GLN A 1 2005 ? 189.401 237.970 235.640 1.00 63.84  ? 2005 GLN A C     1 
ATOM   3735  O  O     . GLN A 1 2005 ? 188.456 237.317 236.094 1.00 65.91  ? 2005 GLN A O     1 
ATOM   3736  C  CB    . GLN A 1 2005 ? 188.138 239.602 234.199 1.00 62.74  ? 2005 GLN A CB    1 
ATOM   3737  C  CG    . GLN A 1 2005 ? 188.023 240.344 232.878 1.00 63.62  ? 2005 GLN A CG    1 
ATOM   3738  C  CD    . GLN A 1 2005 ? 189.267 241.140 232.543 1.00 66.82  ? 2005 GLN A CD    1 
ATOM   3739  O  OE1   . GLN A 1 2005 ? 189.680 242.017 233.300 1.00 70.07  ? 2005 GLN A OE1   1 
ATOM   3740  N  NE2   . GLN A 1 2005 ? 189.870 240.841 231.399 1.00 63.42  ? 2005 GLN A NE2   1 
ATOM   3741  N  N     . VAL A 1 2006 ? 190.539 238.151 236.302 1.00 59.49  ? 2006 VAL A N     1 
ATOM   3742  C  CA    . VAL A 1 2006 ? 190.835 237.501 237.573 1.00 56.72  ? 2006 VAL A CA    1 
ATOM   3743  C  C     . VAL A 1 2006 ? 190.970 238.575 238.641 1.00 54.34  ? 2006 VAL A C     1 
ATOM   3744  O  O     . VAL A 1 2006 ? 191.729 239.535 238.467 1.00 59.28  ? 2006 VAL A O     1 
ATOM   3745  C  CB    . VAL A 1 2006 ? 192.117 236.653 237.485 1.00 50.41  ? 2006 VAL A CB    1 
ATOM   3746  C  CG1   . VAL A 1 2006 ? 192.485 236.096 238.850 1.00 56.38  ? 2006 VAL A CG1   1 
ATOM   3747  C  CG2   . VAL A 1 2006 ? 191.944 235.536 236.476 1.00 53.39  ? 2006 VAL A CG2   1 
ATOM   3748  N  N     . LYS A 1 2007 ? 190.235 238.417 239.738 1.00 50.54  ? 2007 LYS A N     1 
ATOM   3749  C  CA    . LYS A 1 2007 ? 190.351 239.349 240.850 1.00 53.53  ? 2007 LYS A CA    1 
ATOM   3750  C  C     . LYS A 1 2007 ? 191.728 239.226 241.486 1.00 52.32  ? 2007 LYS A C     1 
ATOM   3751  O  O     . LYS A 1 2007 ? 192.183 238.122 241.794 1.00 57.58  ? 2007 LYS A O     1 
ATOM   3752  C  CB    . LYS A 1 2007 ? 189.265 239.080 241.889 1.00 55.20  ? 2007 LYS A CB    1 
ATOM   3753  C  CG    . LYS A 1 2007 ? 187.870 239.487 241.452 1.00 62.86  ? 2007 LYS A CG    1 
ATOM   3754  C  CD    . LYS A 1 2007 ? 186.870 239.316 242.582 1.00 60.77  ? 2007 LYS A CD    1 
ATOM   3755  C  CE    . LYS A 1 2007 ? 185.447 239.538 242.098 1.00 61.26  ? 2007 LYS A CE    1 
ATOM   3756  N  NZ    . LYS A 1 2007 ? 184.459 239.409 243.203 1.00 61.70  ? 2007 LYS A NZ    1 
ATOM   3757  N  N     . VAL A 1 2008 ? 192.388 240.361 241.686 1.00 50.51  ? 2008 VAL A N     1 
ATOM   3758  C  CA    . VAL A 1 2008 ? 193.735 240.404 242.240 1.00 44.87  ? 2008 VAL A CA    1 
ATOM   3759  C  C     . VAL A 1 2008 ? 193.640 240.899 243.674 1.00 47.43  ? 2008 VAL A C     1 
ATOM   3760  O  O     . VAL A 1 2008 ? 193.208 242.031 243.921 1.00 55.32  ? 2008 VAL A O     1 
ATOM   3761  C  CB    . VAL A 1 2008 ? 194.663 241.298 241.407 1.00 38.76  ? 2008 VAL A CB    1 
ATOM   3762  C  CG1   . VAL A 1 2008 ? 196.081 241.224 241.938 1.00 48.05  ? 2008 VAL A CG1   1 
ATOM   3763  C  CG2   . VAL A 1 2008 ? 194.620 240.883 239.953 1.00 43.91  ? 2008 VAL A CG2   1 
ATOM   3764  N  N     . SER A 1 2009 ? 194.034 240.053 244.613 1.00 45.17  ? 2009 SER A N     1 
ATOM   3765  C  CA    . SER A 1 2009 ? 194.071 240.465 246.007 1.00 43.08  ? 2009 SER A CA    1 
ATOM   3766  C  C     . SER A 1 2009 ? 195.293 241.345 246.259 1.00 48.83  ? 2009 SER A C     1 
ATOM   3767  O  O     . SER A 1 2009 ? 196.376 241.066 245.739 1.00 55.18  ? 2009 SER A O     1 
ATOM   3768  C  CB    . SER A 1 2009 ? 194.108 239.249 246.924 1.00 42.44  ? 2009 SER A CB    1 
ATOM   3769  O  OG    . SER A 1 2009 ? 194.172 239.638 248.283 1.00 51.40  ? 2009 SER A OG    1 
ATOM   3770  N  N     . PRO A 1 2010 ? 195.147 242.414 247.043 1.00 46.68  ? 2010 PRO A N     1 
ATOM   3771  C  CA    . PRO A 1 2010 ? 196.309 243.267 247.340 1.00 45.97  ? 2010 PRO A CA    1 
ATOM   3772  C  C     . PRO A 1 2010 ? 197.394 242.558 248.129 1.00 48.88  ? 2010 PRO A C     1 
ATOM   3773  O  O     . PRO A 1 2010 ? 198.537 243.030 248.143 1.00 47.67  ? 2010 PRO A O     1 
ATOM   3774  C  CB    . PRO A 1 2010 ? 195.700 244.426 248.139 1.00 51.58  ? 2010 PRO A CB    1 
ATOM   3775  C  CG    . PRO A 1 2010 ? 194.425 243.885 248.686 1.00 49.81  ? 2010 PRO A CG    1 
ATOM   3776  C  CD    . PRO A 1 2010 ? 193.914 242.920 247.667 1.00 48.09  ? 2010 PRO A CD    1 
ATOM   3777  N  N     . ASP A 1 2011 ? 197.074 241.444 248.787 1.00 43.81  ? 2011 ASP A N     1 
ATOM   3778  C  CA    . ASP A 1 2011 ? 198.046 240.703 249.578 1.00 40.41  ? 2011 ASP A CA    1 
ATOM   3779  C  C     . ASP A 1 2011 ? 198.994 239.865 248.733 1.00 37.80  ? 2011 ASP A C     1 
ATOM   3780  O  O     . ASP A 1 2011 ? 199.960 239.321 249.278 1.00 43.04  ? 2011 ASP A O     1 
ATOM   3781  C  CB    . ASP A 1 2011 ? 197.325 239.795 250.575 1.00 41.18  ? 2011 ASP A CB    1 
ATOM   3782  C  CG    . ASP A 1 2011 ? 196.636 240.572 251.673 1.00 49.60  ? 2011 ASP A CG    1 
ATOM   3783  O  OD1   . ASP A 1 2011 ? 196.383 241.778 251.478 1.00 49.94  ? 2011 ASP A OD1   1 
ATOM   3784  O  OD2   . ASP A 1 2011 ? 196.345 239.976 252.731 1.00 51.82  ? 2011 ASP A OD2   1 
ATOM   3785  N  N     . MET A 1 2012 ? 198.747 239.745 247.432 1.00 38.83  ? 2012 MET A N     1 
ATOM   3786  C  CA    . MET A 1 2012 ? 199.587 238.919 246.580 1.00 39.39  ? 2012 MET A CA    1 
ATOM   3787  C  C     . MET A 1 2012 ? 201.013 239.454 246.512 1.00 49.77  ? 2012 MET A C     1 
ATOM   3788  O  O     . MET A 1 2012 ? 201.252 240.664 246.512 1.00 48.30  ? 2012 MET A O     1 
ATOM   3789  C  CB    . MET A 1 2012 ? 199.016 238.845 245.168 1.00 33.95  ? 2012 MET A CB    1 
ATOM   3790  C  CG    . MET A 1 2012 ? 199.816 237.933 244.264 1.00 40.43  ? 2012 MET A CG    1 
ATOM   3791  S  SD    . MET A 1 2012 ? 199.129 237.754 242.622 1.00 82.84  ? 2012 MET A SD    1 
ATOM   3792  C  CE    . MET A 1 2012 ? 200.375 236.724 241.858 1.00 52.83  ? 2012 MET A CE    1 
ATOM   3793  N  N     . ALA A 1 2013 ? 201.965 238.527 246.453 1.00 33.00  ? 2013 ALA A N     1 
ATOM   3794  C  CA    . ALA A 1 2013 ? 203.355 238.859 246.200 1.00 17.30  ? 2013 ALA A CA    1 
ATOM   3795  C  C     . ALA A 1 2013 ? 203.962 237.771 245.331 1.00 27.03  ? 2013 ALA A C     1 
ATOM   3796  O  O     . ALA A 1 2013 ? 203.548 236.611 245.387 1.00 42.19  ? 2013 ALA A O     1 
ATOM   3797  C  CB    . ALA A 1 2013 ? 204.143 239.007 247.500 1.00 27.63  ? 2013 ALA A CB    1 
ATOM   3798  N  N     . ILE A 1 2014 ? 204.942 238.156 244.520 1.00 25.67  ? 2014 ILE A N     1 
ATOM   3799  C  CA    . ILE A 1 2014 ? 205.688 237.224 243.685 1.00 22.11  ? 2014 ILE A CA    1 
ATOM   3800  C  C     . ILE A 1 2014 ? 207.164 237.371 244.017 1.00 33.40  ? 2014 ILE A C     1 
ATOM   3801  O  O     . ILE A 1 2014 ? 207.705 238.480 243.978 1.00 42.98  ? 2014 ILE A O     1 
ATOM   3802  C  CB    . ILE A 1 2014 ? 205.440 237.469 242.185 1.00 30.06  ? 2014 ILE A CB    1 
ATOM   3803  C  CG1   . ILE A 1 2014 ? 203.954 237.346 241.859 1.00 35.40  ? 2014 ILE A CG1   1 
ATOM   3804  C  CG2   . ILE A 1 2014 ? 206.237 236.490 241.347 1.00 36.88  ? 2014 ILE A CG2   1 
ATOM   3805  C  CD1   . ILE A 1 2014 ? 203.596 237.850 240.482 1.00 34.28  ? 2014 ILE A CD1   1 
ATOM   3806  N  N     . PHE A 1 2015 ? 207.808 236.257 244.345 1.00 23.27  ? 2015 PHE A N     1 
ATOM   3807  C  CA    . PHE A 1 2015 ? 209.231 236.231 244.640 1.00 20.22  ? 2015 PHE A CA    1 
ATOM   3808  C  C     . PHE A 1 2015 ? 209.885 235.136 243.816 1.00 26.57  ? 2015 PHE A C     1 
ATOM   3809  O  O     . PHE A 1 2015 ? 209.327 234.047 243.666 1.00 45.74  ? 2015 PHE A O     1 
ATOM   3810  C  CB    . PHE A 1 2015 ? 209.494 235.991 246.130 1.00 24.63  ? 2015 PHE A CB    1 
ATOM   3811  C  CG    . PHE A 1 2015 ? 209.096 237.139 247.008 1.00 33.50  ? 2015 PHE A CG    1 
ATOM   3812  C  CD1   . PHE A 1 2015 ? 207.802 237.250 247.480 1.00 24.12  ? 2015 PHE A CD1   1 
ATOM   3813  C  CD2   . PHE A 1 2015 ? 210.018 238.105 247.365 1.00 29.15  ? 2015 PHE A CD2   1 
ATOM   3814  C  CE1   . PHE A 1 2015 ? 207.438 238.303 248.286 1.00 24.95  ? 2015 PHE A CE1   1 
ATOM   3815  C  CE2   . PHE A 1 2015 ? 209.655 239.159 248.171 1.00 27.26  ? 2015 PHE A CE2   1 
ATOM   3816  C  CZ    . PHE A 1 2015 ? 208.364 239.258 248.632 1.00 30.29  ? 2015 PHE A CZ    1 
ATOM   3817  N  N     . ILE A 1 2016 ? 211.061 235.433 243.274 1.00 19.87  ? 2016 ILE A N     1 
ATOM   3818  C  CA    . ILE A 1 2016 ? 211.827 234.474 242.491 1.00 20.60  ? 2016 ILE A CA    1 
ATOM   3819  C  C     . ILE A 1 2016 ? 213.245 234.429 243.042 1.00 29.80  ? 2016 ILE A C     1 
ATOM   3820  O  O     . ILE A 1 2016 ? 213.862 235.474 243.271 1.00 47.18  ? 2016 ILE A O     1 
ATOM   3821  C  CB    . ILE A 1 2016 ? 211.821 234.823 240.988 1.00 27.49  ? 2016 ILE A CB    1 
ATOM   3822  C  CG1   . ILE A 1 2016 ? 212.449 236.191 240.730 1.00 28.36  ? 2016 ILE A CG1   1 
ATOM   3823  C  CG2   . ILE A 1 2016 ? 210.403 234.805 240.446 1.00 26.58  ? 2016 ILE A CG2   1 
ATOM   3824  C  CD1   . ILE A 1 2016 ? 212.798 236.437 239.286 1.00 28.46  ? 2016 ILE A CD1   1 
ATOM   3825  N  N     . THR A 1 2017 ? 213.748 233.224 243.290 1.00 25.13  ? 2017 THR A N     1 
ATOM   3826  C  CA    . THR A 1 2017 ? 215.107 233.024 243.772 1.00 26.40  ? 2017 THR A CA    1 
ATOM   3827  C  C     . THR A 1 2017 ? 215.886 232.278 242.702 1.00 36.03  ? 2017 THR A C     1 
ATOM   3828  O  O     . THR A 1 2017 ? 215.380 231.312 242.123 1.00 49.42  ? 2017 THR A O     1 
ATOM   3829  C  CB    . THR A 1 2017 ? 215.133 232.251 245.093 1.00 37.81  ? 2017 THR A CB    1 
ATOM   3830  O  OG1   . THR A 1 2017 ? 214.846 230.870 244.849 1.00 46.41  ? 2017 THR A OG1   1 
ATOM   3831  C  CG2   . THR A 1 2017 ? 214.101 232.811 246.058 1.00 27.69  ? 2017 THR A CG2   1 
ATOM   3832  N  N     . MET A 1 2018 ? 217.010 232.861 242.331 1.00 31.65  ? 2018 MET A N     1 
ATOM   3833  C  CA    . MET A 1 2018 ? 217.762 232.346 241.192 1.00 27.19  ? 2018 MET A CA    1 
ATOM   3834  C  C     . MET A 1 2018 ? 219.214 232.173 241.574 1.00 27.90  ? 2018 MET A C     1 
ATOM   3835  O  O     . MET A 1 2018 ? 219.690 232.916 242.375 1.00 32.55  ? 2018 MET A O     1 
ATOM   3836  C  CB    . MET A 1 2018 ? 217.622 233.328 240.033 1.00 33.44  ? 2018 MET A CB    1 
ATOM   3837  C  CG    . MET A 1 2018 ? 216.306 233.253 239.319 1.00 35.42  ? 2018 MET A CG    1 
ATOM   3838  S  SD    . MET A 1 2018 ? 216.239 234.794 238.398 1.00 44.47  ? 2018 MET A SD    1 
ATOM   3839  C  CE    . MET A 1 2018 ? 216.571 235.855 239.806 1.00 29.40  ? 2018 MET A CE    1 
ATOM   3840  N  N     . ASN A 1 2019 ? 219.855 231.181 240.989 1.00 37.54  ? 2019 ASN A N     1 
ATOM   3841  C  CA    . ASN A 1 2019 ? 221.269 230.837 241.237 1.00 30.94  ? 2019 ASN A CA    1 
ATOM   3842  C  C     . ASN A 1 2019 ? 221.988 231.149 239.922 1.00 38.96  ? 2019 ASN A C     1 
ATOM   3843  O  O     . ASN A 1 2019 ? 222.202 230.234 239.152 1.00 45.16  ? 2019 ASN A O     1 
ATOM   3844  C  CB    . ASN A 1 2019 ? 221.366 229.384 241.682 1.00 25.57  ? 2019 ASN A CB    1 
ATOM   3845  C  CG    . ASN A 1 2019 ? 221.298 229.180 243.164 1.00 27.91  ? 2019 ASN A CG    1 
ATOM   3846  O  OD1   . ASN A 1 2019 ? 222.306 229.350 243.848 1.00 34.89  ? 2019 ASN A OD1   1 
ATOM   3847  N  ND2   . ASN A 1 2019 ? 220.148 228.766 243.664 1.00 38.36  ? 2019 ASN A ND2   1 
ATOM   3848  N  N     . PRO A 1 2020 ? 222.314 232.418 239.613 1.00 40.10  ? 2020 PRO A N     1 
ATOM   3849  C  CA    . PRO A 1 2020 ? 222.928 232.805 238.345 1.00 40.52  ? 2020 PRO A CA    1 
ATOM   3850  C  C     . PRO A 1 2020 ? 224.255 232.197 237.883 1.00 45.46  ? 2020 PRO A C     1 
ATOM   3851  O  O     . PRO A 1 2020 ? 225.099 231.899 238.728 1.00 45.56  ? 2020 PRO A O     1 
ATOM   3852  C  CB    . PRO A 1 2020 ? 223.111 234.265 238.740 1.00 40.01  ? 2020 PRO A CB    1 
ATOM   3853  C  CG    . PRO A 1 2020 ? 223.378 234.250 240.203 1.00 37.41  ? 2020 PRO A CG    1 
ATOM   3854  C  CD    . PRO A 1 2020 ? 222.108 233.531 240.511 1.00 38.42  ? 2020 PRO A CD    1 
ATOM   3855  N  N     . GLY A 1 2021 ? 224.475 232.035 236.582 1.00 33.86  ? 2021 GLY A N     1 
ATOM   3856  C  CA    . GLY A 1 2021 ? 225.692 231.392 236.140 1.00 39.29  ? 2021 GLY A CA    1 
ATOM   3857  C  C     . GLY A 1 2021 ? 225.765 229.899 236.367 1.00 42.01  ? 2021 GLY A C     1 
ATOM   3858  O  O     . GLY A 1 2021 ? 226.762 229.282 235.974 1.00 46.89  ? 2021 GLY A O     1 
ATOM   3859  N  N     . TYR A 1 2022 ? 224.754 229.295 236.983 1.00 37.40  ? 2022 TYR A N     1 
ATOM   3860  C  CA    . TYR A 1 2022 ? 224.779 227.860 237.209 1.00 32.50  ? 2022 TYR A CA    1 
ATOM   3861  C  C     . TYR A 1 2022 ? 224.373 227.112 235.943 1.00 42.46  ? 2022 TYR A C     1 
ATOM   3862  O  O     . TYR A 1 2022 ? 223.722 227.656 235.048 1.00 45.84  ? 2022 TYR A O     1 
ATOM   3863  C  CB    . TYR A 1 2022 ? 223.856 227.474 238.363 1.00 29.98  ? 2022 TYR A CB    1 
ATOM   3864  C  CG    . TYR A 1 2022 ? 224.486 227.612 239.730 1.00 36.07  ? 2022 TYR A CG    1 
ATOM   3865  C  CD1   . TYR A 1 2022 ? 225.537 228.489 239.946 1.00 36.11  ? 2022 TYR A CD1   1 
ATOM   3866  C  CD2   . TYR A 1 2022 ? 224.029 226.863 240.803 1.00 40.04  ? 2022 TYR A CD2   1 
ATOM   3867  C  CE1   . TYR A 1 2022 ? 226.111 228.619 241.191 1.00 36.66  ? 2022 TYR A CE1   1 
ATOM   3868  C  CE2   . TYR A 1 2022 ? 224.597 226.987 242.052 1.00 34.13  ? 2022 TYR A CE2   1 
ATOM   3869  C  CZ    . TYR A 1 2022 ? 225.639 227.866 242.240 1.00 37.41  ? 2022 TYR A CZ    1 
ATOM   3870  O  OH    . TYR A 1 2022 ? 226.211 227.995 243.482 1.00 40.69  ? 2022 TYR A OH    1 
ATOM   3871  N  N     . ALA A 1 2023 ? 224.771 225.845 235.879 1.00 36.16  ? 2023 ALA A N     1 
ATOM   3872  C  CA    . ALA A 1 2023 ? 224.429 225.008 234.740 1.00 30.49  ? 2023 ALA A CA    1 
ATOM   3873  C  C     . ALA A 1 2023 ? 222.943 224.670 234.747 1.00 31.53  ? 2023 ALA A C     1 
ATOM   3874  O  O     . ALA A 1 2023 ? 222.319 224.523 235.800 1.00 41.54  ? 2023 ALA A O     1 
ATOM   3875  C  CB    . ALA A 1 2023 ? 225.256 223.725 234.751 1.00 36.28  ? 2023 ALA A CB    1 
ATOM   3876  N  N     . GLY A 1 2024 ? 222.376 224.547 233.550 1.00 35.02  ? 2024 GLY A N     1 
ATOM   3877  C  CA    . GLY A 1 2024 ? 220.966 224.257 233.413 1.00 44.20  ? 2024 GLY A CA    1 
ATOM   3878  C  C     . GLY A 1 2024 ? 220.045 225.430 233.646 1.00 46.34  ? 2024 GLY A C     1 
ATOM   3879  O  O     . GLY A 1 2024 ? 218.833 225.228 233.781 1.00 46.73  ? 2024 GLY A O     1 
ATOM   3880  N  N     . ARG A 1 2025 ? 220.575 226.646 233.694 1.00 49.75  ? 2025 ARG A N     1 
ATOM   3881  C  CA    . ARG A 1 2025 ? 219.798 227.845 233.962 1.00 39.60  ? 2025 ARG A CA    1 
ATOM   3882  C  C     . ARG A 1 2025 ? 219.767 228.740 232.731 1.00 44.82  ? 2025 ARG A C     1 
ATOM   3883  O  O     . ARG A 1 2025 ? 220.716 228.777 231.944 1.00 48.51  ? 2025 ARG A O     1 
ATOM   3884  C  CB    . ARG A 1 2025 ? 220.377 228.618 235.149 1.00 38.52  ? 2025 ARG A CB    1 
ATOM   3885  C  CG    . ARG A 1 2025 ? 219.778 228.253 236.491 1.00 37.74  ? 2025 ARG A CG    1 
ATOM   3886  C  CD    . ARG A 1 2025 ? 220.294 226.933 237.010 1.00 33.19  ? 2025 ARG A CD    1 
ATOM   3887  N  NE    . ARG A 1 2025 ? 219.921 226.728 238.403 1.00 44.33  ? 2025 ARG A NE    1 
ATOM   3888  C  CZ    . ARG A 1 2025 ? 220.283 225.680 239.127 1.00 44.88  ? 2025 ARG A CZ    1 
ATOM   3889  N  NH1   . ARG A 1 2025 ? 221.027 224.713 238.617 1.00 36.05  ? 2025 ARG A NH1   1 
ATOM   3890  N  NH2   . ARG A 1 2025 ? 219.893 225.602 240.395 1.00 42.10  ? 2025 ARG A NH2   1 
ATOM   3891  N  N     . SER A 1 2026 ? 218.666 229.467 232.577 1.00 47.73  ? 2026 SER A N     1 
ATOM   3892  C  CA    . SER A 1 2026 ? 218.446 230.357 231.448 1.00 42.12  ? 2026 SER A CA    1 
ATOM   3893  C  C     . SER A 1 2026 ? 218.733 231.799 231.854 1.00 39.32  ? 2026 SER A C     1 
ATOM   3894  O  O     . SER A 1 2026 ? 218.966 232.112 233.025 1.00 47.72  ? 2026 SER A O     1 
ATOM   3895  C  CB    . SER A 1 2026 ? 217.018 230.215 230.923 1.00 33.48  ? 2026 SER A CB    1 
ATOM   3896  O  OG    . SER A 1 2026 ? 216.699 228.859 230.673 1.00 38.31  ? 2026 SER A OG    1 
ATOM   3897  N  N     . ASN A 1 2027 ? 218.708 232.685 230.864 1.00 40.48  ? 2027 ASN A N     1 
ATOM   3898  C  CA    . ASN A 1 2027 ? 218.908 234.111 231.075 1.00 46.42  ? 2027 ASN A CA    1 
ATOM   3899  C  C     . ASN A 1 2027 ? 217.563 234.819 231.012 1.00 47.95  ? 2027 ASN A C     1 
ATOM   3900  O  O     . ASN A 1 2027 ? 216.791 234.612 230.071 1.00 54.06  ? 2027 ASN A O     1 
ATOM   3901  C  CB    . ASN A 1 2027 ? 219.860 234.691 230.029 1.00 43.18  ? 2027 ASN A CB    1 
ATOM   3902  C  CG    . ASN A 1 2027 ? 221.314 234.458 230.372 1.00 50.89  ? 2027 ASN A CG    1 
ATOM   3903  O  OD1   . ASN A 1 2027 ? 221.802 234.921 231.402 1.00 51.29  ? 2027 ASN A OD1   1 
ATOM   3904  N  ND2   . ASN A 1 2027 ? 222.017 233.734 229.510 1.00 51.60  ? 2027 ASN A ND2   1 
ATOM   3905  N  N     . LEU A 1 2028 ? 217.287 235.645 232.012 1.00 42.30  ? 2028 LEU A N     1 
ATOM   3906  C  CA    . LEU A 1 2028 ? 216.018 236.349 232.056 1.00 36.64  ? 2028 LEU A CA    1 
ATOM   3907  C  C     . LEU A 1 2028 ? 215.994 237.466 231.016 1.00 41.09  ? 2028 LEU A C     1 
ATOM   3908  O  O     . LEU A 1 2028 ? 216.994 238.165 230.830 1.00 46.43  ? 2028 LEU A O     1 
ATOM   3909  C  CB    . LEU A 1 2028 ? 215.778 236.931 233.447 1.00 36.87  ? 2028 LEU A CB    1 
ATOM   3910  C  CG    . LEU A 1 2028 ? 214.886 236.106 234.370 1.00 35.24  ? 2028 LEU A CG    1 
ATOM   3911  C  CD1   . LEU A 1 2028 ? 215.561 234.798 234.726 1.00 34.28  ? 2028 LEU A CD1   1 
ATOM   3912  C  CD2   . LEU A 1 2028 ? 214.543 236.897 235.618 1.00 36.69  ? 2028 LEU A CD2   1 
ATOM   3913  N  N     . PRO A 1 2029 ? 214.875 237.652 230.318 1.00 40.10  ? 2029 PRO A N     1 
ATOM   3914  C  CA    . PRO A 1 2029 ? 214.748 238.817 229.438 1.00 39.74  ? 2029 PRO A CA    1 
ATOM   3915  C  C     . PRO A 1 2029 ? 214.775 240.105 230.244 1.00 40.37  ? 2029 PRO A C     1 
ATOM   3916  O  O     . PRO A 1 2029 ? 214.376 240.145 231.409 1.00 45.64  ? 2029 PRO A O     1 
ATOM   3917  C  CB    . PRO A 1 2029 ? 213.392 238.605 228.755 1.00 38.98  ? 2029 PRO A CB    1 
ATOM   3918  C  CG    . PRO A 1 2029 ? 212.665 237.646 229.624 1.00 47.54  ? 2029 PRO A CG    1 
ATOM   3919  C  CD    . PRO A 1 2029 ? 213.703 236.768 230.241 1.00 45.55  ? 2029 PRO A CD    1 
ATOM   3920  N  N     . ASP A 1 2030 ? 215.264 241.170 229.607 1.00 44.01  ? 2030 ASP A N     1 
ATOM   3921  C  CA    . ASP A 1 2030 ? 215.454 242.429 230.318 1.00 35.58  ? 2030 ASP A CA    1 
ATOM   3922  C  C     . ASP A 1 2030 ? 214.131 243.082 230.693 1.00 39.48  ? 2030 ASP A C     1 
ATOM   3923  O  O     . ASP A 1 2030 ? 214.081 243.863 231.649 1.00 44.06  ? 2030 ASP A O     1 
ATOM   3924  C  CB    . ASP A 1 2030 ? 216.301 243.380 229.479 1.00 44.68  ? 2030 ASP A CB    1 
ATOM   3925  C  CG    . ASP A 1 2030 ? 217.763 242.998 229.477 1.00 53.99  ? 2030 ASP A CG    1 
ATOM   3926  O  OD1   . ASP A 1 2030 ? 218.372 242.987 230.566 1.00 49.72  ? 2030 ASP A OD1   1 
ATOM   3927  O  OD2   . ASP A 1 2030 ? 218.302 242.702 228.390 1.00 59.30  ? 2030 ASP A OD2   1 
ATOM   3928  N  N     . ASN A 1 2031 ? 213.056 242.793 229.958 1.00 39.51  ? 2031 ASN A N     1 
ATOM   3929  C  CA    . ASN A 1 2031 ? 211.755 243.317 230.357 1.00 37.33  ? 2031 ASN A CA    1 
ATOM   3930  C  C     . ASN A 1 2031 ? 211.221 242.594 231.584 1.00 40.15  ? 2031 ASN A C     1 
ATOM   3931  O  O     . ASN A 1 2031 ? 210.406 243.152 232.326 1.00 48.16  ? 2031 ASN A O     1 
ATOM   3932  C  CB    . ASN A 1 2031 ? 210.756 243.218 229.203 1.00 35.31  ? 2031 ASN A CB    1 
ATOM   3933  C  CG    . ASN A 1 2031 ? 210.537 241.796 228.739 1.00 43.53  ? 2031 ASN A CG    1 
ATOM   3934  O  OD1   . ASN A 1 2031 ? 211.430 241.171 228.171 1.00 44.20  ? 2031 ASN A OD1   1 
ATOM   3935  N  ND2   . ASN A 1 2031 ? 209.340 241.276 228.977 1.00 42.48  ? 2031 ASN A ND2   1 
ATOM   3936  N  N     . LEU A 1 2032 ? 211.659 241.355 231.810 1.00 32.43  ? 2032 LEU A N     1 
ATOM   3937  C  CA    . LEU A 1 2032 ? 211.253 240.623 233.002 1.00 30.90  ? 2032 LEU A CA    1 
ATOM   3938  C  C     . LEU A 1 2032 ? 212.028 241.067 234.235 1.00 31.46  ? 2032 LEU A C     1 
ATOM   3939  O  O     . LEU A 1 2032 ? 211.490 241.032 235.346 1.00 41.07  ? 2032 LEU A O     1 
ATOM   3940  C  CB    . LEU A 1 2032 ? 211.428 239.121 232.779 1.00 35.08  ? 2032 LEU A CB    1 
ATOM   3941  C  CG    . LEU A 1 2032 ? 211.091 238.193 233.945 1.00 34.85  ? 2032 LEU A CG    1 
ATOM   3942  C  CD1   . LEU A 1 2032 ? 209.642 238.353 234.363 1.00 36.44  ? 2032 LEU A CD1   1 
ATOM   3943  C  CD2   . LEU A 1 2032 ? 211.377 236.755 233.572 1.00 33.68  ? 2032 LEU A CD2   1 
ATOM   3944  N  N     . LYS A 1 2033 ? 213.281 241.491 234.062 1.00 34.27  ? 2033 LYS A N     1 
ATOM   3945  C  CA    . LYS A 1 2033 ? 214.101 241.853 235.211 1.00 32.89  ? 2033 LYS A CA    1 
ATOM   3946  C  C     . LYS A 1 2033 ? 213.683 243.186 235.818 1.00 42.51  ? 2033 LYS A C     1 
ATOM   3947  O  O     . LYS A 1 2033 ? 213.932 243.424 237.005 1.00 49.48  ? 2033 LYS A O     1 
ATOM   3948  C  CB    . LYS A 1 2033 ? 215.574 241.887 234.811 1.00 32.48  ? 2033 LYS A CB    1 
ATOM   3949  C  CG    . LYS A 1 2033 ? 216.233 240.522 234.809 1.00 34.49  ? 2033 LYS A CG    1 
ATOM   3950  C  CD    . LYS A 1 2033 ? 217.729 240.627 234.595 1.00 39.97  ? 2033 LYS A CD    1 
ATOM   3951  C  CE    . LYS A 1 2033 ? 218.063 240.782 233.126 1.00 44.24  ? 2033 LYS A CE    1 
ATOM   3952  N  NZ    . LYS A 1 2033 ? 219.515 240.597 232.867 1.00 40.67  ? 2033 LYS A NZ    1 
ATOM   3953  N  N     . LYS A 1 2034 ? 213.058 244.067 235.035 1.00 34.50  ? 2034 LYS A N     1 
ATOM   3954  C  CA    . LYS A 1 2034 ? 212.616 245.342 235.586 1.00 33.02  ? 2034 LYS A CA    1 
ATOM   3955  C  C     . LYS A 1 2034 ? 211.351 245.210 236.421 1.00 44.91  ? 2034 LYS A C     1 
ATOM   3956  O  O     . LYS A 1 2034 ? 210.959 246.182 237.076 1.00 50.53  ? 2034 LYS A O     1 
ATOM   3957  C  CB    . LYS A 1 2034 ? 212.381 246.364 234.475 1.00 34.98  ? 2034 LYS A CB    1 
ATOM   3958  C  CG    . LYS A 1 2034 ? 211.252 246.008 233.532 1.00 37.62  ? 2034 LYS A CG    1 
ATOM   3959  C  CD    . LYS A 1 2034 ? 211.064 247.081 232.476 1.00 44.38  ? 2034 LYS A CD    1 
ATOM   3960  C  CE    . LYS A 1 2034 ? 212.178 247.053 231.451 1.00 49.17  ? 2034 LYS A CE    1 
ATOM   3961  N  NZ    . LYS A 1 2034 ? 211.928 248.014 230.342 1.00 46.60  ? 2034 LYS A NZ    1 
ATOM   3962  N  N     . LEU A 1 2035 ? 210.706 244.048 236.409 1.00 34.44  ? 2035 LEU A N     1 
ATOM   3963  C  CA    . LEU A 1 2035 ? 209.524 243.796 237.219 1.00 24.42  ? 2035 LEU A CA    1 
ATOM   3964  C  C     . LEU A 1 2035 ? 209.866 243.280 238.608 1.00 28.21  ? 2035 LEU A C     1 
ATOM   3965  O  O     . LEU A 1 2035 ? 208.956 243.041 239.406 1.00 32.95  ? 2035 LEU A O     1 
ATOM   3966  C  CB    . LEU A 1 2035 ? 208.608 242.793 236.512 1.00 32.20  ? 2035 LEU A CB    1 
ATOM   3967  C  CG    . LEU A 1 2035 ? 208.135 243.138 235.101 1.00 28.91  ? 2035 LEU A CG    1 
ATOM   3968  C  CD1   . LEU A 1 2035 ? 207.407 241.958 234.492 1.00 28.59  ? 2035 LEU A CD1   1 
ATOM   3969  C  CD2   . LEU A 1 2035 ? 207.242 244.363 235.118 1.00 31.33  ? 2035 LEU A CD2   1 
ATOM   3970  N  N     . PHE A 1 2036 ? 211.149 243.101 238.912 1.00 34.00  ? 2036 PHE A N     1 
ATOM   3971  C  CA    . PHE A 1 2036 ? 211.594 242.568 240.189 1.00 28.17  ? 2036 PHE A CA    1 
ATOM   3972  C  C     . PHE A 1 2036 ? 212.699 243.444 240.758 1.00 29.61  ? 2036 PHE A C     1 
ATOM   3973  O  O     . PHE A 1 2036 ? 213.500 244.020 240.017 1.00 34.18  ? 2036 PHE A O     1 
ATOM   3974  C  CB    . PHE A 1 2036 ? 212.104 241.127 240.045 1.00 25.64  ? 2036 PHE A CB    1 
ATOM   3975  C  CG    . PHE A 1 2036 ? 211.036 240.138 239.682 1.00 29.90  ? 2036 PHE A CG    1 
ATOM   3976  C  CD1   . PHE A 1 2036 ? 210.720 239.895 238.358 1.00 27.45  ? 2036 PHE A CD1   1 
ATOM   3977  C  CD2   . PHE A 1 2036 ? 210.351 239.450 240.664 1.00 32.22  ? 2036 PHE A CD2   1 
ATOM   3978  C  CE1   . PHE A 1 2036 ? 209.740 238.988 238.024 1.00 20.40  ? 2036 PHE A CE1   1 
ATOM   3979  C  CE2   . PHE A 1 2036 ? 209.371 238.541 240.334 1.00 34.96  ? 2036 PHE A CE2   1 
ATOM   3980  C  CZ    . PHE A 1 2036 ? 209.065 238.311 239.012 1.00 24.36  ? 2036 PHE A CZ    1 
ATOM   3981  N  N     . ARG A 1 2037 ? 212.736 243.541 242.085 1.00 23.88  ? 2037 ARG A N     1 
ATOM   3982  C  CA    . ARG A 1 2037 ? 213.826 244.198 242.798 1.00 21.29  ? 2037 ARG A CA    1 
ATOM   3983  C  C     . ARG A 1 2037 ? 214.800 243.123 243.260 1.00 32.41  ? 2037 ARG A C     1 
ATOM   3984  O  O     . ARG A 1 2037 ? 214.506 242.369 244.192 1.00 41.79  ? 2037 ARG A O     1 
ATOM   3985  C  CB    . ARG A 1 2037 ? 213.309 245.013 243.980 1.00 25.65  ? 2037 ARG A CB    1 
ATOM   3986  C  CG    . ARG A 1 2037 ? 212.856 246.413 243.617 1.00 36.39  ? 2037 ARG A CG    1 
ATOM   3987  C  CD    . ARG A 1 2037 ? 214.004 247.404 243.635 1.00 32.97  ? 2037 ARG A CD    1 
ATOM   3988  N  NE    . ARG A 1 2037 ? 214.319 247.842 244.988 1.00 40.46  ? 2037 ARG A NE    1 
ATOM   3989  C  CZ    . ARG A 1 2037 ? 213.724 248.856 245.601 1.00 46.21  ? 2037 ARG A CZ    1 
ATOM   3990  N  NH1   . ARG A 1 2037 ? 212.760 249.547 245.017 1.00 37.55  ? 2037 ARG A NH1   1 
ATOM   3991  N  NH2   . ARG A 1 2037 ? 214.105 249.184 246.832 1.00 44.40  ? 2037 ARG A NH2   1 
ATOM   3992  N  N     . SER A 1 2038 ? 215.956 243.057 242.612 1.00 27.27  ? 2038 SER A N     1 
ATOM   3993  C  CA    . SER A 1 2038 ? 216.934 242.030 242.920 1.00 25.67  ? 2038 SER A CA    1 
ATOM   3994  C  C     . SER A 1 2038 ? 217.676 242.356 244.211 1.00 25.38  ? 2038 SER A C     1 
ATOM   3995  O  O     . SER A 1 2038 ? 217.698 243.497 244.679 1.00 42.66  ? 2038 SER A O     1 
ATOM   3996  C  CB    . SER A 1 2038 ? 217.930 241.877 241.773 1.00 33.78  ? 2038 SER A CB    1 
ATOM   3997  O  OG    . SER A 1 2038 ? 218.706 243.050 241.618 1.00 37.37  ? 2038 SER A OG    1 
ATOM   3998  N  N     . LEU A 1 2039 ? 218.284 241.325 244.790 1.00 18.87  ? 2039 LEU A N     1 
ATOM   3999  C  CA    . LEU A 1 2039 ? 219.125 241.483 245.970 1.00 22.01  ? 2039 LEU A CA    1 
ATOM   4000  C  C     . LEU A 1 2039 ? 220.151 240.366 245.985 1.00 24.98  ? 2039 LEU A C     1 
ATOM   4001  O  O     . LEU A 1 2039 ? 219.784 239.189 245.957 1.00 36.06  ? 2039 LEU A O     1 
ATOM   4002  C  CB    . LEU A 1 2039 ? 218.305 241.454 247.254 1.00 28.29  ? 2039 LEU A CB    1 
ATOM   4003  C  CG    . LEU A 1 2039 ? 219.194 241.576 248.490 1.00 35.85  ? 2039 LEU A CG    1 
ATOM   4004  C  CD1   . LEU A 1 2039 ? 219.821 242.959 248.593 1.00 35.69  ? 2039 LEU A CD1   1 
ATOM   4005  C  CD2   . LEU A 1 2039 ? 218.430 241.231 249.730 1.00 28.85  ? 2039 LEU A CD2   1 
ATOM   4006  N  N     . ALA A 1 2040 ? 221.426 240.730 246.042 1.00 19.72  ? 2040 ALA A N     1 
ATOM   4007  C  CA    . ALA A 1 2040 ? 222.496 239.744 246.079 1.00 21.48  ? 2040 ALA A CA    1 
ATOM   4008  C  C     . ALA A 1 2040 ? 222.646 239.208 247.495 1.00 39.67  ? 2040 ALA A C     1 
ATOM   4009  O  O     . ALA A 1 2040 ? 223.013 239.950 248.411 1.00 49.04  ? 2040 ALA A O     1 
ATOM   4010  C  CB    . ALA A 1 2040 ? 223.803 240.360 245.594 1.00 33.40  ? 2040 ALA A CB    1 
ATOM   4011  N  N     . MET A 1 2041 ? 222.363 237.923 247.673 1.00 40.01  ? 2041 MET A N     1 
ATOM   4012  C  CA    . MET A 1 2041 ? 222.545 237.234 248.946 1.00 33.71  ? 2041 MET A CA    1 
ATOM   4013  C  C     . MET A 1 2041 ? 223.650 236.205 248.730 1.00 35.42  ? 2041 MET A C     1 
ATOM   4014  O  O     . MET A 1 2041 ? 223.388 235.060 248.364 1.00 47.68  ? 2041 MET A O     1 
ATOM   4015  C  CB    . MET A 1 2041 ? 221.252 236.585 249.415 1.00 30.42  ? 2041 MET A CB    1 
ATOM   4016  C  CG    . MET A 1 2041 ? 220.166 237.575 249.774 1.00 33.29  ? 2041 MET A CG    1 
ATOM   4017  S  SD    . MET A 1 2041 ? 218.632 236.770 250.245 1.00 46.38  ? 2041 MET A SD    1 
ATOM   4018  C  CE    . MET A 1 2041 ? 219.109 236.080 251.822 1.00 31.72  ? 2041 MET A CE    1 
ATOM   4019  N  N     . THR A 1 2042 ? 224.892 236.626 248.953 1.00 34.55  ? 2042 THR A N     1 
ATOM   4020  C  CA    . THR A 1 2042 ? 226.063 235.817 248.638 1.00 37.82  ? 2042 THR A CA    1 
ATOM   4021  C  C     . THR A 1 2042 ? 226.838 235.354 249.860 1.00 38.38  ? 2042 THR A C     1 
ATOM   4022  O  O     . THR A 1 2042 ? 227.398 234.257 249.845 1.00 44.24  ? 2042 THR A O     1 
ATOM   4023  C  CB    . THR A 1 2042 ? 227.007 236.598 247.718 1.00 38.27  ? 2042 THR A CB    1 
ATOM   4024  O  OG1   . THR A 1 2042 ? 227.248 237.895 248.274 1.00 48.75  ? 2042 THR A OG1   1 
ATOM   4025  C  CG2   . THR A 1 2042 ? 226.390 236.761 246.343 1.00 37.71  ? 2042 THR A CG2   1 
ATOM   4026  N  N     . LYS A 1 2043 ? 226.885 236.156 250.924 1.00 40.55  ? 2043 LYS A N     1 
ATOM   4027  C  CA    . LYS A 1 2043 ? 227.688 235.858 252.110 1.00 33.47  ? 2043 LYS A CA    1 
ATOM   4028  C  C     . LYS A 1 2043 ? 226.801 235.896 253.346 1.00 40.01  ? 2043 LYS A C     1 
ATOM   4029  O  O     . LYS A 1 2043 ? 226.701 236.935 254.017 1.00 46.93  ? 2043 LYS A O     1 
ATOM   4030  C  CB    . LYS A 1 2043 ? 228.848 236.840 252.247 1.00 41.27  ? 2043 LYS A CB    1 
ATOM   4031  C  CG    . LYS A 1 2043 ? 229.826 236.801 251.091 1.00 49.21  ? 2043 LYS A CG    1 
ATOM   4032  C  CD    . LYS A 1 2043 ? 230.574 235.483 251.058 1.00 47.68  ? 2043 LYS A CD    1 
ATOM   4033  C  CE    . LYS A 1 2043 ? 231.609 235.464 249.952 1.00 46.36  ? 2043 LYS A CE    1 
ATOM   4034  N  NZ    . LYS A 1 2043 ? 232.312 234.155 249.891 1.00 51.26  ? 2043 LYS A NZ    1 
ATOM   4035  N  N     . PRO A 1 2044 ? 226.134 234.792 253.681 1.00 39.34  ? 2044 PRO A N     1 
ATOM   4036  C  CA    . PRO A 1 2044 ? 225.353 234.757 254.921 1.00 36.35  ? 2044 PRO A CA    1 
ATOM   4037  C  C     . PRO A 1 2044 ? 226.249 234.925 256.137 1.00 40.92  ? 2044 PRO A C     1 
ATOM   4038  O  O     . PRO A 1 2044 ? 227.410 234.512 256.144 1.00 51.31  ? 2044 PRO A O     1 
ATOM   4039  C  CB    . PRO A 1 2044 ? 224.700 233.371 254.889 1.00 33.30  ? 2044 PRO A CB    1 
ATOM   4040  C  CG    . PRO A 1 2044 ? 225.572 232.566 253.989 1.00 36.56  ? 2044 PRO A CG    1 
ATOM   4041  C  CD    . PRO A 1 2044 ? 226.053 233.521 252.945 1.00 39.35  ? 2044 PRO A CD    1 
ATOM   4042  N  N     . ASP A 1 2045 ? 225.694 235.547 257.176 1.00 36.04  ? 2045 ASP A N     1 
ATOM   4043  C  CA    . ASP A 1 2045 ? 226.436 235.815 258.407 1.00 36.72  ? 2045 ASP A CA    1 
ATOM   4044  C  C     . ASP A 1 2045 ? 226.442 234.541 259.243 1.00 40.89  ? 2045 ASP A C     1 
ATOM   4045  O  O     . ASP A 1 2045 ? 225.695 234.383 260.211 1.00 47.64  ? 2045 ASP A O     1 
ATOM   4046  C  CB    . ASP A 1 2045 ? 225.821 236.989 259.153 1.00 36.24  ? 2045 ASP A CB    1 
ATOM   4047  C  CG    . ASP A 1 2045 ? 225.596 238.188 258.256 1.00 51.78  ? 2045 ASP A CG    1 
ATOM   4048  O  OD1   . ASP A 1 2045 ? 226.581 238.695 257.681 1.00 52.59  ? 2045 ASP A OD1   1 
ATOM   4049  O  OD2   . ASP A 1 2045 ? 224.434 238.613 258.111 1.00 55.06  ? 2045 ASP A OD2   1 
ATOM   4050  N  N     . ARG A 1 2046 ? 227.324 233.618 258.856 1.00 42.28  ? 2046 ARG A N     1 
ATOM   4051  C  CA    . ARG A 1 2046 ? 227.305 232.276 259.428 1.00 38.44  ? 2046 ARG A CA    1 
ATOM   4052  C  C     . ARG A 1 2046 ? 227.705 232.265 260.896 1.00 44.83  ? 2046 ARG A C     1 
ATOM   4053  O  O     . ARG A 1 2046 ? 227.223 231.418 261.655 1.00 46.15  ? 2046 ARG A O     1 
ATOM   4054  C  CB    . ARG A 1 2046 ? 228.219 231.355 258.622 1.00 33.96  ? 2046 ARG A CB    1 
ATOM   4055  C  CG    . ARG A 1 2046 ? 227.806 231.198 257.172 1.00 37.28  ? 2046 ARG A CG    1 
ATOM   4056  C  CD    . ARG A 1 2046 ? 228.447 229.977 256.548 1.00 43.85  ? 2046 ARG A CD    1 
ATOM   4057  N  NE    . ARG A 1 2046 ? 229.892 230.120 256.430 1.00 47.42  ? 2046 ARG A NE    1 
ATOM   4058  C  CZ    . ARG A 1 2046 ? 230.712 229.153 256.043 1.00 48.25  ? 2046 ARG A CZ    1 
ATOM   4059  N  NH1   . ARG A 1 2046 ? 230.264 227.944 255.751 1.00 41.78  ? 2046 ARG A NH1   1 
ATOM   4060  N  NH2   . ARG A 1 2046 ? 232.014 229.405 255.949 1.00 46.86  ? 2046 ARG A NH2   1 
ATOM   4061  N  N     . GLN A 1 2047 ? 228.584 233.177 261.317 1.00 46.92  ? 2047 GLN A N     1 
ATOM   4062  C  CA    . GLN A 1 2047 ? 229.008 233.189 262.713 1.00 36.62  ? 2047 GLN A CA    1 
ATOM   4063  C  C     . GLN A 1 2047 ? 227.848 233.519 263.644 1.00 35.40  ? 2047 GLN A C     1 
ATOM   4064  O  O     . GLN A 1 2047 ? 227.675 232.859 264.675 1.00 52.42  ? 2047 GLN A O     1 
ATOM   4065  C  CB    . GLN A 1 2047 ? 230.160 234.176 262.900 1.00 41.08  ? 2047 GLN A CB    1 
ATOM   4066  C  CG    . GLN A 1 2047 ? 230.826 234.140 264.270 1.00 41.46  ? 2047 GLN A CG    1 
ATOM   4067  C  CD    . GLN A 1 2047 ? 230.128 235.007 265.296 1.00 49.96  ? 2047 GLN A CD    1 
ATOM   4068  O  OE1   . GLN A 1 2047 ? 229.518 236.019 264.957 1.00 56.64  ? 2047 GLN A OE1   1 
ATOM   4069  N  NE2   . GLN A 1 2047 ? 230.220 234.617 266.562 1.00 45.89  ? 2047 GLN A NE2   1 
ATOM   4070  N  N     . LEU A 1 2048 ? 226.952 234.416 263.263 1.00 30.54  ? 2048 LEU A N     1 
ATOM   4071  C  CA    . LEU A 1 2048 ? 225.745 234.708 264.075 1.00 38.70  ? 2048 LEU A CA    1 
ATOM   4072  C  C     . LEU A 1 2048 ? 224.773 233.530 264.059 1.00 37.18  ? 2048 LEU A C     1 
ATOM   4073  O  O     . LEU A 1 2048 ? 224.294 233.202 265.126 1.00 46.93  ? 2048 LEU A O     1 
ATOM   4074  C  CB    . LEU A 1 2048 ? 225.033 235.985 263.657 1.00 39.74  ? 2048 LEU A CB    1 
ATOM   4075  C  CG    . LEU A 1 2048 ? 223.873 236.452 264.535 1.00 37.29  ? 2048 LEU A CG    1 
ATOM   4076  C  CD1   . LEU A 1 2048 ? 224.386 236.880 265.886 1.00 40.37  ? 2048 LEU A CD1   1 
ATOM   4077  C  CD2   . LEU A 1 2048 ? 223.218 237.615 263.843 1.00 43.84  ? 2048 LEU A CD2   1 
ATOM   4078  N  N     . ILE A 1 2049 ? 224.523 232.900 262.928 1.00 31.90  ? 2049 ILE A N     1 
ATOM   4079  C  CA    . ILE A 1 2049 ? 223.502 231.822 262.869 1.00 30.95  ? 2049 ILE A CA    1 
ATOM   4080  C  C     . ILE A 1 2049 ? 223.959 230.717 263.807 1.00 37.62  ? 2049 ILE A C     1 
ATOM   4081  O  O     . ILE A 1 2049 ? 223.110 230.151 264.458 1.00 42.74  ? 2049 ILE A O     1 
ATOM   4082  C  CB    . ILE A 1 2049 ? 223.316 231.332 261.429 1.00 41.12  ? 2049 ILE A CB    1 
ATOM   4083  C  CG1   . ILE A 1 2049 ? 223.045 232.495 260.481 1.00 40.29  ? 2049 ILE A CG1   1 
ATOM   4084  C  CG2   . ILE A 1 2049 ? 222.222 230.270 261.352 1.00 42.18  ? 2049 ILE A CG2   1 
ATOM   4085  C  CD1   . ILE A 1 2049 ? 223.294 232.181 259.020 1.00 33.08  ? 2049 ILE A CD1   1 
ATOM   4086  N  N     . ALA A 1 2050 ? 225.250 230.442 263.870 1.00 40.77  ? 2050 ALA A N     1 
ATOM   4087  C  CA    . ALA A 1 2050 ? 225.814 229.361 264.698 1.00 26.66  ? 2050 ALA A CA    1 
ATOM   4088  C  C     . ALA A 1 2050 ? 225.817 229.794 266.141 1.00 28.31  ? 2050 ALA A C     1 
ATOM   4089  O  O     . ALA A 1 2050 ? 225.572 228.977 266.993 1.00 44.15  ? 2050 ALA A O     1 
ATOM   4090  C  CB    . ALA A 1 2050 ? 227.211 229.139 264.250 1.00 30.22  ? 2050 ALA A CB    1 
ATOM   4091  N  N     . GLN A 1 2051 ? 226.147 231.043 266.397 1.00 37.80  ? 2051 GLN A N     1 
ATOM   4092  C  CA    . GLN A 1 2051 ? 226.084 231.454 267.795 1.00 34.83  ? 2051 GLN A CA    1 
ATOM   4093  C  C     . GLN A 1 2051 ? 224.658 231.397 268.324 1.00 38.07  ? 2051 GLN A C     1 
ATOM   4094  O  O     . GLN A 1 2051 ? 224.414 230.860 269.408 1.00 47.79  ? 2051 GLN A O     1 
ATOM   4095  C  CB    . GLN A 1 2051 ? 226.661 232.858 267.953 1.00 39.19  ? 2051 GLN A CB    1 
ATOM   4096  C  CG    . GLN A 1 2051 ? 226.350 233.500 269.287 1.00 45.53  ? 2051 GLN A CG    1 
ATOM   4097  C  CD    . GLN A 1 2051 ? 226.623 234.985 269.287 1.00 54.86  ? 2051 GLN A CD    1 
ATOM   4098  O  OE1   . GLN A 1 2051 ? 227.703 235.429 268.898 1.00 57.68  ? 2051 GLN A OE1   1 
ATOM   4099  N  NE2   . GLN A 1 2051 ? 225.641 235.766 269.717 1.00 49.80  ? 2051 GLN A NE2   1 
ATOM   4100  N  N     . VAL A 1 2052 ? 223.698 231.928 267.565 1.00 34.10  ? 2052 VAL A N     1 
ATOM   4101  C  CA    . VAL A 1 2052 ? 222.315 231.936 268.032 1.00 26.43  ? 2052 VAL A CA    1 
ATOM   4102  C  C     . VAL A 1 2052 ? 221.740 230.525 268.051 1.00 34.78  ? 2052 VAL A C     1 
ATOM   4103  O  O     . VAL A 1 2052 ? 220.971 230.171 268.952 1.00 47.35  ? 2052 VAL A O     1 
ATOM   4104  C  CB    . VAL A 1 2052 ? 221.465 232.891 267.177 1.00 36.48  ? 2052 VAL A CB    1 
ATOM   4105  C  CG1   . VAL A 1 2052 ? 220.005 232.817 267.587 1.00 30.93  ? 2052 VAL A CG1   1 
ATOM   4106  C  CG2   . VAL A 1 2052 ? 221.975 234.309 267.320 1.00 37.95  ? 2052 VAL A CG2   1 
ATOM   4107  N  N     . MET A 1 2053 ? 222.093 229.697 267.065 1.00 32.27  ? 2053 MET A N     1 
ATOM   4108  C  CA    . MET A 1 2053 ? 221.583 228.331 267.035 1.00 30.12  ? 2053 MET A CA    1 
ATOM   4109  C  C     . MET A 1 2053 ? 222.097 227.522 268.216 1.00 34.57  ? 2053 MET A C     1 
ATOM   4110  O  O     . MET A 1 2053 ? 221.349 226.738 268.810 1.00 45.18  ? 2053 MET A O     1 
ATOM   4111  C  CB    . MET A 1 2053 ? 221.960 227.657 265.718 1.00 37.20  ? 2053 MET A CB    1 
ATOM   4112  C  CG    . MET A 1 2053 ? 221.051 228.018 264.558 1.00 37.12  ? 2053 MET A CG    1 
ATOM   4113  S  SD    . MET A 1 2053 ? 221.066 226.768 263.263 1.00 57.05  ? 2053 MET A SD    1 
ATOM   4114  C  CE    . MET A 1 2053 ? 219.890 225.591 263.922 1.00 43.97  ? 2053 MET A CE    1 
ATOM   4115  N  N     . LEU A 1 2054 ? 223.371 227.689 268.569 1.00 38.74  ? 2054 LEU A N     1 
ATOM   4116  C  CA    . LEU A 1 2054 ? 223.899 226.970 269.722 1.00 36.68  ? 2054 LEU A CA    1 
ATOM   4117  C  C     . LEU A 1 2054 ? 223.365 227.549 271.026 1.00 38.12  ? 2054 LEU A C     1 
ATOM   4118  O  O     . LEU A 1 2054 ? 223.105 226.807 271.979 1.00 48.98  ? 2054 LEU A O     1 
ATOM   4119  C  CB    . LEU A 1 2054 ? 225.425 226.992 269.695 1.00 36.45  ? 2054 LEU A CB    1 
ATOM   4120  C  CG    . LEU A 1 2054 ? 226.043 226.237 268.519 1.00 24.12  ? 2054 LEU A CG    1 
ATOM   4121  C  CD1   . LEU A 1 2054 ? 227.547 226.366 268.530 1.00 29.82  ? 2054 LEU A CD1   1 
ATOM   4122  C  CD2   . LEU A 1 2054 ? 225.630 224.777 268.548 1.00 29.81  ? 2054 LEU A CD2   1 
ATOM   4123  N  N     . TYR A 1 2055 ? 223.181 228.870 271.085 1.00 41.94  ? 2055 TYR A N     1 
ATOM   4124  C  CA    . TYR A 1 2055 ? 222.649 229.502 272.287 1.00 36.42  ? 2055 TYR A CA    1 
ATOM   4125  C  C     . TYR A 1 2055 ? 221.216 229.063 272.560 1.00 36.49  ? 2055 TYR A C     1 
ATOM   4126  O  O     . TYR A 1 2055 ? 220.842 228.819 273.712 1.00 45.47  ? 2055 TYR A O     1 
ATOM   4127  C  CB    . TYR A 1 2055 ? 222.729 231.021 272.143 1.00 39.94  ? 2055 TYR A CB    1 
ATOM   4128  C  CG    . TYR A 1 2055 ? 222.279 231.793 273.360 1.00 47.03  ? 2055 TYR A CG    1 
ATOM   4129  C  CD1   . TYR A 1 2055 ? 223.004 231.748 274.541 1.00 49.00  ? 2055 TYR A CD1   1 
ATOM   4130  C  CD2   . TYR A 1 2055 ? 221.135 232.577 273.324 1.00 40.61  ? 2055 TYR A CD2   1 
ATOM   4131  C  CE1   . TYR A 1 2055 ? 222.598 232.456 275.652 1.00 49.20  ? 2055 TYR A CE1   1 
ATOM   4132  C  CE2   . TYR A 1 2055 ? 220.722 233.287 274.430 1.00 40.90  ? 2055 TYR A CE2   1 
ATOM   4133  C  CZ    . TYR A 1 2055 ? 221.456 233.223 275.592 1.00 49.70  ? 2055 TYR A CZ    1 
ATOM   4134  O  OH    . TYR A 1 2055 ? 221.051 233.930 276.699 1.00 52.39  ? 2055 TYR A OH    1 
ATOM   4135  N  N     . SER A 1 2056 ? 220.397 228.960 271.512 1.00 33.63  ? 2056 SER A N     1 
ATOM   4136  C  CA    . SER A 1 2056 ? 219.004 228.569 271.682 1.00 35.40  ? 2056 SER A CA    1 
ATOM   4137  C  C     . SER A 1 2056 ? 218.848 227.085 271.973 1.00 42.50  ? 2056 SER A C     1 
ATOM   4138  O  O     . SER A 1 2056 ? 217.764 226.659 272.385 1.00 47.18  ? 2056 SER A O     1 
ATOM   4139  C  CB    . SER A 1 2056 ? 218.201 228.938 270.436 1.00 37.83  ? 2056 SER A CB    1 
ATOM   4140  O  OG    . SER A 1 2056 ? 218.712 228.282 269.290 1.00 40.29  ? 2056 SER A OG    1 
ATOM   4141  N  N     . GLN A 1 2057 ? 219.893 226.290 271.762 1.00 44.52  ? 2057 GLN A N     1 
ATOM   4142  C  CA    . GLN A 1 2057 ? 219.854 224.862 272.039 1.00 38.72  ? 2057 GLN A CA    1 
ATOM   4143  C  C     . GLN A 1 2057 ? 220.385 224.514 273.421 1.00 39.41  ? 2057 GLN A C     1 
ATOM   4144  O  O     . GLN A 1 2057 ? 220.414 223.333 273.775 1.00 50.50  ? 2057 GLN A O     1 
ATOM   4145  C  CB    . GLN A 1 2057 ? 220.644 224.094 270.976 1.00 35.56  ? 2057 GLN A CB    1 
ATOM   4146  C  CG    . GLN A 1 2057 ? 219.848 223.781 269.723 1.00 38.23  ? 2057 GLN A CG    1 
ATOM   4147  C  CD    . GLN A 1 2057 ? 220.726 223.346 268.570 1.00 51.89  ? 2057 GLN A CD    1 
ATOM   4148  O  OE1   . GLN A 1 2057 ? 221.952 223.365 268.667 1.00 53.39  ? 2057 GLN A OE1   1 
ATOM   4149  N  NE2   . GLN A 1 2057 ? 220.102 222.947 267.469 1.00 51.18  ? 2057 GLN A NE2   1 
ATOM   4150  N  N     . GLY A 1 2058 ? 220.796 225.503 274.206 1.00 39.11  ? 2058 GLY A N     1 
ATOM   4151  C  CA    . GLY A 1 2058 ? 221.296 225.252 275.539 1.00 39.64  ? 2058 GLY A CA    1 
ATOM   4152  C  C     . GLY A 1 2058 ? 222.792 225.086 275.650 1.00 46.21  ? 2058 GLY A C     1 
ATOM   4153  O  O     . GLY A 1 2058 ? 223.267 224.607 276.686 1.00 57.74  ? 2058 GLY A O     1 
ATOM   4154  N  N     . PHE A 1 2059 ? 223.550 225.458 274.623 1.00 43.68  ? 2059 PHE A N     1 
ATOM   4155  C  CA    . PHE A 1 2059 ? 225.003 225.353 274.659 1.00 31.77  ? 2059 PHE A CA    1 
ATOM   4156  C  C     . PHE A 1 2059 ? 225.565 226.539 275.431 1.00 41.84  ? 2059 PHE A C     1 
ATOM   4157  O  O     . PHE A 1 2059 ? 225.571 227.666 274.927 1.00 51.59  ? 2059 PHE A O     1 
ATOM   4158  C  CB    . PHE A 1 2059 ? 225.578 225.324 273.246 1.00 39.43  ? 2059 PHE A CB    1 
ATOM   4159  C  CG    . PHE A 1 2059 ? 225.596 223.963 272.616 1.00 44.51  ? 2059 PHE A CG    1 
ATOM   4160  C  CD1   . PHE A 1 2059 ? 224.452 223.433 272.051 1.00 43.88  ? 2059 PHE A CD1   1 
ATOM   4161  C  CD2   . PHE A 1 2059 ? 226.764 223.226 272.563 1.00 43.04  ? 2059 PHE A CD2   1 
ATOM   4162  C  CE1   . PHE A 1 2059 ? 224.469 222.191 271.461 1.00 45.59  ? 2059 PHE A CE1   1 
ATOM   4163  C  CE2   . PHE A 1 2059 ? 226.787 221.982 271.975 1.00 39.66  ? 2059 PHE A CE2   1 
ATOM   4164  C  CZ    . PHE A 1 2059 ? 225.639 221.463 271.424 1.00 48.43  ? 2059 PHE A CZ    1 
ATOM   4165  N  N     . ARG A 1 2060 ? 226.034 226.298 276.650 1.00 54.38  ? 2060 ARG A N     1 
ATOM   4166  C  CA    . ARG A 1 2060 ? 226.847 227.297 277.324 1.00 55.39  ? 2060 ARG A CA    1 
ATOM   4167  C  C     . ARG A 1 2060 ? 228.132 227.535 276.541 1.00 57.51  ? 2060 ARG A C     1 
ATOM   4168  O  O     . ARG A 1 2060 ? 228.691 226.621 275.930 1.00 62.11  ? 2060 ARG A O     1 
ATOM   4169  C  CB    . ARG A 1 2060 ? 227.165 226.864 278.754 1.00 59.30  ? 2060 ARG A CB    1 
ATOM   4170  C  CG    . ARG A 1 2060 ? 225.946 226.709 279.641 1.00 55.75  ? 2060 ARG A CG    1 
ATOM   4171  C  CD    . ARG A 1 2060 ? 225.343 228.080 279.894 1.00 63.55  ? 2060 ARG A CD    1 
ATOM   4172  N  NE    . ARG A 1 2060 ? 224.202 228.057 280.799 1.00 66.09  ? 2060 ARG A NE    1 
ATOM   4173  C  CZ    . ARG A 1 2060 ? 223.480 229.126 281.106 1.00 64.75  ? 2060 ARG A CZ    1 
ATOM   4174  N  NH1   . ARG A 1 2060 ? 223.755 230.315 280.595 1.00 58.16  ? 2060 ARG A NH1   1 
ATOM   4175  N  NH2   . ARG A 1 2060 ? 222.463 229.002 281.953 1.00 64.54  ? 2060 ARG A NH2   1 
ATOM   4176  N  N     . THR A 1 2061 ? 228.593 228.784 276.558 1.00 52.77  ? 2061 THR A N     1 
ATOM   4177  C  CA    . THR A 1 2061 ? 229.720 229.228 275.738 1.00 59.08  ? 2061 THR A CA    1 
ATOM   4178  C  C     . THR A 1 2061 ? 229.449 228.954 274.260 1.00 52.09  ? 2061 THR A C     1 
ATOM   4179  O  O     . THR A 1 2061 ? 230.222 228.290 273.569 1.00 51.78  ? 2061 THR A O     1 
ATOM   4180  C  CB    . THR A 1 2061 ? 231.036 228.581 276.183 1.00 60.97  ? 2061 THR A CB    1 
ATOM   4181  O  OG1   . THR A 1 2061 ? 230.954 227.158 276.040 1.00 47.22  ? 2061 THR A OG1   1 
ATOM   4182  C  CG2   . THR A 1 2061 ? 231.332 228.924 277.635 1.00 61.92  ? 2061 THR A CG2   1 
ATOM   4183  N  N     . ALA A 1 2062 ? 228.313 229.466 273.781 1.00 52.20  ? 2062 ALA A N     1 
ATOM   4184  C  CA    . ALA A 1 2062 ? 227.969 229.315 272.373 1.00 43.85  ? 2062 ALA A CA    1 
ATOM   4185  C  C     . ALA A 1 2062 ? 228.788 230.245 271.490 1.00 46.40  ? 2062 ALA A C     1 
ATOM   4186  O  O     . ALA A 1 2062 ? 229.045 229.921 270.326 1.00 56.74  ? 2062 ALA A O     1 
ATOM   4187  C  CB    . ALA A 1 2062 ? 226.477 229.568 272.165 1.00 42.89  ? 2062 ALA A CB    1 
ATOM   4188  N  N     . GLU A 1 2063 ? 229.197 231.402 272.015 1.00 42.06  ? 2063 GLU A N     1 
ATOM   4189  C  CA    . GLU A 1 2063 ? 230.014 232.320 271.228 1.00 44.71  ? 2063 GLU A CA    1 
ATOM   4190  C  C     . GLU A 1 2063 ? 231.368 231.709 270.896 1.00 50.07  ? 2063 GLU A C     1 
ATOM   4191  O  O     . GLU A 1 2063 ? 231.851 231.834 269.766 1.00 58.17  ? 2063 GLU A O     1 
ATOM   4192  C  CB    . GLU A 1 2063 ? 230.193 233.641 271.973 1.00 42.78  ? 2063 GLU A CB    1 
ATOM   4193  C  CG    . GLU A 1 2063 ? 228.915 234.441 272.130 1.00 52.65  ? 2063 GLU A CG    1 
ATOM   4194  C  CD    . GLU A 1 2063 ? 229.177 235.880 272.529 1.00 60.82  ? 2063 GLU A CD    1 
ATOM   4195  O  OE1   . GLU A 1 2063 ? 230.362 236.255 272.656 1.00 54.27  ? 2063 GLU A OE1   1 
ATOM   4196  O  OE2   . GLU A 1 2063 ? 228.199 236.636 272.714 1.00 58.19  ? 2063 GLU A OE2   1 
ATOM   4197  N  N     . VAL A 1 2064 ? 231.997 231.049 271.870 1.00 47.22  ? 2064 VAL A N     1 
ATOM   4198  C  CA    . VAL A 1 2064 ? 233.282 230.399 271.623 1.00 43.30  ? 2064 VAL A CA    1 
ATOM   4199  C  C     . VAL A 1 2064 ? 233.129 229.302 270.579 1.00 41.27  ? 2064 VAL A C     1 
ATOM   4200  O  O     . VAL A 1 2064 ? 233.939 229.183 269.649 1.00 51.46  ? 2064 VAL A O     1 
ATOM   4201  C  CB    . VAL A 1 2064 ? 233.858 229.850 272.941 1.00 43.97  ? 2064 VAL A CB    1 
ATOM   4202  C  CG1   . VAL A 1 2064 ? 235.146 229.092 272.684 1.00 44.63  ? 2064 VAL A CG1   1 
ATOM   4203  C  CG2   . VAL A 1 2064 ? 234.079 230.977 273.933 1.00 46.00  ? 2064 VAL A CG2   1 
ATOM   4204  N  N     . LEU A 1 2065 ? 232.079 228.491 270.709 1.00 37.43  ? 2065 LEU A N     1 
ATOM   4205  C  CA    . LEU A 1 2065 ? 231.856 227.412 269.757 1.00 38.94  ? 2065 LEU A CA    1 
ATOM   4206  C  C     . LEU A 1 2065 ? 231.601 227.950 268.355 1.00 41.33  ? 2065 LEU A C     1 
ATOM   4207  O  O     . LEU A 1 2065 ? 232.081 227.376 267.375 1.00 51.71  ? 2065 LEU A O     1 
ATOM   4208  C  CB    . LEU A 1 2065 ? 230.697 226.536 270.223 1.00 40.54  ? 2065 LEU A CB    1 
ATOM   4209  C  CG    . LEU A 1 2065 ? 230.964 225.712 271.482 1.00 42.07  ? 2065 LEU A CG    1 
ATOM   4210  C  CD1   . LEU A 1 2065 ? 229.822 224.757 271.745 1.00 42.75  ? 2065 LEU A CD1   1 
ATOM   4211  C  CD2   . LEU A 1 2065 ? 232.271 224.959 271.352 1.00 40.96  ? 2065 LEU A CD2   1 
ATOM   4212  N  N     . ALA A 1 2066 ? 230.849 229.047 268.233 1.00 32.25  ? 2066 ALA A N     1 
ATOM   4213  C  CA    . ALA A 1 2066 ? 230.612 229.632 266.915 1.00 34.19  ? 2066 ALA A CA    1 
ATOM   4214  C  C     . ALA A 1 2066 ? 231.895 230.202 266.322 1.00 46.32  ? 2066 ALA A C     1 
ATOM   4215  O  O     . ALA A 1 2066 ? 232.204 229.972 265.141 1.00 50.65  ? 2066 ALA A O     1 
ATOM   4216  C  CB    . ALA A 1 2066 ? 229.542 230.715 267.009 1.00 31.03  ? 2066 ALA A CB    1 
ATOM   4217  N  N     . ASN A 1 2067 ? 232.655 230.950 267.128 1.00 42.95  ? 2067 ASN A N     1 
ATOM   4218  C  CA    . ASN A 1 2067 ? 233.923 231.523 266.698 1.00 36.65  ? 2067 ASN A CA    1 
ATOM   4219  C  C     . ASN A 1 2067 ? 234.953 230.465 266.347 1.00 44.49  ? 2067 ASN A C     1 
ATOM   4220  O  O     . ASN A 1 2067 ? 235.936 230.784 265.674 1.00 57.83  ? 2067 ASN A O     1 
ATOM   4221  C  CB    . ASN A 1 2067 ? 234.489 232.431 267.789 1.00 42.22  ? 2067 ASN A CB    1 
ATOM   4222  C  CG    . ASN A 1 2067 ? 233.733 233.734 267.917 1.00 42.58  ? 2067 ASN A CG    1 
ATOM   4223  O  OD1   . ASN A 1 2067 ? 233.332 234.126 269.011 1.00 41.14  ? 2067 ASN A OD1   1 
ATOM   4224  N  ND2   . ASN A 1 2067 ? 233.536 234.416 266.797 1.00 46.70  ? 2067 ASN A ND2   1 
ATOM   4225  N  N     . LYS A 1 2068 ? 234.778 229.235 266.819 1.00 41.19  ? 2068 LYS A N     1 
ATOM   4226  C  CA    . LYS A 1 2068 ? 235.634 228.137 266.391 1.00 34.02  ? 2068 LYS A CA    1 
ATOM   4227  C  C     . LYS A 1 2068 ? 235.079 227.379 265.193 1.00 37.77  ? 2068 LYS A C     1 
ATOM   4228  O  O     . LYS A 1 2068 ? 235.851 226.909 264.355 1.00 48.67  ? 2068 LYS A O     1 
ATOM   4229  C  CB    . LYS A 1 2068 ? 235.861 227.162 267.548 1.00 30.19  ? 2068 LYS A CB    1 
ATOM   4230  C  CG    . LYS A 1 2068 ? 236.729 227.717 268.658 1.00 34.41  ? 2068 LYS A CG    1 
ATOM   4231  C  CD    . LYS A 1 2068 ? 236.877 226.721 269.787 1.00 39.09  ? 2068 LYS A CD    1 
ATOM   4232  C  CE    . LYS A 1 2068 ? 237.924 227.177 270.781 1.00 41.82  ? 2068 LYS A CE    1 
ATOM   4233  N  NZ    . LYS A 1 2068 ? 239.201 227.520 270.104 1.00 44.88  ? 2068 LYS A NZ    1 
ATOM   4234  N  N     . ILE A 1 2069 ? 233.757 227.269 265.071 1.00 36.81  ? 2069 ILE A N     1 
ATOM   4235  C  CA    . ILE A 1 2069 ? 233.194 226.368 264.074 1.00 35.48  ? 2069 ILE A CA    1 
ATOM   4236  C  C     . ILE A 1 2069 ? 233.021 227.050 262.723 1.00 40.59  ? 2069 ILE A C     1 
ATOM   4237  O  O     . ILE A 1 2069 ? 233.049 226.379 261.686 1.00 46.51  ? 2069 ILE A O     1 
ATOM   4238  C  CB    . ILE A 1 2069 ? 231.868 225.774 264.581 1.00 37.99  ? 2069 ILE A CB    1 
ATOM   4239  C  CG1   . ILE A 1 2069 ? 231.521 224.506 263.802 1.00 42.76  ? 2069 ILE A CG1   1 
ATOM   4240  C  CG2   . ILE A 1 2069 ? 230.739 226.785 264.478 1.00 36.10  ? 2069 ILE A CG2   1 
ATOM   4241  C  CD1   . ILE A 1 2069 ? 232.589 223.440 263.871 1.00 37.74  ? 2069 ILE A CD1   1 
ATOM   4242  N  N     . VAL A 1 2070 ? 232.845 228.367 262.684 1.00 38.69  ? 2070 VAL A N     1 
ATOM   4243  C  CA    . VAL A 1 2070 ? 232.686 229.024 261.385 1.00 41.54  ? 2070 VAL A CA    1 
ATOM   4244  C  C     . VAL A 1 2070 ? 234.046 229.205 260.709 1.00 43.85  ? 2070 VAL A C     1 
ATOM   4245  O  O     . VAL A 1 2070 ? 234.183 228.877 259.515 1.00 48.81  ? 2070 VAL A O     1 
ATOM   4246  C  CB    . VAL A 1 2070 ? 231.921 230.349 261.522 1.00 42.27  ? 2070 VAL A CB    1 
ATOM   4247  C  CG1   . VAL A 1 2070 ? 231.963 231.123 260.219 1.00 43.03  ? 2070 VAL A CG1   1 
ATOM   4248  C  CG2   . VAL A 1 2070 ? 230.489 230.070 261.924 1.00 38.95  ? 2070 VAL A CG2   1 
ATOM   4249  N  N     . PRO A 1 2071 ? 235.077 229.708 261.401 1.00 39.28  ? 2071 PRO A N     1 
ATOM   4250  C  CA    . PRO A 1 2071 ? 236.416 229.690 260.793 1.00 34.48  ? 2071 PRO A CA    1 
ATOM   4251  C  C     . PRO A 1 2071 ? 236.890 228.297 260.438 1.00 41.29  ? 2071 PRO A C     1 
ATOM   4252  O  O     . PRO A 1 2071 ? 237.648 228.143 259.476 1.00 53.20  ? 2071 PRO A O     1 
ATOM   4253  C  CB    . PRO A 1 2071 ? 237.298 230.330 261.872 1.00 34.44  ? 2071 PRO A CB    1 
ATOM   4254  C  CG    . PRO A 1 2071 ? 236.381 231.204 262.613 1.00 37.91  ? 2071 PRO A CG    1 
ATOM   4255  C  CD    . PRO A 1 2071 ? 235.089 230.454 262.673 1.00 39.53  ? 2071 PRO A CD    1 
ATOM   4256  N  N     . PHE A 1 2072 ? 236.471 227.273 261.185 1.00 42.37  ? 2072 PHE A N     1 
ATOM   4257  C  CA    . PHE A 1 2072 ? 236.822 225.906 260.819 1.00 37.37  ? 2072 PHE A CA    1 
ATOM   4258  C  C     . PHE A 1 2072 ? 236.280 225.552 259.443 1.00 36.08  ? 2072 PHE A C     1 
ATOM   4259  O  O     . PHE A 1 2072 ? 236.995 224.976 258.616 1.00 46.40  ? 2072 PHE A O     1 
ATOM   4260  C  CB    . PHE A 1 2072 ? 236.296 224.926 261.867 1.00 40.01  ? 2072 PHE A CB    1 
ATOM   4261  C  CG    . PHE A 1 2072 ? 236.276 223.499 261.404 1.00 39.07  ? 2072 PHE A CG    1 
ATOM   4262  C  CD1   . PHE A 1 2072 ? 237.437 222.749 261.383 1.00 44.43  ? 2072 PHE A CD1   1 
ATOM   4263  C  CD2   . PHE A 1 2072 ? 235.097 222.908 260.985 1.00 36.59  ? 2072 PHE A CD2   1 
ATOM   4264  C  CE1   . PHE A 1 2072 ? 237.422 221.439 260.953 1.00 41.40  ? 2072 PHE A CE1   1 
ATOM   4265  C  CE2   . PHE A 1 2072 ? 235.077 221.600 260.554 1.00 33.07  ? 2072 PHE A CE2   1 
ATOM   4266  C  CZ    . PHE A 1 2072 ? 236.241 220.864 260.540 1.00 37.96  ? 2072 PHE A CZ    1 
ATOM   4267  N  N     . PHE A 1 2073 ? 235.018 225.893 259.174 1.00 32.88  ? 2073 PHE A N     1 
ATOM   4268  C  CA    . PHE A 1 2073 ? 234.446 225.617 257.862 1.00 32.28  ? 2073 PHE A CA    1 
ATOM   4269  C  C     . PHE A 1 2073 ? 235.118 226.439 256.772 1.00 36.23  ? 2073 PHE A C     1 
ATOM   4270  O  O     . PHE A 1 2073 ? 235.346 225.929 255.667 1.00 43.20  ? 2073 PHE A O     1 
ATOM   4271  C  CB    . PHE A 1 2073 ? 232.941 225.876 257.878 1.00 34.78  ? 2073 PHE A CB    1 
ATOM   4272  C  CG    . PHE A 1 2073 ? 232.131 224.678 258.268 1.00 31.58  ? 2073 PHE A CG    1 
ATOM   4273  C  CD1   . PHE A 1 2073 ? 231.952 224.353 259.598 1.00 34.20  ? 2073 PHE A CD1   1 
ATOM   4274  C  CD2   . PHE A 1 2073 ? 231.558 223.871 257.304 1.00 37.06  ? 2073 PHE A CD2   1 
ATOM   4275  C  CE1   . PHE A 1 2073 ? 231.214 223.250 259.960 1.00 37.58  ? 2073 PHE A CE1   1 
ATOM   4276  C  CE2   . PHE A 1 2073 ? 230.820 222.767 257.662 1.00 38.97  ? 2073 PHE A CE2   1 
ATOM   4277  C  CZ    . PHE A 1 2073 ? 230.647 222.457 258.991 1.00 39.30  ? 2073 PHE A CZ    1 
ATOM   4278  N  N     . LYS A 1 2074 ? 235.447 227.701 257.055 1.00 44.08  ? 2074 LYS A N     1 
ATOM   4279  C  CA    . LYS A 1 2074 ? 236.148 228.503 256.054 1.00 42.72  ? 2074 LYS A CA    1 
ATOM   4280  C  C     . LYS A 1 2074 ? 237.516 227.910 255.722 1.00 38.71  ? 2074 LYS A C     1 
ATOM   4281  O  O     . LYS A 1 2074 ? 237.901 227.835 254.547 1.00 47.18  ? 2074 LYS A O     1 
ATOM   4282  C  CB    . LYS A 1 2074 ? 236.292 229.943 256.539 1.00 41.29  ? 2074 LYS A CB    1 
ATOM   4283  C  CG    . LYS A 1 2074 ? 236.936 230.859 255.518 1.00 50.78  ? 2074 LYS A CG    1 
ATOM   4284  C  CD    . LYS A 1 2074 ? 237.011 232.288 256.016 1.00 52.56  ? 2074 LYS A CD    1 
ATOM   4285  C  CE    . LYS A 1 2074 ? 237.576 233.199 254.943 1.00 48.79  ? 2074 LYS A CE    1 
ATOM   4286  N  NZ    . LYS A 1 2074 ? 239.006 232.891 254.671 1.00 48.41  ? 2074 LYS A NZ    1 
ATOM   4287  N  N     . LEU A 1 2075 ? 238.258 227.472 256.741 1.00 35.33  ? 2075 LEU A N     1 
ATOM   4288  C  CA    . LEU A 1 2075 ? 239.572 226.887 256.501 1.00 36.37  ? 2075 LEU A CA    1 
ATOM   4289  C  C     . LEU A 1 2075 ? 239.470 225.525 255.829 1.00 41.23  ? 2075 LEU A C     1 
ATOM   4290  O  O     . LEU A 1 2075 ? 240.363 225.148 255.067 1.00 47.25  ? 2075 LEU A O     1 
ATOM   4291  C  CB    . LEU A 1 2075 ? 240.349 226.776 257.812 1.00 39.57  ? 2075 LEU A CB    1 
ATOM   4292  C  CG    . LEU A 1 2075 ? 240.653 228.092 258.530 1.00 42.39  ? 2075 LEU A CG    1 
ATOM   4293  C  CD1   . LEU A 1 2075 ? 240.938 227.845 259.999 1.00 45.78  ? 2075 LEU A CD1   1 
ATOM   4294  C  CD2   . LEU A 1 2075 ? 241.809 228.819 257.874 1.00 40.37  ? 2075 LEU A CD2   1 
ATOM   4295  N  N     . CYS A 1 2076 ? 238.407 224.769 256.107 1.00 47.14  ? 2076 CYS A N     1 
ATOM   4296  C  CA    . CYS A 1 2076 ? 238.182 223.524 255.380 1.00 41.84  ? 2076 CYS A CA    1 
ATOM   4297  C  C     . CYS A 1 2076 ? 237.917 223.794 253.908 1.00 39.82  ? 2076 CYS A C     1 
ATOM   4298  O  O     . CYS A 1 2076 ? 238.411 223.072 253.036 1.00 40.93  ? 2076 CYS A O     1 
ATOM   4299  C  CB    . CYS A 1 2076 ? 237.016 222.755 255.999 1.00 31.74  ? 2076 CYS A CB    1 
ATOM   4300  S  SG    . CYS A 1 2076 ? 237.458 221.763 257.429 1.00 54.39  ? 2076 CYS A SG    1 
ATOM   4301  N  N     . ASP A 1 2077 ? 237.129 224.829 253.613 1.00 40.09  ? 2077 ASP A N     1 
ATOM   4302  C  CA    . ASP A 1 2077 ? 236.876 225.192 252.223 1.00 35.97  ? 2077 ASP A CA    1 
ATOM   4303  C  C     . ASP A 1 2077 ? 238.166 225.613 251.527 1.00 44.78  ? 2077 ASP A C     1 
ATOM   4304  O  O     . ASP A 1 2077 ? 238.420 225.221 250.382 1.00 46.35  ? 2077 ASP A O     1 
ATOM   4305  C  CB    . ASP A 1 2077 ? 235.833 226.310 252.167 1.00 38.79  ? 2077 ASP A CB    1 
ATOM   4306  C  CG    . ASP A 1 2077 ? 235.353 226.607 250.756 1.00 49.57  ? 2077 ASP A CG    1 
ATOM   4307  O  OD1   . ASP A 1 2077 ? 235.839 225.975 249.796 1.00 51.84  ? 2077 ASP A OD1   1 
ATOM   4308  O  OD2   . ASP A 1 2077 ? 234.477 227.483 250.608 1.00 52.06  ? 2077 ASP A OD2   1 
ATOM   4309  N  N     . GLU A 1 2078 ? 238.998 226.403 252.207 1.00 51.35  ? 2078 GLU A N     1 
ATOM   4310  C  CA    . GLU A 1 2078 ? 240.225 226.904 251.591 1.00 39.38  ? 2078 GLU A CA    1 
ATOM   4311  C  C     . GLU A 1 2078 ? 241.272 225.809 251.407 1.00 47.33  ? 2078 GLU A C     1 
ATOM   4312  O  O     . GLU A 1 2078 ? 241.883 225.698 250.339 1.00 43.84  ? 2078 GLU A O     1 
ATOM   4313  C  CB    . GLU A 1 2078 ? 240.802 228.044 252.429 1.00 31.78  ? 2078 GLU A CB    1 
ATOM   4314  C  CG    . GLU A 1 2078 ? 240.037 229.344 252.321 1.00 44.98  ? 2078 GLU A CG    1 
ATOM   4315  C  CD    . GLU A 1 2078 ? 240.810 230.514 252.889 1.00 57.17  ? 2078 GLU A CD    1 
ATOM   4316  O  OE1   . GLU A 1 2078 ? 240.682 231.632 252.348 1.00 56.33  ? 2078 GLU A OE1   1 
ATOM   4317  O  OE2   . GLU A 1 2078 ? 241.545 230.315 253.878 1.00 57.20  ? 2078 GLU A OE2   1 
ATOM   4318  N  N     . GLN A 1 2079 ? 241.496 224.994 252.438 1.00 49.59  ? 2079 GLN A N     1 
ATOM   4319  C  CA    . GLN A 1 2079 ? 242.652 224.104 252.460 1.00 43.59  ? 2079 GLN A CA    1 
ATOM   4320  C  C     . GLN A 1 2079 ? 242.403 222.802 251.709 1.00 45.78  ? 2079 GLN A C     1 
ATOM   4321  O  O     . GLN A 1 2079 ? 243.294 222.314 251.005 1.00 49.07  ? 2079 GLN A O     1 
ATOM   4322  C  CB    . GLN A 1 2079 ? 243.048 223.804 253.904 1.00 36.12  ? 2079 GLN A CB    1 
ATOM   4323  C  CG    . GLN A 1 2079 ? 244.405 223.150 254.047 1.00 39.74  ? 2079 GLN A CG    1 
ATOM   4324  C  CD    . GLN A 1 2079 ? 244.838 223.024 255.489 1.00 46.80  ? 2079 GLN A CD    1 
ATOM   4325  O  OE1   . GLN A 1 2079 ? 244.390 222.131 256.206 1.00 54.20  ? 2079 GLN A OE1   1 
ATOM   4326  N  NE2   . GLN A 1 2079 ? 245.723 223.910 255.920 1.00 48.96  ? 2079 GLN A NE2   1 
ATOM   4327  N  N     . LEU A 1 2080 ? 241.217 222.219 251.852 1.00 47.88  ? 2080 LEU A N     1 
ATOM   4328  C  CA    . LEU A 1 2080 ? 240.969 220.899 251.290 1.00 38.35  ? 2080 LEU A CA    1 
ATOM   4329  C  C     . LEU A 1 2080 ? 240.941 220.946 249.768 1.00 42.48  ? 2080 LEU A C     1 
ATOM   4330  O  O     . LEU A 1 2080 ? 240.690 221.986 249.156 1.00 46.37  ? 2080 LEU A O     1 
ATOM   4331  C  CB    . LEU A 1 2080 ? 239.656 220.326 251.820 1.00 33.46  ? 2080 LEU A CB    1 
ATOM   4332  C  CG    . LEU A 1 2080 ? 239.647 219.986 253.310 1.00 32.80  ? 2080 LEU A CG    1 
ATOM   4333  C  CD1   . LEU A 1 2080 ? 238.289 219.481 253.737 1.00 36.25  ? 2080 LEU A CD1   1 
ATOM   4334  C  CD2   . LEU A 1 2080 ? 240.713 218.964 253.623 1.00 37.73  ? 2080 LEU A CD2   1 
ATOM   4335  N  N     . SER A 1 2081 ? 241.212 219.795 249.159 1.00 37.20  ? 2081 SER A N     1 
ATOM   4336  C  CA    . SER A 1 2081 ? 241.268 219.693 247.711 1.00 38.72  ? 2081 SER A CA    1 
ATOM   4337  C  C     . SER A 1 2081 ? 239.894 219.941 247.099 1.00 45.52  ? 2081 SER A C     1 
ATOM   4338  O  O     . SER A 1 2081 ? 238.855 219.781 247.743 1.00 52.59  ? 2081 SER A O     1 
ATOM   4339  C  CB    . SER A 1 2081 ? 241.788 218.320 247.291 1.00 42.27  ? 2081 SER A CB    1 
ATOM   4340  O  OG    . SER A 1 2081 ? 240.900 217.295 247.699 1.00 39.28  ? 2081 SER A OG    1 
ATOM   4341  N  N     . SER A 1 2082 ? 239.901 220.347 245.834 1.00 38.57  ? 2082 SER A N     1 
ATOM   4342  C  CA    . SER A 1 2082 ? 238.671 220.677 245.125 1.00 39.40  ? 2082 SER A CA    1 
ATOM   4343  C  C     . SER A 1 2082 ? 238.066 219.400 244.558 1.00 44.41  ? 2082 SER A C     1 
ATOM   4344  O  O     . SER A 1 2082 ? 238.566 218.851 243.571 1.00 52.08  ? 2082 SER A O     1 
ATOM   4345  C  CB    . SER A 1 2082 ? 238.951 221.691 244.021 1.00 42.86  ? 2082 SER A CB    1 
ATOM   4346  O  OG    . SER A 1 2082 ? 237.773 222.000 243.299 1.00 49.35  ? 2082 SER A OG    1 
ATOM   4347  N  N     . GLN A 1 2083 ? 236.993 218.924 245.182 1.00 42.22  ? 2083 GLN A N     1 
ATOM   4348  C  CA    . GLN A 1 2083 ? 236.254 217.763 244.713 1.00 31.34  ? 2083 GLN A CA    1 
ATOM   4349  C  C     . GLN A 1 2083 ? 234.840 218.181 244.343 1.00 39.72  ? 2083 GLN A C     1 
ATOM   4350  O  O     . GLN A 1 2083 ? 234.290 219.133 244.903 1.00 45.25  ? 2083 GLN A O     1 
ATOM   4351  C  CB    . GLN A 1 2083 ? 236.215 216.658 245.771 1.00 31.56  ? 2083 GLN A CB    1 
ATOM   4352  C  CG    . GLN A 1 2083 ? 237.574 216.295 246.329 1.00 37.84  ? 2083 GLN A CG    1 
ATOM   4353  C  CD    . GLN A 1 2083 ? 238.335 215.349 245.427 1.00 43.93  ? 2083 GLN A CD    1 
ATOM   4354  O  OE1   . GLN A 1 2083 ? 237.742 214.612 244.643 1.00 47.50  ? 2083 GLN A OE1   1 
ATOM   4355  N  NE2   . GLN A 1 2083 ? 239.658 215.368 245.531 1.00 45.43  ? 2083 GLN A NE2   1 
ATOM   4356  N  N     . SER A 1 2084 ? 234.257 217.460 243.385 1.00 41.95  ? 2084 SER A N     1 
ATOM   4357  C  CA    . SER A 1 2084 ? 232.940 217.822 242.875 1.00 38.63  ? 2084 SER A CA    1 
ATOM   4358  C  C     . SER A 1 2084 ? 231.837 217.640 243.909 1.00 39.72  ? 2084 SER A C     1 
ATOM   4359  O  O     . SER A 1 2084 ? 230.793 218.290 243.797 1.00 39.51  ? 2084 SER A O     1 
ATOM   4360  C  CB    . SER A 1 2084 ? 232.624 217.004 241.624 1.00 39.51  ? 2084 SER A CB    1 
ATOM   4361  O  OG    . SER A 1 2084 ? 232.673 215.615 241.895 1.00 41.68  ? 2084 SER A OG    1 
ATOM   4362  N  N     . HIS A 1 2085 ? 232.037 216.781 244.905 1.00 34.41  ? 2085 HIS A N     1 
ATOM   4363  C  CA    . HIS A 1 2085 ? 231.025 216.509 245.915 1.00 28.15  ? 2085 HIS A CA    1 
ATOM   4364  C  C     . HIS A 1 2085 ? 231.280 217.243 247.225 1.00 36.90  ? 2085 HIS A C     1 
ATOM   4365  O  O     . HIS A 1 2085 ? 230.555 217.018 248.198 1.00 37.94  ? 2085 HIS A O     1 
ATOM   4366  C  CB    . HIS A 1 2085 ? 230.928 215.004 246.169 1.00 31.25  ? 2085 HIS A CB    1 
ATOM   4367  C  CG    . HIS A 1 2085 ? 232.190 214.397 246.695 1.00 35.24  ? 2085 HIS A CG    1 
ATOM   4368  N  ND1   . HIS A 1 2085 ? 233.269 214.107 245.889 1.00 37.82  ? 2085 HIS A ND1   1 
ATOM   4369  C  CD2   . HIS A 1 2085 ? 232.545 214.024 247.946 1.00 32.66  ? 2085 HIS A CD2   1 
ATOM   4370  C  CE1   . HIS A 1 2085 ? 234.234 213.582 246.621 1.00 37.62  ? 2085 HIS A CE1   1 
ATOM   4371  N  NE2   . HIS A 1 2085 ? 233.820 213.520 247.873 1.00 28.89  ? 2085 HIS A NE2   1 
ATOM   4372  N  N     . TYR A 1 2086 ? 232.284 218.113 247.272 1.00 41.25  ? 2086 TYR A N     1 
ATOM   4373  C  CA    . TYR A 1 2086 ? 232.590 218.851 248.488 1.00 32.88  ? 2086 TYR A CA    1 
ATOM   4374  C  C     . TYR A 1 2086 ? 231.672 220.055 248.633 1.00 42.26  ? 2086 TYR A C     1 
ATOM   4375  O  O     . TYR A 1 2086 ? 231.389 220.761 247.661 1.00 46.79  ? 2086 TYR A O     1 
ATOM   4376  C  CB    . TYR A 1 2086 ? 234.044 219.314 248.480 1.00 34.62  ? 2086 TYR A CB    1 
ATOM   4377  C  CG    . TYR A 1 2086 ? 235.020 218.297 249.010 1.00 37.45  ? 2086 TYR A CG    1 
ATOM   4378  C  CD1   . TYR A 1 2086 ? 234.607 217.018 249.345 1.00 29.22  ? 2086 TYR A CD1   1 
ATOM   4379  C  CD2   . TYR A 1 2086 ? 236.356 218.618 249.175 1.00 39.85  ? 2086 TYR A CD2   1 
ATOM   4380  C  CE1   . TYR A 1 2086 ? 235.499 216.089 249.829 1.00 34.29  ? 2086 TYR A CE1   1 
ATOM   4381  C  CE2   . TYR A 1 2086 ? 237.253 217.697 249.658 1.00 33.23  ? 2086 TYR A CE2   1 
ATOM   4382  C  CZ    . TYR A 1 2086 ? 236.820 216.434 249.984 1.00 38.05  ? 2086 TYR A CZ    1 
ATOM   4383  O  OH    . TYR A 1 2086 ? 237.719 215.513 250.464 1.00 51.73  ? 2086 TYR A OH    1 
ATOM   4384  N  N     . ASP A 1 2087 ? 231.212 220.291 249.858 1.00 37.06  ? 2087 ASP A N     1 
ATOM   4385  C  CA    . ASP A 1 2087 ? 230.399 221.463 250.160 1.00 29.37  ? 2087 ASP A CA    1 
ATOM   4386  C  C     . ASP A 1 2087 ? 230.604 221.828 251.620 1.00 38.28  ? 2087 ASP A C     1 
ATOM   4387  O  O     . ASP A 1 2087 ? 230.309 221.022 252.507 1.00 43.92  ? 2087 ASP A O     1 
ATOM   4388  C  CB    . ASP A 1 2087 ? 228.921 221.203 249.874 1.00 37.51  ? 2087 ASP A CB    1 
ATOM   4389  C  CG    . ASP A 1 2087 ? 228.036 222.350 250.313 1.00 52.90  ? 2087 ASP A CG    1 
ATOM   4390  O  OD1   . ASP A 1 2087 ? 228.105 223.425 249.683 1.00 48.22  ? 2087 ASP A OD1   1 
ATOM   4391  O  OD2   . ASP A 1 2087 ? 227.275 222.179 251.288 1.00 48.57  ? 2087 ASP A OD2   1 
ATOM   4392  N  N     . PHE A 1 2088 ? 231.108 223.035 251.866 1.00 33.84  ? 2088 PHE A N     1 
ATOM   4393  C  CA    . PHE A 1 2088 ? 231.303 223.516 253.226 1.00 32.50  ? 2088 PHE A CA    1 
ATOM   4394  C  C     . PHE A 1 2088 ? 230.601 224.852 253.412 1.00 40.99  ? 2088 PHE A C     1 
ATOM   4395  O  O     . PHE A 1 2088 ? 231.168 225.787 253.986 1.00 49.16  ? 2088 PHE A O     1 
ATOM   4396  C  CB    . PHE A 1 2088 ? 232.793 223.637 253.543 1.00 33.54  ? 2088 PHE A CB    1 
ATOM   4397  C  CG    . PHE A 1 2088 ? 233.546 222.350 253.391 1.00 44.14  ? 2088 PHE A CG    1 
ATOM   4398  C  CD1   . PHE A 1 2088 ? 233.505 221.389 254.384 1.00 41.29  ? 2088 PHE A CD1   1 
ATOM   4399  C  CD2   . PHE A 1 2088 ? 234.287 222.098 252.251 1.00 36.41  ? 2088 PHE A CD2   1 
ATOM   4400  C  CE1   . PHE A 1 2088 ? 234.194 220.205 254.244 1.00 40.58  ? 2088 PHE A CE1   1 
ATOM   4401  C  CE2   . PHE A 1 2088 ? 234.976 220.916 252.107 1.00 31.76  ? 2088 PHE A CE2   1 
ATOM   4402  C  CZ    . PHE A 1 2088 ? 234.928 219.967 253.104 1.00 33.59  ? 2088 PHE A CZ    1 
ATOM   4403  N  N     . GLY A 1 2089 ? 229.287 224.882 253.190 1.00 37.47  ? 2089 GLY A N     1 
ATOM   4404  C  CA    . GLY A 1 2089 ? 228.497 226.114 253.260 1.00 32.07  ? 2089 GLY A CA    1 
ATOM   4405  C  C     . GLY A 1 2089 ? 227.600 226.195 254.455 1.00 33.58  ? 2089 GLY A C     1 
ATOM   4406  O  O     . GLY A 1 2089 ? 227.974 225.632 255.469 1.00 46.85  ? 2089 GLY A O     1 
ATOM   4407  N  N     . LEU A 1 2090 ? 226.479 226.900 254.355 1.00 35.64  ? 2090 LEU A N     1 
ATOM   4408  C  CA    . LEU A 1 2090 ? 225.535 227.081 255.480 1.00 34.27  ? 2090 LEU A CA    1 
ATOM   4409  C  C     . LEU A 1 2090 ? 224.662 225.839 255.588 1.00 36.14  ? 2090 LEU A C     1 
ATOM   4410  O  O     . LEU A 1 2090 ? 224.099 225.632 256.640 1.00 42.90  ? 2090 LEU A O     1 
ATOM   4411  C  CB    . LEU A 1 2090 ? 224.693 228.338 255.292 1.00 39.81  ? 2090 LEU A CB    1 
ATOM   4412  C  CG    . LEU A 1 2090 ? 223.787 228.762 256.443 1.00 42.52  ? 2090 LEU A CG    1 
ATOM   4413  C  CD1   . LEU A 1 2090 ? 224.615 229.050 257.673 1.00 46.52  ? 2090 LEU A CD1   1 
ATOM   4414  C  CD2   . LEU A 1 2090 ? 223.079 230.008 255.966 1.00 47.56  ? 2090 LEU A CD2   1 
ATOM   4415  N  N     . ARG A 1 2091 ? 224.603 225.034 254.543 1.00 29.62  ? 2091 ARG A N     1 
ATOM   4416  C  CA    . ARG A 1 2091 ? 223.826 223.780 254.593 1.00 30.89  ? 2091 ARG A CA    1 
ATOM   4417  C  C     . ARG A 1 2091 ? 224.638 222.758 255.374 1.00 36.08  ? 2091 ARG A C     1 
ATOM   4418  O  O     . ARG A 1 2091 ? 224.045 221.895 255.972 1.00 44.51  ? 2091 ARG A O     1 
ATOM   4419  C  CB    . ARG A 1 2091 ? 223.423 223.396 253.171 1.00 27.75  ? 2091 ARG A CB    1 
ATOM   4420  C  CG    . ARG A 1 2091 ? 222.149 224.051 252.673 1.00 32.20  ? 2091 ARG A CG    1 
ATOM   4421  C  CD    . ARG A 1 2091 ? 221.325 223.017 251.964 1.00 27.74  ? 2091 ARG A CD    1 
ATOM   4422  N  NE    . ARG A 1 2091 ? 220.142 223.597 251.330 1.00 27.27  ? 2091 ARG A NE    1 
ATOM   4423  C  CZ    . ARG A 1 2091 ? 220.204 224.399 250.295 1.00 23.77  ? 2091 ARG A CZ    1 
ATOM   4424  N  NH1   . ARG A 1 2091 ? 221.348 224.585 249.687 1.00 21.32  ? 2091 ARG A NH1   1 
ATOM   4425  N  NH2   . ARG A 1 2091 ? 219.120 224.998 249.870 1.00 32.79  ? 2091 ARG A NH2   1 
ATOM   4426  N  N     . ALA A 1 2092 ? 225.940 222.906 255.408 1.00 40.77  ? 2092 ALA A N     1 
ATOM   4427  C  CA    . ALA A 1 2092 ? 226.825 222.033 256.183 1.00 35.16  ? 2092 ALA A CA    1 
ATOM   4428  C  C     . ALA A 1 2092 ? 226.868 222.521 257.617 1.00 39.60  ? 2092 ALA A C     1 
ATOM   4429  O  O     . ALA A 1 2092 ? 226.774 221.684 258.485 1.00 49.89  ? 2092 ALA A O     1 
ATOM   4430  C  CB    . ALA A 1 2092 ? 228.174 222.107 255.586 1.00 37.83  ? 2092 ALA A CB    1 
ATOM   4431  N  N     . LEU A 1 2093 ? 227.029 223.817 257.855 1.00 38.45  ? 2093 LEU A N     1 
ATOM   4432  C  CA    . LEU A 1 2093 ? 226.953 224.348 259.224 1.00 30.86  ? 2093 LEU A CA    1 
ATOM   4433  C  C     . LEU A 1 2093 ? 225.594 223.930 259.748 1.00 37.29  ? 2093 LEU A C     1 
ATOM   4434  O  O     . LEU A 1 2093 ? 225.545 223.209 260.710 1.00 55.32  ? 2093 LEU A O     1 
ATOM   4435  C  CB    . LEU A 1 2093 ? 227.142 225.857 259.197 1.00 30.92  ? 2093 LEU A CB    1 
ATOM   4436  C  CG    . LEU A 1 2093 ? 227.680 226.511 260.469 1.00 34.54  ? 2093 LEU A CG    1 
ATOM   4437  C  CD1   . LEU A 1 2093 ? 229.155 226.247 260.627 1.00 41.09  ? 2093 LEU A CD1   1 
ATOM   4438  C  CD2   . LEU A 1 2093 ? 227.419 227.992 260.354 1.00 38.92  ? 2093 LEU A CD2   1 
ATOM   4439  N  N     . LYS A 1 2094 ? 224.523 224.313 259.099 1.00 33.15  ? 2094 LYS A N     1 
ATOM   4440  C  CA    . LYS A 1 2094 ? 223.198 223.996 259.659 1.00 33.87  ? 2094 LYS A CA    1 
ATOM   4441  C  C     . LYS A 1 2094 ? 223.078 222.497 259.951 1.00 40.56  ? 2094 LYS A C     1 
ATOM   4442  O  O     . LYS A 1 2094 ? 222.283 222.174 260.810 1.00 51.67  ? 2094 LYS A O     1 
ATOM   4443  C  CB    . LYS A 1 2094 ? 222.073 224.519 258.773 1.00 34.75  ? 2094 LYS A CB    1 
ATOM   4444  C  CG    . LYS A 1 2094 ? 220.685 224.468 259.357 1.00 38.62  ? 2094 LYS A CG    1 
ATOM   4445  C  CD    . LYS A 1 2094 ? 220.154 225.852 259.688 1.00 41.92  ? 2094 LYS A CD    1 
ATOM   4446  C  CE    . LYS A 1 2094 ? 218.706 225.774 260.018 1.00 45.83  ? 2094 LYS A CE    1 
ATOM   4447  N  NZ    . LYS A 1 2094 ? 218.116 224.608 259.359 1.00 45.07  ? 2094 LYS A NZ    1 
ATOM   4448  N  N     . SER A 1 2095 ? 223.753 221.609 259.238 1.00 35.45  ? 2095 SER A N     1 
ATOM   4449  C  CA    . SER A 1 2095 ? 223.584 220.156 259.475 1.00 33.54  ? 2095 SER A CA    1 
ATOM   4450  C  C     . SER A 1 2095 ? 224.469 219.781 260.641 1.00 30.64  ? 2095 SER A C     1 
ATOM   4451  O  O     . SER A 1 2095 ? 224.136 218.850 261.358 1.00 42.39  ? 2095 SER A O     1 
ATOM   4452  C  CB    . SER A 1 2095 ? 223.983 219.356 258.310 1.00 36.66  ? 2095 SER A CB    1 
ATOM   4453  O  OG    . SER A 1 2095 ? 225.389 219.395 258.155 1.00 48.34  ? 2095 SER A OG    1 
ATOM   4454  N  N     . VAL A 1 2096 ? 225.578 220.467 260.781 1.00 34.81  ? 2096 VAL A N     1 
ATOM   4455  C  CA    . VAL A 1 2096 ? 226.475 220.242 261.911 1.00 32.49  ? 2096 VAL A CA    1 
ATOM   4456  C  C     . VAL A 1 2096 ? 225.854 220.758 263.204 1.00 31.19  ? 2096 VAL A C     1 
ATOM   4457  O  O     . VAL A 1 2096 ? 225.931 220.102 264.245 1.00 44.53  ? 2096 VAL A O     1 
ATOM   4458  C  CB    . VAL A 1 2096 ? 227.848 220.884 261.638 1.00 28.80  ? 2096 VAL A CB    1 
ATOM   4459  C  CG1   . VAL A 1 2096 ? 228.614 221.080 262.931 1.00 30.39  ? 2096 VAL A CG1   1 
ATOM   4460  C  CG2   . VAL A 1 2096 ? 228.647 220.024 260.677 1.00 34.16  ? 2096 VAL A CG2   1 
ATOM   4461  N  N     . LEU A 1 2097 ? 225.219 221.931 263.160 1.00 31.40  ? 2097 LEU A N     1 
ATOM   4462  C  CA    . LEU A 1 2097 ? 224.614 222.491 264.367 1.00 34.01  ? 2097 LEU A CA    1 
ATOM   4463  C  C     . LEU A 1 2097 ? 223.415 221.669 264.830 1.00 40.22  ? 2097 LEU A C     1 
ATOM   4464  O  O     . LEU A 1 2097 ? 223.232 221.445 266.035 1.00 45.07  ? 2097 LEU A O     1 
ATOM   4465  C  CB    . LEU A 1 2097 ? 224.205 223.942 264.124 1.00 31.98  ? 2097 LEU A CB    1 
ATOM   4466  C  CG    . LEU A 1 2097 ? 225.327 224.926 263.788 1.00 28.80  ? 2097 LEU A CG    1 
ATOM   4467  C  CD1   . LEU A 1 2097 ? 224.744 226.237 263.297 1.00 32.29  ? 2097 LEU A CD1   1 
ATOM   4468  C  CD2   . LEU A 1 2097 ? 226.241 225.151 264.974 1.00 37.23  ? 2097 LEU A CD2   1 
ATOM   4469  N  N     . VAL A 1 2098 ? 222.579 221.220 263.891 1.00 39.94  ? 2098 VAL A N     1 
ATOM   4470  C  CA    . VAL A 1 2098 ? 221.444 220.379 264.262 1.00 40.08  ? 2098 VAL A CA    1 
ATOM   4471  C  C     . VAL A 1 2098 ? 221.929 219.068 264.869 1.00 37.62  ? 2098 VAL A C     1 
ATOM   4472  O  O     . VAL A 1 2098 ? 221.397 218.597 265.885 1.00 47.89  ? 2098 VAL A O     1 
ATOM   4473  C  CB    . VAL A 1 2098 ? 220.536 220.145 263.041 1.00 38.93  ? 2098 VAL A CB    1 
ATOM   4474  C  CG1   . VAL A 1 2098 ? 219.483 219.101 263.354 1.00 42.36  ? 2098 VAL A CG1   1 
ATOM   4475  C  CG2   . VAL A 1 2098 ? 219.884 221.448 262.616 1.00 32.78  ? 2098 VAL A CG2   1 
ATOM   4476  N  N     . SER A 1 2099 ? 222.953 218.462 264.264 1.00 27.98  ? 2099 SER A N     1 
ATOM   4477  C  CA    . SER A 1 2099 ? 223.533 217.253 264.829 1.00 35.09  ? 2099 SER A CA    1 
ATOM   4478  C  C     . SER A 1 2099 ? 224.147 217.514 266.198 1.00 41.71  ? 2099 SER A C     1 
ATOM   4479  O  O     . SER A 1 2099 ? 224.108 216.638 267.062 1.00 45.32  ? 2099 SER A O     1 
ATOM   4480  C  CB    . SER A 1 2099 ? 224.577 216.679 263.872 1.00 36.37  ? 2099 SER A CB    1 
ATOM   4481  O  OG    . SER A 1 2099 ? 225.281 215.604 264.467 1.00 46.55  ? 2099 SER A OG    1 
ATOM   4482  N  N     . ALA A 1 2100 ? 224.717 218.701 266.415 1.00 40.72  ? 2100 ALA A N     1 
ATOM   4483  C  CA    . ALA A 1 2100 ? 225.264 219.033 267.726 1.00 32.25  ? 2100 ALA A CA    1 
ATOM   4484  C  C     . ALA A 1 2100 ? 224.169 219.094 268.778 1.00 38.46  ? 2100 ALA A C     1 
ATOM   4485  O  O     . ALA A 1 2100 ? 224.336 218.580 269.890 1.00 53.92  ? 2100 ALA A O     1 
ATOM   4486  C  CB    . ALA A 1 2100 ? 226.022 220.358 267.659 1.00 35.03  ? 2100 ALA A CB    1 
ATOM   4487  N  N     . GLY A 1 2101 ? 223.040 219.718 268.445 1.00 36.16  ? 2101 GLY A N     1 
ATOM   4488  C  CA    . GLY A 1 2101 ? 221.920 219.729 269.372 1.00 37.23  ? 2101 GLY A CA    1 
ATOM   4489  C  C     . GLY A 1 2101 ? 221.410 218.333 269.682 1.00 40.13  ? 2101 GLY A C     1 
ATOM   4490  O  O     . GLY A 1 2101 ? 221.144 217.997 270.843 1.00 44.11  ? 2101 GLY A O     1 
ATOM   4491  N  N     . ASN A 1 2102 ? 221.284 217.493 268.650 1.00 41.69  ? 2102 ASN A N     1 
ATOM   4492  C  CA    . ASN A 1 2102 ? 220.823 216.124 268.868 1.00 39.82  ? 2102 ASN A CA    1 
ATOM   4493  C  C     . ASN A 1 2102 ? 221.812 215.324 269.712 1.00 44.88  ? 2102 ASN A C     1 
ATOM   4494  O  O     . ASN A 1 2102 ? 221.405 214.553 270.589 1.00 53.80  ? 2102 ASN A O     1 
ATOM   4495  C  CB    . ASN A 1 2102 ? 220.578 215.431 267.529 1.00 47.37  ? 2102 ASN A CB    1 
ATOM   4496  C  CG    . ASN A 1 2102 ? 219.283 215.868 266.880 1.00 56.58  ? 2102 ASN A CG    1 
ATOM   4497  O  OD1   . ASN A 1 2102 ? 218.504 216.615 267.469 1.00 55.03  ? 2102 ASN A OD1   1 
ATOM   4498  N  ND2   . ASN A 1 2102 ? 219.044 215.401 265.661 1.00 47.91  ? 2102 ASN A ND2   1 
ATOM   4499  N  N     . VAL A 1 2103 ? 223.112 215.491 269.460 1.00 49.19  ? 2103 VAL A N     1 
ATOM   4500  C  CA    . VAL A 1 2103 ? 224.131 214.779 270.225 1.00 45.72  ? 2103 VAL A CA    1 
ATOM   4501  C  C     . VAL A 1 2103 ? 224.113 215.228 271.679 1.00 49.38  ? 2103 VAL A C     1 
ATOM   4502  O  O     . VAL A 1 2103 ? 224.268 214.413 272.595 1.00 56.66  ? 2103 VAL A O     1 
ATOM   4503  C  CB    . VAL A 1 2103 ? 225.517 214.979 269.583 1.00 40.99  ? 2103 VAL A CB    1 
ATOM   4504  C  CG1   . VAL A 1 2103 ? 226.619 214.605 270.555 1.00 40.27  ? 2103 VAL A CG1   1 
ATOM   4505  C  CG2   . VAL A 1 2103 ? 225.635 214.154 268.317 1.00 49.07  ? 2103 VAL A CG2   1 
ATOM   4506  N  N     . LYS A 1 2104 ? 223.929 216.528 271.917 1.00 45.50  ? 2104 LYS A N     1 
ATOM   4507  C  CA    . LYS A 1 2104 ? 223.836 217.015 273.288 1.00 42.74  ? 2104 LYS A CA    1 
ATOM   4508  C  C     . LYS A 1 2104 ? 222.625 216.426 274.003 1.00 46.20  ? 2104 LYS A C     1 
ATOM   4509  O  O     . LYS A 1 2104 ? 222.723 216.013 275.165 1.00 52.99  ? 2104 LYS A O     1 
ATOM   4510  C  CB    . LYS A 1 2104 ? 223.775 218.540 273.302 1.00 43.43  ? 2104 LYS A CB    1 
ATOM   4511  C  CG    . LYS A 1 2104 ? 224.054 219.147 274.661 1.00 49.17  ? 2104 LYS A CG    1 
ATOM   4512  C  CD    . LYS A 1 2104 ? 223.910 220.652 274.635 1.00 48.57  ? 2104 LYS A CD    1 
ATOM   4513  C  CE    . LYS A 1 2104 ? 222.452 221.058 274.620 1.00 46.60  ? 2104 LYS A CE    1 
ATOM   4514  N  NZ    . LYS A 1 2104 ? 221.790 220.771 275.917 1.00 49.12  ? 2104 LYS A NZ    1 
ATOM   4515  N  N     . ARG A 1 2105 ? 221.475 216.377 273.325 1.00 49.49  ? 2105 ARG A N     1 
ATOM   4516  C  CA    . ARG A 1 2105 ? 220.292 215.780 273.943 1.00 49.06  ? 2105 ARG A CA    1 
ATOM   4517  C  C     . ARG A 1 2105 ? 220.514 214.303 274.255 1.00 50.55  ? 2105 ARG A C     1 
ATOM   4518  O  O     . ARG A 1 2105 ? 220.156 213.824 275.340 1.00 59.99  ? 2105 ARG A O     1 
ATOM   4519  C  CB    . ARG A 1 2105 ? 219.077 215.958 273.034 1.00 55.42  ? 2105 ARG A CB    1 
ATOM   4520  C  CG    . ARG A 1 2105 ? 218.284 217.224 273.305 1.00 56.34  ? 2105 ARG A CG    1 
ATOM   4521  C  CD    . ARG A 1 2105 ? 216.981 217.244 272.521 1.00 58.96  ? 2105 ARG A CD    1 
ATOM   4522  N  NE    . ARG A 1 2105 ? 217.177 217.621 271.127 1.00 60.88  ? 2105 ARG A NE    1 
ATOM   4523  C  CZ    . ARG A 1 2105 ? 217.430 218.855 270.710 1.00 63.82  ? 2105 ARG A CZ    1 
ATOM   4524  N  NH1   . ARG A 1 2105 ? 217.535 219.865 271.558 1.00 55.10  ? 2105 ARG A NH1   1 
ATOM   4525  N  NH2   . ARG A 1 2105 ? 217.579 219.082 269.408 1.00 61.47  ? 2105 ARG A NH2   1 
ATOM   4526  N  N     . GLU A 1 2106 ? 221.114 213.568 273.315 1.00 56.63  ? 2106 GLU A N     1 
ATOM   4527  C  CA    . GLU A 1 2106 ? 221.380 212.151 273.534 1.00 57.21  ? 2106 GLU A CA    1 
ATOM   4528  C  C     . GLU A 1 2106 ? 222.345 211.942 274.694 1.00 61.49  ? 2106 GLU A C     1 
ATOM   4529  O  O     . GLU A 1 2106 ? 222.162 211.025 275.502 1.00 66.71  ? 2106 GLU A O     1 
ATOM   4530  C  CB    . GLU A 1 2106 ? 221.931 211.519 272.255 1.00 56.16  ? 2106 GLU A CB    1 
ATOM   4531  C  CG    . GLU A 1 2106 ? 222.028 210.000 272.293 1.00 62.68  ? 2106 GLU A CG    1 
ATOM   4532  C  CD    . GLU A 1 2106 ? 223.329 209.505 272.901 1.00 69.51  ? 2106 GLU A CD    1 
ATOM   4533  O  OE1   . GLU A 1 2106 ? 224.290 210.298 272.977 1.00 69.40  ? 2106 GLU A OE1   1 
ATOM   4534  O  OE2   . GLU A 1 2106 ? 223.387 208.325 273.306 1.00 64.33  ? 2106 GLU A OE2   1 
ATOM   4535  N  N     . ARG A 1 2107 ? 223.381 212.777 274.792 1.00 56.21  ? 2107 ARG A N     1 
ATOM   4536  C  CA    . ARG A 1 2107 ? 224.343 212.628 275.877 1.00 54.12  ? 2107 ARG A CA    1 
ATOM   4537  C  C     . ARG A 1 2107 ? 223.716 212.967 277.222 1.00 61.62  ? 2107 ARG A C     1 
ATOM   4538  O  O     . ARG A 1 2107 ? 224.028 212.330 278.233 1.00 65.35  ? 2107 ARG A O     1 
ATOM   4539  C  CB    . ARG A 1 2107 ? 225.571 213.496 275.616 1.00 57.26  ? 2107 ARG A CB    1 
ATOM   4540  C  CG    . ARG A 1 2107 ? 226.779 213.104 276.444 1.00 63.42  ? 2107 ARG A CG    1 
ATOM   4541  C  CD    . ARG A 1 2107 ? 228.059 213.668 275.861 1.00 61.49  ? 2107 ARG A CD    1 
ATOM   4542  N  NE    . ARG A 1 2107 ? 228.277 213.229 274.489 1.00 56.87  ? 2107 ARG A NE    1 
ATOM   4543  C  CZ    . ARG A 1 2107 ? 229.409 213.403 273.821 1.00 59.56  ? 2107 ARG A CZ    1 
ATOM   4544  N  NH1   . ARG A 1 2107 ? 230.447 214.011 274.367 1.00 62.08  ? 2107 ARG A NH1   1 
ATOM   4545  N  NH2   . ARG A 1 2107 ? 229.501 212.954 272.573 1.00 60.18  ? 2107 ARG A NH2   1 
ATOM   4546  N  N     . ILE A 1 2108 ? 222.831 213.965 277.258 1.00 67.36  ? 2108 ILE A N     1 
ATOM   4547  C  CA    . ILE A 1 2108 ? 222.123 214.271 278.498 1.00 61.24  ? 2108 ILE A CA    1 
ATOM   4548  C  C     . ILE A 1 2108 ? 221.249 213.094 278.918 1.00 63.08  ? 2108 ILE A C     1 
ATOM   4549  O  O     . ILE A 1 2108 ? 221.210 212.721 280.098 1.00 73.54  ? 2108 ILE A O     1 
ATOM   4550  C  CB    . ILE A 1 2108 ? 221.303 215.563 278.338 1.00 63.43  ? 2108 ILE A CB    1 
ATOM   4551  C  CG1   . ILE A 1 2108 ? 222.225 216.783 278.372 1.00 61.28  ? 2108 ILE A CG1   1 
ATOM   4552  C  CG2   . ILE A 1 2108 ? 220.245 215.665 279.421 1.00 65.08  ? 2108 ILE A CG2   1 
ATOM   4553  C  CD1   . ILE A 1 2108 ? 221.530 218.079 278.028 1.00 62.94  ? 2108 ILE A CD1   1 
ATOM   4554  N  N     . GLN A 1 2109 ? 220.543 212.484 277.961 1.00 65.14  ? 2109 GLN A N     1 
ATOM   4555  C  CA    . GLN A 1 2109 ? 219.734 211.312 278.286 1.00 66.74  ? 2109 GLN A CA    1 
ATOM   4556  C  C     . GLN A 1 2109 ? 220.602 210.164 278.790 1.00 70.68  ? 2109 GLN A C     1 
ATOM   4557  O  O     . GLN A 1 2109 ? 220.227 209.455 279.732 1.00 74.37  ? 2109 GLN A O     1 
ATOM   4558  C  CB    . GLN A 1 2109 ? 218.925 210.874 277.065 1.00 68.06  ? 2109 GLN A CB    1 
ATOM   4559  C  CG    . GLN A 1 2109 ? 217.806 211.828 276.676 1.00 72.95  ? 2109 GLN A CG    1 
ATOM   4560  C  CD    . GLN A 1 2109 ? 216.939 212.236 277.850 1.00 77.78  ? 2109 GLN A CD    1 
ATOM   4561  O  OE1   . GLN A 1 2109 ? 216.602 211.418 278.706 1.00 75.40  ? 2109 GLN A OE1   1 
ATOM   4562  N  NE2   . GLN A 1 2109 ? 216.575 213.512 277.897 1.00 73.06  ? 2109 GLN A NE2   1 
ATOM   4563  N  N     . LYS A 1 2110 ? 221.765 209.962 278.167 1.00 76.14  ? 2110 LYS A N     1 
ATOM   4564  C  CA    . LYS A 1 2110 ? 222.671 208.904 278.604 1.00 74.09  ? 2110 LYS A CA    1 
ATOM   4565  C  C     . LYS A 1 2110 ? 223.177 209.157 280.018 1.00 74.40  ? 2110 LYS A C     1 
ATOM   4566  O  O     . LYS A 1 2110 ? 223.275 208.225 280.824 1.00 78.53  ? 2110 LYS A O     1 
ATOM   4567  C  CB    . LYS A 1 2110 ? 223.841 208.781 277.629 1.00 73.97  ? 2110 LYS A CB    1 
ATOM   4568  C  CG    . LYS A 1 2110 ? 224.811 207.664 277.964 1.00 77.42  ? 2110 LYS A CG    1 
ATOM   4569  C  CD    . LYS A 1 2110 ? 225.950 207.606 276.963 1.00 79.23  ? 2110 LYS A CD    1 
ATOM   4570  C  CE    . LYS A 1 2110 ? 226.851 206.411 277.226 1.00 78.21  ? 2110 LYS A CE    1 
ATOM   4571  N  NZ    . LYS A 1 2110 ? 227.564 206.529 278.528 1.00 77.19  ? 2110 LYS A NZ    1 
ATOM   4572  N  N     . ILE A 1 2111 ? 223.512 210.409 280.336 1.00 74.94  ? 2111 ILE A N     1 
ATOM   4573  C  CA    . ILE A 1 2111 ? 223.961 210.735 281.688 1.00 74.70  ? 2111 ILE A CA    1 
ATOM   4574  C  C     . ILE A 1 2111 ? 222.841 210.503 282.692 1.00 76.61  ? 2111 ILE A C     1 
ATOM   4575  O  O     . ILE A 1 2111 ? 223.079 210.027 283.807 1.00 77.03  ? 2111 ILE A O     1 
ATOM   4576  C  CB    . ILE A 1 2111 ? 224.493 212.179 281.753 1.00 73.14  ? 2111 ILE A CB    1 
ATOM   4577  C  CG1   . ILE A 1 2111 ? 225.722 212.339 280.859 1.00 75.95  ? 2111 ILE A CG1   1 
ATOM   4578  C  CG2   . ILE A 1 2111 ? 224.831 212.564 283.181 1.00 71.99  ? 2111 ILE A CG2   1 
ATOM   4579  C  CD1   . ILE A 1 2111 ? 226.149 213.774 280.664 1.00 76.19  ? 2111 ILE A CD1   1 
ATOM   4580  N  N     . LYS A 1 2112 ? 221.602 210.834 282.318 1.00 81.45  ? 2112 LYS A N     1 
ATOM   4581  C  CA    . LYS A 1 2112 ? 220.477 210.566 283.211 1.00 79.09  ? 2112 LYS A CA    1 
ATOM   4582  C  C     . LYS A 1 2112 ? 220.310 209.071 283.458 1.00 83.79  ? 2112 LYS A C     1 
ATOM   4583  O  O     . LYS A 1 2112 ? 220.080 208.643 284.597 1.00 85.47  ? 2112 LYS A O     1 
ATOM   4584  C  CB    . LYS A 1 2112 ? 219.192 211.163 282.640 1.00 78.47  ? 2112 LYS A CB    1 
ATOM   4585  C  CG    . LYS A 1 2112 ? 219.144 212.677 282.699 1.00 82.49  ? 2112 LYS A CG    1 
ATOM   4586  C  CD    . LYS A 1 2112 ? 217.811 213.212 282.207 1.00 81.94  ? 2112 LYS A CD    1 
ATOM   4587  C  CE    . LYS A 1 2112 ? 217.796 214.729 282.231 1.00 81.71  ? 2112 LYS A CE    1 
ATOM   4588  N  NZ    . LYS A 1 2112 ? 218.737 215.264 283.251 1.00 83.65  ? 2112 LYS A NZ    1 
ATOM   4589  N  N     . ARG A 1 2113 ? 220.429 208.258 282.406 1.00 91.03  ? 2113 ARG A N     1 
ATOM   4590  C  CA    . ARG A 1 2113 ? 220.331 206.810 282.584 1.00 87.69  ? 2113 ARG A CA    1 
ATOM   4591  C  C     . ARG A 1 2113 ? 221.459 206.281 283.463 1.00 86.70  ? 2113 ARG A C     1 
ATOM   4592  O  O     . ARG A 1 2113 ? 221.238 205.409 284.312 1.00 87.12  ? 2113 ARG A O     1 
ATOM   4593  C  CB    . ARG A 1 2113 ? 220.331 206.102 281.230 1.00 87.71  ? 2113 ARG A CB    1 
ATOM   4594  C  CG    . ARG A 1 2113 ? 219.152 206.451 280.340 1.00 87.49  ? 2113 ARG A CG    1 
ATOM   4595  C  CD    . ARG A 1 2113 ? 219.180 205.641 279.053 1.00 88.93  ? 2113 ARG A CD    1 
ATOM   4596  N  NE    . ARG A 1 2113 ? 220.441 205.789 278.336 1.00 91.81  ? 2113 ARG A NE    1 
ATOM   4597  C  CZ    . ARG A 1 2113 ? 221.296 204.800 278.113 1.00 91.34  ? 2113 ARG A CZ    1 
ATOM   4598  N  NH1   . ARG A 1 2113 ? 221.064 203.574 278.552 1.00 90.20  ? 2113 ARG A NH1   1 
ATOM   4599  N  NH2   . ARG A 1 2113 ? 222.413 205.048 277.434 1.00 89.38  ? 2113 ARG A NH2   1 
ATOM   4600  N  N     . GLU A 1 2114 ? 222.678 206.790 283.270 1.00 91.41  ? 2114 GLU A N     1 
ATOM   4601  C  CA    . GLU A 1 2114 ? 223.801 206.348 284.092 1.00 92.63  ? 2114 GLU A CA    1 
ATOM   4602  C  C     . GLU A 1 2114 ? 223.611 206.749 285.549 1.00 93.83  ? 2114 GLU A C     1 
ATOM   4603  O  O     . GLU A 1 2114 ? 223.967 205.992 286.460 1.00 92.32  ? 2114 GLU A O     1 
ATOM   4604  C  CB    . GLU A 1 2114 ? 225.112 206.912 283.544 1.00 92.45  ? 2114 GLU A CB    1 
ATOM   4605  C  CG    . GLU A 1 2114 ? 225.481 206.369 282.178 1.00 95.49  ? 2114 GLU A CG    1 
ATOM   4606  C  CD    . GLU A 1 2114 ? 225.804 204.889 282.210 1.00 98.00  ? 2114 GLU A CD    1 
ATOM   4607  O  OE1   . GLU A 1 2114 ? 226.322 204.413 283.242 1.00 98.13  ? 2114 GLU A OE1   1 
ATOM   4608  O  OE2   . GLU A 1 2114 ? 225.531 204.200 281.205 1.00 94.48  ? 2114 GLU A OE2   1 
ATOM   4609  N  N     . LYS A 1 2115 ? 223.064 207.942 285.789 1.00 94.31  ? 2115 LYS A N     1 
ATOM   4610  C  CA    . LYS A 1 2115 ? 222.752 208.351 287.154 1.00 93.65  ? 2115 LYS A CA    1 
ATOM   4611  C  C     . LYS A 1 2115 ? 221.678 207.458 287.759 1.00 92.69  ? 2115 LYS A C     1 
ATOM   4612  O  O     . LYS A 1 2115 ? 221.702 207.175 288.961 1.00 92.93  ? 2115 LYS A O     1 
ATOM   4613  C  CB    . LYS A 1 2115 ? 222.316 209.815 287.183 1.00 94.38  ? 2115 LYS A CB    1 
ATOM   4614  C  CG    . LYS A 1 2115 ? 223.458 210.806 287.031 1.00 93.67  ? 2115 LYS A CG    1 
ATOM   4615  C  CD    . LYS A 1 2115 ? 222.957 212.238 287.110 1.00 94.08  ? 2115 LYS A CD    1 
ATOM   4616  C  CE    . LYS A 1 2115 ? 224.091 213.203 287.420 1.00 92.33  ? 2115 LYS A CE    1 
ATOM   4617  N  NZ    . LYS A 1 2115 ? 223.586 214.554 287.791 1.00 91.26  ? 2115 LYS A NZ    1 
ATOM   4618  N  N     . GLU A 1 2116 ? 220.715 207.019 286.946 1.00 97.38  ? 2116 GLU A N     1 
ATOM   4619  C  CA    . GLU A 1 2116 ? 219.739 206.049 287.433 1.00 97.79  ? 2116 GLU A CA    1 
ATOM   4620  C  C     . GLU A 1 2116 ? 220.410 204.730 287.802 1.00 98.29  ? 2116 GLU A C     1 
ATOM   4621  O  O     . GLU A 1 2116 ? 220.057 204.106 288.810 1.00 94.52  ? 2116 GLU A O     1 
ATOM   4622  C  CB    . GLU A 1 2116 ? 218.644 205.825 286.390 1.00 94.70  ? 2116 GLU A CB    1 
ATOM   4623  C  CG    . GLU A 1 2116 ? 217.754 207.035 286.157 1.00 96.90  ? 2116 GLU A CG    1 
ATOM   4624  C  CD    . GLU A 1 2116 ? 216.785 206.836 285.008 1.00 100.02 ? 2116 GLU A CD    1 
ATOM   4625  O  OE1   . GLU A 1 2116 ? 217.247 206.642 283.864 1.00 99.31  ? 2116 GLU A OE1   1 
ATOM   4626  O  OE2   . GLU A 1 2116 ? 215.561 206.870 285.250 1.00 98.37  ? 2116 GLU A OE2   1 
ATOM   4627  N  N     . GLU A 1 2117 ? 221.376 204.286 286.994 1.00 104.92 ? 2117 GLU A N     1 
ATOM   4628  C  CA    . GLU A 1 2117 ? 222.097 203.055 287.311 1.00 102.96 ? 2117 GLU A CA    1 
ATOM   4629  C  C     . GLU A 1 2117 ? 222.945 203.209 288.569 1.00 103.29 ? 2117 GLU A C     1 
ATOM   4630  O  O     . GLU A 1 2117 ? 223.028 202.283 289.384 1.00 103.93 ? 2117 GLU A O     1 
ATOM   4631  C  CB    . GLU A 1 2117 ? 222.970 202.632 286.129 1.00 102.19 ? 2117 GLU A CB    1 
ATOM   4632  C  CG    . GLU A 1 2117 ? 222.197 202.309 284.864 1.00 103.52 ? 2117 GLU A CG    1 
ATOM   4633  C  CD    . GLU A 1 2117 ? 223.086 202.256 283.636 1.00 105.96 ? 2117 GLU A CD    1 
ATOM   4634  O  OE1   . GLU A 1 2117 ? 224.054 201.466 283.635 1.00 102.76 ? 2117 GLU A OE1   1 
ATOM   4635  O  OE2   . GLU A 1 2117 ? 222.817 203.003 282.672 1.00 107.82 ? 2117 GLU A OE2   1 
ATOM   4636  N  N     . ARG A 1 2118 ? 223.586 204.363 288.742 1.00 103.97 ? 2118 ARG A N     1 
ATOM   4637  C  CA    . ARG A 1 2118 ? 224.439 204.633 289.896 1.00 103.25 ? 2118 ARG A CA    1 
ATOM   4638  C  C     . ARG A 1 2118 ? 223.982 205.936 290.540 1.00 104.59 ? 2118 ARG A C     1 
ATOM   4639  O  O     . ARG A 1 2118 ? 224.246 207.021 290.009 1.00 105.37 ? 2118 ARG A O     1 
ATOM   4640  C  CB    . ARG A 1 2118 ? 225.909 204.711 289.486 1.00 102.20 ? 2118 ARG A CB    1 
ATOM   4641  C  CG    . ARG A 1 2118 ? 226.836 205.168 290.599 1.00 101.82 ? 2118 ARG A CG    1 
ATOM   4642  C  CD    . ARG A 1 2118 ? 228.244 205.413 290.086 1.00 102.92 ? 2118 ARG A CD    1 
ATOM   4643  N  NE    . ARG A 1 2118 ? 229.105 205.972 291.121 1.00 106.21 ? 2118 ARG A NE    1 
ATOM   4644  C  CZ    . ARG A 1 2118 ? 229.705 207.152 291.040 1.00 105.65 ? 2118 ARG A CZ    1 
ATOM   4645  N  NH1   . ARG A 1 2118 ? 229.569 207.926 289.976 1.00 103.58 ? 2118 ARG A NH1   1 
ATOM   4646  N  NH2   . ARG A 1 2118 ? 230.461 207.566 292.053 1.00 102.84 ? 2118 ARG A NH2   1 
ATOM   4647  N  N     . GLY A 1 2119 ? 223.315 205.832 291.682 1.00 93.86  ? 2119 GLY A N     1 
ATOM   4648  C  CA    . GLY A 1 2119 ? 222.791 207.001 292.360 1.00 93.40  ? 2119 GLY A CA    1 
ATOM   4649  C  C     . GLY A 1 2119 ? 221.336 207.258 292.019 1.00 96.15  ? 2119 GLY A C     1 
ATOM   4650  O  O     . GLY A 1 2119 ? 220.658 206.454 291.372 1.00 94.95  ? 2119 GLY A O     1 
ATOM   4651  N  N     . GLU A 1 2120 ? 220.840 208.400 292.498 1.00 94.42  ? 2120 GLU A N     1 
ATOM   4652  C  CA    . GLU A 1 2120 ? 219.471 208.809 292.204 1.00 94.97  ? 2120 GLU A CA    1 
ATOM   4653  C  C     . GLU A 1 2120 ? 219.388 210.284 291.830 1.00 91.01  ? 2120 GLU A C     1 
ATOM   4654  O  O     . GLU A 1 2120 ? 218.429 210.710 291.179 1.00 88.51  ? 2120 GLU A O     1 
ATOM   4655  C  CB    . GLU A 1 2120 ? 218.558 208.521 293.398 1.00 92.77  ? 2120 GLU A CB    1 
ATOM   4656  C  CG    . GLU A 1 2120 ? 218.367 207.044 293.700 1.00 92.20  ? 2120 GLU A CG    1 
ATOM   4657  C  CD    . GLU A 1 2120 ? 217.391 206.804 294.833 1.00 92.32  ? 2120 GLU A CD    1 
ATOM   4658  O  OE1   . GLU A 1 2120 ? 216.217 207.211 294.702 1.00 90.41  ? 2120 GLU A OE1   1 
ATOM   4659  O  OE2   . GLU A 1 2120 ? 217.795 206.211 295.854 1.00 92.81  ? 2120 GLU A OE2   1 
ATOM   4660  N  N     . ALA A 1 2121 ? 220.383 211.069 292.234 1.00 88.66  ? 2121 ALA A N     1 
ATOM   4661  C  CA    . ALA A 1 2121 ? 220.311 212.515 292.064 1.00 91.63  ? 2121 ALA A CA    1 
ATOM   4662  C  C     . ALA A 1 2121 ? 220.538 212.903 290.610 1.00 92.57  ? 2121 ALA A C     1 
ATOM   4663  O  O     . ALA A 1 2121 ? 221.631 212.708 290.067 1.00 89.32  ? 2121 ALA A O     1 
ATOM   4664  C  CB    . ALA A 1 2121 ? 221.337 213.199 292.965 1.00 87.82  ? 2121 ALA A CB    1 
ATOM   4665  N  N     . VAL A 1 2122 ? 219.504 213.459 289.982 1.00 92.13  ? 2122 VAL A N     1 
ATOM   4666  C  CA    . VAL A 1 2122 ? 219.596 213.943 288.610 1.00 88.64  ? 2122 VAL A CA    1 
ATOM   4667  C  C     . VAL A 1 2122 ? 219.399 215.453 288.608 1.00 88.47  ? 2122 VAL A C     1 
ATOM   4668  O  O     . VAL A 1 2122 ? 218.266 215.943 288.550 1.00 88.39  ? 2122 VAL A O     1 
ATOM   4669  C  CB    . VAL A 1 2122 ? 218.567 213.249 287.698 1.00 88.47  ? 2122 VAL A CB    1 
ATOM   4670  C  CG1   . VAL A 1 2122 ? 218.736 213.709 286.259 1.00 87.15  ? 2122 VAL A CG1   1 
ATOM   4671  C  CG2   . VAL A 1 2122 ? 218.699 211.738 287.799 1.00 87.90  ? 2122 VAL A CG2   1 
ATOM   4672  N  N     . ASP A 1 2123 ? 220.499 216.199 288.680 1.00 95.80  ? 2123 ASP A N     1 
ATOM   4673  C  CA    . ASP A 1 2123 ? 220.444 217.657 288.670 1.00 94.27  ? 2123 ASP A CA    1 
ATOM   4674  C  C     . ASP A 1 2123 ? 220.766 218.149 287.265 1.00 95.88  ? 2123 ASP A C     1 
ATOM   4675  O  O     . ASP A 1 2123 ? 221.912 218.055 286.813 1.00 96.63  ? 2123 ASP A O     1 
ATOM   4676  C  CB    . ASP A 1 2123 ? 221.413 218.238 289.695 1.00 93.19  ? 2123 ASP A CB    1 
ATOM   4677  C  CG    . ASP A 1 2123 ? 221.320 219.748 289.793 1.00 95.66  ? 2123 ASP A CG    1 
ATOM   4678  O  OD1   . ASP A 1 2123 ? 220.189 220.270 289.880 1.00 95.47  ? 2123 ASP A OD1   1 
ATOM   4679  O  OD2   . ASP A 1 2123 ? 222.376 220.412 289.786 1.00 95.82  ? 2123 ASP A OD2   1 
ATOM   4680  N  N     . GLU A 1 2124 ? 219.753 218.675 286.572 1.00 93.72  ? 2124 GLU A N     1 
ATOM   4681  C  CA    . GLU A 1 2124 ? 219.944 219.119 285.196 1.00 92.81  ? 2124 GLU A CA    1 
ATOM   4682  C  C     . GLU A 1 2124 ? 220.906 220.296 285.106 1.00 92.36  ? 2124 GLU A C     1 
ATOM   4683  O  O     . GLU A 1 2124 ? 221.641 220.417 284.120 1.00 95.21  ? 2124 GLU A O     1 
ATOM   4684  C  CB    . GLU A 1 2124 ? 218.595 219.472 284.575 1.00 90.67  ? 2124 GLU A CB    1 
ATOM   4685  C  CG    . GLU A 1 2124 ? 217.770 218.253 284.204 1.00 92.65  ? 2124 GLU A CG    1 
ATOM   4686  C  CD    . GLU A 1 2124 ? 216.297 218.563 284.051 1.00 95.92  ? 2124 GLU A CD    1 
ATOM   4687  O  OE1   . GLU A 1 2124 ? 215.857 219.621 284.546 1.00 94.87  ? 2124 GLU A OE1   1 
ATOM   4688  O  OE2   . GLU A 1 2124 ? 215.579 217.751 283.432 1.00 94.49  ? 2124 GLU A OE2   1 
ATOM   4689  N  N     . GLY A 1 2125 ? 220.920 221.168 286.115 1.00 89.48  ? 2125 GLY A N     1 
ATOM   4690  C  CA    . GLY A 1 2125 ? 221.878 222.261 286.114 1.00 89.48  ? 2125 GLY A CA    1 
ATOM   4691  C  C     . GLY A 1 2125 ? 223.314 221.775 286.176 1.00 91.92  ? 2125 GLY A C     1 
ATOM   4692  O  O     . GLY A 1 2125 ? 224.179 222.274 285.452 1.00 93.65  ? 2125 GLY A O     1 
ATOM   4693  N  N     . GLU A 1 2126 ? 223.585 220.792 287.037 1.00 93.14  ? 2126 GLU A N     1 
ATOM   4694  C  CA    . GLU A 1 2126 ? 224.927 220.224 287.114 1.00 92.93  ? 2126 GLU A CA    1 
ATOM   4695  C  C     . GLU A 1 2126 ? 225.282 219.475 285.836 1.00 92.78  ? 2126 GLU A C     1 
ATOM   4696  O  O     . GLU A 1 2126 ? 226.431 219.520 285.383 1.00 94.47  ? 2126 GLU A O     1 
ATOM   4697  C  CB    . GLU A 1 2126 ? 225.036 219.302 288.328 1.00 93.29  ? 2126 GLU A CB    1 
ATOM   4698  C  CG    . GLU A 1 2126 ? 226.330 218.507 288.401 1.00 94.72  ? 2126 GLU A CG    1 
ATOM   4699  C  CD    . GLU A 1 2126 ? 226.155 217.171 289.097 1.00 95.94  ? 2126 GLU A CD    1 
ATOM   4700  O  OE1   . GLU A 1 2126 ? 225.011 216.842 289.476 1.00 94.28  ? 2126 GLU A OE1   1 
ATOM   4701  O  OE2   . GLU A 1 2126 ? 227.160 216.451 289.264 1.00 94.76  ? 2126 GLU A OE2   1 
ATOM   4702  N  N     . ILE A 1 2127 ? 224.309 218.779 285.244 1.00 86.91  ? 2127 ILE A N     1 
ATOM   4703  C  CA    . ILE A 1 2127 ? 224.559 218.052 284.002 1.00 88.41  ? 2127 ILE A CA    1 
ATOM   4704  C  C     . ILE A 1 2127 ? 224.939 219.021 282.890 1.00 89.72  ? 2127 ILE A C     1 
ATOM   4705  O  O     . ILE A 1 2127 ? 225.896 218.792 282.141 1.00 91.94  ? 2127 ILE A O     1 
ATOM   4706  C  CB    . ILE A 1 2127 ? 223.332 217.205 283.621 1.00 86.46  ? 2127 ILE A CB    1 
ATOM   4707  C  CG1   . ILE A 1 2127 ? 223.161 216.044 284.600 1.00 87.68  ? 2127 ILE A CG1   1 
ATOM   4708  C  CG2   . ILE A 1 2127 ? 223.460 216.684 282.200 1.00 86.57  ? 2127 ILE A CG2   1 
ATOM   4709  C  CD1   . ILE A 1 2127 ? 221.927 215.215 284.348 1.00 86.44  ? 2127 ILE A CD1   1 
ATOM   4710  N  N     . ALA A 1 2128 ? 224.198 220.124 282.771 1.00 86.46  ? 2128 ALA A N     1 
ATOM   4711  C  CA    . ALA A 1 2128 ? 224.510 221.115 281.747 1.00 83.99  ? 2128 ALA A CA    1 
ATOM   4712  C  C     . ALA A 1 2128 ? 225.819 221.836 282.039 1.00 84.60  ? 2128 ALA A C     1 
ATOM   4713  O  O     . ALA A 1 2128 ? 226.546 222.194 281.105 1.00 85.83  ? 2128 ALA A O     1 
ATOM   4714  C  CB    . ALA A 1 2128 ? 223.366 222.119 281.620 1.00 82.63  ? 2128 ALA A CB    1 
ATOM   4715  N  N     . GLU A 1 2129 ? 226.134 222.063 283.316 1.00 91.10  ? 2129 GLU A N     1 
ATOM   4716  C  CA    . GLU A 1 2129 ? 227.378 222.743 283.666 1.00 92.97  ? 2129 GLU A CA    1 
ATOM   4717  C  C     . GLU A 1 2129 ? 228.593 221.933 283.231 1.00 93.96  ? 2129 GLU A C     1 
ATOM   4718  O  O     . GLU A 1 2129 ? 229.483 222.445 282.542 1.00 95.68  ? 2129 GLU A O     1 
ATOM   4719  C  CB    . GLU A 1 2129 ? 227.422 223.004 285.171 1.00 92.90  ? 2129 GLU A CB    1 
ATOM   4720  C  CG    . GLU A 1 2129 ? 228.444 224.045 285.594 1.00 94.22  ? 2129 GLU A CG    1 
ATOM   4721  C  CD    . GLU A 1 2129 ? 228.660 224.070 287.094 1.00 96.90  ? 2129 GLU A CD    1 
ATOM   4722  O  OE1   . GLU A 1 2129 ? 227.957 223.326 287.809 1.00 95.82  ? 2129 GLU A OE1   1 
ATOM   4723  O  OE2   . GLU A 1 2129 ? 229.537 224.828 287.558 1.00 95.88  ? 2129 GLU A OE2   1 
ATOM   4724  N  N     . ASN A 1 2130 ? 228.646 220.665 283.623 1.00 86.53  ? 2130 ASN A N     1 
ATOM   4725  C  CA    . ASN A 1 2130 ? 229.785 219.799 283.317 1.00 88.38  ? 2130 ASN A CA    1 
ATOM   4726  C  C     . ASN A 1 2130 ? 229.491 218.944 282.086 1.00 89.92  ? 2130 ASN A C     1 
ATOM   4727  O  O     . ASN A 1 2130 ? 229.227 217.745 282.172 1.00 91.68  ? 2130 ASN A O     1 
ATOM   4728  C  CB    . ASN A 1 2130 ? 230.124 218.933 284.525 1.00 91.54  ? 2130 ASN A CB    1 
ATOM   4729  C  CG    . ASN A 1 2130 ? 230.572 219.750 285.719 1.00 94.12  ? 2130 ASN A CG    1 
ATOM   4730  O  OD1   . ASN A 1 2130 ? 229.900 219.782 286.749 1.00 93.85  ? 2130 ASN A OD1   1 
ATOM   4731  N  ND2   . ASN A 1 2130 ? 231.714 220.414 285.588 1.00 92.42  ? 2130 ASN A ND2   1 
ATOM   4732  N  N     . LEU A 1 2131 ? 229.537 219.587 280.923 1.00 79.55  ? 2131 LEU A N     1 
ATOM   4733  C  CA    . LEU A 1 2131 ? 229.236 218.926 279.669 1.00 75.21  ? 2131 LEU A CA    1 
ATOM   4734  C  C     . LEU A 1 2131 ? 230.258 219.329 278.614 1.00 77.39  ? 2131 LEU A C     1 
ATOM   4735  O  O     . LEU A 1 2131 ? 230.468 220.529 278.389 1.00 79.29  ? 2131 LEU A O     1 
ATOM   4736  C  CB    . LEU A 1 2131 ? 227.820 219.286 279.202 1.00 74.35  ? 2131 LEU A CB    1 
ATOM   4737  C  CG    . LEU A 1 2131 ? 227.184 218.417 278.121 1.00 76.16  ? 2131 LEU A CG    1 
ATOM   4738  C  CD1   . LEU A 1 2131 ? 227.060 216.987 278.608 1.00 74.48  ? 2131 LEU A CD1   1 
ATOM   4739  C  CD2   . LEU A 1 2131 ? 225.823 218.970 277.759 1.00 76.01  ? 2131 LEU A CD2   1 
ATOM   4740  N  N     . PRO A 1 2132 ? 230.914 218.371 277.951 1.00 67.58  ? 2132 PRO A N     1 
ATOM   4741  C  CA    . PRO A 1 2132 ? 231.948 218.682 276.938 1.00 64.94  ? 2132 PRO A CA    1 
ATOM   4742  C  C     . PRO A 1 2132 ? 231.363 219.137 275.602 1.00 68.09  ? 2132 PRO A C     1 
ATOM   4743  O  O     . PRO A 1 2132 ? 231.152 218.370 274.665 1.00 73.27  ? 2132 PRO A O     1 
ATOM   4744  C  CB    . PRO A 1 2132 ? 232.700 217.356 276.812 1.00 65.13  ? 2132 PRO A CB    1 
ATOM   4745  C  CG    . PRO A 1 2132 ? 231.676 216.322 277.125 1.00 64.63  ? 2132 PRO A CG    1 
ATOM   4746  C  CD    . PRO A 1 2132 ? 230.748 216.920 278.146 1.00 66.17  ? 2132 PRO A CD    1 
ATOM   4747  N  N     . GLU A 1 2133 ? 231.083 220.439 275.514 1.00 51.82  ? 2133 GLU A N     1 
ATOM   4748  C  CA    . GLU A 1 2133 ? 230.420 220.978 274.332 1.00 48.75  ? 2133 GLU A CA    1 
ATOM   4749  C  C     . GLU A 1 2133 ? 231.334 220.987 273.111 1.00 52.31  ? 2133 GLU A C     1 
ATOM   4750  O  O     . GLU A 1 2133 ? 230.863 220.767 271.988 1.00 60.89  ? 2133 GLU A O     1 
ATOM   4751  C  CB    . GLU A 1 2133 ? 229.899 222.380 274.631 1.00 53.89  ? 2133 GLU A CB    1 
ATOM   4752  C  CG    . GLU A 1 2133 ? 228.601 222.375 275.415 1.00 57.43  ? 2133 GLU A CG    1 
ATOM   4753  C  CD    . GLU A 1 2133 ? 228.515 223.507 276.410 1.00 61.16  ? 2133 GLU A CD    1 
ATOM   4754  O  OE1   . GLU A 1 2133 ? 229.563 224.114 276.710 1.00 65.46  ? 2133 GLU A OE1   1 
ATOM   4755  O  OE2   . GLU A 1 2133 ? 227.400 223.789 276.896 1.00 61.96  ? 2133 GLU A OE2   1 
ATOM   4756  N  N     . GLN A 1 2134 ? 232.630 221.240 273.297 1.00 48.92  ? 2134 GLN A N     1 
ATOM   4757  C  CA    . GLN A 1 2134 ? 233.554 221.158 272.170 1.00 49.43  ? 2134 GLN A CA    1 
ATOM   4758  C  C     . GLN A 1 2134 ? 233.655 219.730 271.652 1.00 51.77  ? 2134 GLN A C     1 
ATOM   4759  O  O     . GLN A 1 2134 ? 233.758 219.507 270.441 1.00 59.98  ? 2134 GLN A O     1 
ATOM   4760  C  CB    . GLN A 1 2134 ? 234.931 221.684 272.572 1.00 45.47  ? 2134 GLN A CB    1 
ATOM   4761  C  CG    . GLN A 1 2134 ? 234.921 223.117 273.060 1.00 50.19  ? 2134 GLN A CG    1 
ATOM   4762  C  CD    . GLN A 1 2134 ? 236.237 223.821 272.825 1.00 53.65  ? 2134 GLN A CD    1 
ATOM   4763  O  OE1   . GLN A 1 2134 ? 237.135 223.284 272.179 1.00 58.29  ? 2134 GLN A OE1   1 
ATOM   4764  N  NE2   . GLN A 1 2134 ? 236.359 225.035 273.346 1.00 56.67  ? 2134 GLN A NE2   1 
ATOM   4765  N  N     . GLU A 1 2135 ? 233.627 218.751 272.558 1.00 49.99  ? 2135 GLU A N     1 
ATOM   4766  C  CA    . GLU A 1 2135 ? 233.612 217.354 272.142 1.00 47.17  ? 2135 GLU A CA    1 
ATOM   4767  C  C     . GLU A 1 2135 ? 232.345 217.026 271.364 1.00 51.38  ? 2135 GLU A C     1 
ATOM   4768  O  O     . GLU A 1 2135 ? 232.391 216.284 270.378 1.00 62.64  ? 2135 GLU A O     1 
ATOM   4769  C  CB    . GLU A 1 2135 ? 233.751 216.448 273.364 1.00 51.26  ? 2135 GLU A CB    1 
ATOM   4770  C  CG    . GLU A 1 2135 ? 233.597 214.969 273.070 1.00 63.50  ? 2135 GLU A CG    1 
ATOM   4771  C  CD    . GLU A 1 2135 ? 233.871 214.107 274.286 1.00 64.96  ? 2135 GLU A CD    1 
ATOM   4772  O  OE1   . GLU A 1 2135 ? 234.766 214.465 275.079 1.00 57.91  ? 2135 GLU A OE1   1 
ATOM   4773  O  OE2   . GLU A 1 2135 ? 233.194 213.070 274.446 1.00 62.32  ? 2135 GLU A OE2   1 
ATOM   4774  N  N     . ILE A 1 2136 ? 231.205 217.576 271.787 1.00 43.16  ? 2136 ILE A N     1 
ATOM   4775  C  CA    . ILE A 1 2136 ? 229.955 217.368 271.061 1.00 40.91  ? 2136 ILE A CA    1 
ATOM   4776  C  C     . ILE A 1 2136 ? 230.045 217.961 269.660 1.00 41.75  ? 2136 ILE A C     1 
ATOM   4777  O  O     . ILE A 1 2136 ? 229.621 217.342 268.674 1.00 53.83  ? 2136 ILE A O     1 
ATOM   4778  C  CB    . ILE A 1 2136 ? 228.781 217.966 271.858 1.00 46.94  ? 2136 ILE A CB    1 
ATOM   4779  C  CG1   . ILE A 1 2136 ? 228.480 217.105 273.084 1.00 48.34  ? 2136 ILE A CG1   1 
ATOM   4780  C  CG2   . ILE A 1 2136 ? 227.552 218.113 270.981 1.00 49.26  ? 2136 ILE A CG2   1 
ATOM   4781  C  CD1   . ILE A 1 2136 ? 227.689 217.818 274.148 1.00 49.81  ? 2136 ILE A CD1   1 
ATOM   4782  N  N     . LEU A 1 2137 ? 230.600 219.169 269.550 1.00 35.50  ? 2137 LEU A N     1 
ATOM   4783  C  CA    . LEU A 1 2137 ? 230.742 219.802 268.243 1.00 40.01  ? 2137 LEU A CA    1 
ATOM   4784  C  C     . LEU A 1 2137 ? 231.680 219.010 267.339 1.00 40.88  ? 2137 LEU A C     1 
ATOM   4785  O  O     . LEU A 1 2137 ? 231.407 218.847 266.143 1.00 49.82  ? 2137 LEU A O     1 
ATOM   4786  C  CB    . LEU A 1 2137 ? 231.237 221.237 268.410 1.00 45.84  ? 2137 LEU A CB    1 
ATOM   4787  C  CG    . LEU A 1 2137 ? 230.775 222.228 267.344 1.00 46.23  ? 2137 LEU A CG    1 
ATOM   4788  C  CD1   . LEU A 1 2137 ? 229.261 222.318 267.321 1.00 45.73  ? 2137 LEU A CD1   1 
ATOM   4789  C  CD2   . LEU A 1 2137 ? 231.390 223.591 267.591 1.00 44.33  ? 2137 LEU A CD2   1 
ATOM   4790  N  N     . ILE A 1 2138 ? 232.790 218.512 267.887 1.00 40.23  ? 2138 ILE A N     1 
ATOM   4791  C  CA    . ILE A 1 2138 ? 233.711 217.704 267.090 1.00 41.23  ? 2138 ILE A CA    1 
ATOM   4792  C  C     . ILE A 1 2138 ? 233.045 216.406 266.654 1.00 42.10  ? 2138 ILE A C     1 
ATOM   4793  O  O     . ILE A 1 2138 ? 233.243 215.940 265.526 1.00 52.14  ? 2138 ILE A O     1 
ATOM   4794  C  CB    . ILE A 1 2138 ? 235.015 217.442 267.867 1.00 45.44  ? 2138 ILE A CB    1 
ATOM   4795  C  CG1   . ILE A 1 2138 ? 235.873 218.703 267.906 1.00 42.71  ? 2138 ILE A CG1   1 
ATOM   4796  C  CG2   . ILE A 1 2138 ? 235.800 216.302 267.247 1.00 45.37  ? 2138 ILE A CG2   1 
ATOM   4797  C  CD1   . ILE A 1 2138 ? 237.168 218.513 268.640 1.00 47.80  ? 2138 ILE A CD1   1 
ATOM   4798  N  N     . GLN A 1 2139 ? 232.249 215.799 267.536 1.00 42.59  ? 2139 GLN A N     1 
ATOM   4799  C  CA    . GLN A 1 2139 ? 231.523 214.592 267.159 1.00 43.11  ? 2139 GLN A CA    1 
ATOM   4800  C  C     . GLN A 1 2139 ? 230.566 214.864 266.008 1.00 48.82  ? 2139 GLN A C     1 
ATOM   4801  O  O     . GLN A 1 2139 ? 230.468 214.064 265.074 1.00 58.56  ? 2139 GLN A O     1 
ATOM   4802  C  CB    . GLN A 1 2139 ? 230.763 214.033 268.358 1.00 44.73  ? 2139 GLN A CB    1 
ATOM   4803  C  CG    . GLN A 1 2139 ? 229.793 212.928 267.989 1.00 46.79  ? 2139 GLN A CG    1 
ATOM   4804  C  CD    . GLN A 1 2139 ? 229.055 212.377 269.184 1.00 53.88  ? 2139 GLN A CD    1 
ATOM   4805  O  OE1   . GLN A 1 2139 ? 229.505 212.513 270.319 1.00 60.50  ? 2139 GLN A OE1   1 
ATOM   4806  N  NE2   . GLN A 1 2139 ? 227.918 211.744 268.936 1.00 50.83  ? 2139 GLN A NE2   1 
ATOM   4807  N  N     . SER A 1 2140 ? 229.851 215.987 266.059 1.00 42.13  ? 2140 SER A N     1 
ATOM   4808  C  CA    . SER A 1 2140 ? 228.944 216.327 264.965 1.00 27.26  ? 2140 SER A CA    1 
ATOM   4809  C  C     . SER A 1 2140 ? 229.702 216.581 263.668 1.00 36.78  ? 2140 SER A C     1 
ATOM   4810  O  O     . SER A 1 2140 ? 229.263 216.158 262.591 1.00 49.74  ? 2140 SER A O     1 
ATOM   4811  C  CB    . SER A 1 2140 ? 228.107 217.540 265.344 1.00 30.29  ? 2140 SER A CB    1 
ATOM   4812  O  OG    . SER A 1 2140 ? 227.301 217.229 266.457 1.00 45.05  ? 2140 SER A OG    1 
ATOM   4813  N  N     . VAL A 1 2141 ? 230.840 217.274 263.751 1.00 35.74  ? 2141 VAL A N     1 
ATOM   4814  C  CA    . VAL A 1 2141 ? 231.644 217.526 262.559 1.00 28.88  ? 2141 VAL A CA    1 
ATOM   4815  C  C     . VAL A 1 2141 ? 232.117 216.213 261.950 1.00 40.49  ? 2141 VAL A C     1 
ATOM   4816  O  O     . VAL A 1 2141 ? 232.065 216.022 260.730 1.00 55.48  ? 2141 VAL A O     1 
ATOM   4817  C  CB    . VAL A 1 2141 ? 232.825 218.454 262.896 1.00 30.52  ? 2141 VAL A CB    1 
ATOM   4818  C  CG1   . VAL A 1 2141 ? 233.899 218.360 261.830 1.00 33.27  ? 2141 VAL A CG1   1 
ATOM   4819  C  CG2   . VAL A 1 2141 ? 232.350 219.884 263.045 1.00 35.64  ? 2141 VAL A CG2   1 
ATOM   4820  N  N     . CYS A 1 2142 ? 232.574 215.284 262.790 1.00 39.66  ? 2142 CYS A N     1 
ATOM   4821  C  CA    . CYS A 1 2142 ? 233.051 214.001 262.289 1.00 33.61  ? 2142 CYS A CA    1 
ATOM   4822  C  C     . CYS A 1 2142 ? 231.913 213.141 261.756 1.00 38.97  ? 2142 CYS A C     1 
ATOM   4823  O  O     . CYS A 1 2142 ? 232.119 212.346 260.834 1.00 52.21  ? 2142 CYS A O     1 
ATOM   4824  C  CB    . CYS A 1 2142 ? 233.808 213.261 263.390 1.00 40.06  ? 2142 CYS A CB    1 
ATOM   4825  S  SG    . CYS A 1 2142 ? 235.361 214.047 263.872 1.00 56.18  ? 2142 CYS A SG    1 
ATOM   4826  N  N     . GLU A 1 2143 ? 230.715 213.275 262.319 1.00 40.57  ? 2143 GLU A N     1 
ATOM   4827  C  CA    . GLU A 1 2143 ? 229.568 212.522 261.836 1.00 36.76  ? 2143 GLU A CA    1 
ATOM   4828  C  C     . GLU A 1 2143 ? 228.942 213.124 260.588 1.00 40.73  ? 2143 GLU A C     1 
ATOM   4829  O  O     . GLU A 1 2143 ? 228.148 212.446 259.931 1.00 49.17  ? 2143 GLU A O     1 
ATOM   4830  C  CB    . GLU A 1 2143 ? 228.505 212.417 262.930 1.00 32.95  ? 2143 GLU A CB    1 
ATOM   4831  C  CG    . GLU A 1 2143 ? 228.864 211.471 264.058 1.00 45.49  ? 2143 GLU A CG    1 
ATOM   4832  C  CD    . GLU A 1 2143 ? 227.718 211.266 265.027 1.00 58.33  ? 2143 GLU A CD    1 
ATOM   4833  O  OE1   . GLU A 1 2143 ? 226.834 212.145 265.100 1.00 53.70  ? 2143 GLU A OE1   1 
ATOM   4834  O  OE2   . GLU A 1 2143 ? 227.701 210.226 265.718 1.00 55.60  ? 2143 GLU A OE2   1 
ATOM   4835  N  N     . THR A 1 2144 ? 229.263 214.368 260.250 1.00 31.95  ? 2144 THR A N     1 
ATOM   4836  C  CA    . THR A 1 2144 ? 228.676 214.996 259.073 1.00 29.72  ? 2144 THR A CA    1 
ATOM   4837  C  C     . THR A 1 2144 ? 229.681 215.282 257.968 1.00 42.79  ? 2144 THR A C     1 
ATOM   4838  O  O     . THR A 1 2144 ? 229.366 215.083 256.792 1.00 48.34  ? 2144 THR A O     1 
ATOM   4839  C  CB    . THR A 1 2144 ? 227.971 216.300 259.469 1.00 44.23  ? 2144 THR A CB    1 
ATOM   4840  O  OG1   . THR A 1 2144 ? 227.140 216.065 260.610 1.00 41.82  ? 2144 THR A OG1   1 
ATOM   4841  C  CG2   . THR A 1 2144 ? 227.099 216.792 258.333 1.00 46.22  ? 2144 THR A CG2   1 
ATOM   4842  N  N     . MET A 1 2145 ? 230.885 215.741 258.306 1.00 39.00  ? 2145 MET A N     1 
ATOM   4843  C  CA    . MET A 1 2145 ? 231.856 216.155 257.298 1.00 31.47  ? 2145 MET A CA    1 
ATOM   4844  C  C     . MET A 1 2145 ? 232.846 215.061 256.928 1.00 40.94  ? 2145 MET A C     1 
ATOM   4845  O  O     . MET A 1 2145 ? 233.299 215.013 255.779 1.00 50.91  ? 2145 MET A O     1 
ATOM   4846  C  CB    . MET A 1 2145 ? 232.627 217.384 257.787 1.00 31.64  ? 2145 MET A CB    1 
ATOM   4847  C  CG    . MET A 1 2145 ? 231.793 218.649 257.917 1.00 41.49  ? 2145 MET A CG    1 
ATOM   4848  S  SD    . MET A 1 2145 ? 231.165 219.241 256.336 1.00 75.00  ? 2145 MET A SD    1 
ATOM   4849  C  CE    . MET A 1 2145 ? 229.455 218.724 256.422 1.00 40.70  ? 2145 MET A CE    1 
ATOM   4850  N  N     . VAL A 1 2146 ? 233.209 214.198 257.879 1.00 37.04  ? 2146 VAL A N     1 
ATOM   4851  C  CA    . VAL A 1 2146 ? 234.196 213.151 257.594 1.00 35.22  ? 2146 VAL A CA    1 
ATOM   4852  C  C     . VAL A 1 2146 ? 233.732 212.171 256.524 1.00 35.13  ? 2146 VAL A C     1 
ATOM   4853  O  O     . VAL A 1 2146 ? 234.548 211.804 255.666 1.00 42.76  ? 2146 VAL A O     1 
ATOM   4854  C  CB    . VAL A 1 2146 ? 234.626 212.464 258.897 1.00 37.15  ? 2146 VAL A CB    1 
ATOM   4855  C  CG1   . VAL A 1 2146 ? 235.270 211.118 258.613 1.00 35.95  ? 2146 VAL A CG1   1 
ATOM   4856  C  CG2   . VAL A 1 2146 ? 235.583 213.355 259.665 1.00 35.80  ? 2146 VAL A CG2   1 
ATOM   4857  N  N     . PRO A 1 2147 ? 232.478 211.695 256.505 1.00 39.28  ? 2147 PRO A N     1 
ATOM   4858  C  CA    . PRO A 1 2147 ? 232.114 210.663 255.515 1.00 37.60  ? 2147 PRO A CA    1 
ATOM   4859  C  C     . PRO A 1 2147 ? 232.390 211.041 254.070 1.00 35.59  ? 2147 PRO A C     1 
ATOM   4860  O  O     . PRO A 1 2147 ? 232.695 210.156 253.263 1.00 43.70  ? 2147 PRO A O     1 
ATOM   4861  C  CB    . PRO A 1 2147 ? 230.613 210.472 255.761 1.00 26.41  ? 2147 PRO A CB    1 
ATOM   4862  C  CG    . PRO A 1 2147 ? 230.449 210.745 257.186 1.00 29.83  ? 2147 PRO A CG    1 
ATOM   4863  C  CD    . PRO A 1 2147 ? 231.406 211.861 257.505 1.00 39.47  ? 2147 PRO A CD    1 
ATOM   4864  N  N     . LYS A 1 2148 ? 232.295 212.318 253.711 1.00 32.96  ? 2148 LYS A N     1 
ATOM   4865  C  CA    . LYS A 1 2148 ? 232.462 212.732 252.326 1.00 26.57  ? 2148 LYS A CA    1 
ATOM   4866  C  C     . LYS A 1 2148 ? 233.912 212.947 251.922 1.00 32.13  ? 2148 LYS A C     1 
ATOM   4867  O  O     . LYS A 1 2148 ? 234.188 213.085 250.726 1.00 38.07  ? 2148 LYS A O     1 
ATOM   4868  C  CB    . LYS A 1 2148 ? 231.684 214.020 252.067 1.00 33.01  ? 2148 LYS A CB    1 
ATOM   4869  C  CG    . LYS A 1 2148 ? 232.373 215.278 252.541 1.00 29.15  ? 2148 LYS A CG    1 
ATOM   4870  C  CD    . LYS A 1 2148 ? 231.460 216.469 252.367 1.00 32.40  ? 2148 LYS A CD    1 
ATOM   4871  C  CE    . LYS A 1 2148 ? 232.114 217.738 252.852 1.00 33.51  ? 2148 LYS A CE    1 
ATOM   4872  N  NZ    . LYS A 1 2148 ? 231.138 218.857 252.893 1.00 36.59  ? 2148 LYS A NZ    1 
ATOM   4873  N  N     . LEU A 1 2149 ? 234.839 212.975 252.872 1.00 37.33  ? 2149 LEU A N     1 
ATOM   4874  C  CA    . LEU A 1 2149 ? 236.218 213.314 252.558 1.00 24.22  ? 2149 LEU A CA    1 
ATOM   4875  C  C     . LEU A 1 2149 ? 236.910 212.182 251.814 1.00 37.55  ? 2149 LEU A C     1 
ATOM   4876  O  O     . LEU A 1 2149 ? 236.670 211.002 252.079 1.00 49.74  ? 2149 LEU A O     1 
ATOM   4877  C  CB    . LEU A 1 2149 ? 236.987 213.641 253.833 1.00 32.56  ? 2149 LEU A CB    1 
ATOM   4878  C  CG    . LEU A 1 2149 ? 236.527 214.882 254.592 1.00 32.60  ? 2149 LEU A CG    1 
ATOM   4879  C  CD1   . LEU A 1 2149 ? 237.454 215.128 255.752 1.00 33.27  ? 2149 LEU A CD1   1 
ATOM   4880  C  CD2   . LEU A 1 2149 ? 236.483 216.087 253.672 1.00 39.42  ? 2149 LEU A CD2   1 
ATOM   4881  N  N     . VAL A 1 2150 ? 237.781 212.555 250.879 1.00 40.71  ? 2150 VAL A N     1 
ATOM   4882  C  CA    . VAL A 1 2150 ? 238.611 211.602 250.154 1.00 38.10  ? 2150 VAL A CA    1 
ATOM   4883  C  C     . VAL A 1 2150 ? 239.793 211.227 251.036 1.00 39.48  ? 2150 VAL A C     1 
ATOM   4884  O  O     . VAL A 1 2150 ? 240.010 211.835 252.089 1.00 46.00  ? 2150 VAL A O     1 
ATOM   4885  C  CB    . VAL A 1 2150 ? 239.075 212.170 248.802 1.00 30.49  ? 2150 VAL A CB    1 
ATOM   4886  C  CG1   . VAL A 1 2150 ? 237.881 212.620 247.982 1.00 32.46  ? 2150 VAL A CG1   1 
ATOM   4887  C  CG2   . VAL A 1 2150 ? 240.031 213.317 249.015 1.00 36.86  ? 2150 VAL A CG2   1 
ATOM   4888  N  N     . ALA A 1 2151 ? 240.556 210.214 250.619 1.00 45.55  ? 2151 ALA A N     1 
ATOM   4889  C  CA    . ALA A 1 2151 ? 241.593 209.654 251.480 1.00 47.87  ? 2151 ALA A CA    1 
ATOM   4890  C  C     . ALA A 1 2151 ? 242.654 210.686 251.844 1.00 50.49  ? 2151 ALA A C     1 
ATOM   4891  O  O     . ALA A 1 2151 ? 243.125 210.723 252.986 1.00 52.12  ? 2151 ALA A O     1 
ATOM   4892  C  CB    . ALA A 1 2151 ? 242.236 208.444 250.805 1.00 46.87  ? 2151 ALA A CB    1 
ATOM   4893  N  N     . GLU A 1 2152 ? 243.051 211.530 250.891 1.00 46.97  ? 2152 GLU A N     1 
ATOM   4894  C  CA    . GLU A 1 2152 ? 244.128 212.478 251.148 1.00 44.73  ? 2152 GLU A CA    1 
ATOM   4895  C  C     . GLU A 1 2152 ? 243.671 213.728 251.888 1.00 46.37  ? 2152 GLU A C     1 
ATOM   4896  O  O     . GLU A 1 2152 ? 244.518 214.528 252.299 1.00 54.70  ? 2152 GLU A O     1 
ATOM   4897  C  CB    . GLU A 1 2152 ? 244.811 212.877 249.837 1.00 45.56  ? 2152 GLU A CB    1 
ATOM   4898  C  CG    . GLU A 1 2152 ? 243.933 213.648 248.867 1.00 49.35  ? 2152 GLU A CG    1 
ATOM   4899  C  CD    . GLU A 1 2152 ? 243.203 212.740 247.895 1.00 57.64  ? 2152 GLU A CD    1 
ATOM   4900  O  OE1   . GLU A 1 2152 ? 243.148 211.517 248.143 1.00 56.48  ? 2152 GLU A OE1   1 
ATOM   4901  O  OE2   . GLU A 1 2152 ? 242.685 213.250 246.880 1.00 53.19  ? 2152 GLU A OE2   1 
ATOM   4902  N  N     . ASP A 1 2153 ? 242.364 213.917 252.074 1.00 42.70  ? 2153 ASP A N     1 
ATOM   4903  C  CA    . ASP A 1 2153 ? 241.851 215.092 252.767 1.00 31.06  ? 2153 ASP A CA    1 
ATOM   4904  C  C     . ASP A 1 2153 ? 241.541 214.846 254.236 1.00 40.03  ? 2153 ASP A C     1 
ATOM   4905  O  O     . ASP A 1 2153 ? 241.417 215.814 254.993 1.00 54.41  ? 2153 ASP A O     1 
ATOM   4906  C  CB    . ASP A 1 2153 ? 240.584 215.607 252.077 1.00 27.68  ? 2153 ASP A CB    1 
ATOM   4907  C  CG    . ASP A 1 2153 ? 240.886 216.400 250.826 1.00 51.16  ? 2153 ASP A CG    1 
ATOM   4908  O  OD1   . ASP A 1 2153 ? 241.976 217.003 250.750 1.00 51.33  ? 2153 ASP A OD1   1 
ATOM   4909  O  OD2   . ASP A 1 2153 ? 240.034 216.421 249.917 1.00 46.91  ? 2153 ASP A OD2   1 
ATOM   4910  N  N     . ILE A 1 2154 ? 241.401 213.587 254.650 1.00 37.80  ? 2154 ILE A N     1 
ATOM   4911  C  CA    . ILE A 1 2154 ? 241.070 213.295 256.046 1.00 38.55  ? 2154 ILE A CA    1 
ATOM   4912  C  C     . ILE A 1 2154 ? 242.136 213.803 257.013 1.00 46.67  ? 2154 ILE A C     1 
ATOM   4913  O  O     . ILE A 1 2154 ? 241.774 214.434 258.021 1.00 53.64  ? 2154 ILE A O     1 
ATOM   4914  C  CB    . ILE A 1 2154 ? 240.779 211.794 256.214 1.00 39.98  ? 2154 ILE A CB    1 
ATOM   4915  C  CG1   . ILE A 1 2154 ? 239.551 211.398 255.397 1.00 43.46  ? 2154 ILE A CG1   1 
ATOM   4916  C  CG2   . ILE A 1 2154 ? 240.577 211.445 257.668 1.00 36.43  ? 2154 ILE A CG2   1 
ATOM   4917  C  CD1   . ILE A 1 2154 ? 239.208 209.936 255.493 1.00 45.64  ? 2154 ILE A CD1   1 
ATOM   4918  N  N     . PRO A 1 2155 ? 243.437 213.564 256.794 1.00 47.55  ? 2155 PRO A N     1 
ATOM   4919  C  CA    . PRO A 1 2155 ? 244.433 214.140 257.710 1.00 43.19  ? 2155 PRO A CA    1 
ATOM   4920  C  C     . PRO A 1 2155 ? 244.376 215.651 257.787 1.00 41.96  ? 2155 PRO A C     1 
ATOM   4921  O  O     . PRO A 1 2155 ? 244.587 216.214 258.867 1.00 45.84  ? 2155 PRO A O     1 
ATOM   4922  C  CB    . PRO A 1 2155 ? 245.767 213.659 257.123 1.00 42.28  ? 2155 PRO A CB    1 
ATOM   4923  C  CG    . PRO A 1 2155 ? 245.425 212.439 256.373 1.00 41.03  ? 2155 PRO A CG    1 
ATOM   4924  C  CD    . PRO A 1 2155 ? 244.078 212.699 255.787 1.00 45.62  ? 2155 PRO A CD    1 
ATOM   4925  N  N     . LEU A 1 2156 ? 244.092 216.328 256.673 1.00 37.51  ? 2156 LEU A N     1 
ATOM   4926  C  CA    . LEU A 1 2156 ? 243.995 217.782 256.696 1.00 39.56  ? 2156 LEU A CA    1 
ATOM   4927  C  C     . LEU A 1 2156 ? 242.859 218.248 257.597 1.00 44.02  ? 2156 LEU A C     1 
ATOM   4928  O  O     . LEU A 1 2156 ? 243.038 219.167 258.406 1.00 50.21  ? 2156 LEU A O     1 
ATOM   4929  C  CB    . LEU A 1 2156 ? 243.800 218.313 255.278 1.00 40.71  ? 2156 LEU A CB    1 
ATOM   4930  C  CG    . LEU A 1 2156 ? 244.946 218.124 254.288 1.00 38.86  ? 2156 LEU A CG    1 
ATOM   4931  C  CD1   . LEU A 1 2156 ? 244.583 218.736 252.950 1.00 42.46  ? 2156 LEU A CD1   1 
ATOM   4932  C  CD2   . LEU A 1 2156 ? 246.219 218.738 254.828 1.00 42.44  ? 2156 LEU A CD2   1 
ATOM   4933  N  N     . LEU A 1 2157 ? 241.687 217.621 257.484 1.00 40.93  ? 2157 LEU A N     1 
ATOM   4934  C  CA    . LEU A 1 2157 ? 240.559 218.035 258.311 1.00 42.60  ? 2157 LEU A CA    1 
ATOM   4935  C  C     . LEU A 1 2157 ? 240.788 217.687 259.773 1.00 44.57  ? 2157 LEU A C     1 
ATOM   4936  O  O     . LEU A 1 2157 ? 240.373 218.435 260.664 1.00 52.97  ? 2157 LEU A O     1 
ATOM   4937  C  CB    . LEU A 1 2157 ? 239.261 217.411 257.802 1.00 33.91  ? 2157 LEU A CB    1 
ATOM   4938  C  CG    . LEU A 1 2157 ? 237.990 217.838 258.543 1.00 37.36  ? 2157 LEU A CG    1 
ATOM   4939  C  CD1   . LEU A 1 2157 ? 236.870 218.156 257.571 1.00 42.42  ? 2157 LEU A CD1   1 
ATOM   4940  C  CD2   . LEU A 1 2157 ? 237.544 216.762 259.521 1.00 37.41  ? 2157 LEU A CD2   1 
ATOM   4941  N  N     . PHE A 1 2158 ? 241.451 216.564 260.052 1.00 38.15  ? 2158 PHE A N     1 
ATOM   4942  C  CA    . PHE A 1 2158 ? 241.710 216.243 261.452 1.00 34.05  ? 2158 PHE A CA    1 
ATOM   4943  C  C     . PHE A 1 2158 ? 242.764 217.162 262.057 1.00 43.55  ? 2158 PHE A C     1 
ATOM   4944  O  O     . PHE A 1 2158 ? 242.672 217.508 263.239 1.00 49.26  ? 2158 PHE A O     1 
ATOM   4945  C  CB    . PHE A 1 2158 ? 242.098 214.776 261.596 1.00 35.61  ? 2158 PHE A CB    1 
ATOM   4946  C  CG    . PHE A 1 2158 ? 240.915 213.863 261.725 1.00 45.95  ? 2158 PHE A CG    1 
ATOM   4947  C  CD1   . PHE A 1 2158 ? 239.963 214.088 262.704 1.00 47.47  ? 2158 PHE A CD1   1 
ATOM   4948  C  CD2   . PHE A 1 2158 ? 240.744 212.795 260.867 1.00 47.29  ? 2158 PHE A CD2   1 
ATOM   4949  C  CE1   . PHE A 1 2158 ? 238.870 213.261 262.828 1.00 45.61  ? 2158 PHE A CE1   1 
ATOM   4950  C  CE2   . PHE A 1 2158 ? 239.648 211.964 260.989 1.00 47.98  ? 2158 PHE A CE2   1 
ATOM   4951  C  CZ    . PHE A 1 2158 ? 238.711 212.198 261.970 1.00 46.40  ? 2158 PHE A CZ    1 
ATOM   4952  N  N     . SER A 1 2159 ? 243.751 217.592 261.268 1.00 45.69  ? 2159 SER A N     1 
ATOM   4953  C  CA    . SER A 1 2159 ? 244.676 218.614 261.745 1.00 42.36  ? 2159 SER A CA    1 
ATOM   4954  C  C     . SER A 1 2159 ? 243.956 219.934 261.992 1.00 43.96  ? 2159 SER A C     1 
ATOM   4955  O  O     . SER A 1 2159 ? 244.220 220.618 262.990 1.00 52.41  ? 2159 SER A O     1 
ATOM   4956  C  CB    . SER A 1 2159 ? 245.811 218.800 260.741 1.00 38.75  ? 2159 SER A CB    1 
ATOM   4957  O  OG    . SER A 1 2159 ? 246.512 217.587 260.541 1.00 48.61  ? 2159 SER A OG    1 
ATOM   4958  N  N     . LEU A 1 2160 ? 243.036 220.303 261.098 1.00 37.90  ? 2160 LEU A N     1 
ATOM   4959  C  CA    . LEU A 1 2160 ? 242.259 221.521 261.300 1.00 42.53  ? 2160 LEU A CA    1 
ATOM   4960  C  C     . LEU A 1 2160 ? 241.420 221.433 262.568 1.00 46.01  ? 2160 LEU A C     1 
ATOM   4961  O  O     . LEU A 1 2160 ? 241.277 222.421 263.295 1.00 50.75  ? 2160 LEU A O     1 
ATOM   4962  C  CB    . LEU A 1 2160 ? 241.367 221.780 260.087 1.00 45.92  ? 2160 LEU A CB    1 
ATOM   4963  C  CG    . LEU A 1 2160 ? 242.007 222.464 258.879 1.00 48.74  ? 2160 LEU A CG    1 
ATOM   4964  C  CD1   . LEU A 1 2160 ? 240.986 222.631 257.770 1.00 43.44  ? 2160 LEU A CD1   1 
ATOM   4965  C  CD2   . LEU A 1 2160 ? 242.600 223.804 259.268 1.00 42.72  ? 2160 LEU A CD2   1 
ATOM   4966  N  N     . LEU A 1 2161 ? 240.841 220.262 262.838 1.00 44.83  ? 2161 LEU A N     1 
ATOM   4967  C  CA    . LEU A 1 2161 ? 240.080 220.077 264.069 1.00 43.08  ? 2161 LEU A CA    1 
ATOM   4968  C  C     . LEU A 1 2161 ? 240.978 220.172 265.295 1.00 41.87  ? 2161 LEU A C     1 
ATOM   4969  O  O     . LEU A 1 2161 ? 240.617 220.813 266.288 1.00 44.76  ? 2161 LEU A O     1 
ATOM   4970  C  CB    . LEU A 1 2161 ? 239.357 218.731 264.043 1.00 41.67  ? 2161 LEU A CB    1 
ATOM   4971  C  CG    . LEU A 1 2161 ? 237.930 218.720 263.501 1.00 38.54  ? 2161 LEU A CG    1 
ATOM   4972  C  CD1   . LEU A 1 2161 ? 237.273 217.388 263.799 1.00 45.78  ? 2161 LEU A CD1   1 
ATOM   4973  C  CD2   . LEU A 1 2161 ? 237.125 219.857 264.097 1.00 40.90  ? 2161 LEU A CD2   1 
ATOM   4974  N  N     . SER A 1 2162 ? 242.151 219.539 265.248 1.00 43.44  ? 2162 SER A N     1 
ATOM   4975  C  CA    . SER A 1 2162 ? 243.060 219.571 266.386 1.00 44.05  ? 2162 SER A CA    1 
ATOM   4976  C  C     . SER A 1 2162 ? 243.674 220.944 266.612 1.00 46.04  ? 2162 SER A C     1 
ATOM   4977  O  O     . SER A 1 2162 ? 244.195 221.197 267.702 1.00 53.02  ? 2162 SER A O     1 
ATOM   4978  C  CB    . SER A 1 2162 ? 244.173 218.539 266.205 1.00 47.05  ? 2162 SER A CB    1 
ATOM   4979  O  OG    . SER A 1 2162 ? 244.833 218.711 264.966 1.00 52.92  ? 2162 SER A OG    1 
ATOM   4980  N  N     . ASP A 1 2163 ? 243.642 221.824 265.614 1.00 45.84  ? 2163 ASP A N     1 
ATOM   4981  C  CA    . ASP A 1 2163 ? 244.134 223.186 265.782 1.00 39.02  ? 2163 ASP A CA    1 
ATOM   4982  C  C     . ASP A 1 2163 ? 243.039 224.163 266.194 1.00 40.75  ? 2163 ASP A C     1 
ATOM   4983  O  O     . ASP A 1 2163 ? 243.262 225.012 267.061 1.00 48.18  ? 2163 ASP A O     1 
ATOM   4984  C  CB    . ASP A 1 2163 ? 244.804 223.661 264.492 1.00 41.33  ? 2163 ASP A CB    1 
ATOM   4985  C  CG    . ASP A 1 2163 ? 246.078 222.908 264.199 1.00 55.03  ? 2163 ASP A CG    1 
ATOM   4986  O  OD1   . ASP A 1 2163 ? 246.404 221.974 264.958 1.00 57.23  ? 2163 ASP A OD1   1 
ATOM   4987  O  OD2   . ASP A 1 2163 ? 246.758 223.249 263.217 1.00 51.93  ? 2163 ASP A OD2   1 
ATOM   4988  N  N     . VAL A 1 2164 ? 241.859 224.068 265.582 1.00 48.19  ? 2164 VAL A N     1 
ATOM   4989  C  CA    . VAL A 1 2164 ? 240.750 224.940 265.951 1.00 43.73  ? 2164 VAL A CA    1 
ATOM   4990  C  C     . VAL A 1 2164 ? 240.210 224.572 267.327 1.00 44.28  ? 2164 VAL A C     1 
ATOM   4991  O  O     . VAL A 1 2164 ? 239.874 225.447 268.133 1.00 49.91  ? 2164 VAL A O     1 
ATOM   4992  C  CB    . VAL A 1 2164 ? 239.653 224.883 264.873 1.00 42.57  ? 2164 VAL A CB    1 
ATOM   4993  C  CG1   . VAL A 1 2164 ? 238.366 225.460 265.400 1.00 40.95  ? 2164 VAL A CG1   1 
ATOM   4994  C  CG2   . VAL A 1 2164 ? 240.100 225.630 263.631 1.00 47.73  ? 2164 VAL A CG2   1 
ATOM   4995  N  N     . PHE A 1 2165 ? 240.119 223.274 267.621 1.00 43.28  ? 2165 PHE A N     1 
ATOM   4996  C  CA    . PHE A 1 2165 ? 239.684 222.769 268.921 1.00 41.09  ? 2165 PHE A CA    1 
ATOM   4997  C  C     . PHE A 1 2165 ? 240.858 222.055 269.582 1.00 49.19  ? 2165 PHE A C     1 
ATOM   4998  O  O     . PHE A 1 2165 ? 240.878 220.820 269.663 1.00 46.96  ? 2165 PHE A O     1 
ATOM   4999  C  CB    . PHE A 1 2165 ? 238.499 221.815 268.781 1.00 43.01  ? 2165 PHE A CB    1 
ATOM   5000  C  CG    . PHE A 1 2165 ? 237.269 222.442 268.195 1.00 42.67  ? 2165 PHE A CG    1 
ATOM   5001  C  CD1   . PHE A 1 2165 ? 236.429 223.217 268.973 1.00 50.03  ? 2165 PHE A CD1   1 
ATOM   5002  C  CD2   . PHE A 1 2165 ? 236.948 222.250 266.864 1.00 46.40  ? 2165 PHE A CD2   1 
ATOM   5003  C  CE1   . PHE A 1 2165 ? 235.294 223.788 268.434 1.00 48.53  ? 2165 PHE A CE1   1 
ATOM   5004  C  CE2   . PHE A 1 2165 ? 235.817 222.822 266.319 1.00 45.72  ? 2165 PHE A CE2   1 
ATOM   5005  C  CZ    . PHE A 1 2165 ? 234.990 223.591 267.105 1.00 41.91  ? 2165 PHE A CZ    1 
ATOM   5006  N  N     . PRO A 1 2166 ? 241.857 222.799 270.057 1.00 52.86  ? 2166 PRO A N     1 
ATOM   5007  C  CA    . PRO A 1 2166 ? 243.046 222.149 270.618 1.00 43.30  ? 2166 PRO A CA    1 
ATOM   5008  C  C     . PRO A 1 2166 ? 242.724 221.414 271.907 1.00 46.43  ? 2166 PRO A C     1 
ATOM   5009  O  O     . PRO A 1 2166 ? 241.935 221.880 272.732 1.00 51.15  ? 2166 PRO A O     1 
ATOM   5010  C  CB    . PRO A 1 2166 ? 244.005 223.318 270.862 1.00 43.95  ? 2166 PRO A CB    1 
ATOM   5011  C  CG    . PRO A 1 2166 ? 243.111 224.476 271.090 1.00 45.53  ? 2166 PRO A CG    1 
ATOM   5012  C  CD    . PRO A 1 2166 ? 241.910 224.263 270.212 1.00 49.32  ? 2166 PRO A CD    1 
ATOM   5013  N  N     . GLY A 1 2167 ? 243.344 220.252 272.074 1.00 48.36  ? 2167 GLY A N     1 
ATOM   5014  C  CA    . GLY A 1 2167 ? 243.167 219.429 273.257 1.00 48.77  ? 2167 GLY A CA    1 
ATOM   5015  C  C     . GLY A 1 2167 ? 241.925 218.563 273.257 1.00 50.06  ? 2167 GLY A C     1 
ATOM   5016  O  O     . GLY A 1 2167 ? 241.931 217.469 273.824 1.00 55.61  ? 2167 GLY A O     1 
ATOM   5017  N  N     . VAL A 1 2168 ? 240.851 219.036 272.627 1.00 59.80  ? 2168 VAL A N     1 
ATOM   5018  C  CA    . VAL A 1 2168 ? 239.602 218.287 272.615 1.00 60.71  ? 2168 VAL A CA    1 
ATOM   5019  C  C     . VAL A 1 2168 ? 239.716 217.128 271.637 1.00 57.93  ? 2168 VAL A C     1 
ATOM   5020  O  O     . VAL A 1 2168 ? 240.088 217.311 270.470 1.00 57.29  ? 2168 VAL A O     1 
ATOM   5021  C  CB    . VAL A 1 2168 ? 238.425 219.205 272.256 1.00 55.66  ? 2168 VAL A CB    1 
ATOM   5022  C  CG1   . VAL A 1 2168 ? 237.135 218.413 272.216 1.00 50.76  ? 2168 VAL A CG1   1 
ATOM   5023  C  CG2   . VAL A 1 2168 ? 238.325 220.344 273.253 1.00 56.32  ? 2168 VAL A CG2   1 
ATOM   5024  N  N     . GLN A 1 2169 ? 239.396 215.927 272.109 1.00 70.54  ? 2169 GLN A N     1 
ATOM   5025  C  CA    . GLN A 1 2169 ? 239.450 214.721 271.298 1.00 72.04  ? 2169 GLN A CA    1 
ATOM   5026  C  C     . GLN A 1 2169 ? 238.122 213.986 271.389 1.00 75.05  ? 2169 GLN A C     1 
ATOM   5027  O  O     . GLN A 1 2169 ? 237.460 214.006 272.431 1.00 73.96  ? 2169 GLN A O     1 
ATOM   5028  C  CB    . GLN A 1 2169 ? 240.595 213.802 271.742 1.00 72.75  ? 2169 GLN A CB    1 
ATOM   5029  C  CG    . GLN A 1 2169 ? 240.438 213.239 273.144 1.00 76.28  ? 2169 GLN A CG    1 
ATOM   5030  C  CD    . GLN A 1 2169 ? 241.616 212.386 273.565 1.00 78.12  ? 2169 GLN A CD    1 
ATOM   5031  O  OE1   . GLN A 1 2169 ? 242.545 212.164 272.789 1.00 77.41  ? 2169 GLN A OE1   1 
ATOM   5032  N  NE2   . GLN A 1 2169 ? 241.587 211.905 274.802 1.00 75.31  ? 2169 GLN A NE2   1 
ATOM   5033  N  N     . TYR A 1 2170 ? 237.732 213.351 270.289 1.00 73.33  ? 2170 TYR A N     1 
ATOM   5034  C  CA    . TYR A 1 2170 ? 236.520 212.550 270.228 1.00 72.53  ? 2170 TYR A CA    1 
ATOM   5035  C  C     . TYR A 1 2170 ? 236.855 211.150 269.738 1.00 74.00  ? 2170 TYR A C     1 
ATOM   5036  O  O     . TYR A 1 2170 ? 237.620 210.982 268.783 1.00 72.28  ? 2170 TYR A O     1 
ATOM   5037  C  CB    . TYR A 1 2170 ? 235.476 213.177 269.303 1.00 73.23  ? 2170 TYR A CB    1 
ATOM   5038  C  CG    . TYR A 1 2170 ? 234.277 212.286 269.070 1.00 75.77  ? 2170 TYR A CG    1 
ATOM   5039  C  CD1   . TYR A 1 2170 ? 233.969 211.821 267.798 1.00 70.01  ? 2170 TYR A CD1   1 
ATOM   5040  C  CD2   . TYR A 1 2170 ? 233.460 211.902 270.125 1.00 74.72  ? 2170 TYR A CD2   1 
ATOM   5041  C  CE1   . TYR A 1 2170 ? 232.878 211.003 267.584 1.00 73.25  ? 2170 TYR A CE1   1 
ATOM   5042  C  CE2   . TYR A 1 2170 ? 232.368 211.086 269.920 1.00 75.60  ? 2170 TYR A CE2   1 
ATOM   5043  C  CZ    . TYR A 1 2170 ? 232.082 210.636 268.649 1.00 80.48  ? 2170 TYR A CZ    1 
ATOM   5044  O  OH    . TYR A 1 2170 ? 230.990 209.824 268.444 1.00 78.76  ? 2170 TYR A OH    1 
ATOM   5045  N  N     . HIS A 1 2171 ? 236.277 210.149 270.395 1.00 83.93  ? 2171 HIS A N     1 
ATOM   5046  C  CA    . HIS A 1 2171 ? 236.421 208.756 269.997 1.00 81.52  ? 2171 HIS A CA    1 
ATOM   5047  C  C     . HIS A 1 2171 ? 235.055 208.236 269.579 1.00 80.52  ? 2171 HIS A C     1 
ATOM   5048  O  O     . HIS A 1 2171 ? 234.090 208.337 270.344 1.00 81.75  ? 2171 HIS A O     1 
ATOM   5049  C  CB    . HIS A 1 2171 ? 237.004 207.913 271.132 1.00 82.74  ? 2171 HIS A CB    1 
ATOM   5050  C  CG    . HIS A 1 2171 ? 238.322 208.413 271.636 1.00 86.36  ? 2171 HIS A CG    1 
ATOM   5051  N  ND1   . HIS A 1 2171 ? 239.505 207.741 271.416 1.00 85.38  ? 2171 HIS A ND1   1 
ATOM   5052  C  CD2   . HIS A 1 2171 ? 238.644 209.518 272.348 1.00 83.01  ? 2171 HIS A CD2   1 
ATOM   5053  C  CE1   . HIS A 1 2171 ? 240.499 208.411 271.971 1.00 84.16  ? 2171 HIS A CE1   1 
ATOM   5054  N  NE2   . HIS A 1 2171 ? 240.003 209.494 272.542 1.00 83.70  ? 2171 HIS A NE2   1 
ATOM   5055  N  N     . ARG A 1 2172 ? 234.978 207.686 268.370 1.00 68.43  ? 2172 ARG A N     1 
ATOM   5056  C  CA    . ARG A 1 2172 ? 233.710 207.213 267.833 1.00 64.13  ? 2172 ARG A CA    1 
ATOM   5057  C  C     . ARG A 1 2172 ? 233.150 206.082 268.683 1.00 70.68  ? 2172 ARG A C     1 
ATOM   5058  O  O     . ARG A 1 2172 ? 233.865 205.142 269.040 1.00 75.18  ? 2172 ARG A O     1 
ATOM   5059  C  CB    . ARG A 1 2172 ? 233.901 206.743 266.391 1.00 67.82  ? 2172 ARG A CB    1 
ATOM   5060  C  CG    . ARG A 1 2172 ? 232.781 207.145 265.451 1.00 72.64  ? 2172 ARG A CG    1 
ATOM   5061  C  CD    . ARG A 1 2172 ? 232.881 206.396 264.133 1.00 72.55  ? 2172 ARG A CD    1 
ATOM   5062  N  NE    . ARG A 1 2172 ? 231.639 206.464 263.372 1.00 72.55  ? 2172 ARG A NE    1 
ATOM   5063  C  CZ    . ARG A 1 2172 ? 231.382 205.741 262.291 1.00 72.98  ? 2172 ARG A CZ    1 
ATOM   5064  N  NH1   . ARG A 1 2172 ? 232.258 204.870 261.816 1.00 66.32  ? 2172 ARG A NH1   1 
ATOM   5065  N  NH2   . ARG A 1 2172 ? 230.217 205.896 261.671 1.00 73.12  ? 2172 ARG A NH2   1 
ATOM   5066  N  N     . GLY A 1 2173 ? 231.864 206.179 269.005 1.00 80.15  ? 2173 GLY A N     1 
ATOM   5067  C  CA    . GLY A 1 2173 ? 231.195 205.136 269.755 1.00 79.22  ? 2173 GLY A CA    1 
ATOM   5068  C  C     . GLY A 1 2173 ? 230.826 203.960 268.877 1.00 78.86  ? 2173 GLY A C     1 
ATOM   5069  O  O     . GLY A 1 2173 ? 230.242 204.142 267.805 1.00 81.55  ? 2173 GLY A O     1 
ATOM   5070  N  N     . GLU A 1 2174 ? 231.168 202.751 269.312 1.00 84.07  ? 2174 GLU A N     1 
ATOM   5071  C  CA    . GLU A 1 2174 ? 230.904 201.565 268.508 1.00 85.14  ? 2174 GLU A CA    1 
ATOM   5072  C  C     . GLU A 1 2174 ? 229.418 201.234 268.521 1.00 86.89  ? 2174 GLU A C     1 
ATOM   5073  O  O     . GLU A 1 2174 ? 228.783 201.225 269.580 1.00 86.92  ? 2174 GLU A O     1 
ATOM   5074  C  CB    . GLU A 1 2174 ? 231.714 200.380 269.032 1.00 82.16  ? 2174 GLU A CB    1 
ATOM   5075  C  CG    . GLU A 1 2174 ? 233.218 200.516 268.862 1.00 83.42  ? 2174 GLU A CG    1 
ATOM   5076  C  CD    . GLU A 1 2174 ? 233.862 201.336 269.962 1.00 87.35  ? 2174 GLU A CD    1 
ATOM   5077  O  OE1   . GLU A 1 2174 ? 233.143 201.749 270.896 1.00 89.91  ? 2174 GLU A OE1   1 
ATOM   5078  O  OE2   . GLU A 1 2174 ? 235.087 201.567 269.894 1.00 85.19  ? 2174 GLU A OE2   1 
ATOM   5079  N  N     . MET A 1 2175 ? 228.863 200.965 267.339 1.00 63.58  ? 2175 MET A N     1 
ATOM   5080  C  CA    . MET A 1 2175 ? 227.493 200.469 267.224 1.00 62.74  ? 2175 MET A CA    1 
ATOM   5081  C  C     . MET A 1 2175 ? 227.519 198.941 267.255 1.00 65.21  ? 2175 MET A C     1 
ATOM   5082  O  O     . MET A 1 2175 ? 227.409 198.259 266.237 1.00 73.16  ? 2175 MET A O     1 
ATOM   5083  C  CB    . MET A 1 2175 ? 226.834 200.994 265.954 1.00 61.60  ? 2175 MET A CB    1 
ATOM   5084  C  CG    . MET A 1 2175 ? 226.382 202.443 266.024 1.00 63.32  ? 2175 MET A CG    1 
ATOM   5085  S  SD    . MET A 1 2175 ? 227.739 203.621 265.963 1.00 83.30  ? 2175 MET A SD    1 
ATOM   5086  C  CE    . MET A 1 2175 ? 228.193 203.523 264.236 1.00 61.49  ? 2175 MET A CE    1 
ATOM   5087  N  N     . THR A 1 2176 ? 227.669 198.410 268.471 1.00 56.62  ? 2176 THR A N     1 
ATOM   5088  C  CA    . THR A 1 2176 ? 227.877 196.975 268.634 1.00 51.85  ? 2176 THR A CA    1 
ATOM   5089  C  C     . THR A 1 2176 ? 226.695 196.175 268.099 1.00 56.41  ? 2176 THR A C     1 
ATOM   5090  O  O     . THR A 1 2176 ? 226.882 195.175 267.394 1.00 59.37  ? 2176 THR A O     1 
ATOM   5091  C  CB    . THR A 1 2176 ? 228.127 196.648 270.106 1.00 56.19  ? 2176 THR A CB    1 
ATOM   5092  O  OG1   . THR A 1 2176 ? 229.450 197.059 270.467 1.00 57.51  ? 2176 THR A OG1   1 
ATOM   5093  C  CG2   . THR A 1 2176 ? 227.989 195.156 270.358 1.00 61.59  ? 2176 THR A CG2   1 
ATOM   5094  N  N     . ALA A 1 2177 ? 225.471 196.605 268.411 1.00 49.74  ? 2177 ALA A N     1 
ATOM   5095  C  CA    . ALA A 1 2177 ? 224.292 195.897 267.922 1.00 46.56  ? 2177 ALA A CA    1 
ATOM   5096  C  C     . ALA A 1 2177 ? 224.211 195.951 266.402 1.00 52.97  ? 2177 ALA A C     1 
ATOM   5097  O  O     . ALA A 1 2177 ? 223.965 194.935 265.739 1.00 60.49  ? 2177 ALA A O     1 
ATOM   5098  C  CB    . ALA A 1 2177 ? 223.031 196.489 268.551 1.00 43.98  ? 2177 ALA A CB    1 
ATOM   5099  N  N     . LEU A 1 2178 ? 224.436 197.135 265.830 1.00 48.89  ? 2178 LEU A N     1 
ATOM   5100  C  CA    . LEU A 1 2178 ? 224.409 197.258 264.378 1.00 46.20  ? 2178 LEU A CA    1 
ATOM   5101  C  C     . LEU A 1 2178 ? 225.553 196.486 263.741 1.00 44.59  ? 2178 LEU A C     1 
ATOM   5102  O  O     . LEU A 1 2178 ? 225.389 195.908 262.665 1.00 58.32  ? 2178 LEU A O     1 
ATOM   5103  C  CB    . LEU A 1 2178 ? 224.463 198.726 263.963 1.00 47.00  ? 2178 LEU A CB    1 
ATOM   5104  C  CG    . LEU A 1 2178 ? 224.250 198.958 262.466 1.00 45.17  ? 2178 LEU A CG    1 
ATOM   5105  C  CD1   . LEU A 1 2178 ? 222.854 198.539 262.035 1.00 42.77  ? 2178 LEU A CD1   1 
ATOM   5106  C  CD2   . LEU A 1 2178 ? 224.516 200.402 262.100 1.00 46.26  ? 2178 LEU A CD2   1 
ATOM   5107  N  N     . ARG A 1 2179 ? 226.719 196.465 264.386 1.00 33.72  ? 2179 ARG A N     1 
ATOM   5108  C  CA    . ARG A 1 2179 ? 227.835 195.696 263.849 1.00 34.19  ? 2179 ARG A CA    1 
ATOM   5109  C  C     . ARG A 1 2179 ? 227.525 194.203 263.834 1.00 44.40  ? 2179 ARG A C     1 
ATOM   5110  O  O     . ARG A 1 2179 ? 227.847 193.508 262.865 1.00 55.86  ? 2179 ARG A O     1 
ATOM   5111  C  CB    . ARG A 1 2179 ? 229.102 195.988 264.649 1.00 46.31  ? 2179 ARG A CB    1 
ATOM   5112  C  CG    . ARG A 1 2179 ? 229.731 197.334 264.326 1.00 41.37  ? 2179 ARG A CG    1 
ATOM   5113  C  CD    . ARG A 1 2179 ? 231.214 197.324 264.630 1.00 39.02  ? 2179 ARG A CD    1 
ATOM   5114  N  NE    . ARG A 1 2179 ? 231.892 198.512 264.129 1.00 44.88  ? 2179 ARG A NE    1 
ATOM   5115  C  CZ    . ARG A 1 2179 ? 232.808 198.502 263.171 1.00 47.99  ? 2179 ARG A CZ    1 
ATOM   5116  N  NH1   . ARG A 1 2179 ? 233.173 197.378 262.578 1.00 49.38  ? 2179 ARG A NH1   1 
ATOM   5117  N  NH2   . ARG A 1 2179 ? 233.375 199.646 262.803 1.00 47.45  ? 2179 ARG A NH2   1 
ATOM   5118  N  N     . GLU A 1 2180 ? 226.886 193.691 264.890 1.00 41.97  ? 2180 GLU A N     1 
ATOM   5119  C  CA    . GLU A 1 2180 ? 226.470 192.290 264.893 1.00 41.51  ? 2180 GLU A CA    1 
ATOM   5120  C  C     . GLU A 1 2180 ? 225.454 192.013 263.792 1.00 46.92  ? 2180 GLU A C     1 
ATOM   5121  O  O     . GLU A 1 2180 ? 225.537 190.992 263.089 1.00 50.42  ? 2180 GLU A O     1 
ATOM   5122  C  CB    . GLU A 1 2180 ? 225.878 191.922 266.254 1.00 45.46  ? 2180 GLU A CB    1 
ATOM   5123  C  CG    . GLU A 1 2180 ? 226.860 191.949 267.408 1.00 49.23  ? 2180 GLU A CG    1 
ATOM   5124  C  CD    . GLU A 1 2180 ? 227.922 190.876 267.296 1.00 61.26  ? 2180 GLU A CD    1 
ATOM   5125  O  OE1   . GLU A 1 2180 ? 227.622 189.795 266.749 1.00 59.56  ? 2180 GLU A OE1   1 
ATOM   5126  O  OE2   . GLU A 1 2180 ? 229.058 191.108 267.759 1.00 59.74  ? 2180 GLU A OE2   1 
ATOM   5127  N  N     . GLU A 1 2181 ? 224.486 192.915 263.630 1.00 45.65  ? 2181 GLU A N     1 
ATOM   5128  C  CA    . GLU A 1 2181 ? 223.434 192.679 262.652 1.00 39.75  ? 2181 GLU A CA    1 
ATOM   5129  C  C     . GLU A 1 2181 ? 224.016 192.710 261.239 1.00 46.34  ? 2181 GLU A C     1 
ATOM   5130  O  O     . GLU A 1 2181 ? 223.647 191.896 260.380 1.00 53.91  ? 2181 GLU A O     1 
ATOM   5131  C  CB    . GLU A 1 2181 ? 222.339 193.728 262.823 1.00 37.81  ? 2181 GLU A CB    1 
ATOM   5132  C  CG    . GLU A 1 2181 ? 221.531 193.562 264.108 1.00 50.19  ? 2181 GLU A CG    1 
ATOM   5133  C  CD    . GLU A 1 2181 ? 221.108 192.137 264.424 1.00 60.92  ? 2181 GLU A CD    1 
ATOM   5134  O  OE1   . GLU A 1 2181 ? 220.521 191.465 263.558 1.00 58.87  ? 2181 GLU A OE1   1 
ATOM   5135  O  OE2   . GLU A 1 2181 ? 221.373 191.688 265.560 1.00 58.65  ? 2181 GLU A OE2   1 
ATOM   5136  N  N     . LEU A 1 2182 ? 224.963 193.625 261.001 1.00 35.52  ? 2182 LEU A N     1 
ATOM   5137  C  CA    . LEU A 1 2182 ? 225.683 193.684 259.733 1.00 32.32  ? 2182 LEU A CA    1 
ATOM   5138  C  C     . LEU A 1 2182 ? 226.520 192.432 259.512 1.00 39.06  ? 2182 LEU A C     1 
ATOM   5139  O  O     . LEU A 1 2182 ? 226.660 191.968 258.377 1.00 52.08  ? 2182 LEU A O     1 
ATOM   5140  C  CB    . LEU A 1 2182 ? 226.586 194.919 259.698 1.00 36.52  ? 2182 LEU A CB    1 
ATOM   5141  C  CG    . LEU A 1 2182 ? 226.009 196.333 259.634 1.00 34.77  ? 2182 LEU A CG    1 
ATOM   5142  C  CD1   . LEU A 1 2182 ? 227.128 197.352 259.764 1.00 35.94  ? 2182 LEU A CD1   1 
ATOM   5143  C  CD2   . LEU A 1 2182 ? 225.250 196.558 258.352 1.00 41.17  ? 2182 LEU A CD2   1 
ATOM   5144  N  N     . LYS A 1 2183 ? 227.132 191.906 260.576 1.00 35.76  ? 2183 LYS A N     1 
ATOM   5145  C  CA    . LYS A 1 2183 ? 227.849 190.640 260.469 1.00 31.68  ? 2183 LYS A CA    1 
ATOM   5146  C  C     . LYS A 1 2183 ? 226.942 189.555 259.921 1.00 38.11  ? 2183 LYS A C     1 
ATOM   5147  O  O     . LYS A 1 2183 ? 227.314 188.830 258.990 1.00 42.68  ? 2183 LYS A O     1 
ATOM   5148  C  CB    . LYS A 1 2183 ? 228.381 190.213 261.835 1.00 35.23  ? 2183 LYS A CB    1 
ATOM   5149  C  CG    . LYS A 1 2183 ? 229.768 190.687 262.170 1.00 45.85  ? 2183 LYS A CG    1 
ATOM   5150  C  CD    . LYS A 1 2183 ? 230.396 189.810 263.239 1.00 44.73  ? 2183 LYS A CD    1 
ATOM   5151  C  CE    . LYS A 1 2183 ? 230.737 188.430 262.708 1.00 48.46  ? 2183 LYS A CE    1 
ATOM   5152  N  NZ    . LYS A 1 2183 ? 231.749 188.486 261.619 1.00 48.68  ? 2183 LYS A NZ    1 
ATOM   5153  N  N     . LYS A 1 2184 ? 225.746 189.432 260.494 1.00 43.22  ? 2184 LYS A N     1 
ATOM   5154  C  CA    . LYS A 1 2184 ? 224.806 188.420 260.019 1.00 32.50  ? 2184 LYS A CA    1 
ATOM   5155  C  C     . LYS A 1 2184 ? 224.408 188.663 258.566 1.00 37.51  ? 2184 LYS A C     1 
ATOM   5156  O  O     . LYS A 1 2184 ? 224.327 187.715 257.772 1.00 43.66  ? 2184 LYS A O     1 
ATOM   5157  C  CB    . LYS A 1 2184 ? 223.580 188.385 260.927 1.00 39.19  ? 2184 LYS A CB    1 
ATOM   5158  C  CG    . LYS A 1 2184 ? 223.902 187.888 262.319 1.00 40.02  ? 2184 LYS A CG    1 
ATOM   5159  C  CD    . LYS A 1 2184 ? 222.677 187.844 263.204 1.00 48.15  ? 2184 LYS A CD    1 
ATOM   5160  C  CE    . LYS A 1 2184 ? 223.015 187.220 264.544 1.00 48.42  ? 2184 LYS A CE    1 
ATOM   5161  N  NZ    . LYS A 1 2184 ? 223.953 188.067 265.330 1.00 50.46  ? 2184 LYS A NZ    1 
ATOM   5162  N  N     . VAL A 1 2185 ? 224.166 189.924 258.195 1.00 38.64  ? 2185 VAL A N     1 
ATOM   5163  C  CA    . VAL A 1 2185 ? 223.776 190.215 256.815 1.00 33.88  ? 2185 VAL A CA    1 
ATOM   5164  C  C     . VAL A 1 2185 ? 224.901 189.868 255.845 1.00 41.41  ? 2185 VAL A C     1 
ATOM   5165  O  O     . VAL A 1 2185 ? 224.662 189.300 254.774 1.00 47.69  ? 2185 VAL A O     1 
ATOM   5166  C  CB    . VAL A 1 2185 ? 223.352 191.686 256.667 1.00 41.24  ? 2185 VAL A CB    1 
ATOM   5167  C  CG1   . VAL A 1 2185 ? 223.118 192.016 255.201 1.00 45.60  ? 2185 VAL A CG1   1 
ATOM   5168  C  CG2   . VAL A 1 2185 ? 222.112 191.959 257.477 1.00 34.86  ? 2185 VAL A CG2   1 
ATOM   5169  N  N     . CYS A 1 2186 ? 226.141 190.213 256.195 1.00 40.87  ? 2186 CYS A N     1 
ATOM   5170  C  CA    . CYS A 1 2186 ? 227.270 189.908 255.323 1.00 32.98  ? 2186 CYS A CA    1 
ATOM   5171  C  C     . CYS A 1 2186 ? 227.484 188.407 255.206 1.00 36.31  ? 2186 CYS A C     1 
ATOM   5172  O  O     . CYS A 1 2186 ? 227.864 187.910 254.141 1.00 53.06  ? 2186 CYS A O     1 
ATOM   5173  C  CB    . CYS A 1 2186 ? 228.535 190.591 255.838 1.00 36.31  ? 2186 CYS A CB    1 
ATOM   5174  S  SG    . CYS A 1 2186 ? 228.559 192.378 255.622 1.00 51.26  ? 2186 CYS A SG    1 
ATOM   5175  N  N     . GLN A 1 2187 ? 227.270 187.670 256.297 1.00 35.77  ? 2187 GLN A N     1 
ATOM   5176  C  CA    . GLN A 1 2187 ? 227.378 186.217 256.219 1.00 37.26  ? 2187 GLN A CA    1 
ATOM   5177  C  C     . GLN A 1 2187 ? 226.324 185.632 255.291 1.00 43.59  ? 2187 GLN A C     1 
ATOM   5178  O  O     . GLN A 1 2187 ? 226.630 184.759 254.470 1.00 50.11  ? 2187 GLN A O     1 
ATOM   5179  C  CB    . GLN A 1 2187 ? 227.274 185.597 257.611 1.00 42.20  ? 2187 GLN A CB    1 
ATOM   5180  C  CG    . GLN A 1 2187 ? 228.439 185.929 258.525 1.00 49.82  ? 2187 GLN A CG    1 
ATOM   5181  C  CD    . GLN A 1 2187 ? 228.291 185.315 259.903 1.00 54.56  ? 2187 GLN A CD    1 
ATOM   5182  O  OE1   . GLN A 1 2187 ? 227.278 184.687 260.210 1.00 48.40  ? 2187 GLN A OE1   1 
ATOM   5183  N  NE2   . GLN A 1 2187 ? 229.306 185.491 260.741 1.00 51.47  ? 2187 GLN A NE2   1 
ATOM   5184  N  N     . GLU A 1 2188 ? 225.077 186.100 255.389 1.00 43.74  ? 2188 GLU A N     1 
ATOM   5185  C  CA    . GLU A 1 2188 ? 224.048 185.523 254.532 1.00 34.65  ? 2188 GLU A CA    1 
ATOM   5186  C  C     . GLU A 1 2188 ? 224.129 186.021 253.094 1.00 40.45  ? 2188 GLU A C     1 
ATOM   5187  O  O     . GLU A 1 2188 ? 223.510 185.419 252.212 1.00 44.11  ? 2188 GLU A O     1 
ATOM   5188  C  CB    . GLU A 1 2188 ? 222.649 185.803 255.086 1.00 35.16  ? 2188 GLU A CB    1 
ATOM   5189  C  CG    . GLU A 1 2188 ? 222.244 187.258 255.095 1.00 49.30  ? 2188 GLU A CG    1 
ATOM   5190  C  CD    . GLU A 1 2188 ? 220.877 187.470 255.712 1.00 56.24  ? 2188 GLU A CD    1 
ATOM   5191  O  OE1   . GLU A 1 2188 ? 220.264 186.475 256.152 1.00 53.34  ? 2188 GLU A OE1   1 
ATOM   5192  O  OE2   . GLU A 1 2188 ? 220.408 188.626 255.744 1.00 61.30  ? 2188 GLU A OE2   1 
ATOM   5193  N  N     . MET A 1 2189 ? 224.869 187.099 252.839 1.00 42.99  ? 2189 MET A N     1 
ATOM   5194  C  CA    . MET A 1 2189 ? 225.012 187.661 251.503 1.00 34.04  ? 2189 MET A CA    1 
ATOM   5195  C  C     . MET A 1 2189 ? 226.374 187.376 250.884 1.00 39.80  ? 2189 MET A C     1 
ATOM   5196  O  O     . MET A 1 2189 ? 226.705 187.962 249.849 1.00 43.55  ? 2189 MET A O     1 
ATOM   5197  C  CB    . MET A 1 2189 ? 224.764 189.169 251.538 1.00 31.04  ? 2189 MET A CB    1 
ATOM   5198  C  CG    . MET A 1 2189 ? 223.335 189.571 251.230 1.00 41.47  ? 2189 MET A CG    1 
ATOM   5199  S  SD    . MET A 1 2189 ? 223.084 191.355 251.275 1.00 49.40  ? 2189 MET A SD    1 
ATOM   5200  C  CE    . MET A 1 2189 ? 223.352 191.780 249.560 1.00 38.54  ? 2189 MET A CE    1 
ATOM   5201  N  N     . TYR A 1 2190 ? 227.168 186.494 251.494 1.00 40.69  ? 2190 TYR A N     1 
ATOM   5202  C  CA    . TYR A 1 2190 ? 228.493 186.118 250.996 1.00 33.13  ? 2190 TYR A CA    1 
ATOM   5203  C  C     . TYR A 1 2190 ? 229.436 187.314 250.912 1.00 37.52  ? 2190 TYR A C     1 
ATOM   5204  O  O     . TYR A 1 2190 ? 230.304 187.371 250.039 1.00 48.19  ? 2190 TYR A O     1 
ATOM   5205  C  CB    . TYR A 1 2190 ? 228.403 185.424 249.634 1.00 37.35  ? 2190 TYR A CB    1 
ATOM   5206  C  CG    . TYR A 1 2190 ? 227.301 184.399 249.540 1.00 37.74  ? 2190 TYR A CG    1 
ATOM   5207  C  CD1   . TYR A 1 2190 ? 227.393 183.190 250.208 1.00 36.67  ? 2190 TYR A CD1   1 
ATOM   5208  C  CD2   . TYR A 1 2190 ? 226.170 184.642 248.778 1.00 36.06  ? 2190 TYR A CD2   1 
ATOM   5209  C  CE1   . TYR A 1 2190 ? 226.388 182.256 250.124 1.00 38.31  ? 2190 TYR A CE1   1 
ATOM   5210  C  CE2   . TYR A 1 2190 ? 225.161 183.712 248.687 1.00 37.20  ? 2190 TYR A CE2   1 
ATOM   5211  C  CZ    . TYR A 1 2190 ? 225.275 182.520 249.361 1.00 45.90  ? 2190 TYR A CZ    1 
ATOM   5212  O  OH    . TYR A 1 2190 ? 224.268 181.587 249.273 1.00 47.35  ? 2190 TYR A OH    1 
ATOM   5213  N  N     . LEU A 1 2191 ? 229.284 188.273 251.817 1.00 34.78  ? 2191 LEU A N     1 
ATOM   5214  C  CA    . LEU A 1 2191 ? 230.126 189.456 251.846 1.00 33.32  ? 2191 LEU A CA    1 
ATOM   5215  C  C     . LEU A 1 2191 ? 231.109 189.374 253.006 1.00 38.61  ? 2191 LEU A C     1 
ATOM   5216  O  O     . LEU A 1 2191 ? 230.904 188.642 253.976 1.00 45.76  ? 2191 LEU A O     1 
ATOM   5217  C  CB    . LEU A 1 2191 ? 229.282 190.729 251.956 1.00 37.29  ? 2191 LEU A CB    1 
ATOM   5218  C  CG    . LEU A 1 2191 ? 228.265 190.959 250.839 1.00 34.77  ? 2191 LEU A CG    1 
ATOM   5219  C  CD1   . LEU A 1 2191 ? 227.672 192.337 250.954 1.00 35.28  ? 2191 LEU A CD1   1 
ATOM   5220  C  CD2   . LEU A 1 2191 ? 228.905 190.775 249.479 1.00 36.57  ? 2191 LEU A CD2   1 
ATOM   5221  N  N     . THR A 1 2192 ? 232.186 190.142 252.890 1.00 39.99  ? 2192 THR A N     1 
ATOM   5222  C  CA    . THR A 1 2192 ? 233.262 190.145 253.869 1.00 39.77  ? 2192 THR A CA    1 
ATOM   5223  C  C     . THR A 1 2192 ? 233.036 191.263 254.877 1.00 42.24  ? 2192 THR A C     1 
ATOM   5224  O  O     . THR A 1 2192 ? 232.838 192.420 254.496 1.00 46.60  ? 2192 THR A O     1 
ATOM   5225  C  CB    . THR A 1 2192 ? 234.620 190.317 253.187 1.00 39.52  ? 2192 THR A CB    1 
ATOM   5226  O  OG1   . THR A 1 2192 ? 234.908 189.159 252.395 1.00 44.53  ? 2192 THR A OG1   1 
ATOM   5227  C  CG2   . THR A 1 2192 ? 235.718 190.500 254.214 1.00 37.33  ? 2192 THR A CG2   1 
ATOM   5228  N  N     . TYR A 1 2193 ? 233.062 190.910 256.157 1.00 48.08  ? 2193 TYR A N     1 
ATOM   5229  C  CA    . TYR A 1 2193 ? 232.917 191.857 257.250 1.00 42.88  ? 2193 TYR A CA    1 
ATOM   5230  C  C     . TYR A 1 2193 ? 234.247 191.992 257.978 1.00 43.88  ? 2193 TYR A C     1 
ATOM   5231  O  O     . TYR A 1 2193 ? 235.006 191.025 258.085 1.00 45.31  ? 2193 TYR A O     1 
ATOM   5232  C  CB    . TYR A 1 2193 ? 231.817 191.405 258.219 1.00 41.92  ? 2193 TYR A CB    1 
ATOM   5233  C  CG    . TYR A 1 2193 ? 231.680 192.264 259.455 1.00 47.81  ? 2193 TYR A CG    1 
ATOM   5234  C  CD1   . TYR A 1 2193 ? 232.488 192.055 260.564 1.00 46.27  ? 2193 TYR A CD1   1 
ATOM   5235  C  CD2   . TYR A 1 2193 ? 230.741 193.283 259.514 1.00 41.67  ? 2193 TYR A CD2   1 
ATOM   5236  C  CE1   . TYR A 1 2193 ? 232.374 192.836 261.685 1.00 40.85  ? 2193 TYR A CE1   1 
ATOM   5237  C  CE2   . TYR A 1 2193 ? 230.618 194.069 260.639 1.00 38.99  ? 2193 TYR A CE2   1 
ATOM   5238  C  CZ    . TYR A 1 2193 ? 231.438 193.838 261.720 1.00 41.42  ? 2193 TYR A CZ    1 
ATOM   5239  O  OH    . TYR A 1 2193 ? 231.328 194.612 262.847 1.00 47.81  ? 2193 TYR A OH    1 
ATOM   5240  N  N     . GLY A 1 2194 ? 234.528 193.194 258.472 1.00 37.78  ? 2194 GLY A N     1 
ATOM   5241  C  CA    . GLY A 1 2194 ? 235.735 193.422 259.243 1.00 38.93  ? 2194 GLY A CA    1 
ATOM   5242  C  C     . GLY A 1 2194 ? 235.538 194.538 260.244 1.00 43.69  ? 2194 GLY A C     1 
ATOM   5243  O  O     . GLY A 1 2194 ? 234.603 195.337 260.142 1.00 46.53  ? 2194 GLY A O     1 
ATOM   5244  N  N     . ASP A 1 2195 ? 236.437 194.580 261.224 1.00 52.77  ? 2195 ASP A N     1 
ATOM   5245  C  CA    . ASP A 1 2195 ? 236.450 195.619 262.247 1.00 50.33  ? 2195 ASP A CA    1 
ATOM   5246  C  C     . ASP A 1 2195 ? 237.764 196.379 262.165 1.00 52.29  ? 2195 ASP A C     1 
ATOM   5247  O  O     . ASP A 1 2195 ? 238.838 195.779 262.264 1.00 56.27  ? 2195 ASP A O     1 
ATOM   5248  C  CB    . ASP A 1 2195 ? 236.271 195.027 263.647 1.00 51.10  ? 2195 ASP A CB    1 
ATOM   5249  C  CG    . ASP A 1 2195 ? 234.886 194.469 263.872 1.00 57.50  ? 2195 ASP A CG    1 
ATOM   5250  O  OD1   . ASP A 1 2195 ? 233.933 194.982 263.251 1.00 60.42  ? 2195 ASP A OD1   1 
ATOM   5251  O  OD2   . ASP A 1 2195 ? 234.747 193.519 264.670 1.00 58.86  ? 2195 ASP A OD2   1 
ATOM   5252  N  N     . GLY A 1 2196 ? 237.676 197.694 261.994 1.00 60.02  ? 2196 GLY A N     1 
ATOM   5253  C  CA    . GLY A 1 2196 ? 238.852 198.538 262.020 1.00 60.11  ? 2196 GLY A CA    1 
ATOM   5254  C  C     . GLY A 1 2196 ? 239.836 198.264 260.904 1.00 61.31  ? 2196 GLY A C     1 
ATOM   5255  O  O     . GLY A 1 2196 ? 239.577 198.591 259.742 1.00 66.03  ? 2196 GLY A O     1 
ATOM   5256  N  N     . GLU A 1 2197 ? 240.975 197.669 261.247 1.00 61.30  ? 2197 GLU A N     1 
ATOM   5257  C  CA    . GLU A 1 2197 ? 242.034 197.400 260.285 1.00 60.75  ? 2197 GLU A CA    1 
ATOM   5258  C  C     . GLU A 1 2197 ? 241.935 196.015 259.660 1.00 64.10  ? 2197 GLU A C     1 
ATOM   5259  O  O     . GLU A 1 2197 ? 242.797 195.658 258.850 1.00 65.20  ? 2197 GLU A O     1 
ATOM   5260  C  CB    . GLU A 1 2197 ? 243.403 197.567 260.949 1.00 63.03  ? 2197 GLU A CB    1 
ATOM   5261  C  CG    . GLU A 1 2197 ? 243.708 198.993 261.372 1.00 66.53  ? 2197 GLU A CG    1 
ATOM   5262  C  CD    . GLU A 1 2197 ? 243.856 199.932 260.193 1.00 70.67  ? 2197 GLU A CD    1 
ATOM   5263  O  OE1   . GLU A 1 2197 ? 244.315 199.479 259.123 1.00 68.99  ? 2197 GLU A OE1   1 
ATOM   5264  O  OE2   . GLU A 1 2197 ? 243.511 201.124 260.334 1.00 72.36  ? 2197 GLU A OE2   1 
ATOM   5265  N  N     . GLU A 1 2198 ? 240.920 195.231 260.012 1.00 56.84  ? 2198 GLU A N     1 
ATOM   5266  C  CA    . GLU A 1 2198 ? 240.720 193.944 259.371 1.00 51.37  ? 2198 GLU A CA    1 
ATOM   5267  C  C     . GLU A 1 2198 ? 240.257 194.140 257.930 1.00 55.08  ? 2198 GLU A C     1 
ATOM   5268  O  O     . GLU A 1 2198 ? 239.841 195.227 257.521 1.00 53.77  ? 2198 GLU A O     1 
ATOM   5269  C  CB    . GLU A 1 2198 ? 239.696 193.109 260.136 1.00 49.84  ? 2198 GLU A CB    1 
ATOM   5270  C  CG    . GLU A 1 2198 ? 240.057 192.826 261.580 1.00 56.97  ? 2198 GLU A CG    1 
ATOM   5271  C  CD    . GLU A 1 2198 ? 238.935 192.132 262.326 1.00 64.80  ? 2198 GLU A CD    1 
ATOM   5272  O  OE1   . GLU A 1 2198 ? 238.035 191.577 261.661 1.00 63.64  ? 2198 GLU A OE1   1 
ATOM   5273  O  OE2   . GLU A 1 2198 ? 238.950 192.142 263.574 1.00 61.94  ? 2198 GLU A OE2   1 
ATOM   5274  N  N     . VAL A 1 2199 ? 240.338 193.062 257.150 1.00 51.94  ? 2199 VAL A N     1 
ATOM   5275  C  CA    . VAL A 1 2199 ? 239.863 193.104 255.774 1.00 50.01  ? 2199 VAL A CA    1 
ATOM   5276  C  C     . VAL A 1 2199 ? 238.357 193.330 255.773 1.00 47.86  ? 2199 VAL A C     1 
ATOM   5277  O  O     . VAL A 1 2199 ? 237.605 192.640 256.472 1.00 50.00  ? 2199 VAL A O     1 
ATOM   5278  C  CB    . VAL A 1 2199 ? 240.256 191.820 255.026 1.00 47.31  ? 2199 VAL A CB    1 
ATOM   5279  C  CG1   . VAL A 1 2199 ? 239.753 190.586 255.759 1.00 50.59  ? 2199 VAL A CG1   1 
ATOM   5280  C  CG2   . VAL A 1 2199 ? 239.722 191.852 253.607 1.00 48.96  ? 2199 VAL A CG2   1 
ATOM   5281  N  N     . GLY A 1 2200 ? 237.912 194.316 255.001 1.00 45.22  ? 2200 GLY A N     1 
ATOM   5282  C  CA    . GLY A 1 2200 ? 236.534 194.743 255.037 1.00 39.95  ? 2200 GLY A CA    1 
ATOM   5283  C  C     . GLY A 1 2200 ? 236.208 195.754 256.112 1.00 41.79  ? 2200 GLY A C     1 
ATOM   5284  O  O     . GLY A 1 2200 ? 235.048 196.167 256.213 1.00 48.11  ? 2200 GLY A O     1 
ATOM   5285  N  N     . GLY A 1 2201 ? 237.189 196.166 256.917 1.00 44.11  ? 2201 GLY A N     1 
ATOM   5286  C  CA    . GLY A 1 2201 ? 236.916 197.130 257.970 1.00 38.47  ? 2201 GLY A CA    1 
ATOM   5287  C  C     . GLY A 1 2201 ? 236.538 198.497 257.434 1.00 42.98  ? 2201 GLY A C     1 
ATOM   5288  O  O     . GLY A 1 2201 ? 235.641 199.156 257.968 1.00 59.02  ? 2201 GLY A O     1 
ATOM   5289  N  N     . MET A 1 2202 ? 237.219 198.945 256.376 1.00 40.08  ? 2202 MET A N     1 
ATOM   5290  C  CA    . MET A 1 2202 ? 236.888 200.227 255.766 1.00 37.19  ? 2202 MET A CA    1 
ATOM   5291  C  C     . MET A 1 2202 ? 235.479 200.229 255.192 1.00 34.11  ? 2202 MET A C     1 
ATOM   5292  O  O     . MET A 1 2202 ? 234.760 201.226 255.314 1.00 50.99  ? 2202 MET A O     1 
ATOM   5293  C  CB    . MET A 1 2202 ? 237.901 200.565 254.675 1.00 46.06  ? 2202 MET A CB    1 
ATOM   5294  C  CG    . MET A 1 2202 ? 239.345 200.547 255.140 1.00 51.31  ? 2202 MET A CG    1 
ATOM   5295  S  SD    . MET A 1 2202 ? 240.463 201.355 253.978 1.00 68.29  ? 2202 MET A SD    1 
ATOM   5296  C  CE    . MET A 1 2202 ? 239.460 202.738 253.446 1.00 49.10  ? 2202 MET A CE    1 
ATOM   5297  N  N     . TRP A 1 2203 ? 235.065 199.126 254.569 1.00 28.00  ? 2203 TRP A N     1 
ATOM   5298  C  CA    . TRP A 1 2203 ? 233.723 199.058 254.003 1.00 30.14  ? 2203 TRP A CA    1 
ATOM   5299  C  C     . TRP A 1 2203 ? 232.656 199.082 255.092 1.00 33.82  ? 2203 TRP A C     1 
ATOM   5300  O  O     . TRP A 1 2203 ? 231.612 199.725 254.932 1.00 42.69  ? 2203 TRP A O     1 
ATOM   5301  C  CB    . TRP A 1 2203 ? 233.594 197.809 253.132 1.00 35.08  ? 2203 TRP A CB    1 
ATOM   5302  C  CG    . TRP A 1 2203 ? 232.250 197.650 252.514 1.00 37.58  ? 2203 TRP A CG    1 
ATOM   5303  C  CD1   . TRP A 1 2203 ? 231.779 198.279 251.401 1.00 28.74  ? 2203 TRP A CD1   1 
ATOM   5304  C  CD2   . TRP A 1 2203 ? 231.195 196.802 252.973 1.00 35.91  ? 2203 TRP A CD2   1 
ATOM   5305  N  NE1   . TRP A 1 2203 ? 230.494 197.878 251.141 1.00 26.58  ? 2203 TRP A NE1   1 
ATOM   5306  C  CE2   . TRP A 1 2203 ? 230.113 196.969 252.093 1.00 25.90  ? 2203 TRP A CE2   1 
ATOM   5307  C  CE3   . TRP A 1 2203 ? 231.061 195.918 254.046 1.00 36.22  ? 2203 TRP A CE3   1 
ATOM   5308  C  CZ2   . TRP A 1 2203 ? 228.915 196.286 252.251 1.00 31.01  ? 2203 TRP A CZ2   1 
ATOM   5309  C  CZ3   . TRP A 1 2203 ? 229.873 195.244 254.201 1.00 34.11  ? 2203 TRP A CZ3   1 
ATOM   5310  C  CH2   . TRP A 1 2203 ? 228.815 195.430 253.310 1.00 32.16  ? 2203 TRP A CH2   1 
ATOM   5311  N  N     . VAL A 1 2204 ? 232.899 198.401 256.213 1.00 36.23  ? 2204 VAL A N     1 
ATOM   5312  C  CA    . VAL A 1 2204 ? 231.941 198.431 257.314 1.00 36.77  ? 2204 VAL A CA    1 
ATOM   5313  C  C     . VAL A 1 2204 ? 231.890 199.818 257.941 1.00 43.87  ? 2204 VAL A C     1 
ATOM   5314  O  O     . VAL A 1 2204 ? 230.821 200.297 258.342 1.00 54.82  ? 2204 VAL A O     1 
ATOM   5315  C  CB    . VAL A 1 2204 ? 232.283 197.347 258.351 1.00 38.74  ? 2204 VAL A CB    1 
ATOM   5316  C  CG1   . VAL A 1 2204 ? 231.296 197.390 259.502 1.00 41.91  ? 2204 VAL A CG1   1 
ATOM   5317  C  CG2   . VAL A 1 2204 ? 232.270 195.981 257.699 1.00 42.08  ? 2204 VAL A CG2   1 
ATOM   5318  N  N     . GLU A 1 2205 ? 233.040 200.488 258.036 1.00 33.96  ? 2205 GLU A N     1 
ATOM   5319  C  CA    . GLU A 1 2205 ? 233.046 201.869 258.504 1.00 27.92  ? 2205 GLU A CA    1 
ATOM   5320  C  C     . GLU A 1 2205 ? 232.231 202.761 257.578 1.00 32.48  ? 2205 GLU A C     1 
ATOM   5321  O  O     . GLU A 1 2205 ? 231.504 203.648 258.038 1.00 48.30  ? 2205 GLU A O     1 
ATOM   5322  C  CB    . GLU A 1 2205 ? 234.480 202.380 258.616 1.00 36.85  ? 2205 GLU A CB    1 
ATOM   5323  C  CG    . GLU A 1 2205 ? 234.603 203.733 259.288 1.00 51.63  ? 2205 GLU A CG    1 
ATOM   5324  C  CD    . GLU A 1 2205 ? 235.992 204.322 259.161 1.00 58.95  ? 2205 GLU A CD    1 
ATOM   5325  O  OE1   . GLU A 1 2205 ? 236.758 203.854 258.294 1.00 55.62  ? 2205 GLU A OE1   1 
ATOM   5326  O  OE2   . GLU A 1 2205 ? 236.317 205.253 259.928 1.00 53.58  ? 2205 GLU A OE2   1 
ATOM   5327  N  N     . LYS A 1 2206 ? 232.343 202.541 256.268 1.00 39.26  ? 2206 LYS A N     1 
ATOM   5328  C  CA    . LYS A 1 2206 ? 231.541 203.303 255.316 1.00 29.21  ? 2206 LYS A CA    1 
ATOM   5329  C  C     . LYS A 1 2206 ? 230.055 203.012 255.483 1.00 25.95  ? 2206 LYS A C     1 
ATOM   5330  O  O     . LYS A 1 2206 ? 229.223 203.913 255.342 1.00 38.72  ? 2206 LYS A O     1 
ATOM   5331  C  CB    . LYS A 1 2206 ? 231.990 202.996 253.890 1.00 24.67  ? 2206 LYS A CB    1 
ATOM   5332  C  CG    . LYS A 1 2206 ? 233.219 203.764 253.459 1.00 29.29  ? 2206 LYS A CG    1 
ATOM   5333  C  CD    . LYS A 1 2206 ? 232.928 205.245 253.367 1.00 32.08  ? 2206 LYS A CD    1 
ATOM   5334  C  CE    . LYS A 1 2206 ? 234.171 206.061 253.645 1.00 24.71  ? 2206 LYS A CE    1 
ATOM   5335  N  NZ    . LYS A 1 2206 ? 233.922 207.513 253.456 1.00 24.50  ? 2206 LYS A NZ    1 
ATOM   5336  N  N     . VAL A 1 2207 ? 229.703 201.758 255.770 1.00 37.91  ? 2207 VAL A N     1 
ATOM   5337  C  CA    . VAL A 1 2207 ? 228.302 201.413 256.009 1.00 41.09  ? 2207 VAL A CA    1 
ATOM   5338  C  C     . VAL A 1 2207 ? 227.774 202.138 257.242 1.00 40.92  ? 2207 VAL A C     1 
ATOM   5339  O  O     . VAL A 1 2207 ? 226.651 202.658 257.245 1.00 45.10  ? 2207 VAL A O     1 
ATOM   5340  C  CB    . VAL A 1 2207 ? 228.140 199.886 256.134 1.00 39.73  ? 2207 VAL A CB    1 
ATOM   5341  C  CG1   . VAL A 1 2207 ? 226.732 199.534 256.568 1.00 36.09  ? 2207 VAL A CG1   1 
ATOM   5342  C  CG2   . VAL A 1 2207 ? 228.464 199.213 254.816 1.00 36.78  ? 2207 VAL A CG2   1 
ATOM   5343  N  N     . LEU A 1 2208 ? 228.572 202.181 258.310 1.00 40.16  ? 2208 LEU A N     1 
ATOM   5344  C  CA    . LEU A 1 2208 ? 228.158 202.904 259.512 1.00 28.33  ? 2208 LEU A CA    1 
ATOM   5345  C  C     . LEU A 1 2208 ? 228.030 204.401 259.245 1.00 30.54  ? 2208 LEU A C     1 
ATOM   5346  O  O     . LEU A 1 2208 ? 227.109 205.055 259.755 1.00 45.75  ? 2208 LEU A O     1 
ATOM   5347  C  CB    . LEU A 1 2208 ? 229.145 202.644 260.647 1.00 33.64  ? 2208 LEU A CB    1 
ATOM   5348  C  CG    . LEU A 1 2208 ? 229.354 201.189 261.068 1.00 33.44  ? 2208 LEU A CG    1 
ATOM   5349  C  CD1   . LEU A 1 2208 ? 230.430 201.098 262.129 1.00 40.72  ? 2208 LEU A CD1   1 
ATOM   5350  C  CD2   . LEU A 1 2208 ? 228.065 200.568 261.558 1.00 32.41  ? 2208 LEU A CD2   1 
ATOM   5351  N  N     . GLN A 1 2209 ? 228.953 204.964 258.462 1.00 32.45  ? 2209 GLN A N     1 
ATOM   5352  C  CA    . GLN A 1 2209 ? 228.854 206.371 258.088 1.00 27.81  ? 2209 GLN A CA    1 
ATOM   5353  C  C     . GLN A 1 2209 ? 227.586 206.638 257.293 1.00 27.69  ? 2209 GLN A C     1 
ATOM   5354  O  O     . GLN A 1 2209 ? 226.924 207.664 257.487 1.00 39.76  ? 2209 GLN A O     1 
ATOM   5355  C  CB    . GLN A 1 2209 ? 230.081 206.787 257.279 1.00 21.38  ? 2209 GLN A CB    1 
ATOM   5356  C  CG    . GLN A 1 2209 ? 231.353 206.893 258.085 1.00 28.61  ? 2209 GLN A CG    1 
ATOM   5357  C  CD    . GLN A 1 2209 ? 232.557 207.162 257.217 1.00 28.44  ? 2209 GLN A CD    1 
ATOM   5358  O  OE1   . GLN A 1 2209 ? 232.432 207.346 256.010 1.00 42.47  ? 2209 GLN A OE1   1 
ATOM   5359  N  NE2   . GLN A 1 2209 ? 233.735 207.178 257.824 1.00 31.29  ? 2209 GLN A NE2   1 
ATOM   5360  N  N     . LEU A 1 2210 ? 227.241 205.730 256.379 1.00 33.94  ? 2210 LEU A N     1 
ATOM   5361  C  CA    . LEU A 1 2210 ? 226.000 205.861 255.628 1.00 32.06  ? 2210 LEU A CA    1 
ATOM   5362  C  C     . LEU A 1 2210 ? 224.793 205.800 256.552 1.00 26.78  ? 2210 LEU A C     1 
ATOM   5363  O  O     . LEU A 1 2210 ? 223.823 206.537 256.363 1.00 34.07  ? 2210 LEU A O     1 
ATOM   5364  C  CB    . LEU A 1 2210 ? 225.918 204.772 254.559 1.00 28.86  ? 2210 LEU A CB    1 
ATOM   5365  C  CG    . LEU A 1 2210 ? 224.613 204.695 253.771 1.00 34.12  ? 2210 LEU A CG    1 
ATOM   5366  C  CD1   . LEU A 1 2210 ? 224.511 205.866 252.819 1.00 42.10  ? 2210 LEU A CD1   1 
ATOM   5367  C  CD2   . LEU A 1 2210 ? 224.531 203.384 253.019 1.00 32.72  ? 2210 LEU A CD2   1 
ATOM   5368  N  N     . TYR A 1 2211 ? 224.839 204.928 257.560 1.00 34.46  ? 2211 TYR A N     1 
ATOM   5369  C  CA    . TYR A 1 2211 ? 223.754 204.868 258.536 1.00 31.02  ? 2211 TYR A CA    1 
ATOM   5370  C  C     . TYR A 1 2211 ? 223.598 206.192 259.274 1.00 33.23  ? 2211 TYR A C     1 
ATOM   5371  O  O     . TYR A 1 2211 ? 222.481 206.697 259.436 1.00 48.11  ? 2211 TYR A O     1 
ATOM   5372  C  CB    . TYR A 1 2211 ? 224.006 203.737 259.528 1.00 29.89  ? 2211 TYR A CB    1 
ATOM   5373  C  CG    . TYR A 1 2211 ? 223.024 203.707 260.672 1.00 39.43  ? 2211 TYR A CG    1 
ATOM   5374  C  CD1   . TYR A 1 2211 ? 221.658 203.694 260.439 1.00 35.56  ? 2211 TYR A CD1   1 
ATOM   5375  C  CD2   . TYR A 1 2211 ? 223.464 203.707 261.986 1.00 39.82  ? 2211 TYR A CD2   1 
ATOM   5376  C  CE1   . TYR A 1 2211 ? 220.760 203.675 261.482 1.00 38.43  ? 2211 TYR A CE1   1 
ATOM   5377  C  CE2   . TYR A 1 2211 ? 222.575 203.686 263.034 1.00 37.37  ? 2211 TYR A CE2   1 
ATOM   5378  C  CZ    . TYR A 1 2211 ? 221.223 203.669 262.778 1.00 45.89  ? 2211 TYR A CZ    1 
ATOM   5379  O  OH    . TYR A 1 2211 ? 220.329 203.648 263.823 1.00 52.77  ? 2211 TYR A OH    1 
ATOM   5380  N  N     . GLN A 1 2212 ? 224.709 206.774 259.725 1.00 36.84  ? 2212 GLN A N     1 
ATOM   5381  C  CA    . GLN A 1 2212 ? 224.631 208.044 260.445 1.00 31.29  ? 2212 GLN A CA    1 
ATOM   5382  C  C     . GLN A 1 2212 ? 224.114 209.167 259.551 1.00 36.82  ? 2212 GLN A C     1 
ATOM   5383  O  O     . GLN A 1 2212 ? 223.244 209.949 259.959 1.00 47.34  ? 2212 GLN A O     1 
ATOM   5384  C  CB    . GLN A 1 2212 ? 226.001 208.414 261.002 1.00 35.82  ? 2212 GLN A CB    1 
ATOM   5385  C  CG    . GLN A 1 2212 ? 226.563 207.444 262.015 1.00 39.16  ? 2212 GLN A CG    1 
ATOM   5386  C  CD    . GLN A 1 2212 ? 227.872 207.932 262.595 1.00 47.36  ? 2212 GLN A CD    1 
ATOM   5387  O  OE1   . GLN A 1 2212 ? 228.807 208.254 261.861 1.00 48.65  ? 2212 GLN A OE1   1 
ATOM   5388  N  NE2   . GLN A 1 2212 ? 227.949 207.988 263.919 1.00 46.27  ? 2212 GLN A NE2   1 
ATOM   5389  N  N     . ILE A 1 2213 ? 224.644 209.268 258.332 1.00 40.08  ? 2213 ILE A N     1 
ATOM   5390  C  CA    . ILE A 1 2213 ? 224.202 210.315 257.417 1.00 35.07  ? 2213 ILE A CA    1 
ATOM   5391  C  C     . ILE A 1 2213 ? 222.736 210.120 257.053 1.00 26.86  ? 2213 ILE A C     1 
ATOM   5392  O  O     . ILE A 1 2213 ? 222.001 211.089 256.836 1.00 28.88  ? 2213 ILE A O     1 
ATOM   5393  C  CB    . ILE A 1 2213 ? 225.116 210.363 256.179 1.00 27.35  ? 2213 ILE A CB    1 
ATOM   5394  C  CG1   . ILE A 1 2213 ? 226.551 210.680 256.601 1.00 26.07  ? 2213 ILE A CG1   1 
ATOM   5395  C  CG2   . ILE A 1 2213 ? 224.639 211.403 255.200 1.00 31.30  ? 2213 ILE A CG2   1 
ATOM   5396  C  CD1   . ILE A 1 2213 ? 226.728 212.083 257.133 1.00 37.55  ? 2213 ILE A CD1   1 
ATOM   5397  N  N     . THR A 1 2214 ? 222.282 208.866 256.992 1.00 34.66  ? 2214 THR A N     1 
ATOM   5398  C  CA    . THR A 1 2214 ? 220.854 208.602 256.860 1.00 32.68  ? 2214 THR A CA    1 
ATOM   5399  C  C     . THR A 1 2214 ? 220.092 209.131 258.064 1.00 32.22  ? 2214 THR A C     1 
ATOM   5400  O  O     . THR A 1 2214 ? 218.999 209.692 257.923 1.00 36.48  ? 2214 THR A O     1 
ATOM   5401  C  CB    . THR A 1 2214 ? 220.610 207.101 256.699 1.00 29.79  ? 2214 THR A CB    1 
ATOM   5402  O  OG1   . THR A 1 2214 ? 221.214 206.640 255.486 1.00 46.79  ? 2214 THR A OG1   1 
ATOM   5403  C  CG2   . THR A 1 2214 ? 219.127 206.807 256.654 1.00 34.88  ? 2214 THR A CG2   1 
ATOM   5404  N  N     . GLN A 1 2215 ? 220.657 208.959 259.260 1.00 38.03  ? 2215 GLN A N     1 
ATOM   5405  C  CA    . GLN A 1 2215 ? 220.001 209.446 260.469 1.00 33.62  ? 2215 GLN A CA    1 
ATOM   5406  C  C     . GLN A 1 2215 ? 219.821 210.957 260.431 1.00 37.63  ? 2215 GLN A C     1 
ATOM   5407  O  O     . GLN A 1 2215 ? 218.779 211.476 260.848 1.00 40.92  ? 2215 GLN A O     1 
ATOM   5408  C  CB    . GLN A 1 2215 ? 220.803 209.039 261.706 1.00 32.29  ? 2215 GLN A CB    1 
ATOM   5409  C  CG    . GLN A 1 2215 ? 220.690 207.575 262.085 1.00 30.28  ? 2215 GLN A CG    1 
ATOM   5410  C  CD    . GLN A 1 2215 ? 219.363 207.247 262.732 1.00 48.14  ? 2215 GLN A CD    1 
ATOM   5411  O  OE1   . GLN A 1 2215 ? 218.347 207.105 262.053 1.00 50.60  ? 2215 GLN A OE1   1 
ATOM   5412  N  NE2   . GLN A 1 2215 ? 219.363 207.127 264.054 1.00 50.39  ? 2215 GLN A NE2   1 
ATOM   5413  N  N     . ILE A 1 2216 ? 220.824 211.683 259.938 1.00 38.25  ? 2216 ILE A N     1 
ATOM   5414  C  CA    . ILE A 1 2216 ? 220.781 213.142 259.987 1.00 35.07  ? 2216 ILE A CA    1 
ATOM   5415  C  C     . ILE A 1 2216 ? 220.218 213.791 258.722 1.00 35.84  ? 2216 ILE A C     1 
ATOM   5416  O  O     . ILE A 1 2216 ? 219.689 214.910 258.803 1.00 39.71  ? 2216 ILE A O     1 
ATOM   5417  C  CB    . ILE A 1 2216 ? 222.176 213.724 260.299 1.00 33.82  ? 2216 ILE A CB    1 
ATOM   5418  C  CG1   . ILE A 1 2216 ? 223.155 213.422 259.166 1.00 31.80  ? 2216 ILE A CG1   1 
ATOM   5419  C  CG2   . ILE A 1 2216 ? 222.700 213.178 261.617 1.00 38.07  ? 2216 ILE A CG2   1 
ATOM   5420  C  CD1   . ILE A 1 2216 ? 224.469 214.155 259.290 1.00 31.24  ? 2216 ILE A CD1   1 
ATOM   5421  N  N     . ASN A 1 2217 ? 220.304 213.133 257.568 1.00 40.46  ? 2217 ASN A N     1 
ATOM   5422  C  CA    . ASN A 1 2217 ? 219.858 213.706 256.304 1.00 30.44  ? 2217 ASN A CA    1 
ATOM   5423  C  C     . ASN A 1 2217 ? 218.717 212.888 255.718 1.00 35.13  ? 2217 ASN A C     1 
ATOM   5424  O  O     . ASN A 1 2217 ? 218.659 211.668 255.898 1.00 53.32  ? 2217 ASN A O     1 
ATOM   5425  C  CB    . ASN A 1 2217 ? 221.003 213.772 255.284 1.00 20.78  ? 2217 ASN A CB    1 
ATOM   5426  C  CG    . ASN A 1 2217 ? 222.081 214.761 255.672 1.00 39.76  ? 2217 ASN A CG    1 
ATOM   5427  O  OD1   . ASN A 1 2217 ? 223.214 214.384 255.967 1.00 38.80  ? 2217 ASN A OD1   1 
ATOM   5428  N  ND2   . ASN A 1 2217 ? 221.736 216.040 255.661 1.00 44.56  ? 2217 ASN A ND2   1 
ATOM   5429  N  N     . HIS A 1 2218 ? 217.810 213.561 255.011 1.00 32.71  ? 2218 HIS A N     1 
ATOM   5430  C  CA    . HIS A 1 2218 ? 216.777 212.884 254.238 1.00 27.51  ? 2218 HIS A CA    1 
ATOM   5431  C  C     . HIS A 1 2218 ? 217.094 212.839 252.747 1.00 32.57  ? 2218 HIS A C     1 
ATOM   5432  O  O     . HIS A 1 2218 ? 216.279 212.335 251.968 1.00 31.05  ? 2218 HIS A O     1 
ATOM   5433  C  CB    . HIS A 1 2218 ? 215.416 213.549 254.464 1.00 32.26  ? 2218 HIS A CB    1 
ATOM   5434  C  CG    . HIS A 1 2218 ? 215.272 214.880 253.799 1.00 37.17  ? 2218 HIS A CG    1 
ATOM   5435  N  ND1   . HIS A 1 2218 ? 215.781 216.042 254.335 1.00 32.43  ? 2218 HIS A ND1   1 
ATOM   5436  C  CD2   . HIS A 1 2218 ? 214.662 215.233 252.644 1.00 38.93  ? 2218 HIS A CD2   1 
ATOM   5437  C  CE1   . HIS A 1 2218 ? 215.497 217.054 253.534 1.00 33.83  ? 2218 HIS A CE1   1 
ATOM   5438  N  NE2   . HIS A 1 2218 ? 214.819 216.589 252.501 1.00 42.70  ? 2218 HIS A NE2   1 
ATOM   5439  N  N     . GLY A 1 2219 ? 218.253 213.352 252.339 1.00 40.50  ? 2219 GLY A N     1 
ATOM   5440  C  CA    . GLY A 1 2219 ? 218.743 213.248 250.978 1.00 25.03  ? 2219 GLY A CA    1 
ATOM   5441  C  C     . GLY A 1 2219 ? 220.189 212.797 250.978 1.00 28.14  ? 2219 GLY A C     1 
ATOM   5442  O  O     . GLY A 1 2219 ? 221.010 213.358 251.708 1.00 52.05  ? 2219 GLY A O     1 
ATOM   5443  N  N     . LEU A 1 2220 ? 220.517 211.788 250.175 1.00 27.11  ? 2220 LEU A N     1 
ATOM   5444  C  CA    . LEU A 1 2220 ? 221.761 211.051 250.329 1.00 23.25  ? 2220 LEU A CA    1 
ATOM   5445  C  C     . LEU A 1 2220 ? 222.454 210.879 248.983 1.00 31.31  ? 2220 LEU A C     1 
ATOM   5446  O  O     . LEU A 1 2220 ? 221.809 210.777 247.940 1.00 46.52  ? 2220 LEU A O     1 
ATOM   5447  C  CB    . LEU A 1 2220 ? 221.494 209.676 250.948 1.00 39.40  ? 2220 LEU A CB    1 
ATOM   5448  C  CG    . LEU A 1 2220 ? 220.967 209.722 252.379 1.00 39.45  ? 2220 LEU A CG    1 
ATOM   5449  C  CD1   . LEU A 1 2220 ? 220.606 208.339 252.855 1.00 39.66  ? 2220 LEU A CD1   1 
ATOM   5450  C  CD2   . LEU A 1 2220 ? 221.982 210.351 253.279 1.00 40.46  ? 2220 LEU A CD2   1 
ATOM   5451  N  N     . MET A 1 2221 ? 223.784 210.844 249.015 1.00 28.86  ? 2221 MET A N     1 
ATOM   5452  C  CA    . MET A 1 2221 ? 224.561 210.448 247.847 1.00 34.11  ? 2221 MET A CA    1 
ATOM   5453  C  C     . MET A 1 2221 ? 225.694 209.521 248.255 1.00 37.61  ? 2221 MET A C     1 
ATOM   5454  O  O     . MET A 1 2221 ? 226.436 209.819 249.194 1.00 40.37  ? 2221 MET A O     1 
ATOM   5455  C  CB    . MET A 1 2221 ? 225.124 211.654 247.082 1.00 27.81  ? 2221 MET A CB    1 
ATOM   5456  C  CG    . MET A 1 2221 ? 224.244 212.113 245.932 1.00 33.43  ? 2221 MET A CG    1 
ATOM   5457  S  SD    . MET A 1 2221 ? 224.509 213.797 245.367 1.00 62.77  ? 2221 MET A SD    1 
ATOM   5458  C  CE    . MET A 1 2221 ? 223.141 214.005 244.237 1.00 37.57  ? 2221 MET A CE    1 
ATOM   5459  N  N     . MET A 1 2222 ? 225.827 208.404 247.536 1.00 33.60  ? 2222 MET A N     1 
ATOM   5460  C  CA    . MET A 1 2222 ? 226.968 207.499 247.654 1.00 27.07  ? 2222 MET A CA    1 
ATOM   5461  C  C     . MET A 1 2222 ? 227.854 207.763 246.443 1.00 36.11  ? 2222 MET A C     1 
ATOM   5462  O  O     . MET A 1 2222 ? 227.611 207.226 245.360 1.00 48.07  ? 2222 MET A O     1 
ATOM   5463  C  CB    . MET A 1 2222 ? 226.537 206.034 247.694 1.00 39.42  ? 2222 MET A CB    1 
ATOM   5464  C  CG    . MET A 1 2222 ? 225.958 205.556 249.011 1.00 39.72  ? 2222 MET A CG    1 
ATOM   5465  S  SD    . MET A 1 2222 ? 224.300 206.194 249.284 1.00 71.15  ? 2222 MET A SD    1 
ATOM   5466  C  CE    . MET A 1 2222 ? 223.376 205.185 248.133 1.00 35.65  ? 2222 MET A CE    1 
ATOM   5467  N  N     . VAL A 1 2223 ? 228.862 208.587 246.616 1.00 39.71  ? 2223 VAL A N     1 
ATOM   5468  C  CA    . VAL A 1 2223 ? 229.759 208.932 245.521 1.00 32.86  ? 2223 VAL A CA    1 
ATOM   5469  C  C     . VAL A 1 2223 ? 231.003 208.065 245.619 1.00 28.15  ? 2223 VAL A C     1 
ATOM   5470  O  O     . VAL A 1 2223 ? 231.475 207.741 246.712 1.00 45.34  ? 2223 VAL A O     1 
ATOM   5471  C  CB    . VAL A 1 2223 ? 230.112 210.433 245.545 1.00 33.87  ? 2223 VAL A CB    1 
ATOM   5472  C  CG1   . VAL A 1 2223 ? 230.844 210.829 244.280 1.00 37.97  ? 2223 VAL A CG1   1 
ATOM   5473  C  CG2   . VAL A 1 2223 ? 228.862 211.268 245.722 1.00 35.52  ? 2223 VAL A CG2   1 
ATOM   5474  N  N     . GLY A 1 2224 ? 231.536 207.674 244.468 1.00 25.64  ? 2224 GLY A N     1 
ATOM   5475  C  CA    . GLY A 1 2224 ? 232.754 206.906 244.421 1.00 26.52  ? 2224 GLY A CA    1 
ATOM   5476  C  C     . GLY A 1 2224 ? 232.884 206.130 243.131 1.00 32.40  ? 2224 GLY A C     1 
ATOM   5477  O  O     . GLY A 1 2224 ? 231.898 205.860 242.444 1.00 42.32  ? 2224 GLY A O     1 
ATOM   5478  N  N     . PRO A 1 2225 ? 234.111 205.746 242.784 1.00 37.98  ? 2225 PRO A N     1 
ATOM   5479  C  CA    . PRO A 1 2225 ? 234.338 205.034 241.523 1.00 34.87  ? 2225 PRO A CA    1 
ATOM   5480  C  C     . PRO A 1 2225 ? 233.514 203.759 241.439 1.00 41.37  ? 2225 PRO A C     1 
ATOM   5481  O  O     . PRO A 1 2225 ? 233.033 203.225 242.440 1.00 47.04  ? 2225 PRO A O     1 
ATOM   5482  C  CB    . PRO A 1 2225 ? 235.837 204.725 241.556 1.00 33.29  ? 2225 PRO A CB    1 
ATOM   5483  C  CG    . PRO A 1 2225 ? 236.411 205.745 242.469 1.00 36.76  ? 2225 PRO A CG    1 
ATOM   5484  C  CD    . PRO A 1 2225 ? 235.367 206.006 243.505 1.00 39.44  ? 2225 PRO A CD    1 
ATOM   5485  N  N     . SER A 1 2226 ? 233.343 203.278 240.210 1.00 42.38  ? 2226 SER A N     1 
ATOM   5486  C  CA    . SER A 1 2226 ? 232.561 202.072 239.991 1.00 36.12  ? 2226 SER A CA    1 
ATOM   5487  C  C     . SER A 1 2226 ? 233.211 200.885 240.687 1.00 43.89  ? 2226 SER A C     1 
ATOM   5488  O  O     . SER A 1 2226 ? 234.437 200.756 240.720 1.00 50.62  ? 2226 SER A O     1 
ATOM   5489  C  CB    . SER A 1 2226 ? 232.419 201.792 238.496 1.00 35.03  ? 2226 SER A CB    1 
ATOM   5490  O  OG    . SER A 1 2226 ? 231.467 200.771 238.264 1.00 46.43  ? 2226 SER A OG    1 
ATOM   5491  N  N     . GLY A 1 2227 ? 232.379 200.015 241.245 1.00 37.93  ? 2227 GLY A N     1 
ATOM   5492  C  CA    . GLY A 1 2227 ? 232.882 198.876 241.987 1.00 30.13  ? 2227 GLY A CA    1 
ATOM   5493  C  C     . GLY A 1 2227 ? 233.604 199.233 243.266 1.00 37.92  ? 2227 GLY A C     1 
ATOM   5494  O  O     . GLY A 1 2227 ? 234.683 198.691 243.536 1.00 46.95  ? 2227 GLY A O     1 
ATOM   5495  N  N     . SER A 1 2228 ? 233.045 200.147 244.056 1.00 42.99  ? 2228 SER A N     1 
ATOM   5496  C  CA    . SER A 1 2228 ? 233.614 200.520 245.342 1.00 37.89  ? 2228 SER A CA    1 
ATOM   5497  C  C     . SER A 1 2228 ? 232.789 200.027 246.523 1.00 40.67  ? 2228 SER A C     1 
ATOM   5498  O  O     . SER A 1 2228 ? 233.188 200.243 247.670 1.00 49.75  ? 2228 SER A O     1 
ATOM   5499  C  CB    . SER A 1 2228 ? 233.778 202.040 245.424 1.00 33.50  ? 2228 SER A CB    1 
ATOM   5500  O  OG    . SER A 1 2228 ? 232.625 202.699 244.936 1.00 40.28  ? 2228 SER A OG    1 
ATOM   5501  N  N     . GLY A 1 2229 ? 231.659 199.370 246.278 1.00 43.46  ? 2229 GLY A N     1 
ATOM   5502  C  CA    . GLY A 1 2229 ? 230.875 198.791 247.349 1.00 32.07  ? 2229 GLY A CA    1 
ATOM   5503  C  C     . GLY A 1 2229 ? 229.650 199.565 247.773 1.00 35.66  ? 2229 GLY A C     1 
ATOM   5504  O  O     . GLY A 1 2229 ? 229.104 199.278 248.842 1.00 48.30  ? 2229 GLY A O     1 
ATOM   5505  N  N     . LYS A 1 2230 ? 229.192 200.531 246.975 1.00 40.10  ? 2230 LYS A N     1 
ATOM   5506  C  CA    . LYS A 1 2230 ? 228.076 201.378 247.391 1.00 32.45  ? 2230 LYS A CA    1 
ATOM   5507  C  C     . LYS A 1 2230 ? 226.765 200.601 247.438 1.00 39.60  ? 2230 LYS A C     1 
ATOM   5508  O  O     . LYS A 1 2230 ? 226.014 200.686 248.421 1.00 55.21  ? 2230 LYS A O     1 
ATOM   5509  C  CB    . LYS A 1 2230 ? 227.957 202.574 246.450 1.00 46.06  ? 2230 LYS A CB    1 
ATOM   5510  C  CG    . LYS A 1 2230 ? 229.225 203.395 246.331 1.00 48.18  ? 2230 LYS A CG    1 
ATOM   5511  C  CD    . LYS A 1 2230 ? 229.141 204.389 245.192 1.00 39.83  ? 2230 LYS A CD    1 
ATOM   5512  C  CE    . LYS A 1 2230 ? 229.041 203.687 243.857 1.00 36.28  ? 2230 LYS A CE    1 
ATOM   5513  N  NZ    . LYS A 1 2230 ? 229.292 204.603 242.721 1.00 48.81  ? 2230 LYS A NZ    1 
ATOM   5514  N  N     . SER A 1 2231 ? 226.462 199.851 246.374 1.00 39.51  ? 2231 SER A N     1 
ATOM   5515  C  CA    . SER A 1 2231 ? 225.203 199.115 246.320 1.00 28.59  ? 2231 SER A CA    1 
ATOM   5516  C  C     . SER A 1 2231 ? 225.124 198.079 247.428 1.00 37.20  ? 2231 SER A C     1 
ATOM   5517  O  O     . SER A 1 2231 ? 224.103 197.973 248.118 1.00 46.22  ? 2231 SER A O     1 
ATOM   5518  C  CB    . SER A 1 2231 ? 225.039 198.442 244.959 1.00 36.55  ? 2231 SER A CB    1 
ATOM   5519  O  OG    . SER A 1 2231 ? 225.179 199.371 243.902 1.00 43.29  ? 2231 SER A OG    1 
ATOM   5520  N  N     . MET A 1 2232 ? 226.195 197.307 247.613 1.00 41.85  ? 2232 MET A N     1 
ATOM   5521  C  CA    . MET A 1 2232 ? 226.237 196.368 248.721 1.00 33.51  ? 2232 MET A CA    1 
ATOM   5522  C  C     . MET A 1 2232 ? 226.163 197.077 250.059 1.00 35.95  ? 2232 MET A C     1 
ATOM   5523  O  O     . MET A 1 2232 ? 225.506 196.574 250.971 1.00 53.88  ? 2232 MET A O     1 
ATOM   5524  C  CB    . MET A 1 2232 ? 227.500 195.514 248.650 1.00 33.16  ? 2232 MET A CB    1 
ATOM   5525  C  CG    . MET A 1 2232 ? 227.461 194.345 247.663 1.00 40.09  ? 2232 MET A CG    1 
ATOM   5526  S  SD    . MET A 1 2232 ? 225.988 193.300 247.644 1.00 58.49  ? 2232 MET A SD    1 
ATOM   5527  C  CE    . MET A 1 2232 ? 224.958 194.123 246.431 1.00 46.85  ? 2232 MET A CE    1 
ATOM   5528  N  N     . ALA A 1 2233 ? 226.799 198.244 250.187 1.00 49.00  ? 2233 ALA A N     1 
ATOM   5529  C  CA    . ALA A 1 2233 ? 226.726 198.991 251.436 1.00 39.59  ? 2233 ALA A CA    1 
ATOM   5530  C  C     . ALA A 1 2233 ? 225.284 199.312 251.801 1.00 34.97  ? 2233 ALA A C     1 
ATOM   5531  O  O     . ALA A 1 2233 ? 224.831 198.992 252.905 1.00 45.22  ? 2233 ALA A O     1 
ATOM   5532  C  CB    . ALA A 1 2233 ? 227.548 200.274 251.337 1.00 32.80  ? 2233 ALA A CB    1 
ATOM   5533  N  N     . TRP A 1 2234 ? 224.531 199.916 250.878 1.00 24.77  ? 2234 TRP A N     1 
ATOM   5534  C  CA    . TRP A 1 2234 ? 223.177 200.306 251.252 1.00 25.40  ? 2234 TRP A CA    1 
ATOM   5535  C  C     . TRP A 1 2234 ? 222.214 199.124 251.313 1.00 36.74  ? 2234 TRP A C     1 
ATOM   5536  O  O     . TRP A 1 2234 ? 221.284 199.155 252.123 1.00 44.60  ? 2234 TRP A O     1 
ATOM   5537  C  CB    . TRP A 1 2234 ? 222.641 201.415 250.332 1.00 29.39  ? 2234 TRP A CB    1 
ATOM   5538  C  CG    . TRP A 1 2234 ? 222.234 201.038 248.941 1.00 28.64  ? 2234 TRP A CG    1 
ATOM   5539  C  CD1   . TRP A 1 2234 ? 222.942 201.256 247.798 1.00 25.28  ? 2234 TRP A CD1   1 
ATOM   5540  C  CD2   . TRP A 1 2234 ? 220.999 200.435 248.537 1.00 36.33  ? 2234 TRP A CD2   1 
ATOM   5541  N  NE1   . TRP A 1 2234 ? 222.239 200.801 246.711 1.00 23.46  ? 2234 TRP A NE1   1 
ATOM   5542  C  CE2   . TRP A 1 2234 ? 221.043 200.291 247.139 1.00 32.43  ? 2234 TRP A CE2   1 
ATOM   5543  C  CE3   . TRP A 1 2234 ? 219.868 199.988 249.224 1.00 32.51  ? 2234 TRP A CE3   1 
ATOM   5544  C  CZ2   . TRP A 1 2234 ? 220.002 199.722 246.417 1.00 34.43  ? 2234 TRP A CZ2   1 
ATOM   5545  C  CZ3   . TRP A 1 2234 ? 218.839 199.422 248.507 1.00 25.34  ? 2234 TRP A CZ3   1 
ATOM   5546  C  CH2   . TRP A 1 2234 ? 218.910 199.294 247.118 1.00 32.65  ? 2234 TRP A CH2   1 
ATOM   5547  N  N     . ARG A 1 2235 ? 222.433 198.063 250.530 1.00 42.62  ? 2235 ARG A N     1 
ATOM   5548  C  CA    . ARG A 1 2235 ? 221.586 196.878 250.658 1.00 29.68  ? 2235 ARG A CA    1 
ATOM   5549  C  C     . ARG A 1 2235 ? 221.799 196.184 252.000 1.00 36.01  ? 2235 ARG A C     1 
ATOM   5550  O  O     . ARG A 1 2235 ? 220.831 195.810 252.680 1.00 47.68  ? 2235 ARG A O     1 
ATOM   5551  C  CB    . ARG A 1 2235 ? 221.867 195.913 249.510 1.00 37.75  ? 2235 ARG A CB    1 
ATOM   5552  C  CG    . ARG A 1 2235 ? 221.317 196.358 248.170 1.00 37.22  ? 2235 ARG A CG    1 
ATOM   5553  C  CD    . ARG A 1 2235 ? 221.574 195.304 247.116 1.00 45.54  ? 2235 ARG A CD    1 
ATOM   5554  N  NE    . ARG A 1 2235 ? 221.336 195.797 245.765 1.00 50.69  ? 2235 ARG A NE    1 
ATOM   5555  C  CZ    . ARG A 1 2235 ? 220.140 195.915 245.206 1.00 56.00  ? 2235 ARG A CZ    1 
ATOM   5556  N  NH1   . ARG A 1 2235 ? 219.036 195.590 245.858 1.00 49.92  ? 2235 ARG A NH1   1 
ATOM   5557  N  NH2   . ARG A 1 2235 ? 220.050 196.369 243.960 1.00 51.78  ? 2235 ARG A NH2   1 
ATOM   5558  N  N     . VAL A 1 2236 ? 223.062 195.998 252.394 1.00 37.72  ? 2236 VAL A N     1 
ATOM   5559  C  CA    . VAL A 1 2236 ? 223.373 195.415 253.692 1.00 31.30  ? 2236 VAL A CA    1 
ATOM   5560  C  C     . VAL A 1 2236 ? 222.844 196.294 254.813 1.00 40.62  ? 2236 VAL A C     1 
ATOM   5561  O  O     . VAL A 1 2236 ? 222.327 195.792 255.817 1.00 47.28  ? 2236 VAL A O     1 
ATOM   5562  C  CB    . VAL A 1 2236 ? 224.890 195.185 253.811 1.00 29.08  ? 2236 VAL A CB    1 
ATOM   5563  C  CG1   . VAL A 1 2236 ? 225.273 194.840 255.229 1.00 40.53  ? 2236 VAL A CG1   1 
ATOM   5564  C  CG2   . VAL A 1 2236 ? 225.312 194.071 252.887 1.00 37.98  ? 2236 VAL A CG2   1 
ATOM   5565  N  N     . LEU A 1 2237 ? 222.958 197.615 254.667 1.00 37.03  ? 2237 LEU A N     1 
ATOM   5566  C  CA    . LEU A 1 2237 ? 222.420 198.507 255.685 1.00 27.32  ? 2237 LEU A CA    1 
ATOM   5567  C  C     . LEU A 1 2237 ? 220.909 198.370 255.795 1.00 26.81  ? 2237 LEU A C     1 
ATOM   5568  O  O     . LEU A 1 2237 ? 220.364 198.357 256.902 1.00 42.71  ? 2237 LEU A O     1 
ATOM   5569  C  CB    . LEU A 1 2237 ? 222.805 199.951 255.378 1.00 34.03  ? 2237 LEU A CB    1 
ATOM   5570  C  CG    . LEU A 1 2237 ? 222.448 200.949 256.476 1.00 35.28  ? 2237 LEU A CG    1 
ATOM   5571  C  CD1   . LEU A 1 2237 ? 223.311 200.702 257.697 1.00 31.27  ? 2237 LEU A CD1   1 
ATOM   5572  C  CD2   . LEU A 1 2237 ? 222.604 202.372 255.980 1.00 36.22  ? 2237 LEU A CD2   1 
ATOM   5573  N  N     . LEU A 1 2238 ? 220.215 198.264 254.661 1.00 28.38  ? 2238 LEU A N     1 
ATOM   5574  C  CA    . LEU A 1 2238 ? 218.765 198.112 254.695 1.00 29.49  ? 2238 LEU A CA    1 
ATOM   5575  C  C     . LEU A 1 2238 ? 218.362 196.822 255.399 1.00 37.20  ? 2238 LEU A C     1 
ATOM   5576  O  O     . LEU A 1 2238 ? 217.460 196.824 256.247 1.00 41.47  ? 2238 LEU A O     1 
ATOM   5577  C  CB    . LEU A 1 2238 ? 218.208 198.149 253.272 1.00 34.92  ? 2238 LEU A CB    1 
ATOM   5578  C  CG    . LEU A 1 2238 ? 216.715 198.419 253.089 1.00 34.28  ? 2238 LEU A CG    1 
ATOM   5579  C  CD1   . LEU A 1 2238 ? 216.296 199.671 253.829 1.00 33.57  ? 2238 LEU A CD1   1 
ATOM   5580  C  CD2   . LEU A 1 2238 ? 216.392 198.541 251.616 1.00 38.45  ? 2238 LEU A CD2   1 
ATOM   5581  N  N     . LYS A 1 2239 ? 219.032 195.713 255.078 1.00 39.19  ? 2239 LYS A N     1 
ATOM   5582  C  CA    . LYS A 1 2239 ? 218.692 194.448 255.728 1.00 31.63  ? 2239 LYS A CA    1 
ATOM   5583  C  C     . LYS A 1 2239 ? 219.021 194.472 257.218 1.00 35.27  ? 2239 LYS A C     1 
ATOM   5584  O  O     . LYS A 1 2239 ? 218.244 193.968 258.041 1.00 44.09  ? 2239 LYS A O     1 
ATOM   5585  C  CB    . LYS A 1 2239 ? 219.405 193.288 255.039 1.00 33.51  ? 2239 LYS A CB    1 
ATOM   5586  C  CG    . LYS A 1 2239 ? 218.940 193.054 253.621 1.00 41.07  ? 2239 LYS A CG    1 
ATOM   5587  C  CD    . LYS A 1 2239 ? 219.238 191.638 253.169 1.00 45.43  ? 2239 LYS A CD    1 
ATOM   5588  C  CE    . LYS A 1 2239 ? 218.810 191.431 251.729 1.00 45.90  ? 2239 LYS A CE    1 
ATOM   5589  N  NZ    . LYS A 1 2239 ? 218.763 189.990 251.363 1.00 45.51  ? 2239 LYS A NZ    1 
ATOM   5590  N  N     . ALA A 1 2240 ? 220.168 195.044 257.585 1.00 34.18  ? 2240 ALA A N     1 
ATOM   5591  C  CA    . ALA A 1 2240 ? 220.540 195.107 258.992 1.00 25.96  ? 2240 ALA A CA    1 
ATOM   5592  C  C     . ALA A 1 2240 ? 219.583 195.990 259.775 1.00 34.61  ? 2240 ALA A C     1 
ATOM   5593  O  O     . ALA A 1 2240 ? 219.231 195.671 260.912 1.00 45.89  ? 2240 ALA A O     1 
ATOM   5594  C  CB    . ALA A 1 2240 ? 221.971 195.611 259.138 1.00 35.35  ? 2240 ALA A CB    1 
ATOM   5595  N  N     . LEU A 1 2241 ? 219.155 197.109 259.190 1.00 44.16  ? 2241 LEU A N     1 
ATOM   5596  C  CA    . LEU A 1 2241 ? 218.172 197.953 259.854 1.00 33.89  ? 2241 LEU A CA    1 
ATOM   5597  C  C     . LEU A 1 2241 ? 216.834 197.243 259.991 1.00 35.59  ? 2241 LEU A C     1 
ATOM   5598  O  O     . LEU A 1 2241 ? 216.154 197.405 261.010 1.00 46.76  ? 2241 LEU A O     1 
ATOM   5599  C  CB    . LEU A 1 2241 ? 218.009 199.265 259.092 1.00 35.63  ? 2241 LEU A CB    1 
ATOM   5600  C  CG    . LEU A 1 2241 ? 219.169 200.245 259.242 1.00 32.87  ? 2241 LEU A CG    1 
ATOM   5601  C  CD1   . LEU A 1 2241 ? 218.824 201.573 258.600 1.00 39.12  ? 2241 LEU A CD1   1 
ATOM   5602  C  CD2   . LEU A 1 2241 ? 219.506 200.427 260.707 1.00 39.35  ? 2241 LEU A CD2   1 
ATOM   5603  N  N     . GLU A 1 2242 ? 216.442 196.455 258.987 1.00 45.70  ? 2242 GLU A N     1 
ATOM   5604  C  CA    . GLU A 1 2242 ? 215.210 195.682 259.105 1.00 44.71  ? 2242 GLU A CA    1 
ATOM   5605  C  C     . GLU A 1 2242 ? 215.286 194.681 260.250 1.00 45.59  ? 2242 GLU A C     1 
ATOM   5606  O  O     . GLU A 1 2242 ? 214.333 194.545 261.025 1.00 50.95  ? 2242 GLU A O     1 
ATOM   5607  C  CB    . GLU A 1 2242 ? 214.904 194.968 257.790 1.00 44.75  ? 2242 GLU A CB    1 
ATOM   5608  C  CG    . GLU A 1 2242 ? 213.599 194.189 257.815 1.00 45.85  ? 2242 GLU A CG    1 
ATOM   5609  C  CD    . GLU A 1 2242 ? 213.268 193.544 256.483 1.00 61.89  ? 2242 GLU A CD    1 
ATOM   5610  O  OE1   . GLU A 1 2242 ? 213.723 194.059 255.440 1.00 59.61  ? 2242 GLU A OE1   1 
ATOM   5611  O  OE2   . GLU A 1 2242 ? 212.557 192.518 256.480 1.00 60.54  ? 2242 GLU A OE2   1 
ATOM   5612  N  N     . ARG A 1 2243 ? 216.404 193.969 260.374 1.00 51.17  ? 2243 ARG A N     1 
ATOM   5613  C  CA    . ARG A 1 2243 ? 216.515 192.977 261.441 1.00 46.35  ? 2243 ARG A CA    1 
ATOM   5614  C  C     . ARG A 1 2243 ? 216.826 193.586 262.808 1.00 43.08  ? 2243 ARG A C     1 
ATOM   5615  O  O     . ARG A 1 2243 ? 216.559 192.941 263.827 1.00 53.81  ? 2243 ARG A O     1 
ATOM   5616  C  CB    . ARG A 1 2243 ? 217.548 191.910 261.059 1.00 36.04  ? 2243 ARG A CB    1 
ATOM   5617  C  CG    . ARG A 1 2243 ? 218.977 192.385 260.978 1.00 50.51  ? 2243 ARG A CG    1 
ATOM   5618  C  CD    . ARG A 1 2243 ? 219.925 191.255 260.586 1.00 54.73  ? 2243 ARG A CD    1 
ATOM   5619  N  NE    . ARG A 1 2243 ? 219.696 190.725 259.250 1.00 57.35  ? 2243 ARG A NE    1 
ATOM   5620  C  CZ    . ARG A 1 2243 ? 219.173 189.532 258.996 1.00 52.08  ? 2243 ARG A CZ    1 
ATOM   5621  N  NH1   . ARG A 1 2243 ? 218.817 188.711 259.969 1.00 47.15  ? 2243 ARG A NH1   1 
ATOM   5622  N  NH2   . ARG A 1 2243 ? 219.012 189.147 257.730 1.00 48.65  ? 2243 ARG A NH2   1 
ATOM   5623  N  N     . LEU A 1 2244 ? 217.360 194.806 262.862 1.00 41.08  ? 2244 LEU A N     1 
ATOM   5624  C  CA    . LEU A 1 2244 ? 217.702 195.454 264.125 1.00 41.49  ? 2244 LEU A CA    1 
ATOM   5625  C  C     . LEU A 1 2244 ? 216.551 196.264 264.708 1.00 49.82  ? 2244 LEU A C     1 
ATOM   5626  O  O     . LEU A 1 2244 ? 216.320 196.227 265.921 1.00 49.00  ? 2244 LEU A O     1 
ATOM   5627  C  CB    . LEU A 1 2244 ? 218.919 196.364 263.935 1.00 43.52  ? 2244 LEU A CB    1 
ATOM   5628  C  CG    . LEU A 1 2244 ? 219.287 197.276 265.108 1.00 45.97  ? 2244 LEU A CG    1 
ATOM   5629  C  CD1   . LEU A 1 2244 ? 220.150 196.530 266.106 1.00 45.63  ? 2244 LEU A CD1   1 
ATOM   5630  C  CD2   . LEU A 1 2244 ? 219.984 198.543 264.639 1.00 44.73  ? 2244 LEU A CD2   1 
ATOM   5631  N  N     . GLU A 1 2245 ? 215.827 197.010 263.872 1.00 58.25  ? 2245 GLU A N     1 
ATOM   5632  C  CA    . GLU A 1 2245 ? 214.740 197.854 264.344 1.00 54.05  ? 2245 GLU A CA    1 
ATOM   5633  C  C     . GLU A 1 2245 ? 213.366 197.232 264.153 1.00 56.06  ? 2245 GLU A C     1 
ATOM   5634  O  O     . GLU A 1 2245 ? 212.396 197.721 264.740 1.00 58.03  ? 2245 GLU A O     1 
ATOM   5635  C  CB    . GLU A 1 2245 ? 214.778 199.211 263.630 1.00 46.23  ? 2245 GLU A CB    1 
ATOM   5636  C  CG    . GLU A 1 2245 ? 216.112 199.928 263.725 1.00 50.46  ? 2245 GLU A CG    1 
ATOM   5637  C  CD    . GLU A 1 2245 ? 216.166 201.169 262.859 1.00 60.53  ? 2245 GLU A CD    1 
ATOM   5638  O  OE1   . GLU A 1 2245 ? 215.168 201.452 262.164 1.00 57.03  ? 2245 GLU A OE1   1 
ATOM   5639  O  OE2   . GLU A 1 2245 ? 217.204 201.862 262.874 1.00 60.20  ? 2245 GLU A OE2   1 
ATOM   5640  N  N     . GLY A 1 2246 ? 213.260 196.175 263.351 1.00 52.83  ? 2246 GLY A N     1 
ATOM   5641  C  CA    . GLY A 1 2246 ? 211.987 195.545 263.085 1.00 50.85  ? 2246 GLY A CA    1 
ATOM   5642  C  C     . GLY A 1 2246 ? 211.158 196.206 262.009 1.00 58.57  ? 2246 GLY A C     1 
ATOM   5643  O  O     . GLY A 1 2246 ? 210.055 195.726 261.719 1.00 62.04  ? 2246 GLY A O     1 
ATOM   5644  N  N     . VAL A 1 2247 ? 211.645 197.285 261.409 1.00 54.84  ? 2247 VAL A N     1 
ATOM   5645  C  CA    . VAL A 1 2247 ? 210.919 197.998 260.366 1.00 49.05  ? 2247 VAL A CA    1 
ATOM   5646  C  C     . VAL A 1 2247 ? 211.330 197.437 259.013 1.00 57.27  ? 2247 VAL A C     1 
ATOM   5647  O  O     . VAL A 1 2247 ? 212.517 197.437 258.666 1.00 61.45  ? 2247 VAL A O     1 
ATOM   5648  C  CB    . VAL A 1 2247 ? 211.193 199.508 260.443 1.00 46.30  ? 2247 VAL A CB    1 
ATOM   5649  C  CG1   . VAL A 1 2247 ? 210.618 200.212 259.232 1.00 54.58  ? 2247 VAL A CG1   1 
ATOM   5650  C  CG2   . VAL A 1 2247 ? 210.620 200.085 261.722 1.00 51.70  ? 2247 VAL A CG2   1 
ATOM   5651  N  N     . GLU A 1 2248 ? 210.352 196.960 258.247 1.00 52.21  ? 2248 GLU A N     1 
ATOM   5652  C  CA    . GLU A 1 2248 ? 210.635 196.397 256.935 1.00 51.02  ? 2248 GLU A CA    1 
ATOM   5653  C  C     . GLU A 1 2248 ? 211.219 197.457 256.012 1.00 51.54  ? 2248 GLU A C     1 
ATOM   5654  O  O     . GLU A 1 2248 ? 210.749 198.595 255.963 1.00 58.51  ? 2248 GLU A O     1 
ATOM   5655  C  CB    . GLU A 1 2248 ? 209.363 195.812 256.322 1.00 50.36  ? 2248 GLU A CB    1 
ATOM   5656  C  CG    . GLU A 1 2248 ? 209.577 195.154 254.970 1.00 57.13  ? 2248 GLU A CG    1 
ATOM   5657  C  CD    . GLU A 1 2248 ? 208.307 194.559 254.400 1.00 62.09  ? 2248 GLU A CD    1 
ATOM   5658  O  OE1   . GLU A 1 2248 ? 207.252 194.660 255.060 1.00 61.90  ? 2248 GLU A OE1   1 
ATOM   5659  O  OE2   . GLU A 1 2248 ? 208.363 193.995 253.287 1.00 59.71  ? 2248 GLU A OE2   1 
ATOM   5660  N  N     . GLY A 1 2249 ? 212.261 197.073 255.266 1.00 38.24  ? 2249 GLY A N     1 
ATOM   5661  C  CA    . GLY A 1 2249 ? 212.947 197.981 254.380 1.00 42.73  ? 2249 GLY A CA    1 
ATOM   5662  C  C     . GLY A 1 2249 ? 212.582 197.734 252.931 1.00 44.62  ? 2249 GLY A C     1 
ATOM   5663  O  O     . GLY A 1 2249 ? 212.748 196.626 252.419 1.00 53.32  ? 2249 GLY A O     1 
ATOM   5664  N  N     . VAL A 1 2250 ? 212.087 198.778 252.272 1.00 31.42  ? 2250 VAL A N     1 
ATOM   5665  C  CA    . VAL A 1 2250 ? 211.698 198.723 250.869 1.00 26.74  ? 2250 VAL A CA    1 
ATOM   5666  C  C     . VAL A 1 2250 ? 212.576 199.694 250.095 1.00 31.13  ? 2250 VAL A C     1 
ATOM   5667  O  O     . VAL A 1 2250 ? 212.726 200.853 250.494 1.00 46.52  ? 2250 VAL A O     1 
ATOM   5668  C  CB    . VAL A 1 2250 ? 210.210 199.061 250.676 1.00 35.28  ? 2250 VAL A CB    1 
ATOM   5669  C  CG1   . VAL A 1 2250 ? 209.811 198.869 249.226 1.00 35.74  ? 2250 VAL A CG1   1 
ATOM   5670  C  CG2   . VAL A 1 2250 ? 209.350 198.205 251.586 1.00 46.18  ? 2250 VAL A CG2   1 
ATOM   5671  N  N     . ALA A 1 2251 ? 213.157 199.219 248.998 1.00 34.88  ? 2251 ALA A N     1 
ATOM   5672  C  CA    . ALA A 1 2251 ? 214.023 200.025 248.151 1.00 27.50  ? 2251 ALA A CA    1 
ATOM   5673  C  C     . ALA A 1 2251 ? 213.428 200.113 246.755 1.00 37.13  ? 2251 ALA A C     1 
ATOM   5674  O  O     . ALA A 1 2251 ? 213.047 199.093 246.173 1.00 50.94  ? 2251 ALA A O     1 
ATOM   5675  C  CB    . ALA A 1 2251 ? 215.430 199.436 248.085 1.00 28.64  ? 2251 ALA A CB    1 
ATOM   5676  N  N     . HIS A 1 2252 ? 213.347 201.329 246.224 1.00 24.13  ? 2252 HIS A N     1 
ATOM   5677  C  CA    . HIS A 1 2252 ? 212.880 201.575 244.863 1.00 19.95  ? 2252 HIS A CA    1 
ATOM   5678  C  C     . HIS A 1 2252 ? 214.053 202.150 244.081 1.00 25.94  ? 2252 HIS A C     1 
ATOM   5679  O  O     . HIS A 1 2252 ? 214.364 203.338 244.200 1.00 37.38  ? 2252 HIS A O     1 
ATOM   5680  C  CB    . HIS A 1 2252 ? 211.684 202.521 244.850 1.00 29.38  ? 2252 HIS A CB    1 
ATOM   5681  C  CG    . HIS A 1 2252 ? 210.648 202.200 245.880 1.00 33.32  ? 2252 HIS A CG    1 
ATOM   5682  N  ND1   . HIS A 1 2252 ? 209.539 201.430 245.605 1.00 39.55  ? 2252 HIS A ND1   1 
ATOM   5683  C  CD2   . HIS A 1 2252 ? 210.552 202.547 247.185 1.00 33.68  ? 2252 HIS A CD2   1 
ATOM   5684  C  CE1   . HIS A 1 2252 ? 208.804 201.317 246.697 1.00 35.89  ? 2252 HIS A CE1   1 
ATOM   5685  N  NE2   . HIS A 1 2252 ? 209.397 201.985 247.669 1.00 40.13  ? 2252 HIS A NE2   1 
ATOM   5686  N  N     . ILE A 1 2253 ? 214.702 201.312 243.283 1.00 35.19  ? 2253 ILE A N     1 
ATOM   5687  C  CA    . ILE A 1 2253 ? 215.876 201.719 242.522 1.00 35.13  ? 2253 ILE A CA    1 
ATOM   5688  C  C     . ILE A 1 2253 ? 215.421 202.207 241.155 1.00 32.54  ? 2253 ILE A C     1 
ATOM   5689  O  O     . ILE A 1 2253 ? 214.742 201.482 240.420 1.00 40.89  ? 2253 ILE A O     1 
ATOM   5690  C  CB    . ILE A 1 2253 ? 216.884 200.569 242.395 1.00 24.24  ? 2253 ILE A CB    1 
ATOM   5691  C  CG1   . ILE A 1 2253 ? 217.094 199.908 243.755 1.00 31.26  ? 2253 ILE A CG1   1 
ATOM   5692  C  CG2   . ILE A 1 2253 ? 218.202 201.081 241.849 1.00 29.78  ? 2253 ILE A CG2   1 
ATOM   5693  C  CD1   . ILE A 1 2253 ? 217.557 198.484 243.669 1.00 38.55  ? 2253 ILE A CD1   1 
ATOM   5694  N  N     . ILE A 1 2254 ? 215.798 203.435 240.814 1.00 20.78  ? 2254 ILE A N     1 
ATOM   5695  C  CA    . ILE A 1 2254 ? 215.397 204.080 239.572 1.00 28.46  ? 2254 ILE A CA    1 
ATOM   5696  C  C     . ILE A 1 2254 ? 216.652 204.519 238.835 1.00 36.43  ? 2254 ILE A C     1 
ATOM   5697  O  O     . ILE A 1 2254 ? 217.556 205.103 239.440 1.00 42.93  ? 2254 ILE A O     1 
ATOM   5698  C  CB    . ILE A 1 2254 ? 214.476 205.288 239.834 1.00 29.69  ? 2254 ILE A CB    1 
ATOM   5699  C  CG1   . ILE A 1 2254 ? 213.201 204.848 240.554 1.00 34.52  ? 2254 ILE A CG1   1 
ATOM   5700  C  CG2   . ILE A 1 2254 ? 214.145 206.005 238.539 1.00 30.86  ? 2254 ILE A CG2   1 
ATOM   5701  C  CD1   . ILE A 1 2254 ? 212.406 205.990 241.140 1.00 32.60  ? 2254 ILE A CD1   1 
ATOM   5702  N  N     . ASP A 1 2255 ? 216.718 204.219 237.540 1.00 33.56  ? 2255 ASP A N     1 
ATOM   5703  C  CA    . ASP A 1 2255 ? 217.753 204.799 236.698 1.00 22.74  ? 2255 ASP A CA    1 
ATOM   5704  C  C     . ASP A 1 2255 ? 217.204 206.085 236.096 1.00 35.62  ? 2255 ASP A C     1 
ATOM   5705  O  O     . ASP A 1 2255 ? 216.421 206.044 235.139 1.00 35.93  ? 2255 ASP A O     1 
ATOM   5706  C  CB    . ASP A 1 2255 ? 218.199 203.829 235.604 1.00 34.47  ? 2255 ASP A CB    1 
ATOM   5707  C  CG    . ASP A 1 2255 ? 219.602 204.120 235.106 1.00 44.22  ? 2255 ASP A CG    1 
ATOM   5708  O  OD1   . ASP A 1 2255 ? 219.924 205.306 234.888 1.00 36.51  ? 2255 ASP A OD1   1 
ATOM   5709  O  OD2   . ASP A 1 2255 ? 220.388 203.165 234.939 1.00 45.79  ? 2255 ASP A OD2   1 
ATOM   5710  N  N     . PRO A 1 2256 ? 217.581 207.241 236.642 1.00 38.37  ? 2256 PRO A N     1 
ATOM   5711  C  CA    . PRO A 1 2256 ? 216.946 208.497 236.219 1.00 25.38  ? 2256 PRO A CA    1 
ATOM   5712  C  C     . PRO A 1 2256 ? 217.216 208.867 234.775 1.00 31.33  ? 2256 PRO A C     1 
ATOM   5713  O  O     . PRO A 1 2256 ? 216.400 209.567 234.163 1.00 35.63  ? 2256 PRO A O     1 
ATOM   5714  C  CB    . PRO A 1 2256 ? 217.552 209.519 237.185 1.00 22.56  ? 2256 PRO A CB    1 
ATOM   5715  C  CG    . PRO A 1 2256 ? 218.885 208.944 237.517 1.00 25.55  ? 2256 PRO A CG    1 
ATOM   5716  C  CD    . PRO A 1 2256 ? 218.689 207.469 237.583 1.00 30.71  ? 2256 PRO A CD    1 
ATOM   5717  N  N     . LYS A 1 2257 ? 218.338 208.431 234.212 1.00 36.98  ? 2257 LYS A N     1 
ATOM   5718  C  CA    . LYS A 1 2257 ? 218.728 208.810 232.864 1.00 33.15  ? 2257 LYS A CA    1 
ATOM   5719  C  C     . LYS A 1 2257 ? 218.481 207.714 231.839 1.00 34.98  ? 2257 LYS A C     1 
ATOM   5720  O  O     . LYS A 1 2257 ? 218.736 207.929 230.651 1.00 45.84  ? 2257 LYS A O     1 
ATOM   5721  C  CB    . LYS A 1 2257 ? 220.201 209.220 232.846 1.00 37.33  ? 2257 LYS A CB    1 
ATOM   5722  C  CG    . LYS A 1 2257 ? 220.511 210.374 233.778 1.00 29.94  ? 2257 LYS A CG    1 
ATOM   5723  C  CD    . LYS A 1 2257 ? 220.659 211.669 233.012 1.00 27.44  ? 2257 LYS A CD    1 
ATOM   5724  C  CE    . LYS A 1 2257 ? 222.096 211.883 232.596 1.00 32.43  ? 2257 LYS A CE    1 
ATOM   5725  N  NZ    . LYS A 1 2257 ? 222.221 212.994 231.620 1.00 34.89  ? 2257 LYS A NZ    1 
ATOM   5726  N  N     . ALA A 1 2258 ? 217.995 206.549 232.263 1.00 34.06  ? 2258 ALA A N     1 
ATOM   5727  C  CA    . ALA A 1 2258 ? 217.578 205.521 231.322 1.00 23.40  ? 2258 ALA A CA    1 
ATOM   5728  C  C     . ALA A 1 2258 ? 216.206 205.802 230.732 1.00 34.92  ? 2258 ALA A C     1 
ATOM   5729  O  O     . ALA A 1 2258 ? 215.801 205.116 229.789 1.00 44.83  ? 2258 ALA A O     1 
ATOM   5730  C  CB    . ALA A 1 2258 ? 217.578 204.151 231.999 1.00 18.71  ? 2258 ALA A CB    1 
ATOM   5731  N  N     . ILE A 1 2259 ? 215.489 206.788 231.267 1.00 37.88  ? 2259 ILE A N     1 
ATOM   5732  C  CA    . ILE A 1 2259 ? 214.180 207.188 230.777 1.00 35.08  ? 2259 ILE A CA    1 
ATOM   5733  C  C     . ILE A 1 2259 ? 214.167 208.703 230.640 1.00 39.07  ? 2259 ILE A C     1 
ATOM   5734  O  O     . ILE A 1 2259 ? 214.965 209.413 231.253 1.00 43.61  ? 2259 ILE A O     1 
ATOM   5735  C  CB    . ILE A 1 2259 ? 213.040 206.726 231.707 1.00 27.41  ? 2259 ILE A CB    1 
ATOM   5736  C  CG1   . ILE A 1 2259 ? 213.315 207.175 233.141 1.00 22.25  ? 2259 ILE A CG1   1 
ATOM   5737  C  CG2   . ILE A 1 2259 ? 212.880 205.221 231.645 1.00 34.16  ? 2259 ILE A CG2   1 
ATOM   5738  C  CD1   . ILE A 1 2259 ? 212.249 206.762 234.120 1.00 30.82  ? 2259 ILE A CD1   1 
ATOM   5739  N  N     . SER A 1 2260 ? 213.245 209.194 229.819 1.00 36.13  ? 2260 SER A N     1 
ATOM   5740  C  CA    . SER A 1 2260 ? 213.113 210.629 229.646 1.00 32.90  ? 2260 SER A CA    1 
ATOM   5741  C  C     . SER A 1 2260 ? 212.584 211.271 230.924 1.00 33.68  ? 2260 SER A C     1 
ATOM   5742  O  O     . SER A 1 2260 ? 211.900 210.639 231.733 1.00 43.76  ? 2260 SER A O     1 
ATOM   5743  C  CB    . SER A 1 2260 ? 212.188 210.947 228.472 1.00 40.79  ? 2260 SER A CB    1 
ATOM   5744  O  OG    . SER A 1 2260 ? 210.846 210.621 228.777 1.00 45.14  ? 2260 SER A OG    1 
ATOM   5745  N  N     . LYS A 1 2261 ? 212.923 212.549 231.106 1.00 40.10  ? 2261 LYS A N     1 
ATOM   5746  C  CA    . LYS A 1 2261 ? 212.438 213.289 232.266 1.00 36.33  ? 2261 LYS A CA    1 
ATOM   5747  C  C     . LYS A 1 2261 ? 210.917 213.320 232.307 1.00 39.28  ? 2261 LYS A C     1 
ATOM   5748  O  O     . LYS A 1 2261 ? 210.322 213.371 233.391 1.00 50.13  ? 2261 LYS A O     1 
ATOM   5749  C  CB    . LYS A 1 2261 ? 213.008 214.706 232.242 1.00 35.56  ? 2261 LYS A CB    1 
ATOM   5750  C  CG    . LYS A 1 2261 ? 212.814 215.493 233.518 1.00 40.79  ? 2261 LYS A CG    1 
ATOM   5751  C  CD    . LYS A 1 2261 ? 213.552 216.814 233.440 1.00 37.02  ? 2261 LYS A CD    1 
ATOM   5752  C  CE    . LYS A 1 2261 ? 212.853 217.884 234.251 1.00 43.03  ? 2261 LYS A CE    1 
ATOM   5753  N  NZ    . LYS A 1 2261 ? 213.625 219.154 234.255 1.00 52.29  ? 2261 LYS A NZ    1 
ATOM   5754  N  N     . ASP A 1 2262 ? 210.275 213.272 231.138 1.00 40.17  ? 2262 ASP A N     1 
ATOM   5755  C  CA    . ASP A 1 2262 ? 208.822 213.170 231.078 1.00 38.00  ? 2262 ASP A CA    1 
ATOM   5756  C  C     . ASP A 1 2262 ? 208.334 211.878 231.718 1.00 39.80  ? 2262 ASP A C     1 
ATOM   5757  O  O     . ASP A 1 2262 ? 207.322 211.872 232.427 1.00 44.49  ? 2262 ASP A O     1 
ATOM   5758  C  CB    . ASP A 1 2262 ? 208.360 213.252 229.625 1.00 39.13  ? 2262 ASP A CB    1 
ATOM   5759  C  CG    . ASP A 1 2262 ? 208.377 214.667 229.088 1.00 52.27  ? 2262 ASP A CG    1 
ATOM   5760  O  OD1   . ASP A 1 2262 ? 208.374 214.833 227.850 1.00 54.52  ? 2262 ASP A OD1   1 
ATOM   5761  O  OD2   . ASP A 1 2262 ? 208.395 215.613 229.902 1.00 52.05  ? 2262 ASP A OD2   1 
ATOM   5762  N  N     . HIS A 1 2263 ? 209.036 210.773 231.475 1.00 35.20  ? 2263 HIS A N     1 
ATOM   5763  C  CA    . HIS A 1 2263 ? 208.688 209.501 232.088 1.00 27.76  ? 2263 HIS A CA    1 
ATOM   5764  C  C     . HIS A 1 2263 ? 209.198 209.374 233.514 1.00 33.47  ? 2263 HIS A C     1 
ATOM   5765  O  O     . HIS A 1 2263 ? 208.747 208.480 234.237 1.00 46.13  ? 2263 HIS A O     1 
ATOM   5766  C  CB    . HIS A 1 2263 ? 209.231 208.349 231.242 1.00 35.41  ? 2263 HIS A CB    1 
ATOM   5767  C  CG    . HIS A 1 2263 ? 208.551 208.205 229.918 1.00 41.86  ? 2263 HIS A CG    1 
ATOM   5768  N  ND1   . HIS A 1 2263 ? 207.187 208.320 229.766 1.00 42.15  ? 2263 HIS A ND1   1 
ATOM   5769  C  CD2   . HIS A 1 2263 ? 209.047 207.959 228.683 1.00 44.69  ? 2263 HIS A CD2   1 
ATOM   5770  C  CE1   . HIS A 1 2263 ? 206.871 208.150 228.495 1.00 41.18  ? 2263 HIS A CE1   1 
ATOM   5771  N  NE2   . HIS A 1 2263 ? 207.982 207.929 227.817 1.00 48.84  ? 2263 HIS A NE2   1 
ATOM   5772  N  N     . LEU A 1 2264 ? 210.117 210.240 233.936 1.00 29.57  ? 2264 LEU A N     1 
ATOM   5773  C  CA    . LEU A 1 2264 ? 210.641 210.200 235.293 1.00 35.31  ? 2264 LEU A CA    1 
ATOM   5774  C  C     . LEU A 1 2264 ? 209.782 210.993 236.268 1.00 36.16  ? 2264 LEU A C     1 
ATOM   5775  O  O     . LEU A 1 2264 ? 209.560 210.547 237.398 1.00 38.01  ? 2264 LEU A O     1 
ATOM   5776  C  CB    . LEU A 1 2264 ? 212.078 210.726 235.317 1.00 34.23  ? 2264 LEU A CB    1 
ATOM   5777  C  CG    . LEU A 1 2264 ? 212.766 210.796 236.681 1.00 27.31  ? 2264 LEU A CG    1 
ATOM   5778  C  CD1   . LEU A 1 2264 ? 212.949 209.408 237.265 1.00 32.82  ? 2264 LEU A CD1   1 
ATOM   5779  C  CD2   . LEU A 1 2264 ? 214.099 211.511 236.564 1.00 32.88  ? 2264 LEU A CD2   1 
ATOM   5780  N  N     . TYR A 1 2265 ? 209.288 212.160 235.859 1.00 39.06  ? 2265 TYR A N     1 
ATOM   5781  C  CA    . TYR A 1 2265 ? 208.488 212.994 236.746 1.00 34.87  ? 2265 TYR A CA    1 
ATOM   5782  C  C     . TYR A 1 2265 ? 207.024 213.088 236.354 1.00 36.09  ? 2265 TYR A C     1 
ATOM   5783  O  O     . TYR A 1 2265 ? 206.178 213.268 237.230 1.00 38.06  ? 2265 TYR A O     1 
ATOM   5784  C  CB    . TYR A 1 2265 ? 209.076 214.407 236.821 1.00 29.55  ? 2265 TYR A CB    1 
ATOM   5785  C  CG    . TYR A 1 2265 ? 210.396 214.469 237.549 1.00 30.86  ? 2265 TYR A CG    1 
ATOM   5786  C  CD1   . TYR A 1 2265 ? 210.490 214.106 238.884 1.00 29.03  ? 2265 TYR A CD1   1 
ATOM   5787  C  CD2   . TYR A 1 2265 ? 211.548 214.883 236.901 1.00 33.17  ? 2265 TYR A CD2   1 
ATOM   5788  C  CE1   . TYR A 1 2265 ? 211.691 214.157 239.552 1.00 30.10  ? 2265 TYR A CE1   1 
ATOM   5789  C  CE2   . TYR A 1 2265 ? 212.754 214.937 237.562 1.00 28.81  ? 2265 TYR A CE2   1 
ATOM   5790  C  CZ    . TYR A 1 2265 ? 212.820 214.574 238.887 1.00 31.57  ? 2265 TYR A CZ    1 
ATOM   5791  O  OH    . TYR A 1 2265 ? 214.023 214.627 239.550 1.00 42.12  ? 2265 TYR A OH    1 
ATOM   5792  N  N     . GLY A 1 2266 ? 206.702 212.970 235.071 1.00 38.62  ? 2266 GLY A N     1 
ATOM   5793  C  CA    . GLY A 1 2266 ? 205.324 213.062 234.636 1.00 36.23  ? 2266 GLY A CA    1 
ATOM   5794  C  C     . GLY A 1 2266 ? 205.098 214.140 233.599 1.00 40.19  ? 2266 GLY A C     1 
ATOM   5795  O  O     . GLY A 1 2266 ? 205.953 215.009 233.404 1.00 49.04  ? 2266 GLY A O     1 
ATOM   5796  N  N     . THR A 1 2267 ? 203.951 214.098 232.927 1.00 42.53  ? 2267 THR A N     1 
ATOM   5797  C  CA    . THR A 1 2267 ? 203.625 215.056 231.883 1.00 49.86  ? 2267 THR A CA    1 
ATOM   5798  C  C     . THR A 1 2267 ? 202.259 215.668 232.144 1.00 46.37  ? 2267 THR A C     1 
ATOM   5799  O  O     . THR A 1 2267 ? 201.365 215.025 232.698 1.00 48.23  ? 2267 THR A O     1 
ATOM   5800  C  CB    . THR A 1 2267 ? 203.618 214.412 230.490 1.00 56.92  ? 2267 THR A CB    1 
ATOM   5801  O  OG1   . THR A 1 2267 ? 202.855 213.200 230.521 1.00 55.52  ? 2267 THR A OG1   1 
ATOM   5802  C  CG2   . THR A 1 2267 ? 205.023 214.107 230.039 1.00 49.25  ? 2267 THR A CG2   1 
ATOM   5803  N  N     . LEU A 1 2268 ? 202.111 216.920 231.730 1.00 53.10  ? 2268 LEU A N     1 
ATOM   5804  C  CA    . LEU A 1 2268 ? 200.835 217.621 231.752 1.00 54.45  ? 2268 LEU A CA    1 
ATOM   5805  C  C     . LEU A 1 2268 ? 200.398 217.829 230.310 1.00 60.28  ? 2268 LEU A C     1 
ATOM   5806  O  O     . LEU A 1 2268 ? 201.129 218.436 229.521 1.00 59.85  ? 2268 LEU A O     1 
ATOM   5807  C  CB    . LEU A 1 2268 ? 200.958 218.954 232.489 1.00 58.58  ? 2268 LEU A CB    1 
ATOM   5808  C  CG    . LEU A 1 2268 ? 199.693 219.784 232.703 1.00 54.64  ? 2268 LEU A CG    1 
ATOM   5809  C  CD1   . LEU A 1 2268 ? 198.628 218.967 233.403 1.00 56.43  ? 2268 LEU A CD1   1 
ATOM   5810  C  CD2   . LEU A 1 2268 ? 200.024 221.022 233.509 1.00 57.12  ? 2268 LEU A CD2   1 
ATOM   5811  N  N     . ASP A 1 2269 ? 199.222 217.324 229.970 1.00 73.89  ? 2269 ASP A N     1 
ATOM   5812  C  CA    . ASP A 1 2269 ? 198.748 217.398 228.593 1.00 71.66  ? 2269 ASP A CA    1 
ATOM   5813  C  C     . ASP A 1 2269 ? 198.466 218.848 228.222 1.00 74.81  ? 2269 ASP A C     1 
ATOM   5814  O  O     . ASP A 1 2269 ? 197.661 219.503 228.895 1.00 74.64  ? 2269 ASP A O     1 
ATOM   5815  C  CB    . ASP A 1 2269 ? 197.494 216.548 228.420 1.00 71.83  ? 2269 ASP A CB    1 
ATOM   5816  C  CG    . ASP A 1 2269 ? 197.416 215.898 227.054 1.00 76.24  ? 2269 ASP A CG    1 
ATOM   5817  O  OD1   . ASP A 1 2269 ? 198.324 216.129 226.230 1.00 79.87  ? 2269 ASP A OD1   1 
ATOM   5818  O  OD2   . ASP A 1 2269 ? 196.447 215.152 226.804 1.00 77.82  ? 2269 ASP A OD2   1 
ATOM   5819  N  N     . PRO A 1 2270 ? 199.098 219.389 227.179 1.00 77.34  ? 2270 PRO A N     1 
ATOM   5820  C  CA    . PRO A 1 2270 ? 198.848 220.795 226.822 1.00 78.73  ? 2270 PRO A CA    1 
ATOM   5821  C  C     . PRO A 1 2270 ? 197.420 221.075 226.392 1.00 78.79  ? 2270 PRO A C     1 
ATOM   5822  O  O     . PRO A 1 2270 ? 196.990 222.233 226.453 1.00 80.99  ? 2270 PRO A O     1 
ATOM   5823  C  CB    . PRO A 1 2270 ? 199.838 221.049 225.677 1.00 77.29  ? 2270 PRO A CB    1 
ATOM   5824  C  CG    . PRO A 1 2270 ? 200.178 219.695 225.149 1.00 75.41  ? 2270 PRO A CG    1 
ATOM   5825  C  CD    . PRO A 1 2270 ? 200.119 218.770 226.321 1.00 73.82  ? 2270 PRO A CD    1 
ATOM   5826  N  N     . ASN A 1 2271 ? 196.668 220.061 225.965 1.00 81.99  ? 2271 ASN A N     1 
ATOM   5827  C  CA    . ASN A 1 2271 ? 195.315 220.274 225.462 1.00 82.78  ? 2271 ASN A CA    1 
ATOM   5828  C  C     . ASN A 1 2271 ? 194.269 220.162 226.570 1.00 83.02  ? 2271 ASN A C     1 
ATOM   5829  O  O     . ASN A 1 2271 ? 193.534 221.117 226.837 1.00 80.14  ? 2271 ASN A O     1 
ATOM   5830  C  CB    . ASN A 1 2271 ? 195.015 219.277 224.338 1.00 83.10  ? 2271 ASN A CB    1 
ATOM   5831  C  CG    . ASN A 1 2271 ? 196.152 219.161 223.346 1.00 84.10  ? 2271 ASN A CG    1 
ATOM   5832  O  OD1   . ASN A 1 2271 ? 196.627 218.065 223.052 1.00 82.72  ? 2271 ASN A OD1   1 
ATOM   5833  N  ND2   . ASN A 1 2271 ? 196.595 220.297 222.821 1.00 81.75  ? 2271 ASN A ND2   1 
ATOM   5834  N  N     . THR A 1 2272 ? 194.193 219.003 227.221 1.00 76.80  ? 2272 THR A N     1 
ATOM   5835  C  CA    . THR A 1 2272 ? 193.180 218.747 228.235 1.00 75.66  ? 2272 THR A CA    1 
ATOM   5836  C  C     . THR A 1 2272 ? 193.670 218.998 229.654 1.00 76.17  ? 2272 THR A C     1 
ATOM   5837  O  O     . THR A 1 2272 ? 192.897 218.812 230.599 1.00 74.60  ? 2272 THR A O     1 
ATOM   5838  C  CB    . THR A 1 2272 ? 192.664 217.309 228.116 1.00 76.26  ? 2272 THR A CB    1 
ATOM   5839  O  OG1   . THR A 1 2272 ? 191.695 217.060 229.141 1.00 78.53  ? 2272 THR A OG1   1 
ATOM   5840  C  CG2   . THR A 1 2272 ? 193.806 216.320 228.250 1.00 72.36  ? 2272 THR A CG2   1 
ATOM   5841  N  N     . ARG A 1 2273 ? 194.925 219.423 229.824 1.00 70.19  ? 2273 ARG A N     1 
ATOM   5842  C  CA    . ARG A 1 2273 ? 195.497 219.713 231.142 1.00 70.36  ? 2273 ARG A CA    1 
ATOM   5843  C  C     . ARG A 1 2273 ? 195.378 218.514 232.080 1.00 68.31  ? 2273 ARG A C     1 
ATOM   5844  O  O     . ARG A 1 2273 ? 195.070 218.657 233.264 1.00 70.09  ? 2273 ARG A O     1 
ATOM   5845  C  CB    . ARG A 1 2273 ? 194.857 220.957 231.764 1.00 68.62  ? 2273 ARG A CB    1 
ATOM   5846  C  CG    . ARG A 1 2273 ? 194.782 222.155 230.830 1.00 70.41  ? 2273 ARG A CG    1 
ATOM   5847  C  CD    . ARG A 1 2273 ? 196.144 222.501 230.253 1.00 70.00  ? 2273 ARG A CD    1 
ATOM   5848  N  NE    . ARG A 1 2273 ? 197.046 223.041 231.263 1.00 71.50  ? 2273 ARG A NE    1 
ATOM   5849  C  CZ    . ARG A 1 2273 ? 198.310 223.370 231.039 1.00 69.33  ? 2273 ARG A CZ    1 
ATOM   5850  N  NH1   . ARG A 1 2273 ? 198.859 223.233 229.844 1.00 64.85  ? 2273 ARG A NH1   1 
ATOM   5851  N  NH2   . ARG A 1 2273 ? 199.042 223.849 232.040 1.00 68.47  ? 2273 ARG A NH2   1 
ATOM   5852  N  N     . GLU A 1 2274 ? 195.628 217.322 231.548 1.00 61.37  ? 2274 GLU A N     1 
ATOM   5853  C  CA    . GLU A 1 2274 ? 195.549 216.089 232.317 1.00 63.38  ? 2274 GLU A CA    1 
ATOM   5854  C  C     . GLU A 1 2274 ? 196.951 215.647 232.714 1.00 65.60  ? 2274 GLU A C     1 
ATOM   5855  O  O     . GLU A 1 2274 ? 197.821 215.478 231.853 1.00 64.74  ? 2274 GLU A O     1 
ATOM   5856  C  CB    . GLU A 1 2274 ? 194.853 214.989 231.514 1.00 62.04  ? 2274 GLU A CB    1 
ATOM   5857  C  CG    . GLU A 1 2274 ? 194.350 213.828 232.356 1.00 67.10  ? 2274 GLU A CG    1 
ATOM   5858  C  CD    . GLU A 1 2274 ? 193.762 214.277 233.679 1.00 70.24  ? 2274 GLU A CD    1 
ATOM   5859  O  OE1   . GLU A 1 2274 ? 192.808 215.084 233.664 1.00 68.45  ? 2274 GLU A OE1   1 
ATOM   5860  O  OE2   . GLU A 1 2274 ? 194.253 213.825 234.734 1.00 67.50  ? 2274 GLU A OE2   1 
ATOM   5861  N  N     . TRP A 1 2275 ? 197.162 215.457 234.012 1.00 50.75  ? 2275 TRP A N     1 
ATOM   5862  C  CA    . TRP A 1 2275 ? 198.470 215.096 234.540 1.00 46.20  ? 2275 TRP A CA    1 
ATOM   5863  C  C     . TRP A 1 2275 ? 198.627 213.583 234.564 1.00 49.19  ? 2275 TRP A C     1 
ATOM   5864  O  O     . TRP A 1 2275 ? 197.764 212.869 235.083 1.00 50.61  ? 2275 TRP A O     1 
ATOM   5865  C  CB    . TRP A 1 2275 ? 198.661 215.665 235.945 1.00 48.70  ? 2275 TRP A CB    1 
ATOM   5866  C  CG    . TRP A 1 2275 ? 199.925 215.211 236.603 1.00 50.10  ? 2275 TRP A CG    1 
ATOM   5867  C  CD1   . TRP A 1 2275 ? 200.057 214.212 237.521 1.00 48.57  ? 2275 TRP A CD1   1 
ATOM   5868  C  CD2   . TRP A 1 2275 ? 201.239 215.736 236.389 1.00 49.04  ? 2275 TRP A CD2   1 
ATOM   5869  N  NE1   . TRP A 1 2275 ? 201.371 214.085 237.894 1.00 47.26  ? 2275 TRP A NE1   1 
ATOM   5870  C  CE2   . TRP A 1 2275 ? 202.117 215.009 237.214 1.00 45.24  ? 2275 TRP A CE2   1 
ATOM   5871  C  CE3   . TRP A 1 2275 ? 201.756 216.752 235.584 1.00 46.04  ? 2275 TRP A CE3   1 
ATOM   5872  C  CZ2   . TRP A 1 2275 ? 203.482 215.264 237.253 1.00 43.26  ? 2275 TRP A CZ2   1 
ATOM   5873  C  CZ3   . TRP A 1 2275 ? 203.111 217.003 235.625 1.00 47.76  ? 2275 TRP A CZ3   1 
ATOM   5874  C  CH2   . TRP A 1 2275 ? 203.959 216.263 236.453 1.00 48.61  ? 2275 TRP A CH2   1 
ATOM   5875  N  N     . THR A 1 2276 ? 199.731 213.101 234.001 1.00 51.18  ? 2276 THR A N     1 
ATOM   5876  C  CA    . THR A 1 2276 ? 200.088 211.689 234.025 1.00 42.09  ? 2276 THR A CA    1 
ATOM   5877  C  C     . THR A 1 2276 ? 201.339 211.529 234.876 1.00 44.01  ? 2276 THR A C     1 
ATOM   5878  O  O     . THR A 1 2276 ? 202.358 212.171 234.608 1.00 50.01  ? 2276 THR A O     1 
ATOM   5879  C  CB    . THR A 1 2276 ? 200.326 211.156 232.613 1.00 41.55  ? 2276 THR A CB    1 
ATOM   5880  O  OG1   . THR A 1 2276 ? 199.160 211.384 231.813 1.00 52.72  ? 2276 THR A OG1   1 
ATOM   5881  C  CG2   . THR A 1 2276 ? 200.622 209.668 232.649 1.00 40.56  ? 2276 THR A CG2   1 
ATOM   5882  N  N     . ASP A 1 2277 ? 201.260 210.680 235.896 1.00 38.21  ? 2277 ASP A N     1 
ATOM   5883  C  CA    . ASP A 1 2277 ? 202.370 210.517 236.823 1.00 36.34  ? 2277 ASP A CA    1 
ATOM   5884  C  C     . ASP A 1 2277 ? 203.573 209.888 236.133 1.00 43.54  ? 2277 ASP A C     1 
ATOM   5885  O  O     . ASP A 1 2277 ? 203.434 209.013 235.274 1.00 46.03  ? 2277 ASP A O     1 
ATOM   5886  C  CB    . ASP A 1 2277 ? 201.952 209.653 238.011 1.00 35.64  ? 2277 ASP A CB    1 
ATOM   5887  C  CG    . ASP A 1 2277 ? 201.376 210.466 239.147 1.00 46.02  ? 2277 ASP A CG    1 
ATOM   5888  O  OD1   . ASP A 1 2277 ? 201.567 211.698 239.154 1.00 51.16  ? 2277 ASP A OD1   1 
ATOM   5889  O  OD2   . ASP A 1 2277 ? 200.738 209.872 240.040 1.00 48.64  ? 2277 ASP A OD2   1 
ATOM   5890  N  N     . GLY A 1 2278 ? 204.759 210.340 236.517 1.00 36.47  ? 2278 GLY A N     1 
ATOM   5891  C  CA    . GLY A 1 2278 ? 205.999 209.729 236.095 1.00 25.89  ? 2278 GLY A CA    1 
ATOM   5892  C  C     . GLY A 1 2278 ? 206.353 208.562 236.986 1.00 33.01  ? 2278 GLY A C     1 
ATOM   5893  O  O     . GLY A 1 2278 ? 205.518 208.031 237.720 1.00 43.87  ? 2278 GLY A O     1 
ATOM   5894  N  N     . LEU A 1 2279 ? 207.618 208.155 236.920 1.00 31.14  ? 2279 LEU A N     1 
ATOM   5895  C  CA    . LEU A 1 2279 ? 208.066 207.029 237.731 1.00 35.30  ? 2279 LEU A CA    1 
ATOM   5896  C  C     . LEU A 1 2279 ? 208.255 207.441 239.186 1.00 36.17  ? 2279 LEU A C     1 
ATOM   5897  O  O     . LEU A 1 2279 ? 207.621 206.881 240.090 1.00 42.58  ? 2279 LEU A O     1 
ATOM   5898  C  CB    . LEU A 1 2279 ? 209.359 206.458 237.152 1.00 30.58  ? 2279 LEU A CB    1 
ATOM   5899  C  CG    . LEU A 1 2279 ? 209.981 205.264 237.868 1.00 33.50  ? 2279 LEU A CG    1 
ATOM   5900  C  CD1   . LEU A 1 2279 ? 208.943 204.191 238.123 1.00 37.96  ? 2279 LEU A CD1   1 
ATOM   5901  C  CD2   . LEU A 1 2279 ? 211.115 204.720 237.033 1.00 39.33  ? 2279 LEU A CD2   1 
ATOM   5902  N  N     . PHE A 1 2280 ? 209.123 208.425 239.428 1.00 29.36  ? 2280 PHE A N     1 
ATOM   5903  C  CA    . PHE A 1 2280 ? 209.360 208.886 240.791 1.00 27.75  ? 2280 PHE A CA    1 
ATOM   5904  C  C     . PHE A 1 2280 ? 208.098 209.477 241.404 1.00 36.68  ? 2280 PHE A C     1 
ATOM   5905  O  O     . PHE A 1 2280 ? 207.825 209.271 242.592 1.00 46.15  ? 2280 PHE A O     1 
ATOM   5906  C  CB    . PHE A 1 2280 ? 210.494 209.911 240.810 1.00 32.52  ? 2280 PHE A CB    1 
ATOM   5907  C  CG    . PHE A 1 2280 ? 210.633 210.628 242.120 1.00 34.26  ? 2280 PHE A CG    1 
ATOM   5908  C  CD1   . PHE A 1 2280 ? 211.206 210.000 243.209 1.00 38.73  ? 2280 PHE A CD1   1 
ATOM   5909  C  CD2   . PHE A 1 2280 ? 210.180 211.925 242.265 1.00 33.54  ? 2280 PHE A CD2   1 
ATOM   5910  C  CE1   . PHE A 1 2280 ? 211.329 210.655 244.414 1.00 36.72  ? 2280 PHE A CE1   1 
ATOM   5911  C  CE2   . PHE A 1 2280 ? 210.299 212.582 243.469 1.00 31.42  ? 2280 PHE A CE2   1 
ATOM   5912  C  CZ    . PHE A 1 2280 ? 210.875 211.947 244.544 1.00 34.33  ? 2280 PHE A CZ    1 
ATOM   5913  N  N     . THR A 1 2281 ? 207.326 210.227 240.616 1.00 34.18  ? 2281 THR A N     1 
ATOM   5914  C  CA    . THR A 1 2281 ? 206.090 210.802 241.132 1.00 21.68  ? 2281 THR A CA    1 
ATOM   5915  C  C     . THR A 1 2281 ? 205.110 209.713 241.544 1.00 29.11  ? 2281 THR A C     1 
ATOM   5916  O  O     . THR A 1 2281 ? 204.485 209.801 242.606 1.00 41.82  ? 2281 THR A O     1 
ATOM   5917  C  CB    . THR A 1 2281 ? 205.459 211.722 240.089 1.00 33.73  ? 2281 THR A CB    1 
ATOM   5918  O  OG1   . THR A 1 2281 ? 206.443 212.642 239.604 1.00 37.43  ? 2281 THR A OG1   1 
ATOM   5919  C  CG2   . THR A 1 2281 ? 204.313 212.504 240.701 1.00 34.27  ? 2281 THR A CG2   1 
ATOM   5920  N  N     . HIS A 1 2282 ? 204.967 208.672 240.719 1.00 31.61  ? 2282 HIS A N     1 
ATOM   5921  C  CA    . HIS A 1 2282 ? 204.077 207.569 241.063 1.00 30.20  ? 2282 HIS A CA    1 
ATOM   5922  C  C     . HIS A 1 2282 ? 204.546 206.853 242.321 1.00 35.88  ? 2282 HIS A C     1 
ATOM   5923  O  O     . HIS A 1 2282 ? 203.735 206.525 243.193 1.00 39.14  ? 2282 HIS A O     1 
ATOM   5924  C  CB    . HIS A 1 2282 ? 203.977 206.591 239.892 1.00 32.61  ? 2282 HIS A CB    1 
ATOM   5925  C  CG    . HIS A 1 2282 ? 203.438 205.245 240.263 1.00 41.65  ? 2282 HIS A CG    1 
ATOM   5926  N  ND1   . HIS A 1 2282 ? 202.089 204.986 240.366 1.00 41.83  ? 2282 HIS A ND1   1 
ATOM   5927  C  CD2   . HIS A 1 2282 ? 204.067 204.079 240.540 1.00 45.22  ? 2282 HIS A CD2   1 
ATOM   5928  C  CE1   . HIS A 1 2282 ? 201.910 203.720 240.698 1.00 37.07  ? 2282 HIS A CE1   1 
ATOM   5929  N  NE2   . HIS A 1 2282 ? 203.094 203.148 240.810 1.00 42.94  ? 2282 HIS A NE2   1 
ATOM   5930  N  N     . VAL A 1 2283 ? 205.853 206.612 242.440 1.00 40.24  ? 2283 VAL A N     1 
ATOM   5931  C  CA    . VAL A 1 2283 ? 206.376 205.923 243.617 1.00 31.00  ? 2283 VAL A CA    1 
ATOM   5932  C  C     . VAL A 1 2283 ? 206.124 206.745 244.877 1.00 36.37  ? 2283 VAL A C     1 
ATOM   5933  O  O     . VAL A 1 2283 ? 205.658 206.223 245.899 1.00 46.88  ? 2283 VAL A O     1 
ATOM   5934  C  CB    . VAL A 1 2283 ? 207.872 205.615 243.433 1.00 31.27  ? 2283 VAL A CB    1 
ATOM   5935  C  CG1   . VAL A 1 2283 ? 208.488 205.170 244.743 1.00 36.94  ? 2283 VAL A CG1   1 
ATOM   5936  C  CG2   . VAL A 1 2283 ? 208.066 204.556 242.364 1.00 31.18  ? 2283 VAL A CG2   1 
ATOM   5937  N  N     . LEU A 1 2284 ? 206.425 208.044 244.823 1.00 35.98  ? 2284 LEU A N     1 
ATOM   5938  C  CA    . LEU A 1 2284 ? 206.240 208.897 245.992 1.00 26.63  ? 2284 LEU A CA    1 
ATOM   5939  C  C     . LEU A 1 2284 ? 204.768 209.024 246.361 1.00 28.61  ? 2284 LEU A C     1 
ATOM   5940  O  O     . LEU A 1 2284 ? 204.417 208.993 247.545 1.00 40.47  ? 2284 LEU A O     1 
ATOM   5941  C  CB    . LEU A 1 2284 ? 206.853 210.273 245.739 1.00 32.77  ? 2284 LEU A CB    1 
ATOM   5942  C  CG    . LEU A 1 2284 ? 206.783 211.251 246.911 1.00 39.39  ? 2284 LEU A CG    1 
ATOM   5943  C  CD1   . LEU A 1 2284 ? 207.588 210.728 248.085 1.00 36.36  ? 2284 LEU A CD1   1 
ATOM   5944  C  CD2   . LEU A 1 2284 ? 207.265 212.629 246.496 1.00 31.05  ? 2284 LEU A CD2   1 
ATOM   5945  N  N     . ARG A 1 2285 ? 203.892 209.170 245.364 1.00 30.13  ? 2285 ARG A N     1 
ATOM   5946  C  CA    . ARG A 1 2285 ? 202.465 209.261 245.643 1.00 28.78  ? 2285 ARG A CA    1 
ATOM   5947  C  C     . ARG A 1 2285 ? 201.939 207.962 246.237 1.00 38.29  ? 2285 ARG A C     1 
ATOM   5948  O  O     . ARG A 1 2285 ? 201.077 207.980 247.122 1.00 43.76  ? 2285 ARG A O     1 
ATOM   5949  C  CB    . ARG A 1 2285 ? 201.709 209.618 244.365 1.00 30.11  ? 2285 ARG A CB    1 
ATOM   5950  C  CG    . ARG A 1 2285 ? 200.229 209.863 244.561 1.00 36.31  ? 2285 ARG A CG    1 
ATOM   5951  C  CD    . ARG A 1 2285 ? 199.528 210.043 243.229 1.00 42.89  ? 2285 ARG A CD    1 
ATOM   5952  N  NE    . ARG A 1 2285 ? 200.121 211.115 242.440 1.00 38.01  ? 2285 ARG A NE    1 
ATOM   5953  C  CZ    . ARG A 1 2285 ? 199.823 212.399 242.578 1.00 37.96  ? 2285 ARG A CZ    1 
ATOM   5954  N  NH1   . ARG A 1 2285 ? 198.948 212.812 243.479 1.00 37.03  ? 2285 ARG A NH1   1 
ATOM   5955  N  NH2   . ARG A 1 2285 ? 200.418 213.291 241.793 1.00 29.98  ? 2285 ARG A NH2   1 
ATOM   5956  N  N     . LYS A 1 2286 ? 202.445 206.823 245.761 1.00 42.20  ? 2286 LYS A N     1 
ATOM   5957  C  CA    . LYS A 1 2286 ? 202.051 205.537 246.322 1.00 35.95  ? 2286 LYS A CA    1 
ATOM   5958  C  C     . LYS A 1 2286 ? 202.497 205.405 247.771 1.00 42.15  ? 2286 LYS A C     1 
ATOM   5959  O  O     . LYS A 1 2286 ? 201.761 204.866 248.605 1.00 49.04  ? 2286 LYS A O     1 
ATOM   5960  C  CB    . LYS A 1 2286 ? 202.629 204.407 245.474 1.00 40.05  ? 2286 LYS A CB    1 
ATOM   5961  C  CG    . LYS A 1 2286 ? 202.250 203.018 245.934 1.00 49.74  ? 2286 LYS A CG    1 
ATOM   5962  C  CD    . LYS A 1 2286 ? 202.847 201.972 245.014 1.00 49.97  ? 2286 LYS A CD    1 
ATOM   5963  C  CE    . LYS A 1 2286 ? 204.360 201.932 245.151 1.00 50.82  ? 2286 LYS A CE    1 
ATOM   5964  N  NZ    . LYS A 1 2286 ? 204.791 201.457 246.495 1.00 51.97  ? 2286 LYS A NZ    1 
ATOM   5965  N  N     . ILE A 1 2287 ? 203.705 205.875 248.088 1.00 44.44  ? 2287 ILE A N     1 
ATOM   5966  C  CA    . ILE A 1 2287 ? 204.163 205.839 249.476 1.00 37.65  ? 2287 ILE A CA    1 
ATOM   5967  C  C     . ILE A 1 2287 ? 203.308 206.751 250.348 1.00 36.37  ? 2287 ILE A C     1 
ATOM   5968  O  O     . ILE A 1 2287 ? 202.934 206.388 251.469 1.00 41.31  ? 2287 ILE A O     1 
ATOM   5969  C  CB    . ILE A 1 2287 ? 205.654 206.206 249.567 1.00 34.32  ? 2287 ILE A CB    1 
ATOM   5970  C  CG1   . ILE A 1 2287 ? 206.504 205.192 248.805 1.00 30.72  ? 2287 ILE A CG1   1 
ATOM   5971  C  CG2   . ILE A 1 2287 ? 206.096 206.267 251.013 1.00 38.31  ? 2287 ILE A CG2   1 
ATOM   5972  C  CD1   . ILE A 1 2287 ? 207.956 205.583 248.703 1.00 35.91  ? 2287 ILE A CD1   1 
ATOM   5973  N  N     . ILE A 1 2288 ? 202.987 207.949 249.852 1.00 40.06  ? 2288 ILE A N     1 
ATOM   5974  C  CA    . ILE A 1 2288 ? 202.196 208.898 250.633 1.00 42.50  ? 2288 ILE A CA    1 
ATOM   5975  C  C     . ILE A 1 2288 ? 200.793 208.356 250.881 1.00 42.27  ? 2288 ILE A C     1 
ATOM   5976  O  O     . ILE A 1 2288 ? 200.243 208.499 251.980 1.00 46.42  ? 2288 ILE A O     1 
ATOM   5977  C  CB    . ILE A 1 2288 ? 202.156 210.267 249.929 1.00 38.76  ? 2288 ILE A CB    1 
ATOM   5978  C  CG1   . ILE A 1 2288 ? 203.536 210.919 249.945 1.00 33.05  ? 2288 ILE A CG1   1 
ATOM   5979  C  CG2   . ILE A 1 2288 ? 201.137 211.180 250.585 1.00 41.41  ? 2288 ILE A CG2   1 
ATOM   5980  C  CD1   . ILE A 1 2288 ? 203.715 211.959 248.873 1.00 30.27  ? 2288 ILE A CD1   1 
ATOM   5981  N  N     . ASP A 1 2289 ? 200.191 207.731 249.867 1.00 42.54  ? 2289 ASP A N     1 
ATOM   5982  C  CA    . ASP A 1 2289 ? 198.830 207.222 250.011 1.00 46.13  ? 2289 ASP A CA    1 
ATOM   5983  C  C     . ASP A 1 2289 ? 198.747 206.154 251.094 1.00 50.44  ? 2289 ASP A C     1 
ATOM   5984  O  O     . ASP A 1 2289 ? 197.768 206.101 251.847 1.00 49.46  ? 2289 ASP A O     1 
ATOM   5985  C  CB    . ASP A 1 2289 ? 198.329 206.675 248.675 1.00 49.39  ? 2289 ASP A CB    1 
ATOM   5986  C  CG    . ASP A 1 2289 ? 198.047 207.771 247.666 1.00 58.92  ? 2289 ASP A CG    1 
ATOM   5987  O  OD1   . ASP A 1 2289 ? 198.179 208.960 248.024 1.00 51.43  ? 2289 ASP A OD1   1 
ATOM   5988  O  OD2   . ASP A 1 2289 ? 197.693 207.444 246.515 1.00 56.94  ? 2289 ASP A OD2   1 
ATOM   5989  N  N     . SER A 1 2290 ? 199.764 205.295 251.182 1.00 52.92  ? 2290 SER A N     1 
ATOM   5990  C  CA    . SER A 1 2290 ? 199.870 204.287 252.238 1.00 54.16  ? 2290 SER A CA    1 
ATOM   5991  C  C     . SER A 1 2290 ? 198.653 203.363 252.259 1.00 64.48  ? 2290 SER A C     1 
ATOM   5992  O  O     . SER A 1 2290 ? 198.106 203.040 253.316 1.00 68.68  ? 2290 SER A O     1 
ATOM   5993  C  CB    . SER A 1 2290 ? 200.080 204.941 253.603 1.00 56.63  ? 2290 SER A CB    1 
ATOM   5994  O  OG    . SER A 1 2290 ? 199.907 204.005 254.651 1.00 62.68  ? 2290 SER A OG    1 
ATOM   5995  N  N     . VAL A 1 2291 ? 198.224 202.940 251.070 1.00 68.73  ? 2291 VAL A N     1 
ATOM   5996  C  CA    . VAL A 1 2291 ? 197.115 201.998 250.982 1.00 68.85  ? 2291 VAL A CA    1 
ATOM   5997  C  C     . VAL A 1 2291 ? 197.521 200.643 251.549 1.00 70.71  ? 2291 VAL A C     1 
ATOM   5998  O  O     . VAL A 1 2291 ? 196.722 199.963 252.204 1.00 70.34  ? 2291 VAL A O     1 
ATOM   5999  C  CB    . VAL A 1 2291 ? 196.624 201.883 249.528 1.00 67.21  ? 2291 VAL A CB    1 
ATOM   6000  C  CG1   . VAL A 1 2291 ? 195.416 200.968 249.447 1.00 66.32  ? 2291 VAL A CG1   1 
ATOM   6001  C  CG2   . VAL A 1 2291 ? 196.288 203.256 248.975 1.00 68.86  ? 2291 VAL A CG2   1 
ATOM   6002  N  N     . ARG A 1 2292 ? 198.764 200.233 251.315 1.00 76.02  ? 2292 ARG A N     1 
ATOM   6003  C  CA    . ARG A 1 2292 ? 199.277 198.944 251.768 1.00 73.65  ? 2292 ARG A CA    1 
ATOM   6004  C  C     . ARG A 1 2292 ? 200.311 199.119 252.876 1.00 72.17  ? 2292 ARG A C     1 
ATOM   6005  O  O     . ARG A 1 2292 ? 201.280 198.365 252.969 1.00 71.88  ? 2292 ARG A O     1 
ATOM   6006  C  CB    . ARG A 1 2292 ? 199.876 198.157 250.604 1.00 72.08  ? 2292 ARG A CB    1 
ATOM   6007  C  CG    . ARG A 1 2292 ? 198.860 197.461 249.704 1.00 74.15  ? 2292 ARG A CG    1 
ATOM   6008  C  CD    . ARG A 1 2292 ? 198.143 198.448 248.794 1.00 75.07  ? 2292 ARG A CD    1 
ATOM   6009  N  NE    . ARG A 1 2292 ? 197.208 197.788 247.891 1.00 75.06  ? 2292 ARG A NE    1 
ATOM   6010  C  CZ    . ARG A 1 2292 ? 197.532 197.304 246.700 1.00 79.62  ? 2292 ARG A CZ    1 
ATOM   6011  N  NH1   . ARG A 1 2292 ? 198.767 197.389 246.233 1.00 79.95  ? 2292 ARG A NH1   1 
ATOM   6012  N  NH2   . ARG A 1 2292 ? 196.594 196.722 245.959 1.00 77.50  ? 2292 ARG A NH2   1 
ATOM   6013  N  N     . GLY A 1 2293 ? 200.111 200.119 253.728 1.00 64.93  ? 2293 GLY A N     1 
ATOM   6014  C  CA    . GLY A 1 2293 ? 201.017 200.364 254.837 1.00 64.91  ? 2293 GLY A CA    1 
ATOM   6015  C  C     . GLY A 1 2293 ? 202.429 200.743 254.440 1.00 65.65  ? 2293 GLY A C     1 
ATOM   6016  O  O     . GLY A 1 2293 ? 203.388 200.261 255.054 1.00 64.58  ? 2293 GLY A O     1 
ATOM   6017  N  N     . GLU A 1 2294 ? 202.583 201.596 253.425 1.00 59.18  ? 2294 GLU A N     1 
ATOM   6018  C  CA    . GLU A 1 2294 ? 203.921 202.013 253.017 1.00 54.72  ? 2294 GLU A CA    1 
ATOM   6019  C  C     . GLU A 1 2294 ? 204.512 203.061 253.952 1.00 55.02  ? 2294 GLU A C     1 
ATOM   6020  O  O     . GLU A 1 2294 ? 205.720 203.312 253.901 1.00 58.58  ? 2294 GLU A O     1 
ATOM   6021  C  CB    . GLU A 1 2294 ? 203.914 202.540 251.581 1.00 57.14  ? 2294 GLU A CB    1 
ATOM   6022  C  CG    . GLU A 1 2294 ? 203.626 201.506 250.498 1.00 57.87  ? 2294 GLU A CG    1 
ATOM   6023  C  CD    . GLU A 1 2294 ? 202.155 201.236 250.297 1.00 66.06  ? 2294 GLU A CD    1 
ATOM   6024  O  OE1   . GLU A 1 2294 ? 201.332 201.894 250.956 1.00 67.91  ? 2294 GLU A OE1   1 
ATOM   6025  O  OE2   . GLU A 1 2294 ? 201.819 200.373 249.460 1.00 67.18  ? 2294 GLU A OE2   1 
ATOM   6026  N  N     . LEU A 1 2295 ? 203.696 203.692 254.798 1.00 52.43  ? 2295 LEU A N     1 
ATOM   6027  C  CA    . LEU A 1 2295 ? 204.237 204.680 255.725 1.00 54.24  ? 2295 LEU A CA    1 
ATOM   6028  C  C     . LEU A 1 2295 ? 204.830 204.056 256.979 1.00 48.69  ? 2295 LEU A C     1 
ATOM   6029  O  O     . LEU A 1 2295 ? 205.552 204.741 257.711 1.00 52.44  ? 2295 LEU A O     1 
ATOM   6030  C  CB    . LEU A 1 2295 ? 203.168 205.697 256.126 1.00 53.23  ? 2295 LEU A CB    1 
ATOM   6031  C  CG    . LEU A 1 2295 ? 202.745 206.712 255.065 1.00 53.30  ? 2295 LEU A CG    1 
ATOM   6032  C  CD1   . LEU A 1 2295 ? 201.567 207.537 255.559 1.00 53.20  ? 2295 LEU A CD1   1 
ATOM   6033  C  CD2   . LEU A 1 2295 ? 203.906 207.603 254.677 1.00 50.11  ? 2295 LEU A CD2   1 
ATOM   6034  N  N     . GLN A 1 2296 ? 204.543 202.788 257.249 1.00 48.02  ? 2296 GLN A N     1 
ATOM   6035  C  CA    . GLN A 1 2296 ? 205.107 202.098 258.400 1.00 53.48  ? 2296 GLN A CA    1 
ATOM   6036  C  C     . GLN A 1 2296 ? 206.385 201.345 258.063 1.00 53.36  ? 2296 GLN A C     1 
ATOM   6037  O  O     . GLN A 1 2296 ? 206.983 200.735 258.956 1.00 49.77  ? 2296 GLN A O     1 
ATOM   6038  C  CB    . GLN A 1 2296 ? 204.076 201.134 258.993 1.00 57.76  ? 2296 GLN A CB    1 
ATOM   6039  C  CG    . GLN A 1 2296 ? 203.082 201.798 259.930 1.00 54.27  ? 2296 GLN A CG    1 
ATOM   6040  C  CD    . GLN A 1 2296 ? 202.072 202.657 259.197 1.00 58.41  ? 2296 GLN A CD    1 
ATOM   6041  O  OE1   . GLN A 1 2296 ? 201.978 203.861 259.433 1.00 54.82  ? 2296 GLN A OE1   1 
ATOM   6042  N  NE2   . GLN A 1 2296 ? 201.309 202.042 258.302 1.00 57.99  ? 2296 GLN A NE2   1 
ATOM   6043  N  N     . LYS A 1 2297 ? 206.815 201.376 256.808 1.00 51.09  ? 2297 LYS A N     1 
ATOM   6044  C  CA    . LYS A 1 2297 ? 208.037 200.730 256.363 1.00 47.55  ? 2297 LYS A CA    1 
ATOM   6045  C  C     . LYS A 1 2297 ? 209.087 201.781 256.034 1.00 46.56  ? 2297 LYS A C     1 
ATOM   6046  O  O     . LYS A 1 2297 ? 208.772 202.932 255.723 1.00 59.18  ? 2297 LYS A O     1 
ATOM   6047  C  CB    . LYS A 1 2297 ? 207.777 199.848 255.138 1.00 45.84  ? 2297 LYS A CB    1 
ATOM   6048  C  CG    . LYS A 1 2297 ? 206.862 198.670 255.410 1.00 51.88  ? 2297 LYS A CG    1 
ATOM   6049  C  CD    . LYS A 1 2297 ? 206.582 197.877 254.146 1.00 52.11  ? 2297 LYS A CD    1 
ATOM   6050  C  CE    . LYS A 1 2297 ? 205.722 198.670 253.180 1.00 58.08  ? 2297 LYS A CE    1 
ATOM   6051  N  NZ    . LYS A 1 2297 ? 205.300 197.852 252.010 1.00 57.01  ? 2297 LYS A NZ    1 
ATOM   6052  N  N     . ARG A 1 2298 ? 210.349 201.372 256.116 1.00 33.97  ? 2298 ARG A N     1 
ATOM   6053  C  CA    . ARG A 1 2298 ? 211.463 202.245 255.768 1.00 28.89  ? 2298 ARG A CA    1 
ATOM   6054  C  C     . ARG A 1 2298 ? 211.616 202.239 254.253 1.00 38.75  ? 2298 ARG A C     1 
ATOM   6055  O  O     . ARG A 1 2298 ? 212.062 201.246 253.671 1.00 51.94  ? 2298 ARG A O     1 
ATOM   6056  C  CB    . ARG A 1 2298 ? 212.738 201.779 256.462 1.00 36.92  ? 2298 ARG A CB    1 
ATOM   6057  C  CG    . ARG A 1 2298 ? 214.017 202.350 255.885 1.00 43.25  ? 2298 ARG A CG    1 
ATOM   6058  C  CD    . ARG A 1 2298 ? 215.228 201.834 256.642 1.00 41.71  ? 2298 ARG A CD    1 
ATOM   6059  N  NE    . ARG A 1 2298 ? 215.420 202.533 257.906 1.00 44.27  ? 2298 ARG A NE    1 
ATOM   6060  C  CZ    . ARG A 1 2298 ? 215.026 202.073 259.085 1.00 43.95  ? 2298 ARG A CZ    1 
ATOM   6061  N  NH1   . ARG A 1 2298 ? 214.403 200.913 259.201 1.00 44.19  ? 2298 ARG A NH1   1 
ATOM   6062  N  NH2   . ARG A 1 2298 ? 215.264 202.795 260.175 1.00 43.44  ? 2298 ARG A NH2   1 
ATOM   6063  N  N     . GLN A 1 2299 ? 211.234 203.337 253.612 1.00 40.46  ? 2299 GLN A N     1 
ATOM   6064  C  CA    . GLN A 1 2299 ? 211.232 203.435 252.160 1.00 32.88  ? 2299 GLN A CA    1 
ATOM   6065  C  C     . GLN A 1 2299 ? 212.432 204.242 251.695 1.00 39.38  ? 2299 GLN A C     1 
ATOM   6066  O  O     . GLN A 1 2299 ? 212.634 205.376 252.137 1.00 50.83  ? 2299 GLN A O     1 
ATOM   6067  C  CB    . GLN A 1 2299 ? 209.939 204.076 251.663 1.00 36.68  ? 2299 GLN A CB    1 
ATOM   6068  C  CG    . GLN A 1 2299 ? 208.689 203.398 252.177 1.00 40.49  ? 2299 GLN A CG    1 
ATOM   6069  C  CD    . GLN A 1 2299 ? 208.156 202.370 251.207 1.00 44.95  ? 2299 GLN A CD    1 
ATOM   6070  O  OE1   . GLN A 1 2299 ? 208.705 202.180 250.125 1.00 46.04  ? 2299 GLN A OE1   1 
ATOM   6071  N  NE2   . GLN A 1 2299 ? 207.084 201.694 251.592 1.00 50.70  ? 2299 GLN A NE2   1 
ATOM   6072  N  N     . TRP A 1 2300 ? 213.227 203.654 250.807 1.00 30.78  ? 2300 TRP A N     1 
ATOM   6073  C  CA    . TRP A 1 2300 ? 214.400 204.305 250.243 1.00 26.96  ? 2300 TRP A CA    1 
ATOM   6074  C  C     . TRP A 1 2300 ? 214.240 204.357 248.733 1.00 30.05  ? 2300 TRP A C     1 
ATOM   6075  O  O     . TRP A 1 2300 ? 214.103 203.315 248.086 1.00 45.89  ? 2300 TRP A O     1 
ATOM   6076  C  CB    . TRP A 1 2300 ? 215.680 203.559 250.624 1.00 25.05  ? 2300 TRP A CB    1 
ATOM   6077  C  CG    . TRP A 1 2300 ? 216.099 203.772 252.041 1.00 27.08  ? 2300 TRP A CG    1 
ATOM   6078  C  CD1   . TRP A 1 2300 ? 215.456 204.520 252.982 1.00 25.53  ? 2300 TRP A CD1   1 
ATOM   6079  C  CD2   . TRP A 1 2300 ? 217.256 203.229 252.684 1.00 32.28  ? 2300 TRP A CD2   1 
ATOM   6080  N  NE1   . TRP A 1 2300 ? 216.141 204.478 254.169 1.00 26.20  ? 2300 TRP A NE1   1 
ATOM   6081  C  CE2   . TRP A 1 2300 ? 217.251 203.690 254.012 1.00 32.27  ? 2300 TRP A CE2   1 
ATOM   6082  C  CE3   . TRP A 1 2300 ? 218.296 202.396 252.264 1.00 30.30  ? 2300 TRP A CE3   1 
ATOM   6083  C  CZ2   . TRP A 1 2300 ? 218.243 203.348 254.923 1.00 27.16  ? 2300 TRP A CZ2   1 
ATOM   6084  C  CZ3   . TRP A 1 2300 ? 219.280 202.059 253.170 1.00 29.78  ? 2300 TRP A CZ3   1 
ATOM   6085  C  CH2   . TRP A 1 2300 ? 219.247 202.533 254.484 1.00 24.77  ? 2300 TRP A CH2   1 
ATOM   6086  N  N     . ILE A 1 2301 ? 214.254 205.561 248.177 1.00 23.08  ? 2301 ILE A N     1 
ATOM   6087  C  CA    . ILE A 1 2301 ? 214.190 205.762 246.736 1.00 31.29  ? 2301 ILE A CA    1 
ATOM   6088  C  C     . ILE A 1 2301 ? 215.613 206.005 246.254 1.00 36.64  ? 2301 ILE A C     1 
ATOM   6089  O  O     . ILE A 1 2301 ? 216.188 207.070 246.496 1.00 45.04  ? 2301 ILE A O     1 
ATOM   6090  C  CB    . ILE A 1 2301 ? 213.258 206.921 246.365 1.00 35.28  ? 2301 ILE A CB    1 
ATOM   6091  C  CG1   . ILE A 1 2301 ? 211.838 206.626 246.848 1.00 29.16  ? 2301 ILE A CG1   1 
ATOM   6092  C  CG2   . ILE A 1 2301 ? 213.272 207.156 244.867 1.00 37.89  ? 2301 ILE A CG2   1 
ATOM   6093  C  CD1   . ILE A 1 2301 ? 210.844 207.713 246.531 1.00 36.75  ? 2301 ILE A CD1   1 
ATOM   6094  N  N     . VAL A 1 2302 ? 216.185 205.017 245.574 1.00 40.72  ? 2302 VAL A N     1 
ATOM   6095  C  CA    . VAL A 1 2302 ? 217.581 205.047 245.159 1.00 36.44  ? 2302 VAL A CA    1 
ATOM   6096  C  C     . VAL A 1 2302 ? 217.650 205.432 243.690 1.00 44.57  ? 2302 VAL A C     1 
ATOM   6097  O  O     . VAL A 1 2302 ? 216.964 204.837 242.851 1.00 52.81  ? 2302 VAL A O     1 
ATOM   6098  C  CB    . VAL A 1 2302 ? 218.265 203.693 245.407 1.00 33.62  ? 2302 VAL A CB    1 
ATOM   6099  C  CG1   . VAL A 1 2302 ? 219.768 203.827 245.276 1.00 36.45  ? 2302 VAL A CG1   1 
ATOM   6100  C  CG2   . VAL A 1 2302 ? 217.898 203.165 246.779 1.00 36.78  ? 2302 VAL A CG2   1 
ATOM   6101  N  N     . PHE A 1 2303 ? 218.470 206.433 243.380 1.00 36.45  ? 2303 PHE A N     1 
ATOM   6102  C  CA    . PHE A 1 2303 ? 218.710 206.866 242.005 1.00 20.46  ? 2303 PHE A CA    1 
ATOM   6103  C  C     . PHE A 1 2303 ? 220.085 206.345 241.606 1.00 29.42  ? 2303 PHE A C     1 
ATOM   6104  O  O     . PHE A 1 2303 ? 221.110 206.966 241.882 1.00 44.09  ? 2303 PHE A O     1 
ATOM   6105  C  CB    . PHE A 1 2303 ? 218.627 208.382 241.883 1.00 25.02  ? 2303 PHE A CB    1 
ATOM   6106  C  CG    . PHE A 1 2303 ? 217.228 208.920 241.917 1.00 28.15  ? 2303 PHE A CG    1 
ATOM   6107  C  CD1   . PHE A 1 2303 ? 216.428 208.876 240.791 1.00 37.70  ? 2303 PHE A CD1   1 
ATOM   6108  C  CD2   . PHE A 1 2303 ? 216.716 209.477 243.072 1.00 24.45  ? 2303 PHE A CD2   1 
ATOM   6109  C  CE1   . PHE A 1 2303 ? 215.144 209.374 240.820 1.00 37.77  ? 2303 PHE A CE1   1 
ATOM   6110  C  CE2   . PHE A 1 2303 ? 215.432 209.975 243.106 1.00 30.90  ? 2303 PHE A CE2   1 
ATOM   6111  C  CZ    . PHE A 1 2303 ? 214.646 209.923 241.979 1.00 32.94  ? 2303 PHE A CZ    1 
ATOM   6112  N  N     . ASP A 1 2304 ? 220.102 205.188 240.953 1.00 37.16  ? 2304 ASP A N     1 
ATOM   6113  C  CA    . ASP A 1 2304 ? 221.342 204.540 240.531 1.00 34.48  ? 2304 ASP A CA    1 
ATOM   6114  C  C     . ASP A 1 2304 ? 221.604 204.932 239.081 1.00 35.44  ? 2304 ASP A C     1 
ATOM   6115  O  O     . ASP A 1 2304 ? 221.245 204.214 238.148 1.00 45.56  ? 2304 ASP A O     1 
ATOM   6116  C  CB    . ASP A 1 2304 ? 221.247 203.029 240.705 1.00 36.57  ? 2304 ASP A CB    1 
ATOM   6117  C  CG    . ASP A 1 2304 ? 222.592 202.344 240.595 1.00 40.39  ? 2304 ASP A CG    1 
ATOM   6118  O  OD1   . ASP A 1 2304 ? 223.602 203.042 240.379 1.00 45.32  ? 2304 ASP A OD1   1 
ATOM   6119  O  OD2   . ASP A 1 2304 ? 222.641 201.103 240.725 1.00 46.91  ? 2304 ASP A OD2   1 
ATOM   6120  N  N     . GLY A 1 2305 ? 222.239 206.082 238.895 1.00 26.11  ? 2305 GLY A N     1 
ATOM   6121  C  CA    . GLY A 1 2305 ? 222.524 206.558 237.557 1.00 35.18  ? 2305 GLY A CA    1 
ATOM   6122  C  C     . GLY A 1 2305 ? 223.239 207.889 237.603 1.00 38.02  ? 2305 GLY A C     1 
ATOM   6123  O  O     . GLY A 1 2305 ? 223.624 208.372 238.669 1.00 42.76  ? 2305 GLY A O     1 
ATOM   6124  N  N     . ASP A 1 2306 ? 223.410 208.478 236.424 1.00 38.18  ? 2306 ASP A N     1 
ATOM   6125  C  CA    . ASP A 1 2306 ? 224.102 209.752 236.307 1.00 27.44  ? 2306 ASP A CA    1 
ATOM   6126  C  C     . ASP A 1 2306 ? 223.218 210.895 236.799 1.00 34.54  ? 2306 ASP A C     1 
ATOM   6127  O  O     . ASP A 1 2306 ? 221.987 210.825 236.769 1.00 45.80  ? 2306 ASP A O     1 
ATOM   6128  C  CB    . ASP A 1 2306 ? 224.523 210.001 234.859 1.00 38.33  ? 2306 ASP A CB    1 
ATOM   6129  C  CG    . ASP A 1 2306 ? 225.615 209.057 234.399 1.00 48.03  ? 2306 ASP A CG    1 
ATOM   6130  O  OD1   . ASP A 1 2306 ? 226.418 208.616 235.247 1.00 54.38  ? 2306 ASP A OD1   1 
ATOM   6131  O  OD2   . ASP A 1 2306 ? 225.673 208.756 233.189 1.00 38.68  ? 2306 ASP A OD2   1 
ATOM   6132  N  N     . VAL A 1 2307 ? 223.868 211.964 237.253 1.00 34.47  ? 2307 VAL A N     1 
ATOM   6133  C  CA    . VAL A 1 2307 ? 223.194 213.143 237.782 1.00 30.79  ? 2307 VAL A CA    1 
ATOM   6134  C  C     . VAL A 1 2307 ? 223.575 214.342 236.925 1.00 43.74  ? 2307 VAL A C     1 
ATOM   6135  O  O     . VAL A 1 2307 ? 224.764 214.608 236.717 1.00 50.97  ? 2307 VAL A O     1 
ATOM   6136  C  CB    . VAL A 1 2307 ? 223.560 213.392 239.257 1.00 26.95  ? 2307 VAL A CB    1 
ATOM   6137  C  CG1   . VAL A 1 2307 ? 223.266 214.826 239.644 1.00 26.16  ? 2307 VAL A CG1   1 
ATOM   6138  C  CG2   . VAL A 1 2307 ? 222.811 212.437 240.161 1.00 35.08  ? 2307 VAL A CG2   1 
ATOM   6139  N  N     . ASP A 1 2308 ? 222.573 215.055 236.428 1.00 36.11  ? 2308 ASP A N     1 
ATOM   6140  C  CA    . ASP A 1 2308 ? 222.776 216.303 235.711 1.00 30.77  ? 2308 ASP A CA    1 
ATOM   6141  C  C     . ASP A 1 2308 ? 221.739 217.308 236.185 1.00 40.28  ? 2308 ASP A C     1 
ATOM   6142  O  O     . ASP A 1 2308 ? 220.685 216.921 236.700 1.00 44.01  ? 2308 ASP A O     1 
ATOM   6143  C  CB    . ASP A 1 2308 ? 222.714 216.106 234.186 1.00 35.51  ? 2308 ASP A CB    1 
ATOM   6144  C  CG    . ASP A 1 2308 ? 221.359 215.612 233.679 1.00 43.72  ? 2308 ASP A CG    1 
ATOM   6145  O  OD1   . ASP A 1 2308 ? 220.310 215.883 234.290 1.00 47.87  ? 2308 ASP A OD1   1 
ATOM   6146  O  OD2   . ASP A 1 2308 ? 221.347 214.948 232.624 1.00 52.32  ? 2308 ASP A OD2   1 
ATOM   6147  N  N     . PRO A 1 2309 ? 222.012 218.609 236.037 1.00 34.43  ? 2309 PRO A N     1 
ATOM   6148  C  CA    . PRO A 1 2309 ? 221.072 219.622 236.538 1.00 33.36  ? 2309 PRO A CA    1 
ATOM   6149  C  C     . PRO A 1 2309 ? 219.735 219.664 235.813 1.00 35.00  ? 2309 PRO A C     1 
ATOM   6150  O  O     . PRO A 1 2309 ? 218.915 220.533 236.125 1.00 43.18  ? 2309 PRO A O     1 
ATOM   6151  C  CB    . PRO A 1 2309 ? 221.840 220.938 236.342 1.00 35.37  ? 2309 PRO A CB    1 
ATOM   6152  C  CG    . PRO A 1 2309 ? 222.855 220.641 235.309 1.00 34.15  ? 2309 PRO A CG    1 
ATOM   6153  C  CD    . PRO A 1 2309 ? 223.243 219.218 235.510 1.00 31.58  ? 2309 PRO A CD    1 
ATOM   6154  N  N     . GLU A 1 2310 ? 219.478 218.774 234.855 1.00 32.53  ? 2310 GLU A N     1 
ATOM   6155  C  CA    . GLU A 1 2310 ? 218.200 218.803 234.153 1.00 33.11  ? 2310 GLU A CA    1 
ATOM   6156  C  C     . GLU A 1 2310 ? 217.115 218.072 234.934 1.00 41.75  ? 2310 GLU A C     1 
ATOM   6157  O  O     . GLU A 1 2310 ? 215.991 218.568 235.059 1.00 46.06  ? 2310 GLU A O     1 
ATOM   6158  C  CB    . GLU A 1 2310 ? 218.350 218.200 232.757 1.00 40.55  ? 2310 GLU A CB    1 
ATOM   6159  C  CG    . GLU A 1 2310 ? 219.236 219.000 231.823 1.00 49.28  ? 2310 GLU A CG    1 
ATOM   6160  C  CD    . GLU A 1 2310 ? 218.647 220.348 231.468 1.00 57.03  ? 2310 GLU A CD    1 
ATOM   6161  O  OE1   . GLU A 1 2310 ? 217.404 220.458 231.406 1.00 57.93  ? 2310 GLU A OE1   1 
ATOM   6162  O  OE2   . GLU A 1 2310 ? 219.426 221.298 231.243 1.00 53.44  ? 2310 GLU A OE2   1 
ATOM   6163  N  N     . TRP A 1 2311 ? 217.430 216.892 235.463 1.00 36.79  ? 2311 TRP A N     1 
ATOM   6164  C  CA    . TRP A 1 2311 ? 216.448 216.090 236.181 1.00 26.91  ? 2311 TRP A CA    1 
ATOM   6165  C  C     . TRP A 1 2311 ? 216.578 216.186 237.693 1.00 33.32  ? 2311 TRP A C     1 
ATOM   6166  O  O     . TRP A 1 2311 ? 215.573 216.044 238.396 1.00 38.51  ? 2311 TRP A O     1 
ATOM   6167  C  CB    . TRP A 1 2311 ? 216.550 214.617 235.758 1.00 24.13  ? 2311 TRP A CB    1 
ATOM   6168  C  CG    . TRP A 1 2311 ? 217.740 213.891 236.320 1.00 26.40  ? 2311 TRP A CG    1 
ATOM   6169  C  CD1   . TRP A 1 2311 ? 218.952 213.731 235.725 1.00 29.20  ? 2311 TRP A CD1   1 
ATOM   6170  C  CD2   . TRP A 1 2311 ? 217.822 213.218 237.582 1.00 31.08  ? 2311 TRP A CD2   1 
ATOM   6171  N  NE1   . TRP A 1 2311 ? 219.790 213.012 236.538 1.00 17.83  ? 2311 TRP A NE1   1 
ATOM   6172  C  CE2   . TRP A 1 2311 ? 219.119 212.686 237.686 1.00 23.06  ? 2311 TRP A CE2   1 
ATOM   6173  C  CE3   . TRP A 1 2311 ? 216.927 213.020 238.637 1.00 27.15  ? 2311 TRP A CE3   1 
ATOM   6174  C  CZ2   . TRP A 1 2311 ? 219.544 211.972 238.799 1.00 25.77  ? 2311 TRP A CZ2   1 
ATOM   6175  C  CZ3   . TRP A 1 2311 ? 217.351 212.311 239.739 1.00 25.22  ? 2311 TRP A CZ3   1 
ATOM   6176  C  CH2   . TRP A 1 2311 ? 218.646 211.792 239.811 1.00 26.09  ? 2311 TRP A CH2   1 
ATOM   6177  N  N     . VAL A 1 2312 ? 217.782 216.422 238.216 1.00 35.67  ? 2312 VAL A N     1 
ATOM   6178  C  CA    . VAL A 1 2312 ? 217.968 216.373 239.661 1.00 35.59  ? 2312 VAL A CA    1 
ATOM   6179  C  C     . VAL A 1 2312 ? 217.513 217.658 240.337 1.00 37.48  ? 2312 VAL A C     1 
ATOM   6180  O  O     . VAL A 1 2312 ? 217.209 217.644 241.536 1.00 53.77  ? 2312 VAL A O     1 
ATOM   6181  C  CB    . VAL A 1 2312 ? 219.436 216.073 240.016 1.00 26.36  ? 2312 VAL A CB    1 
ATOM   6182  C  CG1   . VAL A 1 2312 ? 220.320 217.265 239.719 1.00 31.99  ? 2312 VAL A CG1   1 
ATOM   6183  C  CG2   . VAL A 1 2312 ? 219.568 215.625 241.461 1.00 31.09  ? 2312 VAL A CG2   1 
ATOM   6184  N  N     . GLU A 1 2313 ? 217.433 218.766 239.603 1.00 34.33  ? 2313 GLU A N     1 
ATOM   6185  C  CA    . GLU A 1 2313 ? 217.021 220.025 240.204 1.00 28.73  ? 2313 GLU A CA    1 
ATOM   6186  C  C     . GLU A 1 2313 ? 215.514 220.132 240.380 1.00 36.27  ? 2313 GLU A C     1 
ATOM   6187  O  O     . GLU A 1 2313 ? 215.051 221.069 241.036 1.00 50.21  ? 2313 GLU A O     1 
ATOM   6188  C  CB    . GLU A 1 2313 ? 217.531 221.197 239.369 1.00 32.11  ? 2313 GLU A CB    1 
ATOM   6189  C  CG    . GLU A 1 2313 ? 219.038 221.211 239.207 1.00 41.39  ? 2313 GLU A CG    1 
ATOM   6190  C  CD    . GLU A 1 2313 ? 219.727 222.073 240.239 1.00 50.31  ? 2313 GLU A CD    1 
ATOM   6191  O  OE1   . GLU A 1 2313 ? 219.039 222.574 241.151 1.00 53.35  ? 2313 GLU A OE1   1 
ATOM   6192  O  OE2   . GLU A 1 2313 ? 220.959 222.247 240.139 1.00 53.21  ? 2313 GLU A OE2   1 
ATOM   6193  N  N     . ASN A 1 2314 ? 214.740 219.209 239.809 1.00 34.44  ? 2314 ASN A N     1 
ATOM   6194  C  CA    . ASN A 1 2314 ? 213.330 219.111 240.154 1.00 25.31  ? 2314 ASN A CA    1 
ATOM   6195  C  C     . ASN A 1 2314 ? 213.128 218.609 241.573 1.00 37.10  ? 2314 ASN A C     1 
ATOM   6196  O  O     . ASN A 1 2314 ? 212.024 218.737 242.112 1.00 43.57  ? 2314 ASN A O     1 
ATOM   6197  C  CB    . ASN A 1 2314 ? 212.608 218.188 239.175 1.00 26.25  ? 2314 ASN A CB    1 
ATOM   6198  C  CG    . ASN A 1 2314 ? 212.586 218.736 237.770 1.00 37.68  ? 2314 ASN A CG    1 
ATOM   6199  O  OD1   . ASN A 1 2314 ? 213.614 219.144 237.235 1.00 44.75  ? 2314 ASN A OD1   1 
ATOM   6200  N  ND2   . ASN A 1 2314 ? 211.412 218.741 237.156 1.00 44.58  ? 2314 ASN A ND2   1 
ATOM   6201  N  N     . LEU A 1 2315 ? 214.194 218.123 242.178 1.00 38.26  ? 2315 LEU A N     1 
ATOM   6202  C  CA    . LEU A 1 2315 ? 214.114 217.498 243.505 1.00 28.65  ? 2315 LEU A CA    1 
ATOM   6203  C  C     . LEU A 1 2315 ? 214.782 218.451 244.469 1.00 29.30  ? 2315 LEU A C     1 
ATOM   6204  O  O     . LEU A 1 2315 ? 215.286 217.992 245.469 1.00 43.70  ? 2315 LEU A O     1 
ATOM   6205  C  CB    . LEU A 1 2315 ? 214.891 216.193 243.371 1.00 33.21  ? 2315 LEU A CB    1 
ATOM   6206  C  CG    . LEU A 1 2315 ? 214.170 215.009 242.733 1.00 30.06  ? 2315 LEU A CG    1 
ATOM   6207  C  CD1   . LEU A 1 2315 ? 215.035 213.808 242.996 1.00 31.35  ? 2315 LEU A CD1   1 
ATOM   6208  C  CD2   . LEU A 1 2315 ? 212.803 214.829 243.335 1.00 36.81  ? 2315 LEU A CD2   1 
ATOM   6209  N  N     . ASN A 1 2316 ? 214.792 219.733 244.170 1.00 25.11  ? 2316 ASN A N     1 
ATOM   6210  C  CA    . ASN A 1 2316 ? 215.474 220.741 245.007 1.00 23.00  ? 2316 ASN A CA    1 
ATOM   6211  C  C     . ASN A 1 2316 ? 214.574 221.060 246.182 1.00 33.28  ? 2316 ASN A C     1 
ATOM   6212  O  O     . ASN A 1 2316 ? 215.108 221.224 247.247 1.00 37.43  ? 2316 ASN A O     1 
ATOM   6213  C  CB    . ASN A 1 2316 ? 215.856 221.969 244.197 1.00 26.94  ? 2316 ASN A CB    1 
ATOM   6214  C  CG    . ASN A 1 2316 ? 217.258 221.933 243.656 1.00 39.47  ? 2316 ASN A CG    1 
ATOM   6215  O  OD1   . ASN A 1 2316 ? 217.924 220.895 243.707 1.00 42.93  ? 2316 ASN A OD1   1 
ATOM   6216  N  ND2   . ASN A 1 2316 ? 217.716 223.057 243.134 1.00 31.68  ? 2316 ASN A ND2   1 
ATOM   6217  N  N     . SER A 1 2317 ? 213.276 221.116 245.990 1.00 38.40  ? 2317 SER A N     1 
ATOM   6218  C  CA    . SER A 1 2317 ? 212.292 221.422 247.050 1.00 27.65  ? 2317 SER A CA    1 
ATOM   6219  C  C     . SER A 1 2317 ? 212.057 220.161 247.850 1.00 29.44  ? 2317 SER A C     1 
ATOM   6220  O  O     . SER A 1 2317 ? 211.639 220.266 248.988 1.00 36.77  ? 2317 SER A O     1 
ATOM   6221  C  CB    . SER A 1 2317 ? 211.017 221.903 246.472 1.00 28.37  ? 2317 SER A CB    1 
ATOM   6222  O  OG    . SER A 1 2317 ? 210.601 221.064 245.406 1.00 39.37  ? 2317 SER A OG    1 
ATOM   6223  N  N     . VAL A 1 2318 ? 212.341 219.015 247.251 1.00 25.76  ? 2318 VAL A N     1 
ATOM   6224  C  CA    . VAL A 1 2318 ? 212.228 217.764 247.995 1.00 23.69  ? 2318 VAL A CA    1 
ATOM   6225  C  C     . VAL A 1 2318 ? 213.384 217.623 248.977 1.00 36.30  ? 2318 VAL A C     1 
ATOM   6226  O  O     . VAL A 1 2318 ? 213.198 217.209 250.126 1.00 40.08  ? 2318 VAL A O     1 
ATOM   6227  C  CB    . VAL A 1 2318 ? 212.163 216.568 247.029 1.00 26.37  ? 2318 VAL A CB    1 
ATOM   6228  C  CG1   . VAL A 1 2318 ? 211.793 215.304 247.778 1.00 28.19  ? 2318 VAL A CG1   1 
ATOM   6229  C  CG2   . VAL A 1 2318 ? 211.169 216.840 245.921 1.00 35.84  ? 2318 VAL A CG2   1 
ATOM   6230  N  N     . LEU A 1 2319 ? 214.613 217.786 248.481 1.00 33.68  ? 2319 LEU A N     1 
ATOM   6231  C  CA    . LEU A 1 2319 ? 215.849 217.531 249.248 1.00 27.17  ? 2319 LEU A CA    1 
ATOM   6232  C  C     . LEU A 1 2319 ? 216.252 218.745 250.051 1.00 36.40  ? 2319 LEU A C     1 
ATOM   6233  O  O     . LEU A 1 2319 ? 217.370 218.751 250.548 1.00 45.55  ? 2319 LEU A O     1 
ATOM   6234  C  CB    . LEU A 1 2319 ? 216.843 217.248 248.144 1.00 37.14  ? 2319 LEU A CB    1 
ATOM   6235  C  CG    . LEU A 1 2319 ? 216.644 215.964 247.345 1.00 37.86  ? 2319 LEU A CG    1 
ATOM   6236  C  CD1   . LEU A 1 2319 ? 217.775 215.951 246.346 1.00 29.97  ? 2319 LEU A CD1   1 
ATOM   6237  C  CD2   . LEU A 1 2319 ? 216.737 214.786 248.275 1.00 32.77  ? 2319 LEU A CD2   1 
ATOM   6238  N  N     . ASP A 1 2320 ? 215.337 219.682 250.237 1.00 37.74  ? 2320 ASP A N     1 
ATOM   6239  C  CA    . ASP A 1 2320 ? 215.603 220.910 251.012 1.00 27.25  ? 2320 ASP A CA    1 
ATOM   6240  C  C     . ASP A 1 2320 ? 214.867 220.821 252.328 1.00 40.67  ? 2320 ASP A C     1 
ATOM   6241  O  O     . ASP A 1 2320 ? 214.631 219.712 252.784 1.00 46.19  ? 2320 ASP A O     1 
ATOM   6242  C  CB    . ASP A 1 2320 ? 214.997 222.140 250.384 1.00 32.23  ? 2320 ASP A CB    1 
ATOM   6243  C  CG    . ASP A 1 2320 ? 215.849 222.906 249.402 1.00 48.73  ? 2320 ASP A CG    1 
ATOM   6244  O  OD1   . ASP A 1 2320 ? 217.011 222.524 249.254 1.00 58.51  ? 2320 ASP A OD1   1 
ATOM   6245  O  OD2   . ASP A 1 2320 ? 215.326 223.867 248.806 1.00 49.37  ? 2320 ASP A OD2   1 
ATOM   6246  N  N     . ASP A 1 2321 ? 214.470 221.958 252.869 1.00 45.99  ? 2321 ASP A N     1 
ATOM   6247  C  CA    . ASP A 1 2321 ? 213.809 222.025 254.188 1.00 46.85  ? 2321 ASP A CA    1 
ATOM   6248  C  C     . ASP A 1 2321 ? 212.319 222.140 253.925 1.00 39.82  ? 2321 ASP A C     1 
ATOM   6249  O  O     . ASP A 1 2321 ? 211.559 222.217 254.881 1.00 41.73  ? 2321 ASP A O     1 
ATOM   6250  C  CB    . ASP A 1 2321 ? 214.413 223.178 254.962 1.00 46.47  ? 2321 ASP A CB    1 
ATOM   6251  C  CG    . ASP A 1 2321 ? 215.716 222.869 255.677 1.00 53.41  ? 2321 ASP A CG    1 
ATOM   6252  O  OD1   . ASP A 1 2321 ? 216.004 221.672 255.882 1.00 52.72  ? 2321 ASP A OD1   1 
ATOM   6253  O  OD2   . ASP A 1 2321 ? 216.427 223.828 256.022 1.00 53.72  ? 2321 ASP A OD2   1 
ATOM   6254  N  N     . ASN A 1 2322 ? 211.954 222.143 252.661 1.00 32.73  ? 2322 ASN A N     1 
ATOM   6255  C  CA    . ASN A 1 2322 ? 210.540 222.234 252.268 1.00 37.31  ? 2322 ASN A CA    1 
ATOM   6256  C  C     . ASN A 1 2322 ? 210.013 220.813 252.209 1.00 42.06  ? 2322 ASN A C     1 
ATOM   6257  O  O     . ASN A 1 2322 ? 208.820 220.659 252.445 1.00 43.10  ? 2322 ASN A O     1 
ATOM   6258  C  CB    . ASN A 1 2322 ? 210.412 222.940 250.931 1.00 30.99  ? 2322 ASN A CB    1 
ATOM   6259  C  CG    . ASN A 1 2322 ? 210.970 224.338 250.909 1.00 41.01  ? 2322 ASN A CG    1 
ATOM   6260  O  OD1   . ASN A 1 2322 ? 210.365 225.250 251.471 1.00 48.95  ? 2322 ASN A OD1   1 
ATOM   6261  N  ND2   . ASN A 1 2322 ? 212.087 224.535 250.227 1.00 40.12  ? 2322 ASN A ND2   1 
ATOM   6262  N  N     . LYS A 1 2323 ? 210.851 219.835 251.885 1.00 38.44  ? 2323 LYS A N     1 
ATOM   6263  C  CA    . LYS A 1 2323 ? 210.504 218.416 251.810 1.00 34.00  ? 2323 LYS A CA    1 
ATOM   6264  C  C     . LYS A 1 2323 ? 209.215 218.218 251.018 1.00 32.46  ? 2323 LYS A C     1 
ATOM   6265  O  O     . LYS A 1 2323 ? 208.251 217.608 251.483 1.00 44.23  ? 2323 LYS A O     1 
ATOM   6266  C  CB    . LYS A 1 2323 ? 210.396 217.805 253.207 1.00 31.41  ? 2323 LYS A CB    1 
ATOM   6267  C  CG    . LYS A 1 2323 ? 211.732 217.461 253.830 1.00 37.78  ? 2323 LYS A CG    1 
ATOM   6268  C  CD    . LYS A 1 2323 ? 211.557 216.805 255.185 1.00 35.56  ? 2323 LYS A CD    1 
ATOM   6269  C  CE    . LYS A 1 2323 ? 211.735 217.807 256.307 1.00 40.11  ? 2323 LYS A CE    1 
ATOM   6270  N  NZ    . LYS A 1 2323 ? 213.149 218.250 256.433 1.00 45.50  ? 2323 LYS A NZ    1 
ATOM   6271  N  N     . LEU A 1 2324 ? 209.209 218.745 249.797 1.00 32.28  ? 2324 LEU A N     1 
ATOM   6272  C  CA    . LEU A 1 2324 ? 207.996 218.874 249.008 1.00 30.24  ? 2324 LEU A CA    1 
ATOM   6273  C  C     . LEU A 1 2324 ? 208.320 218.736 247.531 1.00 32.57  ? 2324 LEU A C     1 
ATOM   6274  O  O     . LEU A 1 2324 ? 209.288 219.327 247.046 1.00 45.47  ? 2324 LEU A O     1 
ATOM   6275  C  CB    . LEU A 1 2324 ? 207.332 220.229 249.270 1.00 28.92  ? 2324 LEU A CB    1 
ATOM   6276  C  CG    . LEU A 1 2324 ? 205.885 220.457 248.856 1.00 32.37  ? 2324 LEU A CG    1 
ATOM   6277  C  CD1   . LEU A 1 2324 ? 204.937 219.890 249.890 1.00 31.40  ? 2324 LEU A CD1   1 
ATOM   6278  C  CD2   . LEU A 1 2324 ? 205.658 221.938 248.681 1.00 27.37  ? 2324 LEU A CD2   1 
ATOM   6279  N  N     . LEU A 1 2325 ? 207.507 217.966 246.817 1.00 25.46  ? 2325 LEU A N     1 
ATOM   6280  C  CA    . LEU A 1 2325 ? 207.622 217.825 245.370 1.00 26.83  ? 2325 LEU A CA    1 
ATOM   6281  C  C     . LEU A 1 2325 ? 206.488 218.612 244.730 1.00 34.94  ? 2325 LEU A C     1 
ATOM   6282  O  O     . LEU A 1 2325 ? 205.313 218.277 244.911 1.00 37.10  ? 2325 LEU A O     1 
ATOM   6283  C  CB    . LEU A 1 2325 ? 207.581 216.359 244.947 1.00 36.76  ? 2325 LEU A CB    1 
ATOM   6284  C  CG    . LEU A 1 2325 ? 207.652 216.109 243.440 1.00 34.45  ? 2325 LEU A CG    1 
ATOM   6285  C  CD1   . LEU A 1 2325 ? 209.070 216.296 242.935 1.00 32.23  ? 2325 LEU A CD1   1 
ATOM   6286  C  CD2   . LEU A 1 2325 ? 207.139 214.724 243.095 1.00 32.19  ? 2325 LEU A CD2   1 
ATOM   6287  N  N     . THR A 1 2326 ? 206.838 219.652 243.982 1.00 37.34  ? 2326 THR A N     1 
ATOM   6288  C  CA    . THR A 1 2326 ? 205.860 220.511 243.332 1.00 34.14  ? 2326 THR A CA    1 
ATOM   6289  C  C     . THR A 1 2326 ? 205.821 220.202 241.842 1.00 34.55  ? 2326 THR A C     1 
ATOM   6290  O  O     . THR A 1 2326 ? 206.863 220.181 241.180 1.00 38.84  ? 2326 THR A O     1 
ATOM   6291  C  CB    . THR A 1 2326 ? 206.189 221.987 243.556 1.00 36.43  ? 2326 THR A CB    1 
ATOM   6292  O  OG1   . THR A 1 2326 ? 207.228 222.387 242.657 1.00 41.92  ? 2326 THR A OG1   1 
ATOM   6293  C  CG2   . THR A 1 2326 ? 206.649 222.216 244.983 1.00 34.25  ? 2326 THR A CG2   1 
ATOM   6294  N  N     . LEU A 1 2327 ? 204.625 219.964 241.326 1.00 40.37  ? 2327 LEU A N     1 
ATOM   6295  C  CA    . LEU A 1 2327 ? 204.398 219.640 239.931 1.00 38.05  ? 2327 LEU A CA    1 
ATOM   6296  C  C     . LEU A 1 2327 ? 203.816 220.837 239.191 1.00 45.07  ? 2327 LEU A C     1 
ATOM   6297  O  O     . LEU A 1 2327 ? 203.200 221.717 239.801 1.00 49.57  ? 2327 LEU A O     1 
ATOM   6298  C  CB    . LEU A 1 2327 ? 203.447 218.442 239.808 1.00 38.61  ? 2327 LEU A CB    1 
ATOM   6299  C  CG    . LEU A 1 2327 ? 203.742 217.256 240.725 1.00 37.83  ? 2327 LEU A CG    1 
ATOM   6300  C  CD1   . LEU A 1 2327 ? 202.573 216.294 240.731 1.00 39.42  ? 2327 LEU A CD1   1 
ATOM   6301  C  CD2   . LEU A 1 2327 ? 205.018 216.552 240.301 1.00 39.20  ? 2327 LEU A CD2   1 
ATOM   6302  N  N     . PRO A 1 2328 ? 204.008 220.913 237.872 1.00 42.48  ? 2328 PRO A N     1 
ATOM   6303  C  CA    . PRO A 1 2328 ? 203.489 222.068 237.121 1.00 42.91  ? 2328 PRO A CA    1 
ATOM   6304  C  C     . PRO A 1 2328 ? 201.981 222.229 237.197 1.00 41.44  ? 2328 PRO A C     1 
ATOM   6305  O  O     . PRO A 1 2328 ? 201.489 223.351 237.031 1.00 47.19  ? 2328 PRO A O     1 
ATOM   6306  C  CB    . PRO A 1 2328 ? 203.951 221.794 235.682 1.00 44.73  ? 2328 PRO A CB    1 
ATOM   6307  C  CG    . PRO A 1 2328 ? 204.363 220.360 235.659 1.00 44.96  ? 2328 PRO A CG    1 
ATOM   6308  C  CD    . PRO A 1 2328 ? 204.845 220.045 237.030 1.00 38.03  ? 2328 PRO A CD    1 
ATOM   6309  N  N     . ASN A 1 2329 ? 201.230 221.158 237.442 1.00 41.18  ? 2329 ASN A N     1 
ATOM   6310  C  CA    . ASN A 1 2329 ? 199.783 221.262 237.580 1.00 41.99  ? 2329 ASN A CA    1 
ATOM   6311  C  C     . ASN A 1 2329 ? 199.355 221.767 238.953 1.00 42.18  ? 2329 ASN A C     1 
ATOM   6312  O  O     . ASN A 1 2329 ? 198.175 221.656 239.299 1.00 46.44  ? 2329 ASN A O     1 
ATOM   6313  C  CB    . ASN A 1 2329 ? 199.123 219.910 237.291 1.00 47.10  ? 2329 ASN A CB    1 
ATOM   6314  C  CG    . ASN A 1 2329 ? 199.318 218.913 238.411 1.00 49.45  ? 2329 ASN A CG    1 
ATOM   6315  O  OD1   . ASN A 1 2329 ? 200.401 218.808 238.980 1.00 48.10  ? 2329 ASN A OD1   1 
ATOM   6316  N  ND2   . ASN A 1 2329 ? 198.268 218.168 238.728 1.00 48.24  ? 2329 ASN A ND2   1 
ATOM   6317  N  N     . GLY A 1 2330 ? 200.282 222.316 239.737 1.00 46.98  ? 2330 GLY A N     1 
ATOM   6318  C  CA    . GLY A 1 2330 ? 199.969 222.901 241.020 1.00 43.46  ? 2330 GLY A CA    1 
ATOM   6319  C  C     . GLY A 1 2330 ? 199.973 221.941 242.188 1.00 44.89  ? 2330 GLY A C     1 
ATOM   6320  O  O     . GLY A 1 2330 ? 199.838 222.387 243.333 1.00 48.58  ? 2330 GLY A O     1 
ATOM   6321  N  N     . GLU A 1 2331 ? 200.128 220.644 241.942 1.00 49.45  ? 2331 GLU A N     1 
ATOM   6322  C  CA    . GLU A 1 2331 ? 200.090 219.664 243.016 1.00 40.46  ? 2331 GLU A CA    1 
ATOM   6323  C  C     . GLU A 1 2331 ? 201.393 219.678 243.801 1.00 37.44  ? 2331 GLU A C     1 
ATOM   6324  O  O     . GLU A 1 2331 ? 202.475 219.855 243.236 1.00 48.06  ? 2331 GLU A O     1 
ATOM   6325  C  CB    . GLU A 1 2331 ? 199.831 218.268 242.455 1.00 41.01  ? 2331 GLU A CB    1 
ATOM   6326  C  CG    . GLU A 1 2331 ? 199.187 217.320 243.446 1.00 45.95  ? 2331 GLU A CG    1 
ATOM   6327  C  CD    . GLU A 1 2331 ? 198.390 216.228 242.767 1.00 55.75  ? 2331 GLU A CD    1 
ATOM   6328  O  OE1   . GLU A 1 2331 ? 198.620 215.987 241.564 1.00 52.90  ? 2331 GLU A OE1   1 
ATOM   6329  O  OE2   . GLU A 1 2331 ? 197.534 215.612 243.436 1.00 52.16  ? 2331 GLU A OE2   1 
ATOM   6330  N  N     . ARG A 1 2332 ? 201.281 219.498 245.114 1.00 33.84  ? 2332 ARG A N     1 
ATOM   6331  C  CA    . ARG A 1 2332 ? 202.430 219.461 246.007 1.00 33.91  ? 2332 ARG A CA    1 
ATOM   6332  C  C     . ARG A 1 2332 ? 202.364 218.193 246.841 1.00 44.09  ? 2332 ARG A C     1 
ATOM   6333  O  O     . ARG A 1 2332 ? 201.346 217.924 247.486 1.00 52.22  ? 2332 ARG A O     1 
ATOM   6334  C  CB    . ARG A 1 2332 ? 202.465 220.696 246.909 1.00 34.32  ? 2332 ARG A CB    1 
ATOM   6335  C  CG    . ARG A 1 2332 ? 202.154 221.984 246.173 1.00 44.18  ? 2332 ARG A CG    1 
ATOM   6336  C  CD    . ARG A 1 2332 ? 201.567 223.040 247.089 1.00 36.45  ? 2332 ARG A CD    1 
ATOM   6337  N  NE    . ARG A 1 2332 ? 202.590 223.683 247.904 1.00 42.88  ? 2332 ARG A NE    1 
ATOM   6338  C  CZ    . ARG A 1 2332 ? 203.552 224.463 247.430 1.00 41.15  ? 2332 ARG A CZ    1 
ATOM   6339  N  NH1   . ARG A 1 2332 ? 203.653 224.736 246.140 1.00 24.00  ? 2332 ARG A NH1   1 
ATOM   6340  N  NH2   . ARG A 1 2332 ? 204.438 224.983 248.275 1.00 43.70  ? 2332 ARG A NH2   1 
ATOM   6341  N  N     . LEU A 1 2333 ? 203.445 217.419 246.826 1.00 30.93  ? 2333 LEU A N     1 
ATOM   6342  C  CA    . LEU A 1 2333 ? 203.524 216.153 247.544 1.00 29.06  ? 2333 LEU A CA    1 
ATOM   6343  C  C     . LEU A 1 2333 ? 204.583 216.269 248.628 1.00 36.05  ? 2333 LEU A C     1 
ATOM   6344  O  O     . LEU A 1 2333 ? 205.773 216.390 248.324 1.00 49.57  ? 2333 LEU A O     1 
ATOM   6345  C  CB    . LEU A 1 2333 ? 203.852 215.002 246.590 1.00 39.28  ? 2333 LEU A CB    1 
ATOM   6346  C  CG    . LEU A 1 2333 ? 202.799 214.628 245.545 1.00 33.33  ? 2333 LEU A CG    1 
ATOM   6347  C  CD1   . LEU A 1 2333 ? 203.085 215.314 244.227 1.00 37.86  ? 2333 LEU A CD1   1 
ATOM   6348  C  CD2   . LEU A 1 2333 ? 202.750 213.127 245.356 1.00 32.09  ? 2333 LEU A CD2   1 
ATOM   6349  N  N     . SER A 1 2334 ? 204.151 216.227 249.886 1.00 28.22  ? 2334 SER A N     1 
ATOM   6350  C  CA    . SER A 1 2334 ? 205.074 216.309 251.009 1.00 30.12  ? 2334 SER A CA    1 
ATOM   6351  C  C     . SER A 1 2334 ? 205.821 214.993 251.171 1.00 33.73  ? 2334 SER A C     1 
ATOM   6352  O  O     . SER A 1 2334 ? 205.216 213.918 251.141 1.00 44.77  ? 2334 SER A O     1 
ATOM   6353  C  CB    . SER A 1 2334 ? 204.326 216.649 252.296 1.00 33.69  ? 2334 SER A CB    1 
ATOM   6354  O  OG    . SER A 1 2334 ? 203.799 217.962 252.253 1.00 48.39  ? 2334 SER A OG    1 
ATOM   6355  N  N     . LEU A 1 2335 ? 207.129 215.079 251.345 1.00 36.97  ? 2335 LEU A N     1 
ATOM   6356  C  CA    . LEU A 1 2335 ? 207.936 213.887 251.568 1.00 32.81  ? 2335 LEU A CA    1 
ATOM   6357  C  C     . LEU A 1 2335 ? 207.693 213.357 252.975 1.00 39.76  ? 2335 LEU A C     1 
ATOM   6358  O  O     . LEU A 1 2335 ? 207.858 214.107 253.946 1.00 40.19  ? 2335 LEU A O     1 
ATOM   6359  C  CB    . LEU A 1 2335 ? 209.414 214.202 251.364 1.00 24.58  ? 2335 LEU A CB    1 
ATOM   6360  C  CG    . LEU A 1 2335 ? 210.375 213.016 251.314 1.00 32.95  ? 2335 LEU A CG    1 
ATOM   6361  C  CD1   . LEU A 1 2335 ? 210.336 212.354 249.952 1.00 38.96  ? 2335 LEU A CD1   1 
ATOM   6362  C  CD2   . LEU A 1 2335 ? 211.783 213.464 251.651 1.00 36.80  ? 2335 LEU A CD2   1 
ATOM   6363  N  N     . PRO A 1 2336 ? 207.299 212.092 253.135 1.00 36.43  ? 2336 PRO A N     1 
ATOM   6364  C  CA    . PRO A 1 2336 ? 207.066 211.567 254.477 1.00 26.95  ? 2336 PRO A CA    1 
ATOM   6365  C  C     . PRO A 1 2336 ? 208.371 211.444 255.245 1.00 33.67  ? 2336 PRO A C     1 
ATOM   6366  O  O     . PRO A 1 2336 ? 209.454 211.356 254.644 1.00 40.83  ? 2336 PRO A O     1 
ATOM   6367  C  CB    . PRO A 1 2336 ? 206.436 210.187 254.215 1.00 26.84  ? 2336 PRO A CB    1 
ATOM   6368  C  CG    . PRO A 1 2336 ? 205.983 210.227 252.797 1.00 34.86  ? 2336 PRO A CG    1 
ATOM   6369  C  CD    . PRO A 1 2336 ? 206.945 211.117 252.093 1.00 31.54  ? 2336 PRO A CD    1 
ATOM   6370  N  N     . PRO A 1 2337 ? 208.316 211.440 256.579 1.00 34.54  ? 2337 PRO A N     1 
ATOM   6371  C  CA    . PRO A 1 2337 ? 209.560 211.381 257.363 1.00 36.96  ? 2337 PRO A CA    1 
ATOM   6372  C  C     . PRO A 1 2337 ? 210.277 210.042 257.298 1.00 30.56  ? 2337 PRO A C     1 
ATOM   6373  O  O     . PRO A 1 2337 ? 211.427 209.960 257.746 1.00 28.04  ? 2337 PRO A O     1 
ATOM   6374  C  CB    . PRO A 1 2337 ? 209.088 211.687 258.791 1.00 31.62  ? 2337 PRO A CB    1 
ATOM   6375  C  CG    . PRO A 1 2337 ? 207.651 211.307 258.800 1.00 33.16  ? 2337 PRO A CG    1 
ATOM   6376  C  CD    . PRO A 1 2337 ? 207.132 211.621 257.434 1.00 36.53  ? 2337 PRO A CD    1 
ATOM   6377  N  N     . ASN A 1 2338 ? 209.647 208.994 256.774 1.00 33.16  ? 2338 ASN A N     1 
ATOM   6378  C  CA    . ASN A 1 2338 ? 210.277 207.682 256.692 1.00 38.41  ? 2338 ASN A CA    1 
ATOM   6379  C  C     . ASN A 1 2338 ? 210.945 207.421 255.349 1.00 33.27  ? 2338 ASN A C     1 
ATOM   6380  O  O     . ASN A 1 2338 ? 211.526 206.348 255.162 1.00 35.47  ? 2338 ASN A O     1 
ATOM   6381  C  CB    . ASN A 1 2338 ? 209.249 206.581 256.972 1.00 35.79  ? 2338 ASN A CB    1 
ATOM   6382  C  CG    . ASN A 1 2338 ? 208.214 206.459 255.876 1.00 38.79  ? 2338 ASN A CG    1 
ATOM   6383  O  OD1   . ASN A 1 2338 ? 207.489 207.406 255.585 1.00 50.63  ? 2338 ASN A OD1   1 
ATOM   6384  N  ND2   . ASN A 1 2338 ? 208.138 205.286 255.262 1.00 30.38  ? 2338 ASN A ND2   1 
ATOM   6385  N  N     . VAL A 1 2339 ? 210.890 208.371 254.420 1.00 31.44  ? 2339 VAL A N     1 
ATOM   6386  C  CA    . VAL A 1 2339 ? 211.422 208.197 253.075 1.00 32.56  ? 2339 VAL A CA    1 
ATOM   6387  C  C     . VAL A 1 2339 ? 212.770 208.895 252.982 1.00 34.86  ? 2339 VAL A C     1 
ATOM   6388  O  O     . VAL A 1 2339 ? 212.921 210.035 253.436 1.00 45.09  ? 2339 VAL A O     1 
ATOM   6389  C  CB    . VAL A 1 2339 ? 210.447 208.743 252.018 1.00 32.05  ? 2339 VAL A CB    1 
ATOM   6390  C  CG1   . VAL A 1 2339 ? 210.968 208.465 250.622 1.00 28.87  ? 2339 VAL A CG1   1 
ATOM   6391  C  CG2   . VAL A 1 2339 ? 209.077 208.133 252.205 1.00 34.72  ? 2339 VAL A CG2   1 
ATOM   6392  N  N     . ARG A 1 2340 ? 213.750 208.207 252.402 1.00 31.16  ? 2340 ARG A N     1 
ATOM   6393  C  CA    . ARG A 1 2340 ? 215.064 208.771 252.130 1.00 31.97  ? 2340 ARG A CA    1 
ATOM   6394  C  C     . ARG A 1 2340 ? 215.314 208.742 250.631 1.00 31.76  ? 2340 ARG A C     1 
ATOM   6395  O  O     . ARG A 1 2340 ? 215.195 207.688 250.000 1.00 42.66  ? 2340 ARG A O     1 
ATOM   6396  C  CB    . ARG A 1 2340 ? 216.166 207.997 252.857 1.00 23.30  ? 2340 ARG A CB    1 
ATOM   6397  C  CG    . ARG A 1 2340 ? 216.056 208.016 254.367 1.00 30.24  ? 2340 ARG A CG    1 
ATOM   6398  C  CD    . ARG A 1 2340 ? 216.437 209.370 254.925 1.00 30.95  ? 2340 ARG A CD    1 
ATOM   6399  N  NE    . ARG A 1 2340 ? 216.383 209.401 256.381 1.00 30.33  ? 2340 ARG A NE    1 
ATOM   6400  C  CZ    . ARG A 1 2340 ? 215.264 209.454 257.087 1.00 32.19  ? 2340 ARG A CZ    1 
ATOM   6401  N  NH1   . ARG A 1 2340 ? 214.079 209.485 256.502 1.00 35.85  ? 2340 ARG A NH1   1 
ATOM   6402  N  NH2   . ARG A 1 2340 ? 215.334 209.477 258.414 1.00 29.40  ? 2340 ARG A NH2   1 
ATOM   6403  N  N     . ILE A 1 2341 ? 215.656 209.894 250.066 1.00 37.45  ? 2341 ILE A N     1 
ATOM   6404  C  CA    . ILE A 1 2341 ? 216.037 209.987 248.662 1.00 31.94  ? 2341 ILE A CA    1 
ATOM   6405  C  C     . ILE A 1 2341 ? 217.544 209.804 248.575 1.00 36.94  ? 2341 ILE A C     1 
ATOM   6406  O  O     . ILE A 1 2341 ? 218.308 210.603 249.126 1.00 42.78  ? 2341 ILE A O     1 
ATOM   6407  C  CB    . ILE A 1 2341 ? 215.603 211.325 248.049 1.00 34.28  ? 2341 ILE A CB    1 
ATOM   6408  C  CG1   . ILE A 1 2341 ? 214.130 211.596 248.351 1.00 34.55  ? 2341 ILE A CG1   1 
ATOM   6409  C  CG2   . ILE A 1 2341 ? 215.855 211.330 246.554 1.00 30.19  ? 2341 ILE A CG2   1 
ATOM   6410  C  CD1   . ILE A 1 2341 ? 213.191 210.635 247.670 1.00 34.51  ? 2341 ILE A CD1   1 
ATOM   6411  N  N     . MET A 1 2342 ? 217.972 208.754 247.882 1.00 36.69  ? 2342 MET A N     1 
ATOM   6412  C  CA    . MET A 1 2342 ? 219.366 208.341 247.862 1.00 22.50  ? 2342 MET A CA    1 
ATOM   6413  C  C     . MET A 1 2342 ? 219.842 208.290 246.420 1.00 29.54  ? 2342 MET A C     1 
ATOM   6414  O  O     . MET A 1 2342 ? 219.126 207.794 245.547 1.00 43.12  ? 2342 MET A O     1 
ATOM   6415  C  CB    . MET A 1 2342 ? 219.523 206.975 248.529 1.00 28.63  ? 2342 MET A CB    1 
ATOM   6416  C  CG    . MET A 1 2342 ? 219.211 207.013 250.009 1.00 36.92  ? 2342 MET A CG    1 
ATOM   6417  S  SD    . MET A 1 2342 ? 219.288 205.440 250.880 1.00 52.21  ? 2342 MET A SD    1 
ATOM   6418  C  CE    . MET A 1 2342 ? 221.047 205.131 250.886 1.00 42.53  ? 2342 MET A CE    1 
ATOM   6419  N  N     . PHE A 1 2343 ? 221.039 208.807 246.168 1.00 25.78  ? 2343 PHE A N     1 
ATOM   6420  C  CA    . PHE A 1 2343 ? 221.660 208.730 244.854 1.00 23.57  ? 2343 PHE A CA    1 
ATOM   6421  C  C     . PHE A 1 2343 ? 222.928 207.901 244.966 1.00 35.11  ? 2343 PHE A C     1 
ATOM   6422  O  O     . PHE A 1 2343 ? 223.768 208.161 245.832 1.00 47.42  ? 2343 PHE A O     1 
ATOM   6423  C  CB    . PHE A 1 2343 ? 221.997 210.116 244.289 1.00 29.26  ? 2343 PHE A CB    1 
ATOM   6424  C  CG    . PHE A 1 2343 ? 220.853 211.096 244.314 1.00 36.23  ? 2343 PHE A CG    1 
ATOM   6425  C  CD1   . PHE A 1 2343 ? 220.535 211.786 245.469 1.00 29.68  ? 2343 PHE A CD1   1 
ATOM   6426  C  CD2   . PHE A 1 2343 ? 220.116 211.346 243.174 1.00 40.22  ? 2343 PHE A CD2   1 
ATOM   6427  C  CE1   . PHE A 1 2343 ? 219.496 212.687 245.492 1.00 27.15  ? 2343 PHE A CE1   1 
ATOM   6428  C  CE2   . PHE A 1 2343 ? 219.075 212.248 243.192 1.00 33.06  ? 2343 PHE A CE2   1 
ATOM   6429  C  CZ    . PHE A 1 2343 ? 218.766 212.919 244.353 1.00 34.47  ? 2343 PHE A CZ    1 
ATOM   6430  N  N     . GLU A 1 2344 ? 223.063 206.907 244.100 1.00 32.13  ? 2344 GLU A N     1 
ATOM   6431  C  CA    . GLU A 1 2344 ? 224.276 206.101 244.009 1.00 30.47  ? 2344 GLU A CA    1 
ATOM   6432  C  C     . GLU A 1 2344 ? 224.951 206.465 242.693 1.00 32.12  ? 2344 GLU A C     1 
ATOM   6433  O  O     . GLU A 1 2344 ? 224.538 206.006 241.626 1.00 41.75  ? 2344 GLU A O     1 
ATOM   6434  C  CB    . GLU A 1 2344 ? 223.959 204.614 244.093 1.00 29.87  ? 2344 GLU A CB    1 
ATOM   6435  C  CG    . GLU A 1 2344 ? 225.184 203.732 244.188 1.00 28.71  ? 2344 GLU A CG    1 
ATOM   6436  C  CD    . GLU A 1 2344 ? 224.891 202.304 243.805 1.00 34.12  ? 2344 GLU A CD    1 
ATOM   6437  O  OE1   . GLU A 1 2344 ? 223.868 201.764 244.267 1.00 42.60  ? 2344 GLU A OE1   1 
ATOM   6438  O  OE2   . GLU A 1 2344 ? 225.680 201.715 243.039 1.00 32.64  ? 2344 GLU A OE2   1 
ATOM   6439  N  N     . VAL A 1 2345 ? 225.988 207.295 242.775 1.00 35.47  ? 2345 VAL A N     1 
ATOM   6440  C  CA    . VAL A 1 2345 ? 226.642 207.853 241.602 1.00 34.17  ? 2345 VAL A CA    1 
ATOM   6441  C  C     . VAL A 1 2345 ? 228.127 207.530 241.664 1.00 30.36  ? 2345 VAL A C     1 
ATOM   6442  O  O     . VAL A 1 2345 ? 228.667 207.163 242.709 1.00 48.35  ? 2345 VAL A O     1 
ATOM   6443  C  CB    . VAL A 1 2345 ? 226.428 209.375 241.491 1.00 32.08  ? 2345 VAL A CB    1 
ATOM   6444  C  CG1   . VAL A 1 2345 ? 224.966 209.687 241.270 1.00 41.60  ? 2345 VAL A CG1   1 
ATOM   6445  C  CG2   . VAL A 1 2345 ? 226.931 210.069 242.740 1.00 32.74  ? 2345 VAL A CG2   1 
ATOM   6446  N  N     . GLN A 1 2346 ? 228.790 207.667 240.516 1.00 29.19  ? 2346 GLN A N     1 
ATOM   6447  C  CA    . GLN A 1 2346 ? 230.236 207.516 240.461 1.00 32.31  ? 2346 GLN A CA    1 
ATOM   6448  C  C     . GLN A 1 2346 ? 230.975 208.844 240.408 1.00 38.94  ? 2346 GLN A C     1 
ATOM   6449  O  O     . GLN A 1 2346 ? 232.164 208.885 240.741 1.00 46.96  ? 2346 GLN A O     1 
ATOM   6450  C  CB    . GLN A 1 2346 ? 230.644 206.656 239.259 1.00 31.82  ? 2346 GLN A CB    1 
ATOM   6451  C  CG    . GLN A 1 2346 ? 230.198 207.181 237.912 1.00 39.22  ? 2346 GLN A CG    1 
ATOM   6452  C  CD    . GLN A 1 2346 ? 230.861 206.445 236.766 1.00 48.53  ? 2346 GLN A CD    1 
ATOM   6453  O  OE1   . GLN A 1 2346 ? 231.868 205.763 236.953 1.00 48.08  ? 2346 GLN A OE1   1 
ATOM   6454  N  NE2   . GLN A 1 2346 ? 230.296 206.575 235.572 1.00 43.47  ? 2346 GLN A NE2   1 
ATOM   6455  N  N     . ASP A 1 2347 ? 230.309 209.921 240.002 1.00 37.15  ? 2347 ASP A N     1 
ATOM   6456  C  CA    . ASP A 1 2347 ? 230.895 211.251 240.048 1.00 31.70  ? 2347 ASP A CA    1 
ATOM   6457  C  C     . ASP A 1 2347 ? 229.771 212.273 240.060 1.00 39.92  ? 2347 ASP A C     1 
ATOM   6458  O  O     . ASP A 1 2347 ? 228.634 211.975 239.686 1.00 47.80  ? 2347 ASP A O     1 
ATOM   6459  C  CB    . ASP A 1 2347 ? 231.846 211.499 238.870 1.00 40.14  ? 2347 ASP A CB    1 
ATOM   6460  C  CG    . ASP A 1 2347 ? 231.211 211.191 237.526 1.00 53.83  ? 2347 ASP A CG    1 
ATOM   6461  O  OD1   . ASP A 1 2347 ? 230.278 211.914 237.121 1.00 56.36  ? 2347 ASP A OD1   1 
ATOM   6462  O  OD2   . ASP A 1 2347 ? 231.654 210.226 236.867 1.00 49.08  ? 2347 ASP A OD2   1 
ATOM   6463  N  N     . LEU A 1 2348 ? 230.105 213.483 240.495 1.00 39.58  ? 2348 LEU A N     1 
ATOM   6464  C  CA    . LEU A 1 2348 ? 229.172 214.602 240.531 1.00 36.51  ? 2348 LEU A CA    1 
ATOM   6465  C  C     . LEU A 1 2348 ? 229.718 215.771 239.729 1.00 41.62  ? 2348 LEU A C     1 
ATOM   6466  O  O     . LEU A 1 2348 ? 229.510 216.937 240.073 1.00 46.07  ? 2348 LEU A O     1 
ATOM   6467  C  CB    . LEU A 1 2348 ? 228.884 215.028 241.967 1.00 30.80  ? 2348 LEU A CB    1 
ATOM   6468  C  CG    . LEU A 1 2348 ? 227.941 214.138 242.771 1.00 37.98  ? 2348 LEU A CG    1 
ATOM   6469  C  CD1   . LEU A 1 2348 ? 227.854 214.635 244.197 1.00 34.52  ? 2348 LEU A CD1   1 
ATOM   6470  C  CD2   . LEU A 1 2348 ? 226.569 214.106 242.130 1.00 36.58  ? 2348 LEU A CD2   1 
ATOM   6471  N  N     . LYS A 1 2349 ? 230.424 215.473 238.639 1.00 38.97  ? 2349 LYS A N     1 
ATOM   6472  C  CA    . LYS A 1 2349 ? 231.125 216.502 237.884 1.00 43.89  ? 2349 LYS A CA    1 
ATOM   6473  C  C     . LYS A 1 2349 ? 230.201 217.366 237.039 1.00 47.13  ? 2349 LYS A C     1 
ATOM   6474  O  O     . LYS A 1 2349 ? 230.655 218.381 236.501 1.00 48.41  ? 2349 LYS A O     1 
ATOM   6475  C  CB    . LYS A 1 2349 ? 232.189 215.862 236.992 1.00 45.89  ? 2349 LYS A CB    1 
ATOM   6476  C  CG    . LYS A 1 2349 ? 231.641 215.189 235.753 1.00 49.81  ? 2349 LYS A CG    1 
ATOM   6477  C  CD    . LYS A 1 2349 ? 232.746 214.508 234.963 1.00 48.60  ? 2349 LYS A CD    1 
ATOM   6478  C  CE    . LYS A 1 2349 ? 233.867 215.477 234.632 1.00 51.42  ? 2349 LYS A CE    1 
ATOM   6479  N  NZ    . LYS A 1 2349 ? 233.399 216.603 233.779 1.00 49.50  ? 2349 LYS A NZ    1 
ATOM   6480  N  N     . TYR A 1 2350 ? 228.928 216.999 236.905 1.00 45.50  ? 2350 TYR A N     1 
ATOM   6481  C  CA    . TYR A 1 2350 ? 227.978 217.797 236.146 1.00 42.20  ? 2350 TYR A CA    1 
ATOM   6482  C  C     . TYR A 1 2350 ? 226.869 218.391 236.999 1.00 39.95  ? 2350 TYR A C     1 
ATOM   6483  O  O     . TYR A 1 2350 ? 226.169 219.292 236.529 1.00 47.59  ? 2350 TYR A O     1 
ATOM   6484  C  CB    . TYR A 1 2350 ? 227.363 216.961 235.014 1.00 40.40  ? 2350 TYR A CB    1 
ATOM   6485  C  CG    . TYR A 1 2350 ? 228.333 216.684 233.892 1.00 47.62  ? 2350 TYR A CG    1 
ATOM   6486  C  CD1   . TYR A 1 2350 ? 228.779 217.707 233.068 1.00 41.14  ? 2350 TYR A CD1   1 
ATOM   6487  C  CD2   . TYR A 1 2350 ? 228.817 215.405 233.664 1.00 42.17  ? 2350 TYR A CD2   1 
ATOM   6488  C  CE1   . TYR A 1 2350 ? 229.670 217.464 232.047 1.00 45.93  ? 2350 TYR A CE1   1 
ATOM   6489  C  CE2   . TYR A 1 2350 ? 229.709 215.151 232.644 1.00 36.13  ? 2350 TYR A CE2   1 
ATOM   6490  C  CZ    . TYR A 1 2350 ? 230.132 216.184 231.838 1.00 46.04  ? 2350 TYR A CZ    1 
ATOM   6491  O  OH    . TYR A 1 2350 ? 231.021 215.937 230.819 1.00 48.21  ? 2350 TYR A OH    1 
ATOM   6492  N  N     . ALA A 1 2351 ? 226.696 217.924 238.231 1.00 36.70  ? 2351 ALA A N     1 
ATOM   6493  C  CA    . ALA A 1 2351 ? 225.724 218.527 239.129 1.00 29.63  ? 2351 ALA A CA    1 
ATOM   6494  C  C     . ALA A 1 2351 ? 226.200 219.901 239.581 1.00 36.15  ? 2351 ALA A C     1 
ATOM   6495  O  O     . ALA A 1 2351 ? 227.400 220.140 239.739 1.00 41.27  ? 2351 ALA A O     1 
ATOM   6496  C  CB    . ALA A 1 2351 ? 225.492 217.628 240.342 1.00 23.31  ? 2351 ALA A CB    1 
ATOM   6497  N  N     . THR A 1 2352 ? 225.251 220.808 239.785 1.00 33.63  ? 2352 THR A N     1 
ATOM   6498  C  CA    . THR A 1 2352 ? 225.574 222.135 240.281 1.00 27.81  ? 2352 THR A CA    1 
ATOM   6499  C  C     . THR A 1 2352 ? 225.732 222.108 241.798 1.00 29.66  ? 2352 THR A C     1 
ATOM   6500  O  O     . THR A 1 2352 ? 225.465 221.104 242.462 1.00 38.14  ? 2352 THR A O     1 
ATOM   6501  C  CB    . THR A 1 2352 ? 224.497 223.140 239.876 1.00 32.90  ? 2352 THR A CB    1 
ATOM   6502  O  OG1   . THR A 1 2352 ? 223.209 222.640 240.251 1.00 36.95  ? 2352 THR A OG1   1 
ATOM   6503  C  CG2   . THR A 1 2352 ? 224.523 223.365 238.378 1.00 40.97  ? 2352 THR A CG2   1 
ATOM   6504  N  N     . LEU A 1 2353 ? 226.122 223.222 242.413 1.00 25.93  ? 2353 LEU A N     1 
ATOM   6505  C  CA    . LEU A 1 2353 ? 226.369 223.241 243.879 1.00 26.74  ? 2353 LEU A CA    1 
ATOM   6506  C  C     . LEU A 1 2353 ? 225.047 223.330 244.609 1.00 29.92  ? 2353 LEU A C     1 
ATOM   6507  O  O     . LEU A 1 2353 ? 225.062 223.334 245.818 1.00 35.37  ? 2353 LEU A O     1 
ATOM   6508  C  CB    . LEU A 1 2353 ? 227.260 224.390 244.317 1.00 29.09  ? 2353 LEU A CB    1 
ATOM   6509  C  CG    . LEU A 1 2353 ? 227.651 224.431 245.794 1.00 33.93  ? 2353 LEU A CG    1 
ATOM   6510  C  CD1   . LEU A 1 2353 ? 228.648 223.351 246.153 1.00 29.17  ? 2353 LEU A CD1   1 
ATOM   6511  C  CD2   . LEU A 1 2353 ? 228.159 225.804 246.166 1.00 38.63  ? 2353 LEU A CD2   1 
ATOM   6512  N  N     . ALA A 1 2354 ? 223.943 223.374 243.896 1.00 31.11  ? 2354 ALA A N     1 
ATOM   6513  C  CA    . ALA A 1 2354 ? 222.610 223.501 244.495 1.00 25.62  ? 2354 ALA A CA    1 
ATOM   6514  C  C     . ALA A 1 2354 ? 222.159 222.106 244.875 1.00 34.10  ? 2354 ALA A C     1 
ATOM   6515  O  O     . ALA A 1 2354 ? 221.426 221.981 245.836 1.00 38.55  ? 2354 ALA A O     1 
ATOM   6516  C  CB    . ALA A 1 2354 ? 221.714 224.154 243.507 1.00 25.99  ? 2354 ALA A CB    1 
ATOM   6517  N  N     . THR A 1 2355 ? 222.589 221.103 244.127 1.00 29.71  ? 2355 THR A N     1 
ATOM   6518  C  CA    . THR A 1 2355 ? 222.263 219.706 244.428 1.00 25.58  ? 2355 THR A CA    1 
ATOM   6519  C  C     . THR A 1 2355 ? 223.298 219.194 245.390 1.00 35.50  ? 2355 THR A C     1 
ATOM   6520  O  O     . THR A 1 2355 ? 222.910 218.537 246.343 1.00 45.37  ? 2355 THR A O     1 
ATOM   6521  C  CB    . THR A 1 2355 ? 222.219 218.904 243.134 1.00 33.71  ? 2355 THR A CB    1 
ATOM   6522  O  OG1   . THR A 1 2355 ? 220.915 219.177 242.639 1.00 38.24  ? 2355 THR A OG1   1 
ATOM   6523  C  CG2   . THR A 1 2355 ? 222.385 217.414 243.351 1.00 30.80  ? 2355 THR A CG2   1 
ATOM   6524  N  N     . VAL A 1 2356 ? 224.569 219.544 245.198 1.00 36.73  ? 2356 VAL A N     1 
ATOM   6525  C  CA    . VAL A 1 2356 ? 225.592 219.001 246.087 1.00 24.04  ? 2356 VAL A CA    1 
ATOM   6526  C  C     . VAL A 1 2356 ? 225.385 219.494 247.513 1.00 34.99  ? 2356 VAL A C     1 
ATOM   6527  O  O     . VAL A 1 2356 ? 225.630 218.764 248.481 1.00 42.28  ? 2356 VAL A O     1 
ATOM   6528  C  CB    . VAL A 1 2356 ? 226.993 219.357 245.560 1.00 27.95  ? 2356 VAL A CB    1 
ATOM   6529  C  CG1   . VAL A 1 2356 ? 228.064 218.863 246.511 1.00 37.01  ? 2356 VAL A CG1   1 
ATOM   6530  C  CG2   . VAL A 1 2356 ? 227.195 218.770 244.177 1.00 28.67  ? 2356 VAL A CG2   1 
ATOM   6531  N  N     . SER A 1 2357 ? 224.955 220.731 247.654 1.00 37.44  ? 2357 SER A N     1 
ATOM   6532  C  CA    . SER A 1 2357 ? 224.753 221.349 248.976 1.00 26.93  ? 2357 SER A CA    1 
ATOM   6533  C  C     . SER A 1 2357 ? 223.545 220.792 249.714 1.00 36.78  ? 2357 SER A C     1 
ATOM   6534  O  O     . SER A 1 2357 ? 223.473 221.031 250.901 1.00 47.49  ? 2357 SER A O     1 
ATOM   6535  C  CB    . SER A 1 2357 ? 224.578 222.798 248.783 1.00 26.94  ? 2357 SER A CB    1 
ATOM   6536  O  OG    . SER A 1 2357 ? 223.233 223.141 248.501 1.00 39.40  ? 2357 SER A OG    1 
ATOM   6537  N  N     . ARG A 1 2358 ? 222.662 220.055 249.063 1.00 24.26  ? 2358 ARG A N     1 
ATOM   6538  C  CA    . ARG A 1 2358 ? 221.403 219.682 249.736 1.00 30.80  ? 2358 ARG A CA    1 
ATOM   6539  C  C     . ARG A 1 2358 ? 221.448 218.221 250.139 1.00 42.47  ? 2358 ARG A C     1 
ATOM   6540  O  O     . ARG A 1 2358 ? 220.477 217.747 250.732 1.00 45.05  ? 2358 ARG A O     1 
ATOM   6541  C  CB    . ARG A 1 2358 ? 220.223 219.865 248.788 1.00 33.84  ? 2358 ARG A CB    1 
ATOM   6542  C  CG    . ARG A 1 2358 ? 219.734 221.253 248.444 1.00 29.02  ? 2358 ARG A CG    1 
ATOM   6543  C  CD    . ARG A 1 2358 ? 218.825 221.012 247.280 1.00 20.58  ? 2358 ARG A CD    1 
ATOM   6544  N  NE    . ARG A 1 2358 ? 217.892 222.119 247.094 1.00 24.18  ? 2358 ARG A NE    1 
ATOM   6545  C  CZ    . ARG A 1 2358 ? 218.260 223.342 246.797 1.00 28.02  ? 2358 ARG A CZ    1 
ATOM   6546  N  NH1   . ARG A 1 2358 ? 219.487 223.563 246.390 1.00 37.99  ? 2358 ARG A NH1   1 
ATOM   6547  N  NH2   . ARG A 1 2358 ? 217.406 224.335 246.916 1.00 32.05  ? 2358 ARG A NH2   1 
ATOM   6548  N  N     . CYS A 1 2359 ? 222.555 217.545 249.885 1.00 36.36  ? 2359 CYS A N     1 
ATOM   6549  C  CA    . CYS A 1 2359 ? 222.618 216.092 250.143 1.00 32.82  ? 2359 CYS A CA    1 
ATOM   6550  C  C     . CYS A 1 2359 ? 223.809 215.755 251.038 1.00 33.19  ? 2359 CYS A C     1 
ATOM   6551  O  O     . CYS A 1 2359 ? 224.796 216.459 250.932 1.00 39.45  ? 2359 CYS A O     1 
ATOM   6552  C  CB    . CYS A 1 2359 ? 222.732 215.336 248.825 1.00 37.81  ? 2359 CYS A CB    1 
ATOM   6553  S  SG    . CYS A 1 2359 ? 221.263 215.354 247.773 1.00 50.27  ? 2359 CYS A SG    1 
ATOM   6554  N  N     . GLY A 1 2360 ? 223.695 214.757 251.912 1.00 30.58  ? 2360 GLY A N     1 
ATOM   6555  C  CA    . GLY A 1 2360 ? 224.793 214.277 252.724 1.00 19.77  ? 2360 GLY A CA    1 
ATOM   6556  C  C     . GLY A 1 2360 ? 225.618 213.265 251.963 1.00 20.68  ? 2360 GLY A C     1 
ATOM   6557  O  O     . GLY A 1 2360 ? 225.100 212.229 251.541 1.00 39.86  ? 2360 GLY A O     1 
ATOM   6558  N  N     . MET A 1 2361 ? 226.902 213.551 251.778 1.00 34.84  ? 2361 MET A N     1 
ATOM   6559  C  CA    . MET A 1 2361 ? 227.753 212.753 250.909 1.00 28.62  ? 2361 MET A CA    1 
ATOM   6560  C  C     . MET A 1 2361 ? 228.426 211.650 251.713 1.00 32.04  ? 2361 MET A C     1 
ATOM   6561  O  O     . MET A 1 2361 ? 228.827 211.867 252.859 1.00 44.86  ? 2361 MET A O     1 
ATOM   6562  C  CB    . MET A 1 2361 ? 228.823 213.624 250.255 1.00 28.35  ? 2361 MET A CB    1 
ATOM   6563  C  CG    . MET A 1 2361 ? 228.323 214.753 249.387 1.00 33.94  ? 2361 MET A CG    1 
ATOM   6564  S  SD    . MET A 1 2361 ? 227.598 214.264 247.824 1.00 53.01  ? 2361 MET A SD    1 
ATOM   6565  C  CE    . MET A 1 2361 ? 226.250 215.432 247.768 1.00 29.61  ? 2361 MET A CE    1 
ATOM   6566  N  N     . VAL A 1 2362 ? 228.543 210.470 251.112 1.00 34.83  ? 2362 VAL A N     1 
ATOM   6567  C  CA    . VAL A 1 2362 ? 229.416 209.410 251.605 1.00 36.93  ? 2362 VAL A CA    1 
ATOM   6568  C  C     . VAL A 1 2362 ? 230.313 208.994 250.449 1.00 32.78  ? 2362 VAL A C     1 
ATOM   6569  O  O     . VAL A 1 2362 ? 229.819 208.599 249.387 1.00 42.83  ? 2362 VAL A O     1 
ATOM   6570  C  CB    . VAL A 1 2362 ? 228.628 208.211 252.153 1.00 35.22  ? 2362 VAL A CB    1 
ATOM   6571  C  CG1   . VAL A 1 2362 ? 229.571 207.229 252.823 1.00 29.55  ? 2362 VAL A CG1   1 
ATOM   6572  C  CG2   . VAL A 1 2362 ? 227.568 208.672 253.133 1.00 28.91  ? 2362 VAL A CG2   1 
ATOM   6573  N  N     . TRP A 1 2363 ? 231.623 209.076 250.653 1.00 39.91  ? 2363 TRP A N     1 
ATOM   6574  C  CA    . TRP A 1 2363 ? 232.595 208.839 249.595 1.00 36.58  ? 2363 TRP A CA    1 
ATOM   6575  C  C     . TRP A 1 2363 ? 233.139 207.420 249.706 1.00 50.77  ? 2363 TRP A C     1 
ATOM   6576  O  O     . TRP A 1 2363 ? 233.781 207.075 250.702 1.00 60.18  ? 2363 TRP A O     1 
ATOM   6577  C  CB    . TRP A 1 2363 ? 233.732 209.856 249.672 1.00 43.62  ? 2363 TRP A CB    1 
ATOM   6578  C  CG    . TRP A 1 2363 ? 234.870 209.550 248.760 1.00 47.81  ? 2363 TRP A CG    1 
ATOM   6579  C  CD1   . TRP A 1 2363 ? 236.097 209.081 249.112 1.00 47.56  ? 2363 TRP A CD1   1 
ATOM   6580  C  CD2   . TRP A 1 2363 ? 234.889 209.699 247.338 1.00 49.16  ? 2363 TRP A CD2   1 
ATOM   6581  N  NE1   . TRP A 1 2363 ? 236.881 208.925 247.997 1.00 48.42  ? 2363 TRP A NE1   1 
ATOM   6582  C  CE2   . TRP A 1 2363 ? 236.162 209.300 246.894 1.00 43.60  ? 2363 TRP A CE2   1 
ATOM   6583  C  CE3   . TRP A 1 2363 ? 233.954 210.133 246.396 1.00 52.01  ? 2363 TRP A CE3   1 
ATOM   6584  C  CZ2   . TRP A 1 2363 ? 236.522 209.318 245.553 1.00 43.56  ? 2363 TRP A CZ2   1 
ATOM   6585  C  CZ3   . TRP A 1 2363 ? 234.313 210.151 245.066 1.00 50.15  ? 2363 TRP A CZ3   1 
ATOM   6586  C  CH2   . TRP A 1 2363 ? 235.586 209.745 244.656 1.00 50.61  ? 2363 TRP A CH2   1 
ATOM   6587  N  N     . PHE A 1 2364 ? 232.895 206.610 248.680 1.00 42.14  ? 2364 PHE A N     1 
ATOM   6588  C  CA    . PHE A 1 2364 ? 233.374 205.232 248.614 1.00 41.83  ? 2364 PHE A CA    1 
ATOM   6589  C  C     . PHE A 1 2364 ? 234.549 205.182 247.644 1.00 42.33  ? 2364 PHE A C     1 
ATOM   6590  O  O     . PHE A 1 2364 ? 234.355 205.119 246.429 1.00 54.54  ? 2364 PHE A O     1 
ATOM   6591  C  CB    . PHE A 1 2364 ? 232.269 204.282 248.162 1.00 47.10  ? 2364 PHE A CB    1 
ATOM   6592  C  CG    . PHE A 1 2364 ? 231.221 204.017 249.200 1.00 44.46  ? 2364 PHE A CG    1 
ATOM   6593  C  CD1   . PHE A 1 2364 ? 230.211 204.929 249.430 1.00 41.26  ? 2364 PHE A CD1   1 
ATOM   6594  C  CD2   . PHE A 1 2364 ? 231.235 202.844 249.930 1.00 45.12  ? 2364 PHE A CD2   1 
ATOM   6595  C  CE1   . PHE A 1 2364 ? 229.242 204.682 250.374 1.00 39.91  ? 2364 PHE A CE1   1 
ATOM   6596  C  CE2   . PHE A 1 2364 ? 230.269 202.593 250.876 1.00 43.90  ? 2364 PHE A CE2   1 
ATOM   6597  C  CZ    . PHE A 1 2364 ? 229.272 203.513 251.100 1.00 49.06  ? 2364 PHE A CZ    1 
ATOM   6598  N  N     . SER A 1 2365 ? 235.765 205.198 248.176 1.00 38.14  ? 2365 SER A N     1 
ATOM   6599  C  CA    . SER A 1 2365 ? 236.927 205.023 247.322 1.00 41.56  ? 2365 SER A CA    1 
ATOM   6600  C  C     . SER A 1 2365 ? 237.042 203.566 246.887 1.00 53.08  ? 2365 SER A C     1 
ATOM   6601  O  O     . SER A 1 2365 ? 236.455 202.663 247.487 1.00 61.01  ? 2365 SER A O     1 
ATOM   6602  C  CB    . SER A 1 2365 ? 238.198 205.462 248.044 1.00 49.08  ? 2365 SER A CB    1 
ATOM   6603  O  OG    . SER A 1 2365 ? 238.298 204.848 249.316 1.00 56.63  ? 2365 SER A OG    1 
ATOM   6604  N  N     . GLU A 1 2366 ? 237.802 203.340 245.814 1.00 50.55  ? 2366 GLU A N     1 
ATOM   6605  C  CA    . GLU A 1 2366 ? 238.031 201.970 245.371 1.00 48.37  ? 2366 GLU A CA    1 
ATOM   6606  C  C     . GLU A 1 2366 ? 238.841 201.184 246.391 1.00 48.78  ? 2366 GLU A C     1 
ATOM   6607  O  O     . GLU A 1 2366 ? 238.759 199.952 246.430 1.00 52.03  ? 2366 GLU A O     1 
ATOM   6608  C  CB    . GLU A 1 2366 ? 238.729 201.958 244.012 1.00 47.71  ? 2366 GLU A CB    1 
ATOM   6609  C  CG    . GLU A 1 2366 ? 237.775 201.875 242.835 1.00 51.40  ? 2366 GLU A CG    1 
ATOM   6610  C  CD    . GLU A 1 2366 ? 238.489 201.606 241.527 1.00 57.41  ? 2366 GLU A CD    1 
ATOM   6611  O  OE1   . GLU A 1 2366 ? 239.010 200.485 241.353 1.00 58.56  ? 2366 GLU A OE1   1 
ATOM   6612  O  OE2   . GLU A 1 2366 ? 238.532 202.517 240.674 1.00 56.61  ? 2366 GLU A OE2   1 
ATOM   6613  N  N     . ASP A 1 2367 ? 239.624 201.875 247.220 1.00 48.97  ? 2367 ASP A N     1 
ATOM   6614  C  CA    . ASP A 1 2367 ? 240.370 201.212 248.280 1.00 44.13  ? 2367 ASP A CA    1 
ATOM   6615  C  C     . ASP A 1 2367 ? 239.459 200.666 249.370 1.00 52.67  ? 2367 ASP A C     1 
ATOM   6616  O  O     . ASP A 1 2367 ? 239.886 199.800 250.140 1.00 56.27  ? 2367 ASP A O     1 
ATOM   6617  C  CB    . ASP A 1 2367 ? 241.383 202.180 248.886 1.00 47.38  ? 2367 ASP A CB    1 
ATOM   6618  C  CG    . ASP A 1 2367 ? 242.502 202.522 247.927 1.00 56.12  ? 2367 ASP A CG    1 
ATOM   6619  O  OD1   . ASP A 1 2367 ? 242.832 201.675 247.072 1.00 56.40  ? 2367 ASP A OD1   1 
ATOM   6620  O  OD2   . ASP A 1 2367 ? 243.049 203.639 248.025 1.00 59.48  ? 2367 ASP A OD2   1 
ATOM   6621  N  N     . VAL A 1 2368 ? 238.222 201.159 249.456 1.00 48.99  ? 2368 VAL A N     1 
ATOM   6622  C  CA    . VAL A 1 2368 ? 237.268 200.633 250.429 1.00 43.95  ? 2368 VAL A CA    1 
ATOM   6623  C  C     . VAL A 1 2368 ? 236.992 199.161 250.156 1.00 48.73  ? 2368 VAL A C     1 
ATOM   6624  O  O     . VAL A 1 2368 ? 236.986 198.330 251.072 1.00 52.58  ? 2368 VAL A O     1 
ATOM   6625  C  CB    . VAL A 1 2368 ? 235.975 201.468 250.412 1.00 35.79  ? 2368 VAL A CB    1 
ATOM   6626  C  CG1   . VAL A 1 2368 ? 234.839 200.704 251.043 1.00 43.97  ? 2368 VAL A CG1   1 
ATOM   6627  C  CG2   . VAL A 1 2368 ? 236.188 202.779 251.141 1.00 46.25  ? 2368 VAL A CG2   1 
ATOM   6628  N  N     . LEU A 1 2369 ? 236.773 198.815 248.892 1.00 44.78  ? 2369 LEU A N     1 
ATOM   6629  C  CA    . LEU A 1 2369 ? 236.535 197.436 248.478 1.00 40.25  ? 2369 LEU A CA    1 
ATOM   6630  C  C     . LEU A 1 2369 ? 237.847 196.872 247.947 1.00 33.64  ? 2369 LEU A C     1 
ATOM   6631  O  O     . LEU A 1 2369 ? 238.200 197.081 246.784 1.00 42.45  ? 2369 LEU A O     1 
ATOM   6632  C  CB    . LEU A 1 2369 ? 235.431 197.369 247.430 1.00 37.53  ? 2369 LEU A CB    1 
ATOM   6633  C  CG    . LEU A 1 2369 ? 235.103 195.986 246.874 1.00 34.84  ? 2369 LEU A CG    1 
ATOM   6634  C  CD1   . LEU A 1 2369 ? 234.074 195.311 247.742 1.00 44.85  ? 2369 LEU A CD1   1 
ATOM   6635  C  CD2   . LEU A 1 2369 ? 234.610 196.087 245.448 1.00 31.88  ? 2369 LEU A CD2   1 
ATOM   6636  N  N     . SER A 1 2370 ? 238.575 196.163 248.803 1.00 31.86  ? 2370 SER A N     1 
ATOM   6637  C  CA    . SER A 1 2370 ? 239.825 195.553 248.384 1.00 32.62  ? 2370 SER A CA    1 
ATOM   6638  C  C     . SER A 1 2370 ? 239.555 194.324 247.521 1.00 37.34  ? 2370 SER A C     1 
ATOM   6639  O  O     . SER A 1 2370 ? 238.481 193.720 247.569 1.00 38.51  ? 2370 SER A O     1 
ATOM   6640  C  CB    . SER A 1 2370 ? 240.672 195.176 249.598 1.00 41.93  ? 2370 SER A CB    1 
ATOM   6641  O  OG    . SER A 1 2370 ? 239.923 194.422 250.530 1.00 45.85  ? 2370 SER A OG    1 
ATOM   6642  N  N     . THR A 1 2371 ? 240.554 193.963 246.713 1.00 39.85  ? 2371 THR A N     1 
ATOM   6643  C  CA    . THR A 1 2371 ? 240.403 192.835 245.799 1.00 27.26  ? 2371 THR A CA    1 
ATOM   6644  C  C     . THR A 1 2371 ? 240.242 191.519 246.551 1.00 29.65  ? 2371 THR A C     1 
ATOM   6645  O  O     . THR A 1 2371 ? 239.558 190.608 246.068 1.00 39.55  ? 2371 THR A O     1 
ATOM   6646  C  CB    . THR A 1 2371 ? 241.602 192.769 244.855 1.00 34.30  ? 2371 THR A CB    1 
ATOM   6647  O  OG1   . THR A 1 2371 ? 241.850 194.069 244.308 1.00 45.42  ? 2371 THR A OG1   1 
ATOM   6648  C  CG2   . THR A 1 2371 ? 241.326 191.816 243.716 1.00 36.12  ? 2371 THR A CG2   1 
ATOM   6649  N  N     . ASP A 1 2372 ? 240.860 191.405 247.729 1.00 37.81  ? 2372 ASP A N     1 
ATOM   6650  C  CA    . ASP A 1 2372 ? 240.691 190.209 248.547 1.00 29.46  ? 2372 ASP A CA    1 
ATOM   6651  C  C     . ASP A 1 2372 ? 239.228 189.992 248.905 1.00 32.43  ? 2372 ASP A C     1 
ATOM   6652  O  O     . ASP A 1 2372 ? 238.760 188.851 248.970 1.00 44.19  ? 2372 ASP A O     1 
ATOM   6653  C  CB    . ASP A 1 2372 ? 241.540 190.317 249.812 1.00 35.25  ? 2372 ASP A CB    1 
ATOM   6654  C  CG    . ASP A 1 2372 ? 242.164 188.995 250.212 1.00 54.05  ? 2372 ASP A CG    1 
ATOM   6655  O  OD1   . ASP A 1 2372 ? 241.863 187.972 249.562 1.00 54.59  ? 2372 ASP A OD1   1 
ATOM   6656  O  OD2   . ASP A 1 2372 ? 242.954 188.977 251.179 1.00 51.51  ? 2372 ASP A OD2   1 
ATOM   6657  N  N     . MET A 1 2373 ? 238.491 191.077 249.143 1.00 39.09  ? 2373 MET A N     1 
ATOM   6658  C  CA    . MET A 1 2373 ? 237.073 190.959 249.463 1.00 29.79  ? 2373 MET A CA    1 
ATOM   6659  C  C     . MET A 1 2373 ? 236.287 190.393 248.286 1.00 37.32  ? 2373 MET A C     1 
ATOM   6660  O  O     . MET A 1 2373 ? 235.398 189.553 248.468 1.00 49.19  ? 2373 MET A O     1 
ATOM   6661  C  CB    . MET A 1 2373 ? 236.523 192.322 249.877 1.00 32.35  ? 2373 MET A CB    1 
ATOM   6662  C  CG    . MET A 1 2373 ? 237.205 192.897 251.103 1.00 37.19  ? 2373 MET A CG    1 
ATOM   6663  S  SD    . MET A 1 2373 ? 236.683 194.570 251.505 1.00 45.19  ? 2373 MET A SD    1 
ATOM   6664  C  CE    . MET A 1 2373 ? 234.941 194.477 251.143 1.00 32.29  ? 2373 MET A CE    1 
ATOM   6665  N  N     . ILE A 1 2374 ? 236.602 190.840 247.069 1.00 36.89  ? 2374 ILE A N     1 
ATOM   6666  C  CA    . ILE A 1 2374 ? 235.935 190.307 245.885 1.00 28.77  ? 2374 ILE A CA    1 
ATOM   6667  C  C     . ILE A 1 2374 ? 236.279 188.836 245.691 1.00 35.90  ? 2374 ILE A C     1 
ATOM   6668  O  O     . ILE A 1 2374 ? 235.416 188.026 245.331 1.00 50.43  ? 2374 ILE A O     1 
ATOM   6669  C  CB    . ILE A 1 2374 ? 236.297 191.143 244.647 1.00 36.01  ? 2374 ILE A CB    1 
ATOM   6670  C  CG1   . ILE A 1 2374 ? 236.111 192.630 244.938 1.00 34.19  ? 2374 ILE A CG1   1 
ATOM   6671  C  CG2   . ILE A 1 2374 ? 235.446 190.732 243.464 1.00 40.79  ? 2374 ILE A CG2   1 
ATOM   6672  C  CD1   . ILE A 1 2374 ? 236.698 193.525 243.884 1.00 36.73  ? 2374 ILE A CD1   1 
ATOM   6673  N  N     . PHE A 1 2375 ? 237.543 188.467 245.918 1.00 34.07  ? 2375 PHE A N     1 
ATOM   6674  C  CA    . PHE A 1 2375 ? 237.921 187.058 245.839 1.00 25.04  ? 2375 PHE A CA    1 
ATOM   6675  C  C     . PHE A 1 2375 ? 237.147 186.225 246.852 1.00 36.24  ? 2375 PHE A C     1 
ATOM   6676  O  O     . PHE A 1 2375 ? 236.673 185.126 246.536 1.00 45.24  ? 2375 PHE A O     1 
ATOM   6677  C  CB    . PHE A 1 2375 ? 239.423 186.899 246.071 1.00 27.66  ? 2375 PHE A CB    1 
ATOM   6678  C  CG    . PHE A 1 2375 ? 240.275 187.459 244.971 1.00 38.08  ? 2375 PHE A CG    1 
ATOM   6679  C  CD1   . PHE A 1 2375 ? 239.739 187.734 243.727 1.00 36.10  ? 2375 PHE A CD1   1 
ATOM   6680  C  CD2   . PHE A 1 2375 ? 241.620 187.702 245.182 1.00 34.78  ? 2375 PHE A CD2   1 
ATOM   6681  C  CE1   . PHE A 1 2375 ? 240.529 188.246 242.720 1.00 33.52  ? 2375 PHE A CE1   1 
ATOM   6682  C  CE2   . PHE A 1 2375 ? 242.411 188.213 244.181 1.00 26.90  ? 2375 PHE A CE2   1 
ATOM   6683  C  CZ    . PHE A 1 2375 ? 241.867 188.483 242.949 1.00 35.24  ? 2375 PHE A CZ    1 
ATOM   6684  N  N     . ASN A 1 2376 ? 237.014 186.733 248.079 1.00 32.33  ? 2376 ASN A N     1 
ATOM   6685  C  CA    . ASN A 1 2376 ? 236.266 186.021 249.109 1.00 27.99  ? 2376 ASN A CA    1 
ATOM   6686  C  C     . ASN A 1 2376 ? 234.807 185.859 248.714 1.00 34.58  ? 2376 ASN A C     1 
ATOM   6687  O  O     . ASN A 1 2376 ? 234.219 184.791 248.913 1.00 42.46  ? 2376 ASN A O     1 
ATOM   6688  C  CB    . ASN A 1 2376 ? 236.375 186.760 250.442 1.00 32.80  ? 2376 ASN A CB    1 
ATOM   6689  C  CG    . ASN A 1 2376 ? 237.784 186.774 250.987 1.00 34.86  ? 2376 ASN A CG    1 
ATOM   6690  O  OD1   . ASN A 1 2376 ? 238.686 186.161 250.422 1.00 39.16  ? 2376 ASN A OD1   1 
ATOM   6691  N  ND2   . ASN A 1 2376 ? 237.982 187.483 252.090 1.00 36.62  ? 2376 ASN A ND2   1 
ATOM   6692  N  N     . ASN A 1 2377 ? 234.202 186.913 248.164 1.00 32.68  ? 2377 ASN A N     1 
ATOM   6693  C  CA    . ASN A 1 2377 ? 232.810 186.828 247.732 1.00 32.39  ? 2377 ASN A CA    1 
ATOM   6694  C  C     . ASN A 1 2377 ? 232.641 185.792 246.629 1.00 35.49  ? 2377 ASN A C     1 
ATOM   6695  O  O     . ASN A 1 2377 ? 231.705 184.982 246.663 1.00 42.32  ? 2377 ASN A O     1 
ATOM   6696  C  CB    . ASN A 1 2377 ? 232.327 188.200 247.263 1.00 32.41  ? 2377 ASN A CB    1 
ATOM   6697  C  CG    . ASN A 1 2377 ? 230.893 188.181 246.782 1.00 32.33  ? 2377 ASN A CG    1 
ATOM   6698  O  OD1   . ASN A 1 2377 ? 230.591 188.633 245.680 1.00 35.10  ? 2377 ASN A OD1   1 
ATOM   6699  N  ND2   . ASN A 1 2377 ? 230.001 187.657 247.609 1.00 40.19  ? 2377 ASN A ND2   1 
ATOM   6700  N  N     . PHE A 1 2378 ? 233.550 185.793 245.651 1.00 38.19  ? 2378 PHE A N     1 
ATOM   6701  C  CA    . PHE A 1 2378 ? 233.478 184.813 244.573 1.00 26.93  ? 2378 PHE A CA    1 
ATOM   6702  C  C     . PHE A 1 2378 ? 233.597 183.395 245.108 1.00 35.24  ? 2378 PHE A C     1 
ATOM   6703  O  O     . PHE A 1 2378 ? 232.820 182.513 244.726 1.00 38.61  ? 2378 PHE A O     1 
ATOM   6704  C  CB    . PHE A 1 2378 ? 234.571 185.085 243.541 1.00 23.08  ? 2378 PHE A CB    1 
ATOM   6705  C  CG    . PHE A 1 2378 ? 234.868 183.914 242.647 1.00 36.22  ? 2378 PHE A CG    1 
ATOM   6706  C  CD1   . PHE A 1 2378 ? 233.922 183.450 241.749 1.00 40.69  ? 2378 PHE A CD1   1 
ATOM   6707  C  CD2   . PHE A 1 2378 ? 236.096 183.277 242.702 1.00 32.94  ? 2378 PHE A CD2   1 
ATOM   6708  C  CE1   . PHE A 1 2378 ? 234.196 182.376 240.926 1.00 32.44  ? 2378 PHE A CE1   1 
ATOM   6709  C  CE2   . PHE A 1 2378 ? 236.372 182.202 241.882 1.00 31.29  ? 2378 PHE A CE2   1 
ATOM   6710  C  CZ    . PHE A 1 2378 ? 235.421 181.752 240.993 1.00 25.49  ? 2378 PHE A CZ    1 
ATOM   6711  N  N     . LEU A 1 2379 ? 234.554 183.157 246.008 1.00 40.51  ? 2379 LEU A N     1 
ATOM   6712  C  CA    . LEU A 1 2379 ? 234.751 181.806 246.524 1.00 31.56  ? 2379 LEU A CA    1 
ATOM   6713  C  C     . LEU A 1 2379 ? 233.580 181.361 247.390 1.00 29.20  ? 2379 LEU A C     1 
ATOM   6714  O  O     . LEU A 1 2379 ? 233.181 180.193 247.344 1.00 47.16  ? 2379 LEU A O     1 
ATOM   6715  C  CB    . LEU A 1 2379 ? 236.062 181.724 247.300 1.00 37.14  ? 2379 LEU A CB    1 
ATOM   6716  C  CG    . LEU A 1 2379 ? 237.322 181.755 246.437 1.00 32.14  ? 2379 LEU A CG    1 
ATOM   6717  C  CD1   . LEU A 1 2379 ? 238.565 181.798 247.301 1.00 32.41  ? 2379 LEU A CD1   1 
ATOM   6718  C  CD2   . LEU A 1 2379 ? 237.354 180.556 245.507 1.00 28.90  ? 2379 LEU A CD2   1 
ATOM   6719  N  N     . ALA A 1 2380 ? 233.012 182.270 248.185 1.00 30.49  ? 2380 ALA A N     1 
ATOM   6720  C  CA    . ALA A 1 2380 ? 231.855 181.912 248.999 1.00 32.25  ? 2380 ALA A CA    1 
ATOM   6721  C  C     . ALA A 1 2380 ? 230.658 181.555 248.129 1.00 39.43  ? 2380 ALA A C     1 
ATOM   6722  O  O     . ALA A 1 2380 ? 229.984 180.544 248.368 1.00 42.09  ? 2380 ALA A O     1 
ATOM   6723  C  CB    . ALA A 1 2380 ? 231.506 183.056 249.949 1.00 28.35  ? 2380 ALA A CB    1 
ATOM   6724  N  N     . ARG A 1 2381 ? 230.384 182.365 247.103 1.00 41.04  ? 2381 ARG A N     1 
ATOM   6725  C  CA    . ARG A 1 2381 ? 229.280 182.050 246.204 1.00 29.93  ? 2381 ARG A CA    1 
ATOM   6726  C  C     . ARG A 1 2381 ? 229.524 180.737 245.473 1.00 31.42  ? 2381 ARG A C     1 
ATOM   6727  O  O     . ARG A 1 2381 ? 228.592 179.951 245.272 1.00 44.91  ? 2381 ARG A O     1 
ATOM   6728  C  CB    . ARG A 1 2381 ? 229.072 183.187 245.207 1.00 33.69  ? 2381 ARG A CB    1 
ATOM   6729  C  CG    . ARG A 1 2381 ? 228.669 184.499 245.838 1.00 28.59  ? 2381 ARG A CG    1 
ATOM   6730  C  CD    . ARG A 1 2381 ? 228.479 185.561 244.780 1.00 33.73  ? 2381 ARG A CD    1 
ATOM   6731  N  NE    . ARG A 1 2381 ? 227.488 185.157 243.792 1.00 42.87  ? 2381 ARG A NE    1 
ATOM   6732  C  CZ    . ARG A 1 2381 ? 226.178 185.274 243.957 1.00 45.22  ? 2381 ARG A CZ    1 
ATOM   6733  N  NH1   . ARG A 1 2381 ? 225.664 185.796 245.057 1.00 47.78  ? 2381 ARG A NH1   1 
ATOM   6734  N  NH2   . ARG A 1 2381 ? 225.363 184.857 242.993 1.00 40.30  ? 2381 ARG A NH2   1 
ATOM   6735  N  N     . LEU A 1 2382 ? 230.770 180.485 245.065 1.00 32.31  ? 2382 LEU A N     1 
ATOM   6736  C  CA    . LEU A 1 2382 ? 231.093 179.233 244.391 1.00 40.43  ? 2382 LEU A CA    1 
ATOM   6737  C  C     . LEU A 1 2382 ? 230.879 178.036 245.308 1.00 37.46  ? 2382 LEU A C     1 
ATOM   6738  O  O     . LEU A 1 2382 ? 230.340 177.008 244.883 1.00 41.75  ? 2382 LEU A O     1 
ATOM   6739  C  CB    . LEU A 1 2382 ? 232.535 179.275 243.890 1.00 38.85  ? 2382 LEU A CB    1 
ATOM   6740  C  CG    . LEU A 1 2382 ? 232.980 178.152 242.958 1.00 33.60  ? 2382 LEU A CG    1 
ATOM   6741  C  CD1   . LEU A 1 2382 ? 232.250 178.228 241.632 1.00 26.92  ? 2382 LEU A CD1   1 
ATOM   6742  C  CD2   . LEU A 1 2382 ? 234.471 178.229 242.750 1.00 35.48  ? 2382 LEU A CD2   1 
ATOM   6743  N  N     . ARG A 1 2383 ? 231.296 178.147 246.568 1.00 34.77  ? 2383 ARG A N     1 
ATOM   6744  C  CA    . ARG A 1 2383 ? 231.135 177.056 247.519 1.00 35.14  ? 2383 ARG A CA    1 
ATOM   6745  C  C     . ARG A 1 2383 ? 229.702 176.891 248.002 1.00 42.94  ? 2383 ARG A C     1 
ATOM   6746  O  O     . ARG A 1 2383 ? 229.382 175.847 248.579 1.00 45.53  ? 2383 ARG A O     1 
ATOM   6747  C  CB    . ARG A 1 2383 ? 232.045 177.265 248.731 1.00 25.69  ? 2383 ARG A CB    1 
ATOM   6748  C  CG    . ARG A 1 2383 ? 233.520 177.068 248.452 1.00 32.28  ? 2383 ARG A CG    1 
ATOM   6749  C  CD    . ARG A 1 2383 ? 234.348 177.387 249.682 1.00 37.33  ? 2383 ARG A CD    1 
ATOM   6750  N  NE    . ARG A 1 2383 ? 235.730 176.947 249.541 1.00 44.52  ? 2383 ARG A NE    1 
ATOM   6751  C  CZ    . ARG A 1 2383 ? 236.784 177.737 249.686 1.00 46.91  ? 2383 ARG A CZ    1 
ATOM   6752  N  NH1   . ARG A 1 2383 ? 236.652 179.020 249.975 1.00 40.71  ? 2383 ARG A NH1   1 
ATOM   6753  N  NH2   . ARG A 1 2383 ? 238.003 177.226 249.540 1.00 42.23  ? 2383 ARG A NH2   1 
ATOM   6754  N  N     . SER A 1 2384 ? 228.837 177.881 247.793 1.00 41.83  ? 2384 SER A N     1 
ATOM   6755  C  CA    . SER A 1 2384 ? 227.476 177.804 248.311 1.00 36.59  ? 2384 SER A CA    1 
ATOM   6756  C  C     . SER A 1 2384 ? 226.426 177.624 247.227 1.00 41.14  ? 2384 SER A C     1 
ATOM   6757  O  O     . SER A 1 2384 ? 225.544 176.770 247.367 1.00 50.79  ? 2384 SER A O     1 
ATOM   6758  C  CB    . SER A 1 2384 ? 227.161 179.060 249.135 1.00 48.19  ? 2384 SER A CB    1 
ATOM   6759  O  OG    . SER A 1 2384 ? 226.019 178.860 249.948 1.00 54.09  ? 2384 SER A OG    1 
ATOM   6760  N  N     . ILE A 1 2385 ? 226.486 178.401 246.152 1.00 45.16  ? 2385 ILE A N     1 
ATOM   6761  C  CA    . ILE A 1 2385 ? 225.424 178.439 245.152 1.00 40.08  ? 2385 ILE A CA    1 
ATOM   6762  C  C     . ILE A 1 2385 ? 225.759 177.433 244.055 1.00 48.27  ? 2385 ILE A C     1 
ATOM   6763  O  O     . ILE A 1 2385 ? 226.804 177.577 243.401 1.00 48.17  ? 2385 ILE A O     1 
ATOM   6764  C  CB    . ILE A 1 2385 ? 225.254 179.846 244.569 1.00 40.44  ? 2385 ILE A CB    1 
ATOM   6765  C  CG1   . ILE A 1 2385 ? 224.909 180.840 245.677 1.00 41.97  ? 2385 ILE A CG1   1 
ATOM   6766  C  CG2   . ILE A 1 2385 ? 224.181 179.849 243.498 1.00 40.36  ? 2385 ILE A CG2   1 
ATOM   6767  C  CD1   . ILE A 1 2385 ? 224.730 182.254 245.192 1.00 40.51  ? 2385 ILE A CD1   1 
ATOM   6768  N  N     . PRO A 1 2386 ? 224.926 176.420 243.825 1.00 52.73  ? 2386 PRO A N     1 
ATOM   6769  C  CA    . PRO A 1 2386 ? 225.176 175.498 242.713 1.00 47.63  ? 2386 PRO A CA    1 
ATOM   6770  C  C     . PRO A 1 2386 ? 225.014 176.191 241.370 1.00 49.35  ? 2386 PRO A C     1 
ATOM   6771  O  O     . PRO A 1 2386 ? 224.166 177.068 241.192 1.00 59.41  ? 2386 PRO A O     1 
ATOM   6772  C  CB    . PRO A 1 2386 ? 224.118 174.405 242.904 1.00 53.23  ? 2386 PRO A CB    1 
ATOM   6773  C  CG    . PRO A 1 2386 ? 223.562 174.614 244.281 1.00 55.37  ? 2386 PRO A CG    1 
ATOM   6774  C  CD    . PRO A 1 2386 ? 223.709 176.067 244.571 1.00 52.47  ? 2386 PRO A CD    1 
ATOM   6775  N  N     . LEU A 1 2387 ? 225.846 175.780 240.413 1.00 53.94  ? 2387 LEU A N     1 
ATOM   6776  C  CA    . LEU A 1 2387 ? 225.821 176.404 239.094 1.00 49.02  ? 2387 LEU A CA    1 
ATOM   6777  C  C     . LEU A 1 2387 ? 224.647 175.915 238.255 1.00 58.26  ? 2387 LEU A C     1 
ATOM   6778  O  O     . LEU A 1 2387 ? 224.059 176.696 237.499 1.00 60.42  ? 2387 LEU A O     1 
ATOM   6779  C  CB    . LEU A 1 2387 ? 227.141 176.146 238.369 1.00 45.59  ? 2387 LEU A CB    1 
ATOM   6780  C  CG    . LEU A 1 2387 ? 228.272 177.110 238.724 1.00 48.65  ? 2387 LEU A CG    1 
ATOM   6781  C  CD1   . LEU A 1 2387 ? 229.549 176.736 237.997 1.00 52.58  ? 2387 LEU A CD1   1 
ATOM   6782  C  CD2   . LEU A 1 2387 ? 227.870 178.538 238.411 1.00 50.23  ? 2387 LEU A CD2   1 
ATOM   6783  N  N     . ASP A 1 2388 ? 224.296 174.632 238.364 1.00 69.12  ? 2388 ASP A N     1 
ATOM   6784  C  CA    . ASP A 1 2388 ? 223.209 174.097 237.550 1.00 67.47  ? 2388 ASP A CA    1 
ATOM   6785  C  C     . ASP A 1 2388 ? 221.871 174.723 237.926 1.00 71.34  ? 2388 ASP A C     1 
ATOM   6786  O  O     . ASP A 1 2388 ? 221.051 175.022 237.050 1.00 74.02  ? 2388 ASP A O     1 
ATOM   6787  C  CB    . ASP A 1 2388 ? 223.153 172.575 237.679 1.00 63.75  ? 2388 ASP A CB    1 
ATOM   6788  C  CG    . ASP A 1 2388 ? 223.170 172.109 239.118 1.00 70.05  ? 2388 ASP A CG    1 
ATOM   6789  O  OD1   . ASP A 1 2388 ? 223.279 172.963 240.021 1.00 73.88  ? 2388 ASP A OD1   1 
ATOM   6790  O  OD2   . ASP A 1 2388 ? 223.076 170.886 239.348 1.00 68.43  ? 2388 ASP A OD2   1 
ATOM   6791  N  N     . GLU A 1 2389 ? 221.632 174.930 239.217 1.00 73.16  ? 2389 GLU A N     1 
ATOM   6792  C  CA    . GLU A 1 2389 ? 220.413 175.587 239.674 1.00 70.98  ? 2389 GLU A CA    1 
ATOM   6793  C  C     . GLU A 1 2389 ? 220.595 176.167 241.070 1.00 68.99  ? 2389 GLU A C     1 
ATOM   6794  O  O     . GLU A 1 2389 ? 221.029 175.477 241.991 0.00 73.24  ? 2389 GLU A O     1 
ATOM   6795  C  CB    . GLU A 1 2389 ? 219.235 174.612 239.662 1.00 75.75  ? 2389 GLU A CB    1 
ATOM   6796  C  CG    . GLU A 1 2389 ? 217.912 175.234 240.087 1.00 79.29  ? 2389 GLU A CG    1 
ATOM   6797  C  CD    . GLU A 1 2389 ? 217.425 176.303 239.127 1.00 79.26  ? 2389 GLU A CD    1 
ATOM   6798  O  OE1   . GLU A 1 2389 ? 217.791 176.252 237.934 1.00 77.02  ? 2389 GLU A OE1   1 
ATOM   6799  O  OE2   . GLU A 1 2389 ? 216.674 177.198 239.567 1.00 79.85  ? 2389 GLU A OE2   1 
ATOM   6800  N  N     . SER A 1 2410 ? 224.472 167.564 246.024 1.00 63.68  ? 2410 SER A N     1 
ATOM   6801  C  CA    . SER A 1 2410 ? 224.536 167.850 244.597 1.00 65.63  ? 2410 SER A CA    1 
ATOM   6802  C  C     . SER A 1 2410 ? 225.953 167.655 244.071 1.00 68.39  ? 2410 SER A C     1 
ATOM   6803  O  O     . SER A 1 2410 ? 226.893 168.265 244.578 1.00 66.86  ? 2410 SER A O     1 
ATOM   6804  C  CB    . SER A 1 2410 ? 224.058 169.273 244.313 1.00 66.06  ? 2410 SER A CB    1 
ATOM   6805  O  OG    . SER A 1 2410 ? 224.121 169.566 242.930 1.00 68.48  ? 2410 SER A OG    1 
ATOM   6806  N  N     . PRO A 1 2411 ? 226.107 166.788 243.068 1.00 66.07  ? 2411 PRO A N     1 
ATOM   6807  C  CA    . PRO A 1 2411 ? 227.444 166.568 242.493 1.00 63.68  ? 2411 PRO A CA    1 
ATOM   6808  C  C     . PRO A 1 2411 ? 228.055 167.817 241.883 1.00 65.13  ? 2411 PRO A C     1 
ATOM   6809  O  O     . PRO A 1 2411 ? 229.277 167.998 241.957 1.00 68.93  ? 2411 PRO A O     1 
ATOM   6810  C  CB    . PRO A 1 2411 ? 227.195 165.483 241.437 1.00 65.51  ? 2411 PRO A CB    1 
ATOM   6811  C  CG    . PRO A 1 2411 ? 225.744 165.596 241.107 1.00 61.85  ? 2411 PRO A CG    1 
ATOM   6812  C  CD    . PRO A 1 2411 ? 225.065 166.014 242.373 1.00 61.18  ? 2411 PRO A CD    1 
ATOM   6813  N  N     . MET A 1 2412 ? 227.241 168.686 241.280 1.00 58.56  ? 2412 MET A N     1 
ATOM   6814  C  CA    . MET A 1 2412 ? 227.771 169.926 240.724 1.00 52.90  ? 2412 MET A CA    1 
ATOM   6815  C  C     . MET A 1 2412 ? 228.317 170.830 241.822 1.00 54.23  ? 2412 MET A C     1 
ATOM   6816  O  O     . MET A 1 2412 ? 229.379 171.442 241.659 1.00 54.76  ? 2412 MET A O     1 
ATOM   6817  C  CB    . MET A 1 2412 ? 226.690 170.642 239.914 1.00 53.51  ? 2412 MET A CB    1 
ATOM   6818  C  CG    . MET A 1 2412 ? 226.966 172.113 239.667 1.00 58.22  ? 2412 MET A CG    1 
ATOM   6819  S  SD    . MET A 1 2412 ? 228.103 172.397 238.296 1.00 69.43  ? 2412 MET A SD    1 
ATOM   6820  C  CE    . MET A 1 2412 ? 226.982 172.329 236.904 1.00 58.40  ? 2412 MET A CE    1 
ATOM   6821  N  N     . LEU A 1 2413 ? 227.613 170.918 242.952 1.00 54.48  ? 2413 LEU A N     1 
ATOM   6822  C  CA    . LEU A 1 2413 ? 228.127 171.693 244.075 1.00 51.83  ? 2413 LEU A CA    1 
ATOM   6823  C  C     . LEU A 1 2413 ? 229.399 171.081 244.641 1.00 47.67  ? 2413 LEU A C     1 
ATOM   6824  O  O     . LEU A 1 2413 ? 230.290 171.810 245.086 1.00 60.81  ? 2413 LEU A O     1 
ATOM   6825  C  CB    . LEU A 1 2413 ? 227.068 171.817 245.168 1.00 53.80  ? 2413 LEU A CB    1 
ATOM   6826  C  CG    . LEU A 1 2413 ? 227.353 172.887 246.221 1.00 52.12  ? 2413 LEU A CG    1 
ATOM   6827  C  CD1   . LEU A 1 2413 ? 227.741 174.193 245.555 1.00 51.16  ? 2413 LEU A CD1   1 
ATOM   6828  C  CD2   . LEU A 1 2413 ? 226.149 173.084 247.123 1.00 50.94  ? 2413 LEU A CD2   1 
ATOM   6829  N  N     . GLN A 1 2414 ? 229.505 169.751 244.641 1.00 41.54  ? 2414 GLN A N     1 
ATOM   6830  C  CA    . GLN A 1 2414 ? 230.741 169.115 245.084 1.00 47.47  ? 2414 GLN A CA    1 
ATOM   6831  C  C     . GLN A 1 2414 ? 231.898 169.462 244.156 1.00 52.15  ? 2414 GLN A C     1 
ATOM   6832  O  O     . GLN A 1 2414 ? 233.016 169.734 244.615 1.00 48.82  ? 2414 GLN A O     1 
ATOM   6833  C  CB    . GLN A 1 2414 ? 230.550 167.601 245.166 1.00 45.47  ? 2414 GLN A CB    1 
ATOM   6834  C  CG    . GLN A 1 2414 ? 231.669 166.871 245.882 1.00 49.78  ? 2414 GLN A CG    1 
ATOM   6835  C  CD    . GLN A 1 2414 ? 232.020 167.503 247.214 1.00 56.80  ? 2414 GLN A CD    1 
ATOM   6836  O  OE1   . GLN A 1 2414 ? 231.140 167.838 248.007 1.00 56.57  ? 2414 GLN A OE1   1 
ATOM   6837  N  NE2   . GLN A 1 2414 ? 233.313 167.667 247.468 1.00 52.68  ? 2414 GLN A NE2   1 
ATOM   6838  N  N     . ILE A 1 2415 ? 231.646 169.463 242.845 1.00 54.20  ? 2415 ILE A N     1 
ATOM   6839  C  CA    . ILE A 1 2415 ? 232.670 169.876 241.888 1.00 50.06  ? 2415 ILE A CA    1 
ATOM   6840  C  C     . ILE A 1 2415 ? 233.073 171.322 242.137 1.00 55.64  ? 2415 ILE A C     1 
ATOM   6841  O  O     . ILE A 1 2415 ? 234.260 171.668 242.099 1.00 62.32  ? 2415 ILE A O     1 
ATOM   6842  C  CB    . ILE A 1 2415 ? 232.170 169.667 240.447 1.00 48.27  ? 2415 ILE A CB    1 
ATOM   6843  C  CG1   . ILE A 1 2415 ? 232.076 168.176 240.123 1.00 52.69  ? 2415 ILE A CG1   1 
ATOM   6844  C  CG2   . ILE A 1 2415 ? 233.079 170.370 239.458 1.00 44.19  ? 2415 ILE A CG2   1 
ATOM   6845  C  CD1   . ILE A 1 2415 ? 231.296 167.879 238.868 1.00 53.28  ? 2415 ILE A CD1   1 
ATOM   6846  N  N     . GLN A 1 2416 ? 232.091 172.189 242.393 1.00 47.98  ? 2416 GLN A N     1 
ATOM   6847  C  CA    . GLN A 1 2416 ? 232.388 173.589 242.682 1.00 33.97  ? 2416 GLN A CA    1 
ATOM   6848  C  C     . GLN A 1 2416 ? 233.244 173.727 243.931 1.00 38.73  ? 2416 GLN A C     1 
ATOM   6849  O  O     . GLN A 1 2416 ? 234.180 174.531 243.963 1.00 45.64  ? 2416 GLN A O     1 
ATOM   6850  C  CB    . GLN A 1 2416 ? 231.094 174.381 242.848 1.00 39.79  ? 2416 GLN A CB    1 
ATOM   6851  C  CG    . GLN A 1 2416 ? 230.360 174.673 241.564 1.00 40.24  ? 2416 GLN A CG    1 
ATOM   6852  C  CD    . GLN A 1 2416 ? 228.951 175.151 241.817 1.00 45.56  ? 2416 GLN A CD    1 
ATOM   6853  O  OE1   . GLN A 1 2416 ? 228.021 174.775 241.111 1.00 55.04  ? 2416 GLN A OE1   1 
ATOM   6854  N  NE2   . GLN A 1 2416 ? 228.785 175.983 242.836 1.00 43.50  ? 2416 GLN A NE2   1 
ATOM   6855  N  N     . ARG A 1 2417 ? 232.924 172.968 244.980 1.00 44.68  ? 2417 ARG A N     1 
ATOM   6856  C  CA    . ARG A 1 2417 ? 233.688 173.055 246.220 1.00 42.11  ? 2417 ARG A CA    1 
ATOM   6857  C  C     . ARG A 1 2417 ? 235.120 172.577 246.022 1.00 47.67  ? 2417 ARG A C     1 
ATOM   6858  O  O     . ARG A 1 2417 ? 236.065 173.199 246.522 1.00 55.19  ? 2417 ARG A O     1 
ATOM   6859  C  CB    . ARG A 1 2417 ? 232.995 172.252 247.318 1.00 44.46  ? 2417 ARG A CB    1 
ATOM   6860  C  CG    . ARG A 1 2417 ? 231.662 172.836 247.750 1.00 44.49  ? 2417 ARG A CG    1 
ATOM   6861  C  CD    . ARG A 1 2417 ? 231.234 172.314 249.104 1.00 44.55  ? 2417 ARG A CD    1 
ATOM   6862  N  NE    . ARG A 1 2417 ? 230.094 173.056 249.628 1.00 50.81  ? 2417 ARG A NE    1 
ATOM   6863  C  CZ    . ARG A 1 2417 ? 228.941 172.508 249.984 1.00 56.10  ? 2417 ARG A CZ    1 
ATOM   6864  N  NH1   . ARG A 1 2417 ? 228.739 171.204 249.898 1.00 49.74  ? 2417 ARG A NH1   1 
ATOM   6865  N  NH2   . ARG A 1 2417 ? 227.966 173.288 250.439 1.00 52.15  ? 2417 ARG A NH2   1 
ATOM   6866  N  N     . ASP A 1 2418 ? 235.303 171.478 245.286 1.00 44.25  ? 2418 ASP A N     1 
ATOM   6867  C  CA    . ASP A 1 2418 ? 236.655 171.009 244.995 1.00 41.19  ? 2418 ASP A CA    1 
ATOM   6868  C  C     . ASP A 1 2418 ? 237.433 172.033 244.175 1.00 49.78  ? 2418 ASP A C     1 
ATOM   6869  O  O     . ASP A 1 2418 ? 238.610 172.299 244.452 1.00 53.92  ? 2418 ASP A O     1 
ATOM   6870  C  CB    . ASP A 1 2418 ? 236.600 169.669 244.266 1.00 45.87  ? 2418 ASP A CB    1 
ATOM   6871  C  CG    . ASP A 1 2418 ? 235.770 168.639 245.003 1.00 55.53  ? 2418 ASP A CG    1 
ATOM   6872  O  OD1   . ASP A 1 2418 ? 235.351 168.919 246.145 1.00 55.57  ? 2418 ASP A OD1   1 
ATOM   6873  O  OD2   . ASP A 1 2418 ? 235.534 167.551 244.440 1.00 55.60  ? 2418 ASP A OD2   1 
ATOM   6874  N  N     . ALA A 1 2419 ? 236.788 172.625 243.166 1.00 50.71  ? 2419 ALA A N     1 
ATOM   6875  C  CA    . ALA A 1 2419 ? 237.452 173.637 242.353 1.00 40.70  ? 2419 ALA A CA    1 
ATOM   6876  C  C     . ALA A 1 2419 ? 237.827 174.857 243.184 1.00 42.70  ? 2419 ALA A C     1 
ATOM   6877  O  O     . ALA A 1 2419 ? 238.910 175.424 243.007 1.00 50.48  ? 2419 ALA A O     1 
ATOM   6878  C  CB    . ALA A 1 2419 ? 236.557 174.038 241.183 1.00 42.05  ? 2419 ALA A CB    1 
ATOM   6879  N  N     . ALA A 1 2420 ? 236.942 175.281 244.088 1.00 38.64  ? 2420 ALA A N     1 
ATOM   6880  C  CA    . ALA A 1 2420 ? 237.242 176.418 244.950 1.00 37.64  ? 2420 ALA A CA    1 
ATOM   6881  C  C     . ALA A 1 2420 ? 238.403 176.110 245.883 1.00 40.22  ? 2420 ALA A C     1 
ATOM   6882  O  O     . ALA A 1 2420 ? 239.241 176.978 246.152 1.00 44.61  ? 2420 ALA A O     1 
ATOM   6883  C  CB    . ALA A 1 2420 ? 236.002 176.813 245.749 1.00 37.77  ? 2420 ALA A CB    1 
ATOM   6884  N  N     . THR A 1 2421 ? 238.463 174.880 246.398 1.00 43.77  ? 2421 THR A N     1 
ATOM   6885  C  CA    . THR A 1 2421 ? 239.603 174.485 247.217 1.00 46.25  ? 2421 THR A CA    1 
ATOM   6886  C  C     . THR A 1 2421 ? 240.896 174.527 246.412 1.00 46.24  ? 2421 THR A C     1 
ATOM   6887  O  O     . THR A 1 2421 ? 241.946 174.924 246.930 1.00 43.62  ? 2421 THR A O     1 
ATOM   6888  C  CB    . THR A 1 2421 ? 239.378 173.090 247.796 1.00 43.60  ? 2421 THR A CB    1 
ATOM   6889  O  OG1   . THR A 1 2421 ? 238.113 173.049 248.465 1.00 49.42  ? 2421 THR A OG1   1 
ATOM   6890  C  CG2   . THR A 1 2421 ? 240.477 172.741 248.785 1.00 44.48  ? 2421 THR A CG2   1 
ATOM   6891  N  N     . ILE A 1 2422 ? 240.841 174.114 245.145 1.00 49.55  ? 2422 ILE A N     1 
ATOM   6892  C  CA    . ILE A 1 2422 ? 242.040 174.145 244.311 1.00 46.87  ? 2422 ILE A CA    1 
ATOM   6893  C  C     . ILE A 1 2422 ? 242.463 175.583 244.019 1.00 49.29  ? 2422 ILE A C     1 
ATOM   6894  O  O     . ILE A 1 2422 ? 243.655 175.910 244.047 1.00 50.92  ? 2422 ILE A O     1 
ATOM   6895  C  CB    . ILE A 1 2422 ? 241.815 173.347 243.015 1.00 44.51  ? 2422 ILE A CB    1 
ATOM   6896  C  CG1   . ILE A 1 2422 ? 241.567 171.875 243.334 1.00 41.13  ? 2422 ILE A CG1   1 
ATOM   6897  C  CG2   . ILE A 1 2422 ? 243.016 173.478 242.095 1.00 45.64  ? 2422 ILE A CG2   1 
ATOM   6898  C  CD1   . ILE A 1 2422 ? 240.846 171.138 242.241 1.00 47.53  ? 2422 ILE A CD1   1 
ATOM   6899  N  N     . MET A 1 2423 ? 241.501 176.462 243.736 1.00 46.04  ? 2423 MET A N     1 
ATOM   6900  C  CA    . MET A 1 2423 ? 241.798 177.836 243.346 1.00 39.33  ? 2423 MET A CA    1 
ATOM   6901  C  C     . MET A 1 2423 ? 242.085 178.755 244.523 1.00 44.55  ? 2423 MET A C     1 
ATOM   6902  O  O     . MET A 1 2423 ? 242.503 179.896 244.301 1.00 47.30  ? 2423 MET A O     1 
ATOM   6903  C  CB    . MET A 1 2423 ? 240.638 178.425 242.542 1.00 38.43  ? 2423 MET A CB    1 
ATOM   6904  C  CG    . MET A 1 2423 ? 240.420 177.778 241.200 1.00 42.85  ? 2423 MET A CG    1 
ATOM   6905  S  SD    . MET A 1 2423 ? 239.088 178.557 240.282 1.00 61.71  ? 2423 MET A SD    1 
ATOM   6906  C  CE    . MET A 1 2423 ? 237.663 177.947 241.164 1.00 39.39  ? 2423 MET A CE    1 
ATOM   6907  N  N     . GLN A 1 2424 ? 241.860 178.301 245.753 1.00 44.20  ? 2424 GLN A N     1 
ATOM   6908  C  CA    . GLN A 1 2424 ? 242.061 179.165 246.916 1.00 38.43  ? 2424 GLN A CA    1 
ATOM   6909  C  C     . GLN A 1 2424 ? 243.472 179.736 247.012 1.00 45.51  ? 2424 GLN A C     1 
ATOM   6910  O  O     . GLN A 1 2424 ? 243.601 180.944 247.276 1.00 46.84  ? 2424 GLN A O     1 
ATOM   6911  C  CB    . GLN A 1 2424 ? 241.679 178.401 248.188 1.00 38.32  ? 2424 GLN A CB    1 
ATOM   6912  C  CG    . GLN A 1 2424 ? 242.043 179.114 249.473 1.00 43.11  ? 2424 GLN A CG    1 
ATOM   6913  C  CD    . GLN A 1 2424 ? 241.230 180.370 249.688 1.00 53.03  ? 2424 GLN A CD    1 
ATOM   6914  O  OE1   . GLN A 1 2424 ? 240.032 180.309 249.963 1.00 49.18  ? 2424 GLN A OE1   1 
ATOM   6915  N  NE2   . GLN A 1 2424 ? 241.879 181.523 249.565 1.00 44.93  ? 2424 GLN A NE2   1 
ATOM   6916  N  N     . PRO A 1 2425 ? 244.554 178.964 246.830 1.00 38.78  ? 2425 PRO A N     1 
ATOM   6917  C  CA    . PRO A 1 2425 ? 245.893 179.558 246.981 1.00 29.50  ? 2425 PRO A CA    1 
ATOM   6918  C  C     . PRO A 1 2425 ? 246.177 180.702 246.026 1.00 43.14  ? 2425 PRO A C     1 
ATOM   6919  O  O     . PRO A 1 2425 ? 246.937 181.613 246.377 1.00 48.86  ? 2425 PRO A O     1 
ATOM   6920  C  CB    . PRO A 1 2425 ? 246.831 178.372 246.723 1.00 37.11  ? 2425 PRO A CB    1 
ATOM   6921  C  CG    . PRO A 1 2425 ? 246.027 177.184 247.050 1.00 40.87  ? 2425 PRO A CG    1 
ATOM   6922  C  CD    . PRO A 1 2425 ? 244.641 177.510 246.609 1.00 39.12  ? 2425 PRO A CD    1 
ATOM   6923  N  N     . TYR A 1 2426 ? 245.603 180.683 244.825 1.00 48.30  ? 2426 TYR A N     1 
ATOM   6924  C  CA    . TYR A 1 2426 ? 245.871 181.722 243.842 1.00 41.05  ? 2426 TYR A CA    1 
ATOM   6925  C  C     . TYR A 1 2426 ? 245.013 182.965 244.028 1.00 46.95  ? 2426 TYR A C     1 
ATOM   6926  O  O     . TYR A 1 2426 ? 245.352 184.019 243.480 1.00 51.77  ? 2426 TYR A O     1 
ATOM   6927  C  CB    . TYR A 1 2426 ? 245.661 181.173 242.429 1.00 37.09  ? 2426 TYR A CB    1 
ATOM   6928  C  CG    . TYR A 1 2426 ? 246.366 179.862 242.176 1.00 38.69  ? 2426 TYR A CG    1 
ATOM   6929  C  CD1   . TYR A 1 2426 ? 247.726 179.825 241.912 1.00 46.56  ? 2426 TYR A CD1   1 
ATOM   6930  C  CD2   . TYR A 1 2426 ? 245.673 178.662 242.208 1.00 35.43  ? 2426 TYR A CD2   1 
ATOM   6931  C  CE1   . TYR A 1 2426 ? 248.375 178.631 241.685 1.00 44.88  ? 2426 TYR A CE1   1 
ATOM   6932  C  CE2   . TYR A 1 2426 ? 246.313 177.464 241.981 1.00 41.08  ? 2426 TYR A CE2   1 
ATOM   6933  C  CZ    . TYR A 1 2426 ? 247.664 177.454 241.720 1.00 43.95  ? 2426 TYR A CZ    1 
ATOM   6934  O  OH    . TYR A 1 2426 ? 248.308 176.262 241.493 1.00 46.11  ? 2426 TYR A OH    1 
ATOM   6935  N  N     . PHE A 1 2427 ? 243.924 182.875 244.791 1.00 40.88  ? 2427 PHE A N     1 
ATOM   6936  C  CA    . PHE A 1 2427 ? 243.015 183.993 245.001 1.00 32.82  ? 2427 PHE A CA    1 
ATOM   6937  C  C     . PHE A 1 2427 ? 243.250 184.689 246.336 1.00 43.31  ? 2427 PHE A C     1 
ATOM   6938  O  O     . PHE A 1 2427 ? 242.298 185.145 246.977 1.00 58.68  ? 2427 PHE A O     1 
ATOM   6939  C  CB    . PHE A 1 2427 ? 241.566 183.524 244.892 1.00 36.83  ? 2427 PHE A CB    1 
ATOM   6940  C  CG    . PHE A 1 2427 ? 241.060 183.454 243.484 1.00 32.06  ? 2427 PHE A CG    1 
ATOM   6941  C  CD1   . PHE A 1 2427 ? 240.885 184.606 242.743 1.00 29.54  ? 2427 PHE A CD1   1 
ATOM   6942  C  CD2   . PHE A 1 2427 ? 240.765 182.239 242.901 1.00 39.13  ? 2427 PHE A CD2   1 
ATOM   6943  C  CE1   . PHE A 1 2427 ? 240.424 184.547 241.450 1.00 33.64  ? 2427 PHE A CE1   1 
ATOM   6944  C  CE2   . PHE A 1 2427 ? 240.305 182.175 241.607 1.00 42.03  ? 2427 PHE A CE2   1 
ATOM   6945  C  CZ    . PHE A 1 2427 ? 240.133 183.330 240.881 1.00 40.64  ? 2427 PHE A CZ    1 
ATOM   6946  N  N     . THR A 1 2428 ? 244.501 184.771 246.770 1.00 43.26  ? 2428 THR A N     1 
ATOM   6947  C  CA    . THR A 1 2428 ? 244.868 185.450 248.000 1.00 44.84  ? 2428 THR A CA    1 
ATOM   6948  C  C     . THR A 1 2428 ? 245.533 186.781 247.679 1.00 49.86  ? 2428 THR A C     1 
ATOM   6949  O  O     . THR A 1 2428 ? 245.988 187.016 246.557 1.00 63.12  ? 2428 THR A O     1 
ATOM   6950  C  CB    . THR A 1 2428 ? 245.811 184.589 248.845 1.00 50.99  ? 2428 THR A CB    1 
ATOM   6951  O  OG1   . THR A 1 2428 ? 247.054 184.420 248.153 1.00 46.89  ? 2428 THR A OG1   1 
ATOM   6952  C  CG2   . THR A 1 2428 ? 245.196 183.227 249.106 1.00 47.98  ? 2428 THR A CG2   1 
ATOM   6953  N  N     . SER A 1 2429 ? 245.574 187.657 248.680 1.00 54.60  ? 2429 SER A N     1 
ATOM   6954  C  CA    . SER A 1 2429 ? 246.300 188.911 248.538 1.00 54.28  ? 2429 SER A CA    1 
ATOM   6955  C  C     . SER A 1 2429 ? 247.770 188.622 248.275 1.00 59.94  ? 2429 SER A C     1 
ATOM   6956  O  O     . SER A 1 2429 ? 248.358 187.729 248.892 1.00 58.83  ? 2429 SER A O     1 
ATOM   6957  C  CB    . SER A 1 2429 ? 246.138 189.765 249.794 1.00 55.56  ? 2429 SER A CB    1 
ATOM   6958  O  OG    . SER A 1 2429 ? 246.630 189.086 250.936 1.00 61.49  ? 2429 SER A OG    1 
ATOM   6959  N  N     . ASN A 1 2430 ? 248.359 189.375 247.347 1.00 64.80  ? 2430 ASN A N     1 
ATOM   6960  C  CA    . ASN A 1 2430 ? 249.694 189.134 246.810 1.00 62.07  ? 2430 ASN A CA    1 
ATOM   6961  C  C     . ASN A 1 2430 ? 249.778 187.744 246.184 1.00 64.48  ? 2430 ASN A C     1 
ATOM   6962  O  O     . ASN A 1 2430 ? 250.789 187.050 246.339 1.00 66.35  ? 2430 ASN A O     1 
ATOM   6963  C  CB    . ASN A 1 2430 ? 250.776 189.324 247.885 1.00 62.93  ? 2430 ASN A CB    1 
ATOM   6964  C  CG    . ASN A 1 2430 ? 252.194 189.304 247.324 1.00 69.93  ? 2430 ASN A CG    1 
ATOM   6965  O  OD1   . ASN A 1 2430 ? 252.406 189.126 246.124 1.00 75.37  ? 2430 ASN A OD1   1 
ATOM   6966  N  ND2   . ASN A 1 2430 ? 253.173 189.485 248.203 1.00 66.64  ? 2430 ASN A ND2   1 
ATOM   6967  N  N     . GLY A 1 2431 ? 248.712 187.293 245.530 1.00 53.52  ? 2431 GLY A N     1 
ATOM   6968  C  CA    . GLY A 1 2431 ? 248.704 186.018 244.849 1.00 51.74  ? 2431 GLY A CA    1 
ATOM   6969  C  C     . GLY A 1 2431 ? 248.935 186.166 243.358 1.00 49.69  ? 2431 GLY A C     1 
ATOM   6970  O  O     . GLY A 1 2431 ? 249.271 187.233 242.845 1.00 57.88  ? 2431 GLY A O     1 
ATOM   6971  N  N     . LEU A 1 2432 ? 248.745 185.051 242.648 1.00 43.94  ? 2432 LEU A N     1 
ATOM   6972  C  CA    . LEU A 1 2432 ? 248.922 185.061 241.200 1.00 40.18  ? 2432 LEU A CA    1 
ATOM   6973  C  C     . LEU A 1 2432 ? 247.915 185.981 240.523 1.00 39.06  ? 2432 LEU A C     1 
ATOM   6974  O  O     . LEU A 1 2432 ? 248.278 186.769 239.643 1.00 46.00  ? 2432 LEU A O     1 
ATOM   6975  C  CB    . LEU A 1 2432 ? 248.803 183.643 240.646 1.00 36.88  ? 2432 LEU A CB    1 
ATOM   6976  C  CG    . LEU A 1 2432 ? 248.581 183.537 239.137 1.00 37.50  ? 2432 LEU A CG    1 
ATOM   6977  C  CD1   . LEU A 1 2432 ? 249.856 183.868 238.381 1.00 40.93  ? 2432 LEU A CD1   1 
ATOM   6978  C  CD2   . LEU A 1 2432 ? 248.074 182.157 238.763 1.00 37.50  ? 2432 LEU A CD2   1 
ATOM   6979  N  N     . VAL A 1 2433 ? 246.646 185.899 240.922 1.00 39.69  ? 2433 VAL A N     1 
ATOM   6980  C  CA    . VAL A 1 2433 ? 245.620 186.722 240.293 1.00 38.24  ? 2433 VAL A CA    1 
ATOM   6981  C  C     . VAL A 1 2433 ? 245.846 188.194 240.605 1.00 35.68  ? 2433 VAL A C     1 
ATOM   6982  O  O     . VAL A 1 2433 ? 245.707 189.054 239.729 1.00 45.20  ? 2433 VAL A O     1 
ATOM   6983  C  CB    . VAL A 1 2433 ? 244.220 186.257 240.727 1.00 34.59  ? 2433 VAL A CB    1 
ATOM   6984  C  CG1   . VAL A 1 2433 ? 243.156 186.980 239.928 1.00 26.38  ? 2433 VAL A CG1   1 
ATOM   6985  C  CG2   . VAL A 1 2433 ? 244.090 184.757 240.555 1.00 37.29  ? 2433 VAL A CG2   1 
ATOM   6986  N  N     . THR A 1 2434 ? 246.207 188.509 241.850 1.00 41.99  ? 2434 THR A N     1 
ATOM   6987  C  CA    . THR A 1 2434 ? 246.439 189.900 242.227 1.00 42.26  ? 2434 THR A CA    1 
ATOM   6988  C  C     . THR A 1 2434 ? 247.634 190.487 241.483 1.00 44.88  ? 2434 THR A C     1 
ATOM   6989  O  O     . THR A 1 2434 ? 247.560 191.601 240.953 1.00 42.92  ? 2434 THR A O     1 
ATOM   6990  C  CB    . THR A 1 2434 ? 246.643 190.002 243.738 1.00 41.99  ? 2434 THR A CB    1 
ATOM   6991  O  OG1   . THR A 1 2434 ? 245.534 189.393 244.409 1.00 44.76  ? 2434 THR A OG1   1 
ATOM   6992  C  CG2   . THR A 1 2434 ? 246.745 191.453 244.162 1.00 43.81  ? 2434 THR A CG2   1 
ATOM   6993  N  N     . LYS A 1 2435 ? 248.746 189.750 241.433 1.00 46.22  ? 2435 LYS A N     1 
ATOM   6994  C  CA    . LYS A 1 2435 ? 249.925 190.239 240.725 1.00 36.76  ? 2435 LYS A CA    1 
ATOM   6995  C  C     . LYS A 1 2435 ? 249.659 190.374 239.232 1.00 41.77  ? 2435 LYS A C     1 
ATOM   6996  O  O     . LYS A 1 2435 ? 250.100 191.343 238.602 1.00 46.74  ? 2435 LYS A O     1 
ATOM   6997  C  CB    . LYS A 1 2435 ? 251.113 189.315 240.978 1.00 41.24  ? 2435 LYS A CB    1 
ATOM   6998  C  CG    . LYS A 1 2435 ? 251.607 189.322 242.412 1.00 46.97  ? 2435 LYS A CG    1 
ATOM   6999  C  CD    . LYS A 1 2435 ? 252.689 188.280 242.626 1.00 46.23  ? 2435 LYS A CD    1 
ATOM   7000  C  CE    . LYS A 1 2435 ? 254.042 188.790 242.161 1.00 51.00  ? 2435 LYS A CE    1 
ATOM   7001  N  NZ    . LYS A 1 2435 ? 255.142 187.842 242.490 1.00 53.76  ? 2435 LYS A NZ    1 
ATOM   7002  N  N     . ALA A 1 2436 ? 248.943 189.411 238.648 1.00 47.77  ? 2436 ALA A N     1 
ATOM   7003  C  CA    . ALA A 1 2436 ? 248.605 189.497 237.232 1.00 41.91  ? 2436 ALA A CA    1 
ATOM   7004  C  C     . ALA A 1 2436 ? 247.715 190.699 236.949 1.00 37.53  ? 2436 ALA A C     1 
ATOM   7005  O  O     . ALA A 1 2436 ? 247.897 191.388 235.940 1.00 47.03  ? 2436 ALA A O     1 
ATOM   7006  C  CB    . ALA A 1 2436 ? 247.927 188.206 236.776 1.00 35.15  ? 2436 ALA A CB    1 
ATOM   7007  N  N     . LEU A 1 2437 ? 246.740 190.963 237.822 1.00 35.30  ? 2437 LEU A N     1 
ATOM   7008  C  CA    . LEU A 1 2437 ? 245.882 192.128 237.646 1.00 34.96  ? 2437 LEU A CA    1 
ATOM   7009  C  C     . LEU A 1 2437 ? 246.676 193.420 237.773 1.00 42.95  ? 2437 LEU A C     1 
ATOM   7010  O  O     . LEU A 1 2437 ? 246.450 194.372 237.018 1.00 50.82  ? 2437 LEU A O     1 
ATOM   7011  C  CB    . LEU A 1 2437 ? 244.741 192.090 238.661 1.00 34.87  ? 2437 LEU A CB    1 
ATOM   7012  C  CG    . LEU A 1 2437 ? 243.690 193.193 238.576 1.00 40.43  ? 2437 LEU A CG    1 
ATOM   7013  C  CD1   . LEU A 1 2437 ? 243.025 193.195 237.214 1.00 41.07  ? 2437 LEU A CD1   1 
ATOM   7014  C  CD2   . LEU A 1 2437 ? 242.661 193.008 239.673 1.00 41.37  ? 2437 LEU A CD2   1 
ATOM   7015  N  N     . GLU A 1 2438 ? 247.609 193.474 238.725 1.00 45.85  ? 2438 GLU A N     1 
ATOM   7016  C  CA    . GLU A 1 2438 ? 248.445 194.662 238.868 1.00 40.12  ? 2438 GLU A CA    1 
ATOM   7017  C  C     . GLU A 1 2438 ? 249.301 194.886 237.630 1.00 43.15  ? 2438 GLU A C     1 
ATOM   7018  O  O     . GLU A 1 2438 ? 249.477 196.026 237.186 1.00 50.13  ? 2438 GLU A O     1 
ATOM   7019  C  CB    . GLU A 1 2438 ? 249.321 194.542 240.114 1.00 40.67  ? 2438 GLU A CB    1 
ATOM   7020  C  CG    . GLU A 1 2438 ? 248.544 194.567 241.416 1.00 45.93  ? 2438 GLU A CG    1 
ATOM   7021  C  CD    . GLU A 1 2438 ? 249.364 195.090 242.576 1.00 55.36  ? 2438 GLU A CD    1 
ATOM   7022  O  OE1   . GLU A 1 2438 ? 249.355 196.317 242.807 1.00 58.21  ? 2438 GLU A OE1   1 
ATOM   7023  O  OE2   . GLU A 1 2438 ? 250.017 194.272 243.258 1.00 51.80  ? 2438 GLU A OE2   1 
ATOM   7024  N  N     . HIS A 1 2439 ? 249.852 193.811 237.062 1.00 44.66  ? 2439 HIS A N     1 
ATOM   7025  C  CA    . HIS A 1 2439 ? 250.629 193.948 235.834 1.00 44.48  ? 2439 HIS A CA    1 
ATOM   7026  C  C     . HIS A 1 2439 ? 249.743 194.320 234.653 1.00 45.24  ? 2439 HIS A C     1 
ATOM   7027  O  O     . HIS A 1 2439 ? 250.155 195.093 233.781 1.00 52.15  ? 2439 HIS A O     1 
ATOM   7028  C  CB    . HIS A 1 2439 ? 251.385 192.656 235.541 1.00 46.38  ? 2439 HIS A CB    1 
ATOM   7029  C  CG    . HIS A 1 2439 ? 252.339 192.764 234.393 1.00 51.46  ? 2439 HIS A CG    1 
ATOM   7030  N  ND1   . HIS A 1 2439 ? 253.562 193.389 234.498 1.00 51.82  ? 2439 HIS A ND1   1 
ATOM   7031  C  CD2   . HIS A 1 2439 ? 252.247 192.330 233.114 1.00 52.61  ? 2439 HIS A CD2   1 
ATOM   7032  C  CE1   . HIS A 1 2439 ? 254.184 193.334 233.334 1.00 50.68  ? 2439 HIS A CE1   1 
ATOM   7033  N  NE2   . HIS A 1 2439 ? 253.407 192.697 232.477 1.00 52.46  ? 2439 HIS A NE2   1 
ATOM   7034  N  N     . ALA A 1 2440 ? 248.525 193.773 234.602 1.00 45.10  ? 2440 ALA A N     1 
ATOM   7035  C  CA    . ALA A 1 2440 ? 247.636 194.039 233.476 1.00 35.17  ? 2440 ALA A CA    1 
ATOM   7036  C  C     . ALA A 1 2440 ? 247.249 195.507 233.393 1.00 41.54  ? 2440 ALA A C     1 
ATOM   7037  O  O     . ALA A 1 2440 ? 246.955 196.009 232.303 1.00 54.02  ? 2440 ALA A O     1 
ATOM   7038  C  CB    . ALA A 1 2440 ? 246.384 193.170 233.579 1.00 38.58  ? 2440 ALA A CB    1 
ATOM   7039  N  N     . PHE A 1 2441 ? 247.236 196.211 234.524 1.00 40.97  ? 2441 PHE A N     1 
ATOM   7040  C  CA    . PHE A 1 2441 ? 246.906 197.629 234.515 1.00 40.82  ? 2441 PHE A CA    1 
ATOM   7041  C  C     . PHE A 1 2441 ? 248.003 198.484 233.898 1.00 43.75  ? 2441 PHE A C     1 
ATOM   7042  O  O     . PHE A 1 2441 ? 247.752 199.654 233.594 1.00 45.63  ? 2441 PHE A O     1 
ATOM   7043  C  CB    . PHE A 1 2441 ? 246.613 198.106 235.936 1.00 45.53  ? 2441 PHE A CB    1 
ATOM   7044  C  CG    . PHE A 1 2441 ? 245.170 197.983 236.330 1.00 51.86  ? 2441 PHE A CG    1 
ATOM   7045  C  CD1   . PHE A 1 2441 ? 244.244 198.922 235.915 1.00 49.96  ? 2441 PHE A CD1   1 
ATOM   7046  C  CD2   . PHE A 1 2441 ? 244.741 196.929 237.116 1.00 46.92  ? 2441 PHE A CD2   1 
ATOM   7047  C  CE1   . PHE A 1 2441 ? 242.917 198.811 236.275 1.00 47.13  ? 2441 PHE A CE1   1 
ATOM   7048  C  CE2   . PHE A 1 2441 ? 243.415 196.813 237.479 1.00 43.70  ? 2441 PHE A CE2   1 
ATOM   7049  C  CZ    . PHE A 1 2441 ? 242.503 197.755 237.059 1.00 43.06  ? 2441 PHE A CZ    1 
ATOM   7050  N  N     . GLN A 1 2442 ? 249.204 197.938 233.712 1.00 46.11  ? 2442 GLN A N     1 
ATOM   7051  C  CA    . GLN A 1 2442 ? 250.294 198.664 233.076 1.00 45.12  ? 2442 GLN A CA    1 
ATOM   7052  C  C     . GLN A 1 2442 ? 250.323 198.490 231.564 1.00 52.45  ? 2442 GLN A C     1 
ATOM   7053  O  O     . GLN A 1 2442 ? 251.049 199.225 230.887 1.00 56.88  ? 2442 GLN A O     1 
ATOM   7054  C  CB    . GLN A 1 2442 ? 251.639 198.221 233.663 1.00 43.91  ? 2442 GLN A CB    1 
ATOM   7055  C  CG    . GLN A 1 2442 ? 251.595 197.904 235.149 1.00 52.19  ? 2442 GLN A CG    1 
ATOM   7056  C  CD    . GLN A 1 2442 ? 251.244 199.111 235.996 1.00 58.67  ? 2442 GLN A CD    1 
ATOM   7057  O  OE1   . GLN A 1 2442 ? 251.569 200.245 235.648 1.00 56.87  ? 2442 GLN A OE1   1 
ATOM   7058  N  NE2   . GLN A 1 2442 ? 250.574 198.871 237.117 1.00 53.36  ? 2442 GLN A NE2   1 
ATOM   7059  N  N     . LEU A 1 2443 ? 249.563 197.545 231.023 1.00 51.24  ? 2443 LEU A N     1 
ATOM   7060  C  CA    . LEU A 1 2443 ? 249.433 197.383 229.585 1.00 45.95  ? 2443 LEU A CA    1 
ATOM   7061  C  C     . LEU A 1 2443 ? 248.331 198.297 229.062 1.00 52.83  ? 2443 LEU A C     1 
ATOM   7062  O  O     . LEU A 1 2443 ? 247.530 198.845 229.822 1.00 56.64  ? 2443 LEU A O     1 
ATOM   7063  C  CB    . LEU A 1 2443 ? 249.136 195.926 229.231 1.00 39.51  ? 2443 LEU A CB    1 
ATOM   7064  C  CG    . LEU A 1 2443 ? 249.905 194.850 229.999 1.00 41.55  ? 2443 LEU A CG    1 
ATOM   7065  C  CD1   . LEU A 1 2443 ? 249.501 193.468 229.521 1.00 39.63  ? 2443 LEU A CD1   1 
ATOM   7066  C  CD2   . LEU A 1 2443 ? 251.402 195.048 229.856 1.00 50.59  ? 2443 LEU A CD2   1 
ATOM   7067  N  N     . GLU A 1 2444 ? 248.291 198.465 227.745 1.00 47.36  ? 2444 GLU A N     1 
ATOM   7068  C  CA    . GLU A 1 2444 ? 247.287 199.307 227.111 1.00 48.11  ? 2444 GLU A CA    1 
ATOM   7069  C  C     . GLU A 1 2444 ? 246.238 198.434 226.436 1.00 53.91  ? 2444 GLU A C     1 
ATOM   7070  O  O     . GLU A 1 2444 ? 246.571 197.514 225.683 1.00 54.90  ? 2444 GLU A O     1 
ATOM   7071  C  CB    . GLU A 1 2444 ? 247.926 200.279 226.115 1.00 44.59  ? 2444 GLU A CB    1 
ATOM   7072  C  CG    . GLU A 1 2444 ? 248.633 199.646 224.938 1.00 54.14  ? 2444 GLU A CG    1 
ATOM   7073  C  CD    . GLU A 1 2444 ? 249.264 200.677 224.026 1.00 60.17  ? 2444 GLU A CD    1 
ATOM   7074  O  OE1   . GLU A 1 2444 ? 249.182 201.882 224.347 1.00 60.11  ? 2444 GLU A OE1   1 
ATOM   7075  O  OE2   . GLU A 1 2444 ? 249.844 200.286 222.993 1.00 55.12  ? 2444 GLU A OE2   1 
ATOM   7076  N  N     . HIS A 1 2445 ? 244.974 198.720 226.726 1.00 51.69  ? 2445 HIS A N     1 
ATOM   7077  C  CA    . HIS A 1 2445 ? 243.848 197.932 226.256 1.00 38.59  ? 2445 HIS A CA    1 
ATOM   7078  C  C     . HIS A 1 2445 ? 242.980 198.785 225.344 1.00 42.27  ? 2445 HIS A C     1 
ATOM   7079  O  O     . HIS A 1 2445 ? 243.042 200.017 225.378 1.00 49.04  ? 2445 HIS A O     1 
ATOM   7080  C  CB    . HIS A 1 2445 ? 243.020 197.405 227.433 1.00 37.48  ? 2445 HIS A CB    1 
ATOM   7081  C  CG    . HIS A 1 2445 ? 243.837 196.726 228.488 1.00 42.60  ? 2445 HIS A CG    1 
ATOM   7082  N  ND1   . HIS A 1 2445 ? 244.210 195.402 228.404 1.00 44.02  ? 2445 HIS A ND1   1 
ATOM   7083  C  CD2   . HIS A 1 2445 ? 244.362 197.192 229.645 1.00 41.40  ? 2445 HIS A CD2   1 
ATOM   7084  C  CE1   . HIS A 1 2445 ? 244.926 195.081 229.466 1.00 37.91  ? 2445 HIS A CE1   1 
ATOM   7085  N  NE2   . HIS A 1 2445 ? 245.034 196.149 230.235 1.00 38.72  ? 2445 HIS A NE2   1 
ATOM   7086  N  N     . ILE A 1 2446 ? 242.166 198.119 224.521 1.00 38.73  ? 2446 ILE A N     1 
ATOM   7087  C  CA    . ILE A 1 2446 ? 241.305 198.847 223.599 1.00 42.21  ? 2446 ILE A CA    1 
ATOM   7088  C  C     . ILE A 1 2446 ? 240.210 199.605 224.337 1.00 43.75  ? 2446 ILE A C     1 
ATOM   7089  O  O     . ILE A 1 2446 ? 239.568 200.485 223.754 1.00 47.09  ? 2446 ILE A O     1 
ATOM   7090  C  CB    . ILE A 1 2446 ? 240.706 197.890 222.553 1.00 40.96  ? 2446 ILE A CB    1 
ATOM   7091  C  CG1   . ILE A 1 2446 ? 240.399 198.649 221.263 1.00 42.48  ? 2446 ILE A CG1   1 
ATOM   7092  C  CG2   . ILE A 1 2446 ? 239.453 197.221 223.089 1.00 43.35  ? 2446 ILE A CG2   1 
ATOM   7093  C  CD1   . ILE A 1 2446 ? 241.631 199.188 220.575 1.00 42.44  ? 2446 ILE A CD1   1 
ATOM   7094  N  N     . MET A 1 2447 ? 239.978 199.286 225.607 1.00 38.26  ? 2447 MET A N     1 
ATOM   7095  C  CA    . MET A 1 2447 ? 239.052 200.022 226.451 1.00 35.40  ? 2447 MET A CA    1 
ATOM   7096  C  C     . MET A 1 2447 ? 239.704 200.263 227.803 1.00 49.44  ? 2447 MET A C     1 
ATOM   7097  O  O     . MET A 1 2447 ? 240.619 199.542 228.209 1.00 54.90  ? 2447 MET A O     1 
ATOM   7098  C  CB    . MET A 1 2447 ? 237.728 199.272 226.628 1.00 37.65  ? 2447 MET A CB    1 
ATOM   7099  C  CG    . MET A 1 2447 ? 236.965 199.061 225.338 1.00 38.09  ? 2447 MET A CG    1 
ATOM   7100  S  SD    . MET A 1 2447 ? 235.186 199.061 225.574 1.00 53.41  ? 2447 MET A SD    1 
ATOM   7101  C  CE    . MET A 1 2447 ? 234.639 199.065 223.875 1.00 41.12  ? 2447 MET A CE    1 
ATOM   7102  N  N     . ASP A 1 2448 ? 239.232 201.298 228.493 1.00 44.74  ? 2448 ASP A N     1 
ATOM   7103  C  CA    . ASP A 1 2448 ? 239.757 201.618 229.814 1.00 38.98  ? 2448 ASP A CA    1 
ATOM   7104  C  C     . ASP A 1 2448 ? 239.542 200.446 230.761 1.00 41.72  ? 2448 ASP A C     1 
ATOM   7105  O  O     . ASP A 1 2448 ? 238.403 200.088 231.074 1.00 43.93  ? 2448 ASP A O     1 
ATOM   7106  C  CB    . ASP A 1 2448 ? 239.086 202.878 230.358 1.00 45.79  ? 2448 ASP A CB    1 
ATOM   7107  C  CG    . ASP A 1 2448 ? 239.552 204.136 229.654 1.00 56.08  ? 2448 ASP A CG    1 
ATOM   7108  O  OD1   . ASP A 1 2448 ? 240.702 204.154 229.169 1.00 59.66  ? 2448 ASP A OD1   1 
ATOM   7109  O  OD2   . ASP A 1 2448 ? 238.771 205.108 229.587 1.00 49.21  ? 2448 ASP A OD2   1 
ATOM   7110  N  N     . LEU A 1 2449 ? 240.642 199.849 231.212 1.00 43.04  ? 2449 LEU A N     1 
ATOM   7111  C  CA    . LEU A 1 2449 ? 240.561 198.653 232.036 1.00 42.68  ? 2449 LEU A CA    1 
ATOM   7112  C  C     . LEU A 1 2449 ? 240.059 198.996 233.431 1.00 48.35  ? 2449 LEU A C     1 
ATOM   7113  O  O     . LEU A 1 2449 ? 240.497 199.977 234.038 1.00 50.71  ? 2449 LEU A O     1 
ATOM   7114  C  CB    . LEU A 1 2449 ? 241.926 197.977 232.129 1.00 42.16  ? 2449 LEU A CB    1 
ATOM   7115  C  CG    . LEU A 1 2449 ? 241.875 196.519 232.578 1.00 40.41  ? 2449 LEU A CG    1 
ATOM   7116  C  CD1   . LEU A 1 2449 ? 241.374 195.658 231.435 1.00 40.81  ? 2449 LEU A CD1   1 
ATOM   7117  C  CD2   . LEU A 1 2449 ? 243.228 196.043 233.065 1.00 37.97  ? 2449 LEU A CD2   1 
ATOM   7118  N  N     . THR A 1 2450 ? 239.140 198.181 233.937 1.00 41.04  ? 2450 THR A N     1 
ATOM   7119  C  CA    . THR A 1 2450 ? 238.660 198.284 235.304 1.00 38.20  ? 2450 THR A CA    1 
ATOM   7120  C  C     . THR A 1 2450 ? 238.795 196.927 235.978 1.00 42.10  ? 2450 THR A C     1 
ATOM   7121  O  O     . THR A 1 2450 ? 238.745 195.884 235.321 1.00 49.15  ? 2450 THR A O     1 
ATOM   7122  C  CB    . THR A 1 2450 ? 237.206 198.764 235.360 1.00 40.69  ? 2450 THR A CB    1 
ATOM   7123  O  OG1   . THR A 1 2450 ? 236.416 198.021 234.425 1.00 47.82  ? 2450 THR A OG1   1 
ATOM   7124  C  CG2   . THR A 1 2450 ? 237.125 200.240 235.017 1.00 36.73  ? 2450 THR A CG2   1 
ATOM   7125  N  N     . ARG A 1 2451 ? 238.983 196.953 237.299 1.00 35.92  ? 2451 ARG A N     1 
ATOM   7126  C  CA    . ARG A 1 2451 ? 239.240 195.723 238.040 1.00 31.66  ? 2451 ARG A CA    1 
ATOM   7127  C  C     . ARG A 1 2451 ? 238.073 194.750 237.931 1.00 37.18  ? 2451 ARG A C     1 
ATOM   7128  O  O     . ARG A 1 2451 ? 238.273 193.549 237.708 1.00 47.16  ? 2451 ARG A O     1 
ATOM   7129  C  CB    . ARG A 1 2451 ? 239.528 196.056 239.503 1.00 34.21  ? 2451 ARG A CB    1 
ATOM   7130  C  CG    . ARG A 1 2451 ? 239.487 194.870 240.442 1.00 40.62  ? 2451 ARG A CG    1 
ATOM   7131  C  CD    . ARG A 1 2451 ? 239.593 195.320 241.889 1.00 43.24  ? 2451 ARG A CD    1 
ATOM   7132  N  NE    . ARG A 1 2451 ? 238.516 196.229 242.260 1.00 40.90  ? 2451 ARG A NE    1 
ATOM   7133  C  CZ    . ARG A 1 2451 ? 238.411 196.822 243.441 1.00 36.38  ? 2451 ARG A CZ    1 
ATOM   7134  N  NH1   . ARG A 1 2451 ? 239.307 196.629 244.392 1.00 33.64  ? 2451 ARG A NH1   1 
ATOM   7135  N  NH2   . ARG A 1 2451 ? 237.382 197.633 243.670 1.00 31.79  ? 2451 ARG A NH2   1 
ATOM   7136  N  N     . LEU A 1 2452 ? 236.846 195.250 238.066 1.00 39.97  ? 2452 LEU A N     1 
ATOM   7137  C  CA    . LEU A 1 2452 ? 235.695 194.361 238.121 1.00 31.49  ? 2452 LEU A CA    1 
ATOM   7138  C  C     . LEU A 1 2452 ? 235.322 193.768 236.773 1.00 33.57  ? 2452 LEU A C     1 
ATOM   7139  O  O     . LEU A 1 2452 ? 234.754 192.677 236.744 1.00 42.43  ? 2452 LEU A O     1 
ATOM   7140  C  CB    . LEU A 1 2452 ? 234.489 195.078 238.722 1.00 31.12  ? 2452 LEU A CB    1 
ATOM   7141  C  CG    . LEU A 1 2452 ? 234.543 195.123 240.247 1.00 30.23  ? 2452 LEU A CG    1 
ATOM   7142  C  CD1   . LEU A 1 2452 ? 233.251 195.652 240.795 1.00 34.37  ? 2452 LEU A CD1   1 
ATOM   7143  C  CD2   . LEU A 1 2452 ? 234.824 193.741 240.795 1.00 34.49  ? 2452 LEU A CD2   1 
ATOM   7144  N  N     . ARG A 1 2453 ? 235.637 194.431 235.660 1.00 28.53  ? 2453 ARG A N     1 
ATOM   7145  C  CA    . ARG A 1 2453 ? 235.423 193.799 234.361 1.00 27.42  ? 2453 ARG A CA    1 
ATOM   7146  C  C     . ARG A 1 2453 ? 236.281 192.547 234.218 1.00 35.75  ? 2453 ARG A C     1 
ATOM   7147  O  O     . ARG A 1 2453 ? 235.780 191.469 233.863 1.00 42.57  ? 2453 ARG A O     1 
ATOM   7148  C  CB    . ARG A 1 2453 ? 235.723 194.793 233.241 1.00 30.76  ? 2453 ARG A CB    1 
ATOM   7149  C  CG    . ARG A 1 2453 ? 235.816 194.159 231.869 1.00 38.94  ? 2453 ARG A CG    1 
ATOM   7150  C  CD    . ARG A 1 2453 ? 235.510 195.159 230.774 1.00 35.34  ? 2453 ARG A CD    1 
ATOM   7151  N  NE    . ARG A 1 2453 ? 236.581 196.128 230.591 1.00 34.60  ? 2453 ARG A NE    1 
ATOM   7152  C  CZ    . ARG A 1 2453 ? 237.659 195.916 229.851 1.00 37.42  ? 2453 ARG A CZ    1 
ATOM   7153  N  NH1   . ARG A 1 2453 ? 237.855 194.766 229.230 1.00 31.53  ? 2453 ARG A NH1   1 
ATOM   7154  N  NH2   . ARG A 1 2453 ? 238.563 196.883 229.730 1.00 40.86  ? 2453 ARG A NH2   1 
ATOM   7155  N  N     . CYS A 1 2454 ? 237.576 192.670 234.518 1.00 33.86  ? 2454 CYS A N     1 
ATOM   7156  C  CA    . CYS A 1 2454 ? 238.472 191.521 234.479 1.00 27.13  ? 2454 CYS A CA    1 
ATOM   7157  C  C     . CYS A 1 2454 ? 238.034 190.448 235.463 1.00 34.70  ? 2454 CYS A C     1 
ATOM   7158  O  O     . CYS A 1 2454 ? 238.039 189.256 235.134 1.00 42.15  ? 2454 CYS A O     1 
ATOM   7159  C  CB    . CYS A 1 2454 ? 239.901 191.960 234.789 1.00 20.72  ? 2454 CYS A CB    1 
ATOM   7160  S  SG    . CYS A 1 2454 ? 240.616 193.082 233.590 1.00 56.25  ? 2454 CYS A SG    1 
ATOM   7161  N  N     . LEU A 1 2455 ? 237.660 190.852 236.678 1.00 24.28  ? 2455 LEU A N     1 
ATOM   7162  C  CA    . LEU A 1 2455 ? 237.272 189.869 237.681 1.00 18.23  ? 2455 LEU A CA    1 
ATOM   7163  C  C     . LEU A 1 2455 ? 235.997 189.135 237.283 1.00 29.79  ? 2455 LEU A C     1 
ATOM   7164  O  O     . LEU A 1 2455 ? 235.902 187.919 237.462 1.00 48.22  ? 2455 LEU A O     1 
ATOM   7165  C  CB    . LEU A 1 2455 ? 237.121 190.544 239.042 1.00 32.33  ? 2455 LEU A CB    1 
ATOM   7166  C  CG    . LEU A 1 2455 ? 238.450 190.960 239.680 1.00 38.02  ? 2455 LEU A CG    1 
ATOM   7167  C  CD1   . LEU A 1 2455 ? 238.282 191.238 241.160 1.00 32.61  ? 2455 LEU A CD1   1 
ATOM   7168  C  CD2   . LEU A 1 2455 ? 239.520 189.901 239.452 1.00 30.63  ? 2455 LEU A CD2   1 
ATOM   7169  N  N     . GLY A 1 2456 ? 235.010 189.846 236.736 1.00 14.63  ? 2456 GLY A N     1 
ATOM   7170  C  CA    . GLY A 1 2456 ? 233.797 189.184 236.289 1.00 14.48  ? 2456 GLY A CA    1 
ATOM   7171  C  C     . GLY A 1 2456 ? 234.050 188.225 235.144 1.00 32.46  ? 2456 GLY A C     1 
ATOM   7172  O  O     . GLY A 1 2456 ? 233.496 187.121 235.113 1.00 47.72  ? 2456 GLY A O     1 
ATOM   7173  N  N     . SER A 1 2457 ? 234.898 188.627 234.192 1.00 33.72  ? 2457 SER A N     1 
ATOM   7174  C  CA    . SER A 1 2457 ? 235.268 187.714 233.116 1.00 14.36  ? 2457 SER A CA    1 
ATOM   7175  C  C     . SER A 1 2457 ? 235.927 186.457 233.668 1.00 28.74  ? 2457 SER A C     1 
ATOM   7176  O  O     . SER A 1 2457 ? 235.575 185.338 233.276 1.00 39.17  ? 2457 SER A O     1 
ATOM   7177  C  CB    . SER A 1 2457 ? 236.207 188.412 232.137 1.00 17.11  ? 2457 SER A CB    1 
ATOM   7178  O  OG    . SER A 1 2457 ? 235.676 189.652 231.716 1.00 35.43  ? 2457 SER A OG    1 
ATOM   7179  N  N     . LEU A 1 2458 ? 236.875 186.628 234.592 1.00 29.43  ? 2458 LEU A N     1 
ATOM   7180  C  CA    . LEU A 1 2458 ? 237.582 185.486 235.161 1.00 20.95  ? 2458 LEU A CA    1 
ATOM   7181  C  C     . LEU A 1 2458 ? 236.633 184.572 235.925 1.00 25.31  ? 2458 LEU A C     1 
ATOM   7182  O  O     . LEU A 1 2458 ? 236.729 183.343 235.828 1.00 39.29  ? 2458 LEU A O     1 
ATOM   7183  C  CB    . LEU A 1 2458 ? 238.707 185.985 236.068 1.00 20.79  ? 2458 LEU A CB    1 
ATOM   7184  C  CG    . LEU A 1 2458 ? 239.502 184.987 236.904 1.00 29.52  ? 2458 LEU A CG    1 
ATOM   7185  C  CD1   . LEU A 1 2458 ? 240.423 184.167 236.028 1.00 36.26  ? 2458 LEU A CD1   1 
ATOM   7186  C  CD2   . LEU A 1 2458 ? 240.296 185.721 237.959 1.00 34.32  ? 2458 LEU A CD2   1 
ATOM   7187  N  N     . PHE A 1 2459 ? 235.702 185.153 236.683 1.00 24.52  ? 2459 PHE A N     1 
ATOM   7188  C  CA    . PHE A 1 2459 ? 234.775 184.345 237.467 1.00 21.13  ? 2459 PHE A CA    1 
ATOM   7189  C  C     . PHE A 1 2459 ? 233.827 183.561 236.570 1.00 27.79  ? 2459 PHE A C     1 
ATOM   7190  O  O     . PHE A 1 2459 ? 233.557 182.380 236.825 1.00 36.15  ? 2459 PHE A O     1 
ATOM   7191  C  CB    . PHE A 1 2459 ? 233.990 185.230 238.435 1.00 23.51  ? 2459 PHE A CB    1 
ATOM   7192  C  CG    . PHE A 1 2459 ? 234.853 185.998 239.399 1.00 30.18  ? 2459 PHE A CG    1 
ATOM   7193  C  CD1   . PHE A 1 2459 ? 236.144 185.587 239.683 1.00 23.98  ? 2459 PHE A CD1   1 
ATOM   7194  C  CD2   . PHE A 1 2459 ? 234.370 187.134 240.021 1.00 33.08  ? 2459 PHE A CD2   1 
ATOM   7195  C  CE1   . PHE A 1 2459 ? 236.933 186.296 240.565 1.00 24.27  ? 2459 PHE A CE1   1 
ATOM   7196  C  CE2   . PHE A 1 2459 ? 235.155 187.844 240.902 1.00 26.88  ? 2459 PHE A CE2   1 
ATOM   7197  C  CZ    . PHE A 1 2459 ? 236.437 187.424 241.174 1.00 29.35  ? 2459 PHE A CZ    1 
ATOM   7198  N  N     . SER A 1 2460 ? 233.312 184.192 235.511 1.00 20.38  ? 2460 SER A N     1 
ATOM   7199  C  CA    . SER A 1 2460 ? 232.469 183.459 234.573 1.00 23.31  ? 2460 SER A CA    1 
ATOM   7200  C  C     . SER A 1 2460 ? 233.246 182.351 233.875 1.00 30.38  ? 2460 SER A C     1 
ATOM   7201  O  O     . SER A 1 2460 ? 232.711 181.257 233.655 1.00 44.28  ? 2460 SER A O     1 
ATOM   7202  C  CB    . SER A 1 2460 ? 231.862 184.414 233.548 1.00 26.77  ? 2460 SER A CB    1 
ATOM   7203  O  OG    . SER A 1 2460 ? 232.861 184.962 232.709 1.00 39.91  ? 2460 SER A OG    1 
ATOM   7204  N  N     . MET A 1 2461 ? 234.509 182.608 233.533 1.00 29.20  ? 2461 MET A N     1 
ATOM   7205  C  CA    . MET A 1 2461 ? 235.323 181.579 232.898 1.00 14.74  ? 2461 MET A CA    1 
ATOM   7206  C  C     . MET A 1 2461 ? 235.542 180.397 233.836 1.00 32.02  ? 2461 MET A C     1 
ATOM   7207  O  O     . MET A 1 2461 ? 235.508 179.236 233.410 1.00 44.00  ? 2461 MET A O     1 
ATOM   7208  C  CB    . MET A 1 2461 ? 236.653 182.186 232.458 1.00 27.18  ? 2461 MET A CB    1 
ATOM   7209  C  CG    . MET A 1 2461 ? 236.584 182.867 231.105 1.00 29.44  ? 2461 MET A CG    1 
ATOM   7210  S  SD    . MET A 1 2461 ? 238.177 183.432 230.493 1.00 40.60  ? 2461 MET A SD    1 
ATOM   7211  C  CE    . MET A 1 2461 ? 238.546 182.145 229.313 1.00 33.86  ? 2461 MET A CE    1 
ATOM   7212  N  N     . LEU A 1 2462 ? 235.752 180.670 235.125 1.00 39.96  ? 2462 LEU A N     1 
ATOM   7213  C  CA    . LEU A 1 2462 ? 235.926 179.586 236.088 1.00 32.04  ? 2462 LEU A CA    1 
ATOM   7214  C  C     . LEU A 1 2462 ? 234.630 178.812 236.310 1.00 24.35  ? 2462 LEU A C     1 
ATOM   7215  O  O     . LEU A 1 2462 ? 234.660 177.590 236.512 1.00 40.76  ? 2462 LEU A O     1 
ATOM   7216  C  CB    . LEU A 1 2462 ? 236.460 180.148 237.401 1.00 27.80  ? 2462 LEU A CB    1 
ATOM   7217  C  CG    . LEU A 1 2462 ? 237.860 180.743 237.253 1.00 23.92  ? 2462 LEU A CG    1 
ATOM   7218  C  CD1   . LEU A 1 2462 ? 238.264 181.524 238.486 1.00 25.80  ? 2462 LEU A CD1   1 
ATOM   7219  C  CD2   . LEU A 1 2462 ? 238.870 179.658 236.936 1.00 31.40  ? 2462 LEU A CD2   1 
ATOM   7220  N  N     . HIS A 1 2463 ? 233.485 179.497 236.276 1.00 27.33  ? 2463 HIS A N     1 
ATOM   7221  C  CA    . HIS A 1 2463 ? 232.212 178.785 236.295 1.00 32.73  ? 2463 HIS A CA    1 
ATOM   7222  C  C     . HIS A 1 2463 ? 232.078 177.863 235.091 1.00 33.50  ? 2463 HIS A C     1 
ATOM   7223  O  O     . HIS A 1 2463 ? 231.581 176.736 235.219 1.00 40.60  ? 2463 HIS A O     1 
ATOM   7224  C  CB    . HIS A 1 2463 ? 231.049 179.773 236.328 1.00 31.64  ? 2463 HIS A CB    1 
ATOM   7225  C  CG    . HIS A 1 2463 ? 230.971 180.575 237.588 1.00 39.11  ? 2463 HIS A CG    1 
ATOM   7226  N  ND1   . HIS A 1 2463 ? 230.189 181.703 237.703 1.00 35.55  ? 2463 HIS A ND1   1 
ATOM   7227  C  CD2   . HIS A 1 2463 ? 231.578 180.414 238.787 1.00 40.28  ? 2463 HIS A CD2   1 
ATOM   7228  C  CE1   . HIS A 1 2463 ? 230.316 182.202 238.919 1.00 37.06  ? 2463 HIS A CE1   1 
ATOM   7229  N  NE2   . HIS A 1 2463 ? 231.154 181.439 239.596 1.00 39.33  ? 2463 HIS A NE2   1 
ATOM   7230  N  N     . GLN A 1 2464 ? 232.513 178.324 233.918 1.00 40.07  ? 2464 GLN A N     1 
ATOM   7231  C  CA    . GLN A 1 2464 ? 232.509 177.455 232.746 1.00 35.40  ? 2464 GLN A CA    1 
ATOM   7232  C  C     . GLN A 1 2464 ? 233.453 176.273 232.921 1.00 32.47  ? 2464 GLN A C     1 
ATOM   7233  O  O     . GLN A 1 2464 ? 233.170 175.183 232.422 1.00 43.43  ? 2464 GLN A O     1 
ATOM   7234  C  CB    . GLN A 1 2464 ? 232.873 178.248 231.495 1.00 34.55  ? 2464 GLN A CB    1 
ATOM   7235  C  CG    . GLN A 1 2464 ? 232.615 177.497 230.201 1.00 43.04  ? 2464 GLN A CG    1 
ATOM   7236  C  CD    . GLN A 1 2464 ? 231.166 177.085 230.046 1.00 49.00  ? 2464 GLN A CD    1 
ATOM   7237  O  OE1   . GLN A 1 2464 ? 230.255 177.870 230.299 1.00 44.76  ? 2464 GLN A OE1   1 
ATOM   7238  N  NE2   . GLN A 1 2464 ? 230.946 175.847 229.622 1.00 38.11  ? 2464 GLN A NE2   1 
ATOM   7239  N  N     . ALA A 1 2465 ? 234.577 176.468 233.611 1.00 36.52  ? 2465 ALA A N     1 
ATOM   7240  C  CA    . ALA A 1 2465 ? 235.463 175.343 233.909 1.00 32.86  ? 2465 ALA A CA    1 
ATOM   7241  C  C     . ALA A 1 2465 ? 234.770 174.310 234.792 1.00 32.85  ? 2465 ALA A C     1 
ATOM   7242  O  O     . ALA A 1 2465 ? 234.901 173.097 234.573 1.00 42.91  ? 2465 ALA A O     1 
ATOM   7243  C  CB    . ALA A 1 2465 ? 236.740 175.840 234.581 1.00 23.71  ? 2465 ALA A CB    1 
ATOM   7244  N  N     . CYS A 1 2466 ? 234.039 174.774 235.805 1.00 44.35  ? 2466 CYS A N     1 
ATOM   7245  C  CA    . CYS A 1 2466 ? 233.278 173.850 236.643 1.00 39.08  ? 2466 CYS A CA    1 
ATOM   7246  C  C     . CYS A 1 2466 ? 232.230 173.102 235.825 1.00 46.42  ? 2466 CYS A C     1 
ATOM   7247  O  O     . CYS A 1 2466 ? 232.032 171.893 236.007 1.00 51.69  ? 2466 CYS A O     1 
ATOM   7248  C  CB    . CYS A 1 2466 ? 232.624 174.602 237.801 1.00 32.72  ? 2466 CYS A CB    1 
ATOM   7249  S  SG    . CYS A 1 2466 ? 233.785 175.182 239.055 1.00 43.24  ? 2466 CYS A SG    1 
ATOM   7250  N  N     . ARG A 1 2467 ? 231.552 173.804 234.915 1.00 47.23  ? 2467 ARG A N     1 
ATOM   7251  C  CA    . ARG A 1 2467 ? 230.587 173.138 234.044 1.00 39.46  ? 2467 ARG A CA    1 
ATOM   7252  C  C     . ARG A 1 2467 ? 231.262 172.129 233.122 1.00 41.53  ? 2467 ARG A C     1 
ATOM   7253  O  O     . ARG A 1 2467 ? 230.678 171.086 232.815 1.00 50.71  ? 2467 ARG A O     1 
ATOM   7254  C  CB    . ARG A 1 2467 ? 229.815 174.169 233.225 1.00 39.33  ? 2467 ARG A CB    1 
ATOM   7255  C  CG    . ARG A 1 2467 ? 228.829 174.980 234.036 1.00 41.56  ? 2467 ARG A CG    1 
ATOM   7256  C  CD    . ARG A 1 2467 ? 228.038 175.920 233.151 1.00 43.12  ? 2467 ARG A CD    1 
ATOM   7257  N  NE    . ARG A 1 2467 ? 227.432 177.005 233.912 1.00 44.73  ? 2467 ARG A NE    1 
ATOM   7258  C  CZ    . ARG A 1 2467 ? 226.300 176.900 234.593 1.00 52.13  ? 2467 ARG A CZ    1 
ATOM   7259  N  NH1   . ARG A 1 2467 ? 225.621 175.766 234.634 1.00 46.21  ? 2467 ARG A NH1   1 
ATOM   7260  N  NH2   . ARG A 1 2467 ? 225.838 177.959 235.250 1.00 48.47  ? 2467 ARG A NH2   1 
ATOM   7261  N  N     . ASN A 1 2468 ? 232.480 172.426 232.664 1.00 41.30  ? 2468 ASN A N     1 
ATOM   7262  C  CA    . ASN A 1 2468 ? 233.226 171.470 231.853 1.00 36.73  ? 2468 ASN A CA    1 
ATOM   7263  C  C     . ASN A 1 2468 ? 233.540 170.209 232.643 1.00 47.69  ? 2468 ASN A C     1 
ATOM   7264  O  O     . ASN A 1 2468 ? 233.442 169.095 232.116 1.00 56.61  ? 2468 ASN A O     1 
ATOM   7265  C  CB    . ASN A 1 2468 ? 234.517 172.109 231.343 1.00 35.65  ? 2468 ASN A CB    1 
ATOM   7266  C  CG    . ASN A 1 2468 ? 234.267 173.198 230.327 1.00 45.77  ? 2468 ASN A CG    1 
ATOM   7267  O  OD1   . ASN A 1 2468 ? 233.131 173.437 229.923 1.00 49.51  ? 2468 ASN A OD1   1 
ATOM   7268  N  ND2   . ASN A 1 2468 ? 235.332 173.869 229.909 1.00 51.18  ? 2468 ASN A ND2   1 
ATOM   7269  N  N     . VAL A 1 2469 ? 233.934 170.366 233.908 1.00 45.25  ? 2469 VAL A N     1 
ATOM   7270  C  CA    . VAL A 1 2469 ? 234.186 169.197 234.748 1.00 43.88  ? 2469 VAL A CA    1 
ATOM   7271  C  C     . VAL A 1 2469 ? 232.905 168.394 234.945 1.00 44.58  ? 2469 VAL A C     1 
ATOM   7272  O  O     . VAL A 1 2469 ? 232.921 167.156 234.928 1.00 45.14  ? 2469 VAL A O     1 
ATOM   7273  C  CB    . VAL A 1 2469 ? 234.802 169.622 236.092 1.00 49.27  ? 2469 VAL A CB    1 
ATOM   7274  C  CG1   . VAL A 1 2469 ? 234.955 168.419 237.006 1.00 43.88  ? 2469 VAL A CG1   1 
ATOM   7275  C  CG2   . VAL A 1 2469 ? 236.145 170.289 235.862 1.00 45.33  ? 2469 VAL A CG2   1 
ATOM   7276  N  N     . ALA A 1 2470 ? 231.778 169.081 235.142 1.00 51.46  ? 2470 ALA A N     1 
ATOM   7277  C  CA    . ALA A 1 2470 ? 230.505 168.380 235.285 1.00 44.26  ? 2470 ALA A CA    1 
ATOM   7278  C  C     . ALA A 1 2470 ? 230.152 167.609 234.019 1.00 47.28  ? 2470 ALA A C     1 
ATOM   7279  O  O     . ALA A 1 2470 ? 229.665 166.474 234.086 1.00 54.60  ? 2470 ALA A O     1 
ATOM   7280  C  CB    . ALA A 1 2470 ? 229.395 169.368 235.638 1.00 47.03  ? 2470 ALA A CB    1 
ATOM   7281  N  N     . GLN A 1 2471 ? 230.388 168.213 232.853 1.00 56.31  ? 2471 GLN A N     1 
ATOM   7282  C  CA    . GLN A 1 2471 ? 230.131 167.525 231.592 1.00 51.88  ? 2471 GLN A CA    1 
ATOM   7283  C  C     . GLN A 1 2471 ? 231.036 166.310 231.433 1.00 52.68  ? 2471 GLN A C     1 
ATOM   7284  O  O     . GLN A 1 2471 ? 230.598 165.261 230.949 1.00 59.50  ? 2471 GLN A O     1 
ATOM   7285  C  CB    . GLN A 1 2471 ? 230.315 168.489 230.422 1.00 49.03  ? 2471 GLN A CB    1 
ATOM   7286  C  CG    . GLN A 1 2471 ? 230.299 167.821 229.061 1.00 52.53  ? 2471 GLN A CG    1 
ATOM   7287  C  CD    . GLN A 1 2471 ? 230.309 168.821 227.925 1.00 64.40  ? 2471 GLN A CD    1 
ATOM   7288  O  OE1   . GLN A 1 2471 ? 230.313 170.030 228.150 1.00 66.33  ? 2471 GLN A OE1   1 
ATOM   7289  N  NE2   . GLN A 1 2471 ? 230.313 168.320 226.696 1.00 59.82  ? 2471 GLN A NE2   1 
ATOM   7290  N  N     . TYR A 1 2472 ? 232.305 166.435 231.826 1.00 57.33  ? 2472 TYR A N     1 
ATOM   7291  C  CA    . TYR A 1 2472 ? 233.209 165.290 231.782 1.00 56.63  ? 2472 TYR A CA    1 
ATOM   7292  C  C     . TYR A 1 2472 ? 232.711 164.163 232.676 1.00 62.27  ? 2472 TYR A C     1 
ATOM   7293  O  O     . TYR A 1 2472 ? 232.755 162.990 232.290 1.00 68.20  ? 2472 TYR A O     1 
ATOM   7294  C  CB    . TYR A 1 2472 ? 234.619 165.716 232.192 1.00 58.26  ? 2472 TYR A CB    1 
ATOM   7295  C  CG    . TYR A 1 2472 ? 235.642 164.596 232.218 1.00 59.88  ? 2472 TYR A CG    1 
ATOM   7296  C  CD1   . TYR A 1 2472 ? 235.765 163.762 233.322 1.00 61.31  ? 2472 TYR A CD1   1 
ATOM   7297  C  CD2   . TYR A 1 2472 ? 236.487 164.379 231.142 1.00 61.07  ? 2472 TYR A CD2   1 
ATOM   7298  C  CE1   . TYR A 1 2472 ? 236.696 162.745 233.349 1.00 63.36  ? 2472 TYR A CE1   1 
ATOM   7299  C  CE2   . TYR A 1 2472 ? 237.423 163.365 231.161 1.00 61.43  ? 2472 TYR A CE2   1 
ATOM   7300  C  CZ    . TYR A 1 2472 ? 237.523 162.552 232.266 1.00 62.38  ? 2472 TYR A CZ    1 
ATOM   7301  O  OH    . TYR A 1 2472 ? 238.453 161.539 232.288 1.00 61.76  ? 2472 TYR A OH    1 
ATOM   7302  N  N     . ASN A 1 2473 ? 232.244 164.499 233.880 1.00 64.90  ? 2473 ASN A N     1 
ATOM   7303  C  CA    . ASN A 1 2473 ? 231.701 163.475 234.768 1.00 57.59  ? 2473 ASN A CA    1 
ATOM   7304  C  C     . ASN A 1 2473 ? 230.468 162.818 234.161 1.00 54.11  ? 2473 ASN A C     1 
ATOM   7305  O  O     . ASN A 1 2473 ? 230.286 161.601 234.271 1.00 55.73  ? 2473 ASN A O     1 
ATOM   7306  C  CB    . ASN A 1 2473 ? 231.373 164.075 236.133 1.00 58.62  ? 2473 ASN A CB    1 
ATOM   7307  C  CG    . ASN A 1 2473 ? 232.593 164.210 237.015 1.00 66.55  ? 2473 ASN A CG    1 
ATOM   7308  O  OD1   . ASN A 1 2473 ? 233.726 164.185 236.536 1.00 64.44  ? 2473 ASN A OD1   1 
ATOM   7309  N  ND2   . ASN A 1 2473 ? 232.370 164.346 238.316 1.00 67.06  ? 2473 ASN A ND2   1 
ATOM   7310  N  N     . ALA A 1 2474 ? 229.606 163.610 233.521 1.00 62.08  ? 2474 ALA A N     1 
ATOM   7311  C  CA    . ALA A 1 2474 ? 228.417 163.046 232.889 1.00 66.22  ? 2474 ALA A CA    1 
ATOM   7312  C  C     . ALA A 1 2474 ? 228.772 162.157 231.704 1.00 66.50  ? 2474 ALA A C     1 
ATOM   7313  O  O     . ALA A 1 2474 ? 228.059 161.187 231.424 1.00 64.97  ? 2474 ALA A O     1 
ATOM   7314  C  CB    . ALA A 1 2474 ? 227.472 164.164 232.450 1.00 63.11  ? 2474 ALA A CB    1 
ATOM   7315  N  N     . ASN A 1 2475 ? 229.857 162.471 230.994 1.00 68.31  ? 2475 ASN A N     1 
ATOM   7316  C  CA    . ASN A 1 2475 ? 230.274 161.667 229.852 1.00 69.42  ? 2475 ASN A CA    1 
ATOM   7317  C  C     . ASN A 1 2475 ? 231.091 160.447 230.254 1.00 67.46  ? 2475 ASN A C     1 
ATOM   7318  O  O     . ASN A 1 2475 ? 231.305 159.562 229.420 1.00 68.61  ? 2475 ASN A O     1 
ATOM   7319  C  CB    . ASN A 1 2475 ? 231.083 162.519 228.872 1.00 65.44  ? 2475 ASN A CB    1 
ATOM   7320  C  CG    . ASN A 1 2475 ? 230.206 163.390 227.998 1.00 69.79  ? 2475 ASN A CG    1 
ATOM   7321  O  OD1   . ASN A 1 2475 ? 228.985 163.241 227.980 1.00 70.30  ? 2475 ASN A OD1   1 
ATOM   7322  N  ND2   . ASN A 1 2475 ? 230.826 164.307 227.264 1.00 69.09  ? 2475 ASN A ND2   1 
ATOM   7323  N  N     . HIS A 1 2476 ? 231.553 160.380 231.499 1.00 70.58  ? 2476 HIS A N     1 
ATOM   7324  C  CA    . HIS A 1 2476 ? 232.302 159.233 232.012 1.00 68.00  ? 2476 HIS A CA    1 
ATOM   7325  C  C     . HIS A 1 2476 ? 231.677 158.782 233.326 1.00 75.63  ? 2476 HIS A C     1 
ATOM   7326  O  O     . HIS A 1 2476 ? 232.275 158.934 234.397 1.00 76.24  ? 2476 HIS A O     1 
ATOM   7327  C  CB    . HIS A 1 2476 ? 233.779 159.577 232.207 1.00 67.73  ? 2476 HIS A CB    1 
ATOM   7328  C  CG    . HIS A 1 2476 ? 234.512 159.870 230.935 1.00 74.03  ? 2476 HIS A CG    1 
ATOM   7329  N  ND1   . HIS A 1 2476 ? 234.135 160.876 230.071 1.00 74.92  ? 2476 HIS A ND1   1 
ATOM   7330  C  CD2   . HIS A 1 2476 ? 235.606 159.294 230.385 1.00 73.32  ? 2476 HIS A CD2   1 
ATOM   7331  C  CE1   . HIS A 1 2476 ? 234.963 160.904 229.043 1.00 70.76  ? 2476 HIS A CE1   1 
ATOM   7332  N  NE2   . HIS A 1 2476 ? 235.865 159.954 229.209 1.00 70.47  ? 2476 HIS A NE2   1 
ATOM   7333  N  N     . PRO A 1 2477 ? 230.462 158.224 233.280 1.00 76.63  ? 2477 PRO A N     1 
ATOM   7334  C  CA    . PRO A 1 2477 ? 229.822 157.776 234.528 1.00 75.40  ? 2477 PRO A CA    1 
ATOM   7335  C  C     . PRO A 1 2477 ? 230.611 156.704 235.255 1.00 82.37  ? 2477 PRO A C     1 
ATOM   7336  O  O     . PRO A 1 2477 ? 230.594 156.662 236.492 1.00 78.55  ? 2477 PRO A O     1 
ATOM   7337  C  CB    . PRO A 1 2477 ? 228.458 157.251 234.057 1.00 73.40  ? 2477 PRO A CB    1 
ATOM   7338  C  CG    . PRO A 1 2477 ? 228.273 157.800 232.678 1.00 74.77  ? 2477 PRO A CG    1 
ATOM   7339  C  CD    . PRO A 1 2477 ? 229.642 157.909 232.100 1.00 73.38  ? 2477 PRO A CD    1 
ATOM   7340  N  N     . ASP A 1 2478 ? 231.299 155.828 234.520 1.00 90.70  ? 2478 ASP A N     1 
ATOM   7341  C  CA    . ASP A 1 2478 ? 232.115 154.800 235.159 1.00 89.10  ? 2478 ASP A CA    1 
ATOM   7342  C  C     . ASP A 1 2478 ? 233.321 155.408 235.863 1.00 87.02  ? 2478 ASP A C     1 
ATOM   7343  O  O     . ASP A 1 2478 ? 233.677 154.988 236.970 1.00 83.37  ? 2478 ASP A O     1 
ATOM   7344  C  CB    . ASP A 1 2478 ? 232.564 153.772 234.120 1.00 89.63  ? 2478 ASP A CB    1 
ATOM   7345  C  CG    . ASP A 1 2478 ? 233.172 152.532 234.749 1.00 92.91  ? 2478 ASP A CG    1 
ATOM   7346  O  OD1   . ASP A 1 2478 ? 233.053 152.363 235.981 1.00 91.92  ? 2478 ASP A OD1   1 
ATOM   7347  O  OD2   . ASP A 1 2478 ? 233.773 151.725 234.008 1.00 89.67  ? 2478 ASP A OD2   1 
ATOM   7348  N  N     . PHE A 1 2479 ? 233.957 156.399 235.243 1.00 85.12  ? 2479 PHE A N     1 
ATOM   7349  C  CA    . PHE A 1 2479 ? 235.209 156.972 235.735 1.00 85.73  ? 2479 PHE A CA    1 
ATOM   7350  C  C     . PHE A 1 2479 ? 235.063 158.483 235.851 1.00 88.52  ? 2479 PHE A C     1 
ATOM   7351  O  O     . PHE A 1 2479 ? 235.493 159.230 234.961 1.00 87.61  ? 2479 PHE A O     1 
ATOM   7352  C  CB    . PHE A 1 2479 ? 236.376 156.609 234.817 1.00 85.50  ? 2479 PHE A CB    1 
ATOM   7353  C  CG    . PHE A 1 2479 ? 236.770 155.163 234.879 1.00 89.23  ? 2479 PHE A CG    1 
ATOM   7354  C  CD1   . PHE A 1 2479 ? 237.368 154.642 236.013 1.00 87.68  ? 2479 PHE A CD1   1 
ATOM   7355  C  CD2   . PHE A 1 2479 ? 236.544 154.324 233.801 1.00 90.78  ? 2479 PHE A CD2   1 
ATOM   7356  C  CE1   . PHE A 1 2479 ? 237.733 153.311 236.071 1.00 89.05  ? 2479 PHE A CE1   1 
ATOM   7357  C  CE2   . PHE A 1 2479 ? 236.905 152.993 233.853 1.00 87.51  ? 2479 PHE A CE2   1 
ATOM   7358  C  CZ    . PHE A 1 2479 ? 237.501 152.486 234.989 1.00 88.85  ? 2479 PHE A CZ    1 
ATOM   7359  N  N     . PRO A 1 2480 ? 234.464 158.969 236.935 1.00 82.16  ? 2480 PRO A N     1 
ATOM   7360  C  CA    . PRO A 1 2480 ? 234.406 160.417 237.151 1.00 79.49  ? 2480 PRO A CA    1 
ATOM   7361  C  C     . PRO A 1 2480 ? 235.795 160.989 237.375 1.00 79.21  ? 2480 PRO A C     1 
ATOM   7362  O  O     . PRO A 1 2480 ? 236.726 160.286 237.776 1.00 80.67  ? 2480 PRO A O     1 
ATOM   7363  C  CB    . PRO A 1 2480 ? 233.535 160.557 238.404 1.00 75.81  ? 2480 PRO A CB    1 
ATOM   7364  C  CG    . PRO A 1 2480 ? 233.666 159.251 239.102 1.00 74.98  ? 2480 PRO A CG    1 
ATOM   7365  C  CD    . PRO A 1 2480 ? 233.823 158.218 238.026 1.00 80.55  ? 2480 PRO A CD    1 
ATOM   7366  N  N     . MET A 1 2481 ? 235.931 162.282 237.092 1.00 67.51  ? 2481 MET A N     1 
ATOM   7367  C  CA    . MET A 1 2481 ? 237.225 162.942 237.212 1.00 68.49  ? 2481 MET A CA    1 
ATOM   7368  C  C     . MET A 1 2481 ? 237.720 162.903 238.651 1.00 69.56  ? 2481 MET A C     1 
ATOM   7369  O  O     . MET A 1 2481 ? 236.992 163.254 239.584 1.00 71.82  ? 2481 MET A O     1 
ATOM   7370  C  CB    . MET A 1 2481 ? 237.124 164.385 236.719 1.00 66.17  ? 2481 MET A CB    1 
ATOM   7371  C  CG    . MET A 1 2481 ? 238.418 164.929 236.156 1.00 66.24  ? 2481 MET A CG    1 
ATOM   7372  S  SD    . MET A 1 2481 ? 238.411 166.716 235.970 1.00 69.29  ? 2481 MET A SD    1 
ATOM   7373  C  CE    . MET A 1 2481 ? 237.246 166.899 234.628 1.00 67.29  ? 2481 MET A CE    1 
ATOM   7374  N  N     . GLN A 1 2482 ? 238.967 162.474 238.827 1.00 69.86  ? 2482 GLN A N     1 
ATOM   7375  C  CA    . GLN A 1 2482 ? 239.552 162.353 240.152 1.00 73.94  ? 2482 GLN A CA    1 
ATOM   7376  C  C     . GLN A 1 2482 ? 240.155 163.686 240.587 1.00 72.04  ? 2482 GLN A C     1 
ATOM   7377  O  O     . GLN A 1 2482 ? 240.152 164.674 239.850 1.00 76.25  ? 2482 GLN A O     1 
ATOM   7378  C  CB    . GLN A 1 2482 ? 240.593 161.237 240.172 1.00 75.83  ? 2482 GLN A CB    1 
ATOM   7379  C  CG    . GLN A 1 2482 ? 240.039 159.867 239.812 1.00 74.37  ? 2482 GLN A CG    1 
ATOM   7380  C  CD    . GLN A 1 2482 ? 238.968 159.390 240.775 1.00 73.58  ? 2482 GLN A CD    1 
ATOM   7381  O  OE1   . GLN A 1 2482 ? 238.931 159.795 241.936 1.00 73.00  ? 2482 GLN A OE1   1 
ATOM   7382  N  NE2   . GLN A 1 2482 ? 238.087 158.522 240.294 1.00 72.49  ? 2482 GLN A NE2   1 
ATOM   7383  N  N     . ILE A 1 2483 ? 240.684 163.710 241.812 1.00 68.94  ? 2483 ILE A N     1 
ATOM   7384  C  CA    . ILE A 1 2483 ? 241.168 164.959 242.390 1.00 65.62  ? 2483 ILE A CA    1 
ATOM   7385  C  C     . ILE A 1 2483 ? 242.405 165.461 241.653 1.00 69.91  ? 2483 ILE A C     1 
ATOM   7386  O  O     . ILE A 1 2483 ? 242.595 166.670 241.494 1.00 75.74  ? 2483 ILE A O     1 
ATOM   7387  C  CB    . ILE A 1 2483 ? 241.427 164.784 243.898 1.00 71.79  ? 2483 ILE A CB    1 
ATOM   7388  C  CG1   . ILE A 1 2483 ? 241.925 166.094 244.512 1.00 71.67  ? 2483 ILE A CG1   1 
ATOM   7389  C  CG2   . ILE A 1 2483 ? 242.404 163.645 244.157 1.00 73.60  ? 2483 ILE A CG2   1 
ATOM   7390  C  CD1   . ILE A 1 2483 ? 240.973 167.253 244.318 1.00 72.15  ? 2483 ILE A CD1   1 
ATOM   7391  N  N     . GLU A 1 2484 ? 243.267 164.551 241.192 1.00 65.88  ? 2484 GLU A N     1 
ATOM   7392  C  CA    . GLU A 1 2484 ? 244.497 164.972 240.523 1.00 66.06  ? 2484 GLU A CA    1 
ATOM   7393  C  C     . GLU A 1 2484 ? 244.209 165.576 239.153 1.00 70.35  ? 2484 GLU A C     1 
ATOM   7394  O  O     . GLU A 1 2484 ? 244.747 166.635 238.801 1.00 70.04  ? 2484 GLU A O     1 
ATOM   7395  C  CB    . GLU A 1 2484 ? 245.456 163.789 240.400 1.00 68.43  ? 2484 GLU A CB    1 
ATOM   7396  C  CG    . GLU A 1 2484 ? 246.785 164.141 239.750 1.00 71.89  ? 2484 GLU A CG    1 
ATOM   7397  C  CD    . GLU A 1 2484 ? 247.605 165.111 240.578 1.00 77.21  ? 2484 GLU A CD    1 
ATOM   7398  O  OE1   . GLU A 1 2484 ? 247.424 165.144 241.813 1.00 78.07  ? 2484 GLU A OE1   1 
ATOM   7399  O  OE2   . GLU A 1 2484 ? 248.428 165.843 239.991 1.00 74.71  ? 2484 GLU A OE2   1 
ATOM   7400  N  N     . GLN A 1 2485 ? 243.371 164.905 238.358 1.00 62.90  ? 2485 GLN A N     1 
ATOM   7401  C  CA    . GLN A 1 2485 ? 243.000 165.444 237.055 1.00 58.46  ? 2485 GLN A CA    1 
ATOM   7402  C  C     . GLN A 1 2485 ? 242.254 166.761 237.205 1.00 58.46  ? 2485 GLN A C     1 
ATOM   7403  O  O     . GLN A 1 2485 ? 242.494 167.712 236.451 1.00 66.35  ? 2485 GLN A O     1 
ATOM   7404  C  CB    . GLN A 1 2485 ? 242.151 164.428 236.292 1.00 56.11  ? 2485 GLN A CB    1 
ATOM   7405  C  CG    . GLN A 1 2485 ? 242.011 164.725 234.813 1.00 56.38  ? 2485 GLN A CG    1 
ATOM   7406  C  CD    . GLN A 1 2485 ? 240.966 163.862 234.142 1.00 59.78  ? 2485 GLN A CD    1 
ATOM   7407  O  OE1   . GLN A 1 2485 ? 240.909 162.654 234.362 1.00 60.73  ? 2485 GLN A OE1   1 
ATOM   7408  N  NE2   . GLN A 1 2485 ? 240.132 164.479 233.317 1.00 58.84  ? 2485 GLN A NE2   1 
ATOM   7409  N  N     . LEU A 1 2486 ? 241.352 166.835 238.185 1.00 49.16  ? 2486 LEU A N     1 
ATOM   7410  C  CA    . LEU A 1 2486 ? 240.629 168.074 238.441 1.00 49.85  ? 2486 LEU A CA    1 
ATOM   7411  C  C     . LEU A 1 2486 ? 241.580 169.191 238.842 1.00 51.94  ? 2486 LEU A C     1 
ATOM   7412  O  O     . LEU A 1 2486 ? 241.427 170.332 238.396 1.00 63.63  ? 2486 LEU A O     1 
ATOM   7413  C  CB    . LEU A 1 2486 ? 239.577 167.845 239.523 1.00 50.21  ? 2486 LEU A CB    1 
ATOM   7414  C  CG    . LEU A 1 2486 ? 238.783 169.055 240.007 1.00 48.10  ? 2486 LEU A CG    1 
ATOM   7415  C  CD1   . LEU A 1 2486 ? 238.116 169.747 238.842 1.00 55.45  ? 2486 LEU A CD1   1 
ATOM   7416  C  CD2   . LEU A 1 2486 ? 237.752 168.620 241.023 1.00 52.03  ? 2486 LEU A CD2   1 
ATOM   7417  N  N     . GLU A 1 2487 ? 242.575 168.880 239.673 1.00 48.76  ? 2487 GLU A N     1 
ATOM   7418  C  CA    . GLU A 1 2487 ? 243.546 169.884 240.094 1.00 48.30  ? 2487 GLU A CA    1 
ATOM   7419  C  C     . GLU A 1 2487 ? 244.344 170.411 238.909 1.00 50.70  ? 2487 GLU A C     1 
ATOM   7420  O  O     . GLU A 1 2487 ? 244.496 171.628 238.742 1.00 56.99  ? 2487 GLU A O     1 
ATOM   7421  C  CB    . GLU A 1 2487 ? 244.478 169.287 241.146 1.00 50.75  ? 2487 GLU A CB    1 
ATOM   7422  C  CG    . GLU A 1 2487 ? 245.699 170.128 241.448 1.00 57.30  ? 2487 GLU A CG    1 
ATOM   7423  C  CD    . GLU A 1 2487 ? 246.348 169.747 242.760 1.00 63.29  ? 2487 GLU A CD    1 
ATOM   7424  O  OE1   . GLU A 1 2487 ? 245.707 169.022 243.550 1.00 63.67  ? 2487 GLU A OE1   1 
ATOM   7425  O  OE2   . GLU A 1 2487 ? 247.498 170.171 243.003 1.00 58.60  ? 2487 GLU A OE2   1 
ATOM   7426  N  N     . ARG A 1 2488 ? 244.869 169.505 238.078 1.00 48.31  ? 2488 ARG A N     1 
ATOM   7427  C  CA    . ARG A 1 2488 ? 245.646 169.938 236.920 1.00 45.26  ? 2488 ARG A CA    1 
ATOM   7428  C  C     . ARG A 1 2488 ? 244.800 170.784 235.978 1.00 50.39  ? 2488 ARG A C     1 
ATOM   7429  O  O     . ARG A 1 2488 ? 245.230 171.862 235.533 1.00 56.20  ? 2488 ARG A O     1 
ATOM   7430  C  CB    . ARG A 1 2488 ? 246.209 168.725 236.181 1.00 49.15  ? 2488 ARG A CB    1 
ATOM   7431  C  CG    . ARG A 1 2488 ? 247.273 167.960 236.944 1.00 55.88  ? 2488 ARG A CG    1 
ATOM   7432  C  CD    . ARG A 1 2488 ? 247.885 166.869 236.081 1.00 51.50  ? 2488 ARG A CD    1 
ATOM   7433  N  NE    . ARG A 1 2488 ? 246.938 166.359 235.097 1.00 55.10  ? 2488 ARG A NE    1 
ATOM   7434  C  CZ    . ARG A 1 2488 ? 246.408 165.144 235.125 1.00 57.78  ? 2488 ARG A CZ    1 
ATOM   7435  N  NH1   . ARG A 1 2488 ? 246.706 164.281 236.082 1.00 58.51  ? 2488 ARG A NH1   1 
ATOM   7436  N  NH2   . ARG A 1 2488 ? 245.555 164.786 234.169 1.00 52.48  ? 2488 ARG A NH2   1 
ATOM   7437  N  N     . TYR A 1 2489 ? 243.584 170.319 235.677 1.00 39.86  ? 2489 TYR A N     1 
ATOM   7438  C  CA    . TYR A 1 2489 ? 242.707 171.062 234.785 1.00 33.07  ? 2489 TYR A CA    1 
ATOM   7439  C  C     . TYR A 1 2489 ? 242.381 172.435 235.348 1.00 41.35  ? 2489 TYR A C     1 
ATOM   7440  O  O     . TYR A 1 2489 ? 242.408 173.427 234.617 1.00 50.89  ? 2489 TYR A O     1 
ATOM   7441  C  CB    . TYR A 1 2489 ? 241.422 170.275 234.532 1.00 38.99  ? 2489 TYR A CB    1 
ATOM   7442  C  CG    . TYR A 1 2489 ? 240.408 171.026 233.702 1.00 44.84  ? 2489 TYR A CG    1 
ATOM   7443  C  CD1   . TYR A 1 2489 ? 240.648 171.306 232.365 1.00 42.45  ? 2489 TYR A CD1   1 
ATOM   7444  C  CD2   . TYR A 1 2489 ? 239.216 171.463 234.258 1.00 41.45  ? 2489 TYR A CD2   1 
ATOM   7445  C  CE1   . TYR A 1 2489 ? 239.726 171.996 231.605 1.00 39.96  ? 2489 TYR A CE1   1 
ATOM   7446  C  CE2   . TYR A 1 2489 ? 238.290 172.153 233.505 1.00 39.39  ? 2489 TYR A CE2   1 
ATOM   7447  C  CZ    . TYR A 1 2489 ? 238.549 172.416 232.180 1.00 43.87  ? 2489 TYR A CZ    1 
ATOM   7448  O  OH    . TYR A 1 2489 ? 237.627 173.103 231.427 1.00 45.15  ? 2489 TYR A OH    1 
ATOM   7449  N  N     . ILE A 1 2490 ? 242.087 172.517 236.646 1.00 43.33  ? 2490 ILE A N     1 
ATOM   7450  C  CA    . ILE A 1 2490 ? 241.672 173.785 237.231 1.00 38.88  ? 2490 ILE A CA    1 
ATOM   7451  C  C     . ILE A 1 2490 ? 242.833 174.769 237.268 1.00 37.53  ? 2490 ILE A C     1 
ATOM   7452  O  O     . ILE A 1 2490 ? 242.653 175.959 236.998 1.00 49.92  ? 2490 ILE A O     1 
ATOM   7453  C  CB    . ILE A 1 2490 ? 241.066 173.554 238.626 1.00 40.87  ? 2490 ILE A CB    1 
ATOM   7454  C  CG1   . ILE A 1 2490 ? 239.654 172.986 238.499 1.00 36.01  ? 2490 ILE A CG1   1 
ATOM   7455  C  CG2   . ILE A 1 2490 ? 241.018 174.843 239.404 1.00 45.09  ? 2490 ILE A CG2   1 
ATOM   7456  C  CD1   . ILE A 1 2490 ? 238.690 173.906 237.794 1.00 39.37  ? 2490 ILE A CD1   1 
ATOM   7457  N  N     . GLN A 1 2491 ? 244.042 174.300 237.582 1.00 34.93  ? 2491 GLN A N     1 
ATOM   7458  C  CA    . GLN A 1 2491 ? 245.188 175.208 237.591 1.00 37.04  ? 2491 GLN A CA    1 
ATOM   7459  C  C     . GLN A 1 2491 ? 245.485 175.743 236.193 1.00 48.04  ? 2491 GLN A C     1 
ATOM   7460  O  O     . GLN A 1 2491 ? 245.648 176.961 235.998 1.00 53.33  ? 2491 GLN A O     1 
ATOM   7461  C  CB    . GLN A 1 2491 ? 246.413 174.499 238.163 1.00 37.06  ? 2491 GLN A CB    1 
ATOM   7462  C  CG    . GLN A 1 2491 ? 246.284 174.133 239.626 1.00 44.33  ? 2491 GLN A CG    1 
ATOM   7463  C  CD    . GLN A 1 2491 ? 247.506 173.415 240.154 1.00 48.60  ? 2491 GLN A CD    1 
ATOM   7464  O  OE1   . GLN A 1 2491 ? 248.501 173.256 239.448 1.00 46.29  ? 2491 GLN A OE1   1 
ATOM   7465  N  NE2   . GLN A 1 2491 ? 247.437 172.973 241.403 1.00 48.46  ? 2491 GLN A NE2   1 
ATOM   7466  N  N     . ARG A 1 2492 ? 245.554 174.850 235.201 1.00 44.02  ? 2492 ARG A N     1 
ATOM   7467  C  CA    . ARG A 1 2492 ? 245.837 175.307 233.846 1.00 34.72  ? 2492 ARG A CA    1 
ATOM   7468  C  C     . ARG A 1 2492 ? 244.728 176.215 233.328 1.00 34.52  ? 2492 ARG A C     1 
ATOM   7469  O  O     . ARG A 1 2492 ? 245.002 177.223 232.663 1.00 49.22  ? 2492 ARG A O     1 
ATOM   7470  C  CB    . ARG A 1 2492 ? 246.044 174.109 232.925 1.00 41.33  ? 2492 ARG A CB    1 
ATOM   7471  C  CG    . ARG A 1 2492 ? 247.374 173.415 233.133 1.00 38.07  ? 2492 ARG A CG    1 
ATOM   7472  C  CD    . ARG A 1 2492 ? 247.335 171.989 232.628 1.00 46.37  ? 2492 ARG A CD    1 
ATOM   7473  N  NE    . ARG A 1 2492 ? 248.617 171.314 232.785 1.00 49.04  ? 2492 ARG A NE    1 
ATOM   7474  C  CZ    . ARG A 1 2492 ? 249.095 170.869 233.939 1.00 48.60  ? 2492 ARG A CZ    1 
ATOM   7475  N  NH1   . ARG A 1 2492 ? 248.431 171.034 235.072 1.00 44.77  ? 2492 ARG A NH1   1 
ATOM   7476  N  NH2   . ARG A 1 2492 ? 250.266 170.241 233.957 1.00 48.93  ? 2492 ARG A NH2   1 
ATOM   7477  N  N     . TYR A 1 2493 ? 243.472 175.891 233.637 1.00 28.83  ? 2493 TYR A N     1 
ATOM   7478  C  CA    . TYR A 1 2493 ? 242.369 176.730 233.197 1.00 32.07  ? 2493 TYR A CA    1 
ATOM   7479  C  C     . TYR A 1 2493 ? 242.364 178.067 233.916 1.00 32.18  ? 2493 TYR A C     1 
ATOM   7480  O  O     . TYR A 1 2493 ? 241.920 179.062 233.348 1.00 46.84  ? 2493 TYR A O     1 
ATOM   7481  C  CB    . TYR A 1 2493 ? 241.037 176.015 233.406 1.00 26.79  ? 2493 TYR A CB    1 
ATOM   7482  C  CG    . TYR A 1 2493 ? 239.917 176.604 232.585 1.00 30.17  ? 2493 TYR A CG    1 
ATOM   7483  C  CD1   . TYR A 1 2493 ? 239.188 177.688 233.046 1.00 32.21  ? 2493 TYR A CD1   1 
ATOM   7484  C  CD2   . TYR A 1 2493 ? 239.590 176.077 231.346 1.00 31.42  ? 2493 TYR A CD2   1 
ATOM   7485  C  CE1   . TYR A 1 2493 ? 238.169 178.231 232.299 1.00 30.92  ? 2493 TYR A CE1   1 
ATOM   7486  C  CE2   . TYR A 1 2493 ? 238.570 176.613 230.591 1.00 38.29  ? 2493 TYR A CE2   1 
ATOM   7487  C  CZ    . TYR A 1 2493 ? 237.862 177.690 231.074 1.00 41.31  ? 2493 TYR A CZ    1 
ATOM   7488  O  OH    . TYR A 1 2493 ? 236.842 178.230 230.327 1.00 43.84  ? 2493 TYR A OH    1 
ATOM   7489  N  N     . LEU A 1 2494 ? 242.842 178.115 235.160 1.00 37.27  ? 2494 LEU A N     1 
ATOM   7490  C  CA    . LEU A 1 2494 ? 242.971 179.396 235.841 1.00 31.54  ? 2494 LEU A CA    1 
ATOM   7491  C  C     . LEU A 1 2494 ? 243.994 180.279 235.146 1.00 26.39  ? 2494 LEU A C     1 
ATOM   7492  O  O     . LEU A 1 2494 ? 243.761 181.476 234.955 1.00 37.71  ? 2494 LEU A O     1 
ATOM   7493  C  CB    . LEU A 1 2494 ? 243.349 179.181 237.304 1.00 35.11  ? 2494 LEU A CB    1 
ATOM   7494  C  CG    . LEU A 1 2494 ? 243.366 180.431 238.183 1.00 34.68  ? 2494 LEU A CG    1 
ATOM   7495  C  CD1   . LEU A 1 2494 ? 241.991 181.066 238.254 1.00 35.56  ? 2494 LEU A CD1   1 
ATOM   7496  C  CD2   . LEU A 1 2494 ? 243.859 180.081 239.565 1.00 38.02  ? 2494 LEU A CD2   1 
ATOM   7497  N  N     . VAL A 1 2495 ? 245.129 179.704 234.746 1.00 29.29  ? 2495 VAL A N     1 
ATOM   7498  C  CA    . VAL A 1 2495 ? 246.113 180.497 234.005 1.00 32.38  ? 2495 VAL A CA    1 
ATOM   7499  C  C     . VAL A 1 2495 ? 245.522 180.984 232.683 1.00 31.78  ? 2495 VAL A C     1 
ATOM   7500  O  O     . VAL A 1 2495 ? 245.654 182.162 232.314 1.00 36.25  ? 2495 VAL A O     1 
ATOM   7501  C  CB    . VAL A 1 2495 ? 247.402 179.685 233.783 1.00 37.19  ? 2495 VAL A CB    1 
ATOM   7502  C  CG1   . VAL A 1 2495 ? 248.368 180.460 232.906 1.00 32.88  ? 2495 VAL A CG1   1 
ATOM   7503  C  CG2   . VAL A 1 2495 ? 248.043 179.347 235.112 1.00 38.88  ? 2495 VAL A CG2   1 
ATOM   7504  N  N     . TYR A 1 2496 ? 244.847 180.087 231.962 1.00 38.60  ? 2496 TYR A N     1 
ATOM   7505  C  CA    . TYR A 1 2496 ? 244.243 180.431 230.676 1.00 35.35  ? 2496 TYR A CA    1 
ATOM   7506  C  C     . TYR A 1 2496 ? 243.179 181.517 230.830 1.00 36.34  ? 2496 TYR A C     1 
ATOM   7507  O  O     . TYR A 1 2496 ? 243.121 182.465 230.035 1.00 44.69  ? 2496 TYR A O     1 
ATOM   7508  C  CB    . TYR A 1 2496 ? 243.673 179.150 230.060 1.00 25.56  ? 2496 TYR A CB    1 
ATOM   7509  C  CG    . TYR A 1 2496 ? 242.656 179.293 228.953 1.00 30.99  ? 2496 TYR A CG    1 
ATOM   7510  C  CD1   . TYR A 1 2496 ? 243.052 179.365 227.627 1.00 38.07  ? 2496 TYR A CD1   1 
ATOM   7511  C  CD2   . TYR A 1 2496 ? 241.298 179.292 229.229 1.00 37.69  ? 2496 TYR A CD2   1 
ATOM   7512  C  CE1   . TYR A 1 2496 ? 242.125 179.468 226.613 1.00 43.18  ? 2496 TYR A CE1   1 
ATOM   7513  C  CE2   . TYR A 1 2496 ? 240.365 179.398 228.221 1.00 33.19  ? 2496 TYR A CE2   1 
ATOM   7514  C  CZ    . TYR A 1 2496 ? 240.783 179.486 226.916 1.00 35.37  ? 2496 TYR A CZ    1 
ATOM   7515  O  OH    . TYR A 1 2496 ? 239.853 179.591 225.909 1.00 34.89  ? 2496 TYR A OH    1 
ATOM   7516  N  N     . ALA A 1 2497 ? 242.345 181.410 231.866 1.00 25.43  ? 2497 ALA A N     1 
ATOM   7517  C  CA    . ALA A 1 2497 ? 241.300 182.393 232.112 1.00 22.75  ? 2497 ALA A CA    1 
ATOM   7518  C  C     . ALA A 1 2497 ? 241.871 183.732 232.552 1.00 31.06  ? 2497 ALA A C     1 
ATOM   7519  O  O     . ALA A 1 2497 ? 241.327 184.775 232.185 1.00 37.28  ? 2497 ALA A O     1 
ATOM   7520  C  CB    . ALA A 1 2497 ? 240.323 181.863 233.159 1.00 31.71  ? 2497 ALA A CB    1 
ATOM   7521  N  N     . ILE A 1 2498 ? 242.951 183.733 233.336 1.00 33.34  ? 2498 ILE A N     1 
ATOM   7522  C  CA    . ILE A 1 2498 ? 243.597 184.996 233.682 1.00 29.13  ? 2498 ILE A CA    1 
ATOM   7523  C  C     . ILE A 1 2498 ? 244.111 185.678 232.424 1.00 30.59  ? 2498 ILE A C     1 
ATOM   7524  O  O     . ILE A 1 2498 ? 243.914 186.885 232.228 1.00 34.57  ? 2498 ILE A O     1 
ATOM   7525  C  CB    . ILE A 1 2498 ? 244.728 184.767 234.701 1.00 31.73  ? 2498 ILE A CB    1 
ATOM   7526  C  CG1   . ILE A 1 2498 ? 244.159 184.420 236.074 1.00 32.99  ? 2498 ILE A CG1   1 
ATOM   7527  C  CG2   . ILE A 1 2498 ? 245.588 186.006 234.820 1.00 35.49  ? 2498 ILE A CG2   1 
ATOM   7528  C  CD1   . ILE A 1 2498 ? 245.213 184.011 237.070 1.00 36.13  ? 2498 ILE A CD1   1 
ATOM   7529  N  N     . LEU A 1 2499 ? 244.755 184.910 231.539 1.00 39.46  ? 2499 LEU A N     1 
ATOM   7530  C  CA    . LEU A 1 2499 ? 245.231 185.481 230.282 1.00 29.66  ? 2499 LEU A CA    1 
ATOM   7531  C  C     . LEU A 1 2499 ? 244.091 186.072 229.463 1.00 31.76  ? 2499 LEU A C     1 
ATOM   7532  O  O     . LEU A 1 2499 ? 244.203 187.190 228.950 1.00 39.19  ? 2499 LEU A O     1 
ATOM   7533  C  CB    . LEU A 1 2499 ? 245.971 184.427 229.462 1.00 33.55  ? 2499 LEU A CB    1 
ATOM   7534  C  CG    . LEU A 1 2499 ? 247.331 183.988 229.988 1.00 41.32  ? 2499 LEU A CG    1 
ATOM   7535  C  CD1   . LEU A 1 2499 ? 247.877 182.848 229.152 1.00 40.19  ? 2499 LEU A CD1   1 
ATOM   7536  C  CD2   . LEU A 1 2499 ? 248.267 185.170 229.943 1.00 38.89  ? 2499 LEU A CD2   1 
ATOM   7537  N  N     . TRP A 1 2500 ? 242.984 185.343 229.330 1.00 32.30  ? 2500 TRP A N     1 
ATOM   7538  C  CA    . TRP A 1 2500 ? 241.921 185.811 228.449 1.00 27.25  ? 2500 TRP A CA    1 
ATOM   7539  C  C     . TRP A 1 2500 ? 241.008 186.846 229.094 1.00 30.20  ? 2500 TRP A C     1 
ATOM   7540  O  O     . TRP A 1 2500 ? 240.257 187.513 228.377 1.00 37.73  ? 2500 TRP A O     1 
ATOM   7541  C  CB    . TRP A 1 2500 ? 241.094 184.631 227.946 1.00 22.03  ? 2500 TRP A CB    1 
ATOM   7542  C  CG    . TRP A 1 2500 ? 241.697 183.999 226.739 1.00 26.83  ? 2500 TRP A CG    1 
ATOM   7543  C  CD1   . TRP A 1 2500 ? 242.213 182.747 226.647 1.00 28.44  ? 2500 TRP A CD1   1 
ATOM   7544  C  CD2   . TRP A 1 2500 ? 241.870 184.603 225.452 1.00 30.85  ? 2500 TRP A CD2   1 
ATOM   7545  N  NE1   . TRP A 1 2500 ? 242.689 182.523 225.379 1.00 33.86  ? 2500 TRP A NE1   1 
ATOM   7546  C  CE2   . TRP A 1 2500 ? 242.488 183.649 224.626 1.00 33.67  ? 2500 TRP A CE2   1 
ATOM   7547  C  CE3   . TRP A 1 2500 ? 241.556 185.855 224.918 1.00 30.19  ? 2500 TRP A CE3   1 
ATOM   7548  C  CZ2   . TRP A 1 2500 ? 242.802 183.907 223.296 1.00 32.37  ? 2500 TRP A CZ2   1 
ATOM   7549  C  CZ3   . TRP A 1 2500 ? 241.867 186.108 223.598 1.00 28.68  ? 2500 TRP A CZ3   1 
ATOM   7550  C  CH2   . TRP A 1 2500 ? 242.482 185.139 222.802 1.00 32.29  ? 2500 TRP A CH2   1 
ATOM   7551  N  N     . SER A 1 2501 ? 241.055 187.005 230.414 1.00 39.66  ? 2501 SER A N     1 
ATOM   7552  C  CA    . SER A 1 2501 ? 240.227 188.000 231.078 1.00 23.78  ? 2501 SER A CA    1 
ATOM   7553  C  C     . SER A 1 2501 ? 240.975 189.290 231.357 1.00 35.97  ? 2501 SER A C     1 
ATOM   7554  O  O     . SER A 1 2501 ? 240.347 190.349 231.467 1.00 44.82  ? 2501 SER A O     1 
ATOM   7555  C  CB    . SER A 1 2501 ? 239.683 187.438 232.393 1.00 19.56  ? 2501 SER A CB    1 
ATOM   7556  O  OG    . SER A 1 2501 ? 239.151 186.142 232.204 1.00 40.17  ? 2501 SER A OG    1 
ATOM   7557  N  N     . LEU A 1 2502 ? 242.300 189.231 231.471 1.00 38.23  ? 2502 LEU A N     1 
ATOM   7558  C  CA    . LEU A 1 2502 ? 243.087 190.418 231.767 1.00 24.73  ? 2502 LEU A CA    1 
ATOM   7559  C  C     . LEU A 1 2502 ? 243.683 191.068 230.530 1.00 36.00  ? 2502 LEU A C     1 
ATOM   7560  O  O     . LEU A 1 2502 ? 244.037 192.250 230.577 1.00 54.23  ? 2502 LEU A O     1 
ATOM   7561  C  CB    . LEU A 1 2502 ? 244.210 190.068 232.747 1.00 29.80  ? 2502 LEU A CB    1 
ATOM   7562  C  CG    . LEU A 1 2502 ? 243.929 190.253 234.237 1.00 35.67  ? 2502 LEU A CG    1 
ATOM   7563  C  CD1   . LEU A 1 2502 ? 242.685 189.504 234.677 1.00 28.36  ? 2502 LEU A CD1   1 
ATOM   7564  C  CD2   . LEU A 1 2502 ? 245.119 189.765 235.014 1.00 39.67  ? 2502 LEU A CD2   1 
ATOM   7565  N  N     . SER A 1 2503 ? 243.804 190.330 229.429 1.00 42.33  ? 2503 SER A N     1 
ATOM   7566  C  CA    . SER A 1 2503 ? 244.360 190.861 228.191 1.00 31.53  ? 2503 SER A CA    1 
ATOM   7567  C  C     . SER A 1 2503 ? 243.515 190.515 226.973 1.00 37.66  ? 2503 SER A C     1 
ATOM   7568  O  O     . SER A 1 2503 ? 244.019 190.580 225.847 1.00 42.94  ? 2503 SER A O     1 
ATOM   7569  C  CB    . SER A 1 2503 ? 245.789 190.354 227.994 1.00 29.66  ? 2503 SER A CB    1 
ATOM   7570  O  OG    . SER A 1 2503 ? 245.802 188.951 227.809 1.00 41.18  ? 2503 SER A OG    1 
ATOM   7571  N  N     . GLY A 1 2504 ? 242.249 190.144 227.165 1.00 36.68  ? 2504 GLY A N     1 
ATOM   7572  C  CA    . GLY A 1 2504 ? 241.397 189.832 226.032 1.00 25.11  ? 2504 GLY A CA    1 
ATOM   7573  C  C     . GLY A 1 2504 ? 241.117 191.028 225.147 1.00 33.13  ? 2504 GLY A C     1 
ATOM   7574  O  O     . GLY A 1 2504 ? 241.006 190.889 223.927 1.00 42.56  ? 2504 GLY A O     1 
ATOM   7575  N  N     . ASP A 1 2505 ? 240.996 192.215 225.741 1.00 35.66  ? 2505 ASP A N     1 
ATOM   7576  C  CA    . ASP A 1 2505 ? 240.716 193.439 225.004 1.00 31.19  ? 2505 ASP A CA    1 
ATOM   7577  C  C     . ASP A 1 2505 ? 241.982 194.185 224.603 1.00 34.45  ? 2505 ASP A C     1 
ATOM   7578  O  O     . ASP A 1 2505 ? 241.943 195.405 224.419 1.00 47.14  ? 2505 ASP A O     1 
ATOM   7579  C  CB    . ASP A 1 2505 ? 239.807 194.355 225.825 1.00 32.91  ? 2505 ASP A CB    1 
ATOM   7580  C  CG    . ASP A 1 2505 ? 240.402 194.711 227.171 1.00 46.39  ? 2505 ASP A CG    1 
ATOM   7581  O  OD1   . ASP A 1 2505 ? 241.431 194.117 227.549 1.00 46.38  ? 2505 ASP A OD1   1 
ATOM   7582  O  OD2   . ASP A 1 2505 ? 239.843 195.594 227.851 1.00 50.03  ? 2505 ASP A OD2   1 
ATOM   7583  N  N     . SER A 1 2506 ? 243.100 193.482 224.468 1.00 30.94  ? 2506 SER A N     1 
ATOM   7584  C  CA    . SER A 1 2506 ? 244.360 194.083 224.068 1.00 33.16  ? 2506 SER A CA    1 
ATOM   7585  C  C     . SER A 1 2506 ? 244.941 193.319 222.886 1.00 44.72  ? 2506 SER A C     1 
ATOM   7586  O  O     . SER A 1 2506 ? 244.597 192.161 222.638 1.00 53.53  ? 2506 SER A O     1 
ATOM   7587  C  CB    . SER A 1 2506 ? 245.358 194.107 225.230 1.00 36.05  ? 2506 SER A CB    1 
ATOM   7588  O  OG    . SER A 1 2506 ? 245.643 192.797 225.680 1.00 48.28  ? 2506 SER A OG    1 
ATOM   7589  N  N     . ARG A 1 2507 ? 245.828 193.984 222.152 1.00 47.24  ? 2507 ARG A N     1 
ATOM   7590  C  CA    . ARG A 1 2507 ? 246.378 193.401 220.940 1.00 43.23  ? 2507 ARG A CA    1 
ATOM   7591  C  C     . ARG A 1 2507 ? 247.356 192.276 221.276 1.00 47.09  ? 2507 ARG A C     1 
ATOM   7592  O  O     . ARG A 1 2507 ? 247.599 191.947 222.439 1.00 56.42  ? 2507 ARG A O     1 
ATOM   7593  C  CB    . ARG A 1 2507 ? 247.061 194.471 220.091 1.00 48.62  ? 2507 ARG A CB    1 
ATOM   7594  C  CG    . ARG A 1 2507 ? 248.298 195.071 220.722 1.00 53.25  ? 2507 ARG A CG    1 
ATOM   7595  C  CD    . ARG A 1 2507 ? 248.850 196.204 219.875 1.00 51.91  ? 2507 ARG A CD    1 
ATOM   7596  N  NE    . ARG A 1 2507 ? 250.090 196.737 220.424 1.00 55.68  ? 2507 ARG A NE    1 
ATOM   7597  C  CZ    . ARG A 1 2507 ? 250.156 197.695 221.337 1.00 61.56  ? 2507 ARG A CZ    1 
ATOM   7598  N  NH1   . ARG A 1 2507 ? 249.067 198.281 221.804 1.00 55.76  ? 2507 ARG A NH1   1 
ATOM   7599  N  NH2   . ARG A 1 2507 ? 251.346 198.078 221.790 1.00 60.05  ? 2507 ARG A NH2   1 
ATOM   7600  N  N     . LEU A 1 2508 ? 247.927 191.687 220.223 1.00 53.73  ? 2508 LEU A N     1 
ATOM   7601  C  CA    . LEU A 1 2508 ? 248.731 190.478 220.382 1.00 57.07  ? 2508 LEU A CA    1 
ATOM   7602  C  C     . LEU A 1 2508 ? 249.963 190.726 221.243 1.00 58.09  ? 2508 LEU A C     1 
ATOM   7603  O  O     . LEU A 1 2508 ? 250.352 189.867 222.045 1.00 58.65  ? 2508 LEU A O     1 
ATOM   7604  C  CB    . LEU A 1 2508 ? 249.133 189.943 219.009 1.00 57.89  ? 2508 LEU A CB    1 
ATOM   7605  C  CG    . LEU A 1 2508 ? 249.898 188.622 218.971 1.00 63.50  ? 2508 LEU A CG    1 
ATOM   7606  C  CD1   . LEU A 1 2508 ? 249.001 187.474 219.402 1.00 63.26  ? 2508 LEU A CD1   1 
ATOM   7607  C  CD2   . LEU A 1 2508 ? 250.451 188.378 217.578 1.00 58.27  ? 2508 LEU A CD2   1 
ATOM   7608  N  N     . LYS A 1 2509 ? 250.597 191.889 221.088 1.00 54.90  ? 2509 LYS A N     1 
ATOM   7609  C  CA    . LYS A 1 2509 ? 251.804 192.186 221.853 1.00 51.82  ? 2509 LYS A CA    1 
ATOM   7610  C  C     . LYS A 1 2509 ? 251.514 192.222 223.349 1.00 58.24  ? 2509 LYS A C     1 
ATOM   7611  O  O     . LYS A 1 2509 ? 252.292 191.705 224.157 1.00 61.77  ? 2509 LYS A O     1 
ATOM   7612  C  CB    . LYS A 1 2509 ? 252.406 193.512 221.388 1.00 56.86  ? 2509 LYS A CB    1 
ATOM   7613  C  CG    . LYS A 1 2509 ? 253.282 193.411 220.146 1.00 65.20  ? 2509 LYS A CG    1 
ATOM   7614  C  CD    . LYS A 1 2509 ? 252.451 193.194 218.891 1.00 66.43  ? 2509 LYS A CD    1 
ATOM   7615  C  CE    . LYS A 1 2509 ? 251.640 194.429 218.541 1.00 61.89  ? 2509 LYS A CE    1 
ATOM   7616  N  NZ    . LYS A 1 2509 ? 250.869 194.250 217.282 1.00 59.22  ? 2509 LYS A NZ    1 
ATOM   7617  N  N     . MET A 1 2510 ? 250.389 192.825 223.737 1.00 53.38  ? 2510 MET A N     1 
ATOM   7618  C  CA    . MET A 1 2510 ? 250.070 192.936 225.156 1.00 44.07  ? 2510 MET A CA    1 
ATOM   7619  C  C     . MET A 1 2510 ? 249.679 191.585 225.742 1.00 50.70  ? 2510 MET A C     1 
ATOM   7620  O  O     . MET A 1 2510 ? 250.002 191.283 226.898 1.00 60.04  ? 2510 MET A O     1 
ATOM   7621  C  CB    . MET A 1 2510 ? 248.962 193.965 225.361 1.00 43.89  ? 2510 MET A CB    1 
ATOM   7622  C  CG    . MET A 1 2510 ? 249.426 195.382 225.085 1.00 49.44  ? 2510 MET A CG    1 
ATOM   7623  S  SD    . MET A 1 2510 ? 251.136 195.604 225.605 1.00 59.17  ? 2510 MET A SD    1 
ATOM   7624  C  CE    . MET A 1 2510 ? 251.282 197.383 225.595 1.00 51.11  ? 2510 MET A CE    1 
ATOM   7625  N  N     . ARG A 1 2511 ? 248.988 190.755 224.959 1.00 41.69  ? 2511 ARG A N     1 
ATOM   7626  C  CA    . ARG A 1 2511 ? 248.696 189.396 225.403 1.00 41.66  ? 2511 ARG A CA    1 
ATOM   7627  C  C     . ARG A 1 2511 ? 249.978 188.602 225.606 1.00 42.55  ? 2511 ARG A C     1 
ATOM   7628  O  O     . ARG A 1 2511 ? 250.115 187.866 226.591 1.00 45.65  ? 2511 ARG A O     1 
ATOM   7629  C  CB    . ARG A 1 2511 ? 247.787 188.701 224.392 1.00 46.82  ? 2511 ARG A CB    1 
ATOM   7630  C  CG    . ARG A 1 2511 ? 246.505 189.453 224.108 1.00 43.96  ? 2511 ARG A CG    1 
ATOM   7631  C  CD    . ARG A 1 2511 ? 245.644 188.722 223.101 1.00 41.49  ? 2511 ARG A CD    1 
ATOM   7632  N  NE    . ARG A 1 2511 ? 244.412 189.447 222.822 1.00 33.71  ? 2511 ARG A NE    1 
ATOM   7633  C  CZ    . ARG A 1 2511 ? 243.503 189.062 221.938 1.00 42.30  ? 2511 ARG A CZ    1 
ATOM   7634  N  NH1   . ARG A 1 2511 ? 243.657 187.961 221.223 1.00 50.18  ? 2511 ARG A NH1   1 
ATOM   7635  N  NH2   . ARG A 1 2511 ? 242.414 189.803 221.765 1.00 40.64  ? 2511 ARG A NH2   1 
ATOM   7636  N  N     . ALA A 1 2512 ? 250.933 188.744 224.684 1.00 48.64  ? 2512 ALA A N     1 
ATOM   7637  C  CA    . ALA A 1 2512 ? 252.220 188.076 224.846 1.00 47.22  ? 2512 ALA A CA    1 
ATOM   7638  C  C     . ALA A 1 2512 ? 252.956 188.584 226.080 1.00 53.10  ? 2512 ALA A C     1 
ATOM   7639  O  O     . ALA A 1 2512 ? 253.590 187.803 226.797 1.00 56.63  ? 2512 ALA A O     1 
ATOM   7640  C  CB    . ALA A 1 2512 ? 253.072 188.268 223.593 1.00 43.69  ? 2512 ALA A CB    1 
ATOM   7641  N  N     . GLU A 1 2513 ? 252.892 189.892 226.339 1.00 47.74  ? 2513 GLU A N     1 
ATOM   7642  C  CA    . GLU A 1 2513 ? 253.551 190.444 227.519 1.00 43.26  ? 2513 GLU A CA    1 
ATOM   7643  C  C     . GLU A 1 2513 ? 252.943 189.893 228.803 1.00 50.43  ? 2513 GLU A C     1 
ATOM   7644  O  O     . GLU A 1 2513 ? 253.664 189.538 229.743 1.00 58.65  ? 2513 GLU A O     1 
ATOM   7645  C  CB    . GLU A 1 2513 ? 253.472 191.969 227.505 1.00 47.87  ? 2513 GLU A CB    1 
ATOM   7646  C  CG    . GLU A 1 2513 ? 254.656 192.642 226.842 1.00 54.91  ? 2513 GLU A CG    1 
ATOM   7647  C  CD    . GLU A 1 2513 ? 254.535 194.150 226.844 1.00 59.58  ? 2513 GLU A CD    1 
ATOM   7648  O  OE1   . GLU A 1 2513 ? 253.521 194.661 227.361 1.00 52.55  ? 2513 GLU A OE1   1 
ATOM   7649  O  OE2   . GLU A 1 2513 ? 255.453 194.823 226.331 1.00 63.19  ? 2513 GLU A OE2   1 
ATOM   7650  N  N     . LEU A 1 2514 ? 251.611 189.831 228.869 1.00 49.35  ? 2514 LEU A N     1 
ATOM   7651  C  CA    . LEU A 1 2514 ? 250.968 189.288 230.061 1.00 45.46  ? 2514 LEU A CA    1 
ATOM   7652  C  C     . LEU A 1 2514 ? 251.288 187.810 230.230 1.00 45.34  ? 2514 LEU A C     1 
ATOM   7653  O  O     . LEU A 1 2514 ? 251.497 187.336 231.353 1.00 52.75  ? 2514 LEU A O     1 
ATOM   7654  C  CB    . LEU A 1 2514 ? 249.458 189.510 230.004 1.00 41.32  ? 2514 LEU A CB    1 
ATOM   7655  C  CG    . LEU A 1 2514 ? 248.718 189.085 231.273 1.00 45.53  ? 2514 LEU A CG    1 
ATOM   7656  C  CD1   . LEU A 1 2514 ? 248.994 190.061 232.401 1.00 45.03  ? 2514 LEU A CD1   1 
ATOM   7657  C  CD2   . LEU A 1 2514 ? 247.232 188.969 231.021 1.00 47.08  ? 2514 LEU A CD2   1 
ATOM   7658  N  N     . GLY A 1 2515 ? 251.342 187.064 229.124 1.00 43.01  ? 2515 GLY A N     1 
ATOM   7659  C  CA    . GLY A 1 2515 ? 251.742 185.669 229.209 1.00 43.09  ? 2515 GLY A CA    1 
ATOM   7660  C  C     . GLY A 1 2515 ? 253.159 185.504 229.723 1.00 48.19  ? 2515 GLY A C     1 
ATOM   7661  O  O     . GLY A 1 2515 ? 253.438 184.629 230.545 1.00 52.91  ? 2515 GLY A O     1 
ATOM   7662  N  N     . GLU A 1 2516 ? 254.075 186.349 229.244 1.00 44.36  ? 2516 GLU A N     1 
ATOM   7663  C  CA    . GLU A 1 2516 ? 255.457 186.287 229.706 1.00 46.15  ? 2516 GLU A CA    1 
ATOM   7664  C  C     . GLU A 1 2516 ? 255.561 186.619 231.189 1.00 53.76  ? 2516 GLU A C     1 
ATOM   7665  O  O     . GLU A 1 2516 ? 256.294 185.955 231.932 1.00 61.34  ? 2516 GLU A O     1 
ATOM   7666  C  CB    . GLU A 1 2516 ? 256.326 187.234 228.881 1.00 45.92  ? 2516 GLU A CB    1 
ATOM   7667  C  CG    . GLU A 1 2516 ? 256.835 186.631 227.586 1.00 52.52  ? 2516 GLU A CG    1 
ATOM   7668  C  CD    . GLU A 1 2516 ? 256.903 187.643 226.462 1.00 59.97  ? 2516 GLU A CD    1 
ATOM   7669  O  OE1   . GLU A 1 2516 ? 256.928 188.857 226.754 1.00 62.41  ? 2516 GLU A OE1   1 
ATOM   7670  O  OE2   . GLU A 1 2516 ? 256.929 187.227 225.285 1.00 55.21  ? 2516 GLU A OE2   1 
ATOM   7671  N  N     . TYR A 1 2517 ? 254.834 187.643 231.640 1.00 47.74  ? 2517 TYR A N     1 
ATOM   7672  C  CA    . TYR A 1 2517 ? 254.855 187.986 233.059 1.00 39.57  ? 2517 TYR A CA    1 
ATOM   7673  C  C     . TYR A 1 2517 ? 254.295 186.854 233.909 1.00 43.79  ? 2517 TYR A C     1 
ATOM   7674  O  O     . TYR A 1 2517 ? 254.859 186.518 234.959 1.00 51.88  ? 2517 TYR A O     1 
ATOM   7675  C  CB    . TYR A 1 2517 ? 254.074 189.275 233.305 1.00 43.78  ? 2517 TYR A CB    1 
ATOM   7676  C  CG    . TYR A 1 2517 ? 254.066 189.711 234.752 1.00 50.34  ? 2517 TYR A CG    1 
ATOM   7677  C  CD1   . TYR A 1 2517 ? 255.134 190.414 235.290 1.00 48.69  ? 2517 TYR A CD1   1 
ATOM   7678  C  CD2   . TYR A 1 2517 ? 252.993 189.417 235.581 1.00 51.77  ? 2517 TYR A CD2   1 
ATOM   7679  C  CE1   . TYR A 1 2517 ? 255.132 190.814 236.611 1.00 49.23  ? 2517 TYR A CE1   1 
ATOM   7680  C  CE2   . TYR A 1 2517 ? 252.983 189.811 236.902 1.00 51.81  ? 2517 TYR A CE2   1 
ATOM   7681  C  CZ    . TYR A 1 2517 ? 254.054 190.509 237.412 1.00 54.46  ? 2517 TYR A CZ    1 
ATOM   7682  O  OH    . TYR A 1 2517 ? 254.045 190.904 238.730 1.00 54.00  ? 2517 TYR A OH    1 
ATOM   7683  N  N     . ILE A 1 2518 ? 253.188 186.250 233.471 1.00 43.04  ? 2518 ILE A N     1 
ATOM   7684  C  CA    . ILE A 1 2518 ? 252.612 185.132 234.210 1.00 39.26  ? 2518 ILE A CA    1 
ATOM   7685  C  C     . ILE A 1 2518 ? 253.598 183.976 234.274 1.00 45.55  ? 2518 ILE A C     1 
ATOM   7686  O  O     . ILE A 1 2518 ? 253.786 183.361 235.329 1.00 53.42  ? 2518 ILE A O     1 
ATOM   7687  C  CB    . ILE A 1 2518 ? 251.273 184.708 233.582 1.00 43.01  ? 2518 ILE A CB    1 
ATOM   7688  C  CG1   . ILE A 1 2518 ? 250.162 185.659 234.024 1.00 45.82  ? 2518 ILE A CG1   1 
ATOM   7689  C  CG2   . ILE A 1 2518 ? 250.930 183.275 233.951 1.00 48.23  ? 2518 ILE A CG2   1 
ATOM   7690  C  CD1   . ILE A 1 2518 ? 248.815 185.302 233.475 1.00 46.36  ? 2518 ILE A CD1   1 
ATOM   7691  N  N     . ARG A 1 2519 ? 254.259 183.676 233.154 1.00 51.89  ? 2519 ARG A N     1 
ATOM   7692  C  CA    . ARG A 1 2519 ? 255.272 182.626 233.150 1.00 47.61  ? 2519 ARG A CA    1 
ATOM   7693  C  C     . ARG A 1 2519 ? 256.390 182.939 234.134 1.00 47.23  ? 2519 ARG A C     1 
ATOM   7694  O  O     . ARG A 1 2519 ? 256.901 182.041 234.813 1.00 49.26  ? 2519 ARG A O     1 
ATOM   7695  C  CB    . ARG A 1 2519 ? 255.834 182.448 231.741 1.00 50.92  ? 2519 ARG A CB    1 
ATOM   7696  C  CG    . ARG A 1 2519 ? 256.843 181.321 231.613 1.00 53.79  ? 2519 ARG A CG    1 
ATOM   7697  C  CD    . ARG A 1 2519 ? 257.473 181.300 230.232 1.00 51.43  ? 2519 ARG A CD    1 
ATOM   7698  N  NE    . ARG A 1 2519 ? 256.563 180.780 229.218 1.00 49.32  ? 2519 ARG A NE    1 
ATOM   7699  C  CZ    . ARG A 1 2519 ? 256.267 179.497 229.062 1.00 55.06  ? 2519 ARG A CZ    1 
ATOM   7700  N  NH1   . ARG A 1 2519 ? 256.790 178.566 229.842 1.00 49.58  ? 2519 ARG A NH1   1 
ATOM   7701  N  NH2   . ARG A 1 2519 ? 255.426 179.139 228.096 1.00 53.24  ? 2519 ARG A NH2   1 
ATOM   7702  N  N     . ARG A 1 2520 ? 256.788 184.209 234.218 1.00 50.23  ? 2520 ARG A N     1 
ATOM   7703  C  CA    . ARG A 1 2520 ? 257.833 184.594 235.160 1.00 53.74  ? 2520 ARG A CA    1 
ATOM   7704  C  C     . ARG A 1 2520 ? 257.390 184.395 236.605 1.00 55.12  ? 2520 ARG A C     1 
ATOM   7705  O  O     . ARG A 1 2520 ? 258.177 183.930 237.438 1.00 54.09  ? 2520 ARG A O     1 
ATOM   7706  C  CB    . ARG A 1 2520 ? 258.247 186.045 234.924 1.00 47.69  ? 2520 ARG A CB    1 
ATOM   7707  C  CG    . ARG A 1 2520 ? 259.347 186.210 233.893 1.00 49.78  ? 2520 ARG A CG    1 
ATOM   7708  C  CD    . ARG A 1 2520 ? 259.196 187.510 233.122 1.00 53.36  ? 2520 ARG A CD    1 
ATOM   7709  N  NE    . ARG A 1 2520 ? 259.228 188.674 233.999 1.00 55.37  ? 2520 ARG A NE    1 
ATOM   7710  C  CZ    . ARG A 1 2520 ? 258.701 189.852 233.698 1.00 57.53  ? 2520 ARG A CZ    1 
ATOM   7711  N  NH1   . ARG A 1 2520 ? 258.085 190.059 232.545 1.00 56.16  ? 2520 ARG A NH1   1 
ATOM   7712  N  NH2   . ARG A 1 2520 ? 258.793 190.848 234.574 1.00 51.42  ? 2520 ARG A NH2   1 
ATOM   7713  N  N     . ILE A 1 2521 ? 256.142 184.736 236.927 1.00 52.42  ? 2521 ILE A N     1 
ATOM   7714  C  CA    . ILE A 1 2521 ? 255.716 184.766 238.324 1.00 48.45  ? 2521 ILE A CA    1 
ATOM   7715  C  C     . ILE A 1 2521 ? 255.043 183.482 238.809 1.00 51.22  ? 2521 ILE A C     1 
ATOM   7716  O  O     . ILE A 1 2521 ? 255.080 183.203 240.016 1.00 56.57  ? 2521 ILE A O     1 
ATOM   7717  C  CB    . ILE A 1 2521 ? 254.781 185.965 238.590 1.00 50.13  ? 2521 ILE A CB    1 
ATOM   7718  C  CG1   . ILE A 1 2521 ? 253.428 185.758 237.907 1.00 52.21  ? 2521 ILE A CG1   1 
ATOM   7719  C  CG2   . ILE A 1 2521 ? 255.431 187.260 238.137 1.00 48.00  ? 2521 ILE A CG2   1 
ATOM   7720  C  CD1   . ILE A 1 2521 ? 252.341 186.672 238.411 1.00 47.52  ? 2521 ILE A CD1   1 
ATOM   7721  N  N     . THR A 1 2522 ? 254.436 182.699 237.924 1.00 48.84  ? 2522 THR A N     1 
ATOM   7722  C  CA    . THR A 1 2522 ? 253.593 181.602 238.376 1.00 49.10  ? 2522 THR A CA    1 
ATOM   7723  C  C     . THR A 1 2522 ? 254.408 180.341 238.643 1.00 51.89  ? 2522 THR A C     1 
ATOM   7724  O  O     . THR A 1 2522 ? 255.566 180.216 238.240 1.00 57.00  ? 2522 THR A O     1 
ATOM   7725  C  CB    . THR A 1 2522 ? 252.498 181.290 237.355 1.00 54.58  ? 2522 THR A CB    1 
ATOM   7726  O  OG1   . THR A 1 2522 ? 251.454 180.545 237.992 1.00 61.36  ? 2522 THR A OG1   1 
ATOM   7727  C  CG2   . THR A 1 2522 ? 253.056 180.461 236.212 1.00 52.14  ? 2522 THR A CG2   1 
ATOM   7728  N  N     . THR A 1 2523 ? 253.776 179.403 239.348 1.00 58.13  ? 2523 THR A N     1 
ATOM   7729  C  CA    . THR A 1 2523 ? 254.315 178.068 239.563 1.00 59.71  ? 2523 THR A CA    1 
ATOM   7730  C  C     . THR A 1 2523 ? 253.465 176.990 238.908 1.00 59.48  ? 2523 THR A C     1 
ATOM   7731  O  O     . THR A 1 2523 ? 253.823 175.809 238.975 1.00 57.25  ? 2523 THR A O     1 
ATOM   7732  C  CB    . THR A 1 2523 ? 254.445 177.779 241.062 1.00 58.55  ? 2523 THR A CB    1 
ATOM   7733  O  OG1   . THR A 1 2523 ? 253.269 178.235 241.742 1.00 56.92  ? 2523 THR A OG1   1 
ATOM   7734  C  CG2   . THR A 1 2523 ? 255.663 178.486 241.636 1.00 56.85  ? 2523 THR A CG2   1 
ATOM   7735  N  N     . VAL A 1 2524 ? 252.348 177.364 238.289 1.00 55.11  ? 2524 VAL A N     1 
ATOM   7736  C  CA    . VAL A 1 2524 ? 251.502 176.405 237.573 1.00 54.84  ? 2524 VAL A CA    1 
ATOM   7737  C  C     . VAL A 1 2524 ? 252.278 175.849 236.387 1.00 56.84  ? 2524 VAL A C     1 
ATOM   7738  O  O     . VAL A 1 2524 ? 253.063 176.591 235.762 1.00 56.53  ? 2524 VAL A O     1 
ATOM   7739  C  CB    . VAL A 1 2524 ? 250.201 177.085 237.113 1.00 52.90  ? 2524 VAL A CB    1 
ATOM   7740  C  CG1   . VAL A 1 2524 ? 249.243 176.085 236.492 1.00 51.72  ? 2524 VAL A CG1   1 
ATOM   7741  C  CG2   . VAL A 1 2524 ? 249.542 177.805 238.277 1.00 49.76  ? 2524 VAL A CG2   1 
ATOM   7742  N  N     . PRO A 1 2525 ? 252.140 174.567 236.047 1.00 53.72  ? 2525 PRO A N     1 
ATOM   7743  C  CA    . PRO A 1 2525 ? 252.809 174.054 234.846 1.00 54.35  ? 2525 PRO A CA    1 
ATOM   7744  C  C     . PRO A 1 2525 ? 252.355 174.796 233.598 1.00 58.80  ? 2525 PRO A C     1 
ATOM   7745  O  O     . PRO A 1 2525 ? 251.174 175.107 233.430 1.00 61.96  ? 2525 PRO A O     1 
ATOM   7746  C  CB    . PRO A 1 2525 ? 252.393 172.581 234.811 1.00 50.70  ? 2525 PRO A CB    1 
ATOM   7747  C  CG    . PRO A 1 2525 ? 252.089 172.247 236.226 1.00 52.36  ? 2525 PRO A CG    1 
ATOM   7748  C  CD    . PRO A 1 2525 ? 251.508 173.489 236.828 1.00 50.67  ? 2525 PRO A CD    1 
ATOM   7749  N  N     . LEU A 1 2526 ? 253.308 175.073 232.720 1.00 56.18  ? 2526 LEU A N     1 
ATOM   7750  C  CA    . LEU A 1 2526 ? 253.106 175.865 231.519 1.00 54.50  ? 2526 LEU A CA    1 
ATOM   7751  C  C     . LEU A 1 2526 ? 253.759 175.168 230.339 1.00 59.17  ? 2526 LEU A C     1 
ATOM   7752  O  O     . LEU A 1 2526 ? 254.664 174.345 230.519 1.00 60.45  ? 2526 LEU A O     1 
ATOM   7753  C  CB    . LEU A 1 2526 ? 253.691 177.275 231.692 1.00 55.27  ? 2526 LEU A CB    1 
ATOM   7754  C  CG    . LEU A 1 2526 ? 252.942 178.195 232.656 1.00 52.54  ? 2526 LEU A CG    1 
ATOM   7755  C  CD1   . LEU A 1 2526 ? 253.451 179.611 232.536 1.00 45.57  ? 2526 LEU A CD1   1 
ATOM   7756  C  CD2   . LEU A 1 2526 ? 251.448 178.146 232.398 1.00 54.45  ? 2526 LEU A CD2   1 
ATOM   7757  N  N     . PRO A 1 2527 ? 253.315 175.462 229.115 1.00 61.75  ? 2527 PRO A N     1 
ATOM   7758  C  CA    . PRO A 1 2527 ? 253.922 174.821 227.942 1.00 59.38  ? 2527 PRO A CA    1 
ATOM   7759  C  C     . PRO A 1 2527 ? 255.406 175.140 227.833 1.00 64.67  ? 2527 PRO A C     1 
ATOM   7760  O  O     . PRO A 1 2527 ? 255.851 176.242 228.160 1.00 64.20  ? 2527 PRO A O     1 
ATOM   7761  C  CB    . PRO A 1 2527 ? 253.131 175.409 226.768 1.00 60.61  ? 2527 PRO A CB    1 
ATOM   7762  C  CG    . PRO A 1 2527 ? 251.851 175.874 227.367 1.00 56.65  ? 2527 PRO A CG    1 
ATOM   7763  C  CD    . PRO A 1 2527 ? 252.192 176.338 228.741 1.00 56.25  ? 2527 PRO A CD    1 
ATOM   7764  N  N     . THR A 1 2528 ? 256.169 174.158 227.362 1.00 72.62  ? 2528 THR A N     1 
ATOM   7765  C  CA    . THR A 1 2528 ? 257.621 174.246 227.293 1.00 71.53  ? 2528 THR A CA    1 
ATOM   7766  C  C     . THR A 1 2528 ? 258.127 174.779 225.958 1.00 75.68  ? 2528 THR A C     1 
ATOM   7767  O  O     . THR A 1 2528 ? 259.338 174.754 225.718 1.00 76.86  ? 2528 THR A O     1 
ATOM   7768  C  CB    . THR A 1 2528 ? 258.243 172.875 227.566 1.00 72.89  ? 2528 THR A CB    1 
ATOM   7769  O  OG1   . THR A 1 2528 ? 257.806 171.945 226.568 1.00 76.41  ? 2528 THR A OG1   1 
ATOM   7770  C  CG2   . THR A 1 2528 ? 257.831 172.370 228.939 1.00 69.91  ? 2528 THR A CG2   1 
ATOM   7771  N  N     . ALA A 1 2529 ? 257.238 175.245 225.088 1.00 79.57  ? 2529 ALA A N     1 
ATOM   7772  C  CA    . ALA A 1 2529 ? 257.669 175.771 223.802 1.00 75.47  ? 2529 ALA A CA    1 
ATOM   7773  C  C     . ALA A 1 2529 ? 258.531 177.014 224.009 1.00 80.17  ? 2529 ALA A C     1 
ATOM   7774  O  O     . ALA A 1 2529 ? 258.245 177.829 224.894 1.00 77.99  ? 2529 ALA A O     1 
ATOM   7775  C  CB    . ALA A 1 2529 ? 256.463 176.105 222.925 1.00 75.26  ? 2529 ALA A CB    1 
ATOM   7776  N  N     . PRO A 1 2530 ? 259.589 177.194 223.215 1.00 85.56  ? 2530 PRO A N     1 
ATOM   7777  C  CA    . PRO A 1 2530 ? 260.515 178.303 223.484 1.00 84.57  ? 2530 PRO A CA    1 
ATOM   7778  C  C     . PRO A 1 2530 ? 260.032 179.648 222.973 1.00 84.37  ? 2530 PRO A C     1 
ATOM   7779  O  O     . PRO A 1 2530 ? 260.446 180.681 223.513 1.00 85.36  ? 2530 PRO A O     1 
ATOM   7780  C  CB    . PRO A 1 2530 ? 261.797 177.860 222.769 1.00 82.68  ? 2530 PRO A CB    1 
ATOM   7781  C  CG    . PRO A 1 2530 ? 261.307 177.020 221.639 1.00 80.97  ? 2530 PRO A CG    1 
ATOM   7782  C  CD    . PRO A 1 2530 ? 260.069 176.317 222.133 1.00 83.31  ? 2530 PRO A CD    1 
ATOM   7783  N  N     . ASN A 1 2531 ? 259.174 179.679 221.954 1.00 79.70  ? 2531 ASN A N     1 
ATOM   7784  C  CA    . ASN A 1 2531 ? 258.791 180.949 221.348 1.00 82.83  ? 2531 ASN A CA    1 
ATOM   7785  C  C     . ASN A 1 2531 ? 257.280 181.124 221.276 1.00 83.26  ? 2531 ASN A C     1 
ATOM   7786  O  O     . ASN A 1 2531 ? 256.784 182.254 221.237 1.00 82.15  ? 2531 ASN A O     1 
ATOM   7787  C  CB    . ASN A 1 2531 ? 259.401 181.070 219.951 1.00 81.48  ? 2531 ASN A CB    1 
ATOM   7788  C  CG    . ASN A 1 2531 ? 260.879 181.405 219.989 1.00 85.68  ? 2531 ASN A CG    1 
ATOM   7789  O  OD1   . ASN A 1 2531 ? 261.427 181.723 221.044 1.00 83.68  ? 2531 ASN A OD1   1 
ATOM   7790  N  ND2   . ASN A 1 2531 ? 261.533 181.332 218.836 1.00 84.46  ? 2531 ASN A ND2   1 
ATOM   7791  N  N     . ILE A 1 2532 ? 256.543 180.022 221.249 1.00 74.50  ? 2532 ILE A N     1 
ATOM   7792  C  CA    . ILE A 1 2532 ? 255.083 180.104 221.127 1.00 67.21  ? 2532 ILE A CA    1 
ATOM   7793  C  C     . ILE A 1 2532 ? 254.501 180.646 222.428 1.00 68.49  ? 2532 ILE A C     1 
ATOM   7794  O  O     . ILE A 1 2532 ? 254.805 180.112 223.510 1.00 67.54  ? 2532 ILE A O     1 
ATOM   7795  C  CB    . ILE A 1 2532 ? 254.494 178.732 220.787 1.00 63.85  ? 2532 ILE A CB    1 
ATOM   7796  C  CG1   . ILE A 1 2532 ? 255.000 178.237 219.428 1.00 69.13  ? 2532 ILE A CG1   1 
ATOM   7797  C  CG2   . ILE A 1 2532 ? 252.979 178.795 220.783 1.00 64.27  ? 2532 ILE A CG2   1 
ATOM   7798  C  CD1   . ILE A 1 2532 ? 256.291 177.441 219.481 1.00 70.02  ? 2532 ILE A CD1   1 
ATOM   7799  N  N     . PRO A 1 2533 ? 253.676 181.688 222.384 1.00 63.35  ? 2533 PRO A N     1 
ATOM   7800  C  CA    . PRO A 1 2533 ? 253.116 182.247 223.619 1.00 60.13  ? 2533 PRO A CA    1 
ATOM   7801  C  C     . PRO A 1 2533 ? 252.097 181.310 224.248 1.00 60.69  ? 2533 PRO A C     1 
ATOM   7802  O  O     . PRO A 1 2533 ? 251.551 180.407 223.613 1.00 67.63  ? 2533 PRO A O     1 
ATOM   7803  C  CB    . PRO A 1 2533 ? 252.463 183.550 223.156 1.00 57.13  ? 2533 PRO A CB    1 
ATOM   7804  C  CG    . PRO A 1 2533 ? 252.172 183.331 221.716 1.00 54.30  ? 2533 PRO A CG    1 
ATOM   7805  C  CD    . PRO A 1 2533 ? 253.279 182.463 221.198 1.00 62.08  ? 2533 PRO A CD    1 
ATOM   7806  N  N     . ILE A 1 2534 ? 251.849 181.543 225.539 1.00 47.12  ? 2534 ILE A N     1 
ATOM   7807  C  CA    . ILE A 1 2534 ? 250.863 180.750 226.264 1.00 47.69  ? 2534 ILE A CA    1 
ATOM   7808  C  C     . ILE A 1 2534 ? 249.461 181.018 225.738 1.00 47.75  ? 2534 ILE A C     1 
ATOM   7809  O  O     . ILE A 1 2534 ? 248.580 180.155 225.830 1.00 50.20  ? 2534 ILE A O     1 
ATOM   7810  C  CB    . ILE A 1 2534 ? 250.956 181.034 227.773 1.00 49.68  ? 2534 ILE A CB    1 
ATOM   7811  C  CG1   . ILE A 1 2534 ? 252.414 181.200 228.193 1.00 54.43  ? 2534 ILE A CG1   1 
ATOM   7812  C  CG2   . ILE A 1 2534 ? 250.303 179.920 228.569 1.00 51.16  ? 2534 ILE A CG2   1 
ATOM   7813  C  CD1   . ILE A 1 2534 ? 252.579 181.676 229.611 1.00 52.35  ? 2534 ILE A CD1   1 
ATOM   7814  N  N     . ILE A 1 2535 ? 249.227 182.207 225.182 1.00 49.86  ? 2535 ILE A N     1 
ATOM   7815  C  CA    . ILE A 1 2535 ? 247.913 182.583 224.685 1.00 50.46  ? 2535 ILE A CA    1 
ATOM   7816  C  C     . ILE A 1 2535 ? 247.462 181.702 223.528 1.00 47.48  ? 2535 ILE A C     1 
ATOM   7817  O  O     . ILE A 1 2535 ? 246.268 181.649 223.225 1.00 48.96  ? 2535 ILE A O     1 
ATOM   7818  C  CB    . ILE A 1 2535 ? 247.927 184.074 224.275 1.00 49.05  ? 2535 ILE A CB    1 
ATOM   7819  C  CG1   . ILE A 1 2535 ? 246.511 184.600 224.052 1.00 44.41  ? 2535 ILE A CG1   1 
ATOM   7820  C  CG2   . ILE A 1 2535 ? 248.774 184.282 223.031 1.00 50.83  ? 2535 ILE A CG2   1 
ATOM   7821  C  CD1   . ILE A 1 2535 ? 245.684 184.630 225.312 1.00 42.71  ? 2535 ILE A CD1   1 
ATOM   7822  N  N     . ASP A 1 2536 ? 248.389 180.989 222.891 1.00 45.01  ? 2536 ASP A N     1 
ATOM   7823  C  CA    . ASP A 1 2536 ? 248.092 180.120 221.761 1.00 41.13  ? 2536 ASP A CA    1 
ATOM   7824  C  C     . ASP A 1 2536 ? 247.716 178.707 222.179 1.00 50.48  ? 2536 ASP A C     1 
ATOM   7825  O  O     . ASP A 1 2536 ? 247.542 177.847 221.310 1.00 54.89  ? 2536 ASP A O     1 
ATOM   7826  C  CB    . ASP A 1 2536 ? 249.292 180.063 220.812 1.00 40.71  ? 2536 ASP A CB    1 
ATOM   7827  C  CG    . ASP A 1 2536 ? 249.445 181.324 219.989 1.00 58.30  ? 2536 ASP A CG    1 
ATOM   7828  O  OD1   . ASP A 1 2536 ? 248.637 182.258 220.174 1.00 60.93  ? 2536 ASP A OD1   1 
ATOM   7829  O  OD2   . ASP A 1 2536 ? 250.374 181.383 219.156 1.00 59.49  ? 2536 ASP A OD2   1 
ATOM   7830  N  N     . TYR A 1 2537 ? 247.597 178.443 223.476 1.00 50.28  ? 2537 TYR A N     1 
ATOM   7831  C  CA    . TYR A 1 2537 ? 247.287 177.119 223.989 1.00 37.13  ? 2537 TYR A CA    1 
ATOM   7832  C  C     . TYR A 1 2537 ? 245.921 177.121 224.656 1.00 45.48  ? 2537 TYR A C     1 
ATOM   7833  O  O     . TYR A 1 2537 ? 245.453 178.151 225.149 1.00 55.26  ? 2537 TYR A O     1 
ATOM   7834  C  CB    . TYR A 1 2537 ? 248.337 176.653 225.001 1.00 38.65  ? 2537 TYR A CB    1 
ATOM   7835  C  CG    . TYR A 1 2537 ? 249.671 176.302 224.395 1.00 41.90  ? 2537 TYR A CG    1 
ATOM   7836  C  CD1   . TYR A 1 2537 ? 250.626 177.278 224.164 1.00 42.32  ? 2537 TYR A CD1   1 
ATOM   7837  C  CD2   . TYR A 1 2537 ? 249.976 174.994 224.057 1.00 45.67  ? 2537 TYR A CD2   1 
ATOM   7838  C  CE1   . TYR A 1 2537 ? 251.846 176.961 223.611 1.00 49.14  ? 2537 TYR A CE1   1 
ATOM   7839  C  CE2   . TYR A 1 2537 ? 251.192 174.667 223.504 1.00 46.65  ? 2537 TYR A CE2   1 
ATOM   7840  C  CZ    . TYR A 1 2537 ? 252.123 175.654 223.284 1.00 52.81  ? 2537 TYR A CZ    1 
ATOM   7841  O  OH    . TYR A 1 2537 ? 253.339 175.330 222.732 1.00 55.25  ? 2537 TYR A OH    1 
ATOM   7842  N  N     . GLU A 1 2538 ? 245.286 175.958 224.666 1.00 41.40  ? 2538 GLU A N     1 
ATOM   7843  C  CA    . GLU A 1 2538 ? 244.074 175.725 225.436 1.00 39.19  ? 2538 GLU A CA    1 
ATOM   7844  C  C     . GLU A 1 2538 ? 244.358 174.664 226.490 1.00 49.16  ? 2538 GLU A C     1 
ATOM   7845  O  O     . GLU A 1 2538 ? 245.467 174.136 226.591 1.00 55.82  ? 2538 GLU A O     1 
ATOM   7846  C  CB    . GLU A 1 2538 ? 242.915 175.303 224.532 1.00 39.94  ? 2538 GLU A CB    1 
ATOM   7847  C  CG    . GLU A 1 2538 ? 243.149 174.012 223.779 1.00 42.04  ? 2538 GLU A CG    1 
ATOM   7848  C  CD    . GLU A 1 2538 ? 241.858 173.342 223.365 1.00 51.34  ? 2538 GLU A CD    1 
ATOM   7849  O  OE1   . GLU A 1 2538 ? 240.788 173.761 223.850 1.00 54.16  ? 2538 GLU A OE1   1 
ATOM   7850  O  OE2   . GLU A 1 2538 ? 241.911 172.396 222.555 1.00 52.05  ? 2538 GLU A OE2   1 
ATOM   7851  N  N     . VAL A 1 2539 ? 243.342 174.354 227.288 1.00 46.64  ? 2539 VAL A N     1 
ATOM   7852  C  CA    . VAL A 1 2539 ? 243.440 173.336 228.325 1.00 44.30  ? 2539 VAL A CA    1 
ATOM   7853  C  C     . VAL A 1 2539 ? 242.451 172.230 227.995 1.00 47.21  ? 2539 VAL A C     1 
ATOM   7854  O  O     . VAL A 1 2539 ? 241.235 172.453 227.994 1.00 52.72  ? 2539 VAL A O     1 
ATOM   7855  C  CB    . VAL A 1 2539 ? 243.172 173.917 229.721 1.00 39.77  ? 2539 VAL A CB    1 
ATOM   7856  C  CG1   . VAL A 1 2539 ? 243.457 172.874 230.780 1.00 41.38  ? 2539 VAL A CG1   1 
ATOM   7857  C  CG2   . VAL A 1 2539 ? 244.020 175.151 229.949 1.00 34.89  ? 2539 VAL A CG2   1 
ATOM   7858  N  N     . SER A 1 2540 ? 242.971 171.039 227.717 1.00 34.05  ? 2540 SER A N     1 
ATOM   7859  C  CA    . SER A 1 2540 ? 242.109 169.888 227.510 1.00 40.42  ? 2540 SER A CA    1 
ATOM   7860  C  C     . SER A 1 2540 ? 241.513 169.437 228.838 1.00 47.10  ? 2540 SER A C     1 
ATOM   7861  O  O     . SER A 1 2540 ? 242.086 169.658 229.907 1.00 48.12  ? 2540 SER A O     1 
ATOM   7862  C  CB    . SER A 1 2540 ? 242.890 168.746 226.864 1.00 44.05  ? 2540 SER A CB    1 
ATOM   7863  O  OG    . SER A 1 2540 ? 244.122 168.537 227.528 1.00 57.68  ? 2540 SER A OG    1 
ATOM   7864  N  N     . ILE A 1 2541 ? 240.343 168.800 228.762 1.00 46.88  ? 2541 ILE A N     1 
ATOM   7865  C  CA    . ILE A 1 2541 ? 239.658 168.359 229.970 1.00 45.31  ? 2541 ILE A CA    1 
ATOM   7866  C  C     . ILE A 1 2541 ? 240.476 167.323 230.728 1.00 48.90  ? 2541 ILE A C     1 
ATOM   7867  O  O     . ILE A 1 2541 ? 240.266 167.127 231.929 1.00 56.53  ? 2541 ILE A O     1 
ATOM   7868  C  CB    . ILE A 1 2541 ? 238.255 167.822 229.623 1.00 48.88  ? 2541 ILE A CB    1 
ATOM   7869  C  CG1   . ILE A 1 2541 ? 237.393 167.727 230.883 1.00 53.62  ? 2541 ILE A CG1   1 
ATOM   7870  C  CG2   . ILE A 1 2541 ? 238.353 166.475 228.931 1.00 47.66  ? 2541 ILE A CG2   1 
ATOM   7871  C  CD1   . ILE A 1 2541 ? 236.933 169.059 231.415 1.00 48.38  ? 2541 ILE A CD1   1 
ATOM   7872  N  N     . SER A 1 2542 ? 241.416 166.656 230.057 1.00 45.33  ? 2542 SER A N     1 
ATOM   7873  C  CA    . SER A 1 2542 ? 242.321 165.744 230.742 1.00 46.93  ? 2542 SER A CA    1 
ATOM   7874  C  C     . SER A 1 2542 ? 243.307 166.468 231.648 1.00 51.61  ? 2542 SER A C     1 
ATOM   7875  O  O     . SER A 1 2542 ? 243.962 165.815 232.467 1.00 54.37  ? 2542 SER A O     1 
ATOM   7876  C  CB    . SER A 1 2542 ? 243.082 164.898 229.722 1.00 51.51  ? 2542 SER A CB    1 
ATOM   7877  O  OG    . SER A 1 2542 ? 244.098 165.654 229.089 1.00 56.40  ? 2542 SER A OG    1 
ATOM   7878  N  N     . GLY A 1 2543 ? 243.434 167.786 231.519 1.00 43.50  ? 2543 GLY A N     1 
ATOM   7879  C  CA    . GLY A 1 2543 ? 244.306 168.551 232.385 1.00 44.15  ? 2543 GLY A CA    1 
ATOM   7880  C  C     . GLY A 1 2543 ? 245.691 168.771 231.816 1.00 48.65  ? 2543 GLY A C     1 
ATOM   7881  O  O     . GLY A 1 2543 ? 246.679 168.751 232.554 1.00 52.60  ? 2543 GLY A O     1 
ATOM   7882  N  N     . GLU A 1 2544 ? 245.780 168.979 230.505 1.00 41.52  ? 2544 GLU A N     1 
ATOM   7883  C  CA    . GLU A 1 2544 ? 247.057 169.211 229.848 1.00 45.57  ? 2544 GLU A CA    1 
ATOM   7884  C  C     . GLU A 1 2544 ? 246.913 170.330 228.829 1.00 45.78  ? 2544 GLU A C     1 
ATOM   7885  O  O     . GLU A 1 2544 ? 245.847 170.520 228.238 1.00 51.05  ? 2544 GLU A O     1 
ATOM   7886  C  CB    . GLU A 1 2544 ? 247.576 167.942 229.161 1.00 49.26  ? 2544 GLU A CB    1 
ATOM   7887  C  CG    . GLU A 1 2544 ? 249.085 167.899 228.989 1.00 48.29  ? 2544 GLU A CG    1 
ATOM   7888  C  CD    . GLU A 1 2544 ? 249.832 168.292 230.249 1.00 56.52  ? 2544 GLU A CD    1 
ATOM   7889  O  OE1   . GLU A 1 2544 ? 250.340 169.432 230.309 1.00 50.56  ? 2544 GLU A OE1   1 
ATOM   7890  O  OE2   . GLU A 1 2544 ? 249.912 167.461 231.177 1.00 57.09  ? 2544 GLU A OE2   1 
ATOM   7891  N  N     . TRP A 1 2545 ? 248.000 171.071 228.631 1.00 45.40  ? 2545 TRP A N     1 
ATOM   7892  C  CA    . TRP A 1 2545 ? 248.023 172.110 227.613 1.00 42.91  ? 2545 TRP A CA    1 
ATOM   7893  C  C     . TRP A 1 2545 ? 248.042 171.482 226.226 1.00 49.66  ? 2545 TRP A C     1 
ATOM   7894  O  O     . TRP A 1 2545 ? 248.865 170.608 225.940 1.00 56.65  ? 2545 TRP A O     1 
ATOM   7895  C  CB    . TRP A 1 2545 ? 249.247 173.005 227.790 1.00 45.08  ? 2545 TRP A CB    1 
ATOM   7896  C  CG    . TRP A 1 2545 ? 249.246 173.832 229.031 1.00 47.37  ? 2545 TRP A CG    1 
ATOM   7897  C  CD1   . TRP A 1 2545 ? 249.959 173.601 230.167 1.00 49.61  ? 2545 TRP A CD1   1 
ATOM   7898  C  CD2   . TRP A 1 2545 ? 248.515 175.043 229.255 1.00 48.38  ? 2545 TRP A CD2   1 
ATOM   7899  N  NE1   . TRP A 1 2545 ? 249.711 174.585 231.090 1.00 50.88  ? 2545 TRP A NE1   1 
ATOM   7900  C  CE2   . TRP A 1 2545 ? 248.827 175.483 230.553 1.00 50.74  ? 2545 TRP A CE2   1 
ATOM   7901  C  CE3   . TRP A 1 2545 ? 247.623 175.793 228.485 1.00 46.31  ? 2545 TRP A CE3   1 
ATOM   7902  C  CZ2   . TRP A 1 2545 ? 248.280 176.639 231.099 1.00 47.05  ? 2545 TRP A CZ2   1 
ATOM   7903  C  CZ3   . TRP A 1 2545 ? 247.081 176.940 229.030 1.00 35.99  ? 2545 TRP A CZ3   1 
ATOM   7904  C  CH2   . TRP A 1 2545 ? 247.411 177.351 230.322 1.00 35.90  ? 2545 TRP A CH2   1 
ATOM   7905  N  N     . SER A 1 2546 ? 247.140 171.935 225.360 1.00 44.96  ? 2546 SER A N     1 
ATOM   7906  C  CA    . SER A 1 2546 ? 247.107 171.493 223.976 1.00 43.77  ? 2546 SER A CA    1 
ATOM   7907  C  C     . SER A 1 2546 ? 247.074 172.727 223.084 1.00 49.59  ? 2546 SER A C     1 
ATOM   7908  O  O     . SER A 1 2546 ? 246.309 173.668 223.358 1.00 49.61  ? 2546 SER A O     1 
ATOM   7909  C  CB    . SER A 1 2546 ? 245.895 170.598 223.703 1.00 41.18  ? 2546 SER A CB    1 
ATOM   7910  O  OG    . SER A 1 2546 ? 244.707 171.188 224.194 1.00 53.58  ? 2546 SER A OG    1 
ATOM   7911  N  N     . PRO A 1 2547 ? 247.883 172.776 222.029 1.00 52.32  ? 2547 PRO A N     1 
ATOM   7912  C  CA    . PRO A 1 2547 ? 247.901 173.965 221.174 1.00 48.66  ? 2547 PRO A CA    1 
ATOM   7913  C  C     . PRO A 1 2547 ? 246.576 174.165 220.460 1.00 50.67  ? 2547 PRO A C     1 
ATOM   7914  O  O     . PRO A 1 2547 ? 245.861 173.213 220.139 1.00 45.58  ? 2547 PRO A O     1 
ATOM   7915  C  CB    . PRO A 1 2547 ? 249.030 173.673 220.180 1.00 36.90  ? 2547 PRO A CB    1 
ATOM   7916  C  CG    . PRO A 1 2547 ? 249.166 172.194 220.185 1.00 40.25  ? 2547 PRO A CG    1 
ATOM   7917  C  CD    . PRO A 1 2547 ? 248.836 171.752 221.573 1.00 43.58  ? 2547 PRO A CD    1 
ATOM   7918  N  N     . TRP A 1 2548 ? 246.247 175.436 220.224 1.00 49.00  ? 2548 TRP A N     1 
ATOM   7919  C  CA    . TRP A 1 2548 ? 245.063 175.764 219.442 1.00 39.93  ? 2548 TRP A CA    1 
ATOM   7920  C  C     . TRP A 1 2548 ? 245.217 175.376 217.979 1.00 45.85  ? 2548 TRP A C     1 
ATOM   7921  O  O     . TRP A 1 2548 ? 244.207 175.185 217.295 1.00 51.77  ? 2548 TRP A O     1 
ATOM   7922  C  CB    . TRP A 1 2548 ? 244.760 177.258 219.545 1.00 39.58  ? 2548 TRP A CB    1 
ATOM   7923  C  CG    . TRP A 1 2548 ? 243.926 177.643 220.719 1.00 39.57  ? 2548 TRP A CG    1 
ATOM   7924  C  CD1   . TRP A 1 2548 ? 244.261 178.518 221.706 1.00 40.76  ? 2548 TRP A CD1   1 
ATOM   7925  C  CD2   . TRP A 1 2548 ? 242.606 177.181 221.023 1.00 39.89  ? 2548 TRP A CD2   1 
ATOM   7926  N  NE1   . TRP A 1 2548 ? 243.233 178.629 222.609 1.00 42.68  ? 2548 TRP A NE1   1 
ATOM   7927  C  CE2   . TRP A 1 2548 ? 242.205 177.817 222.211 1.00 36.94  ? 2548 TRP A CE2   1 
ATOM   7928  C  CE3   . TRP A 1 2548 ? 241.725 176.291 220.405 1.00 44.07  ? 2548 TRP A CE3   1 
ATOM   7929  C  CZ2   . TRP A 1 2548 ? 240.967 177.589 222.795 1.00 35.48  ? 2548 TRP A CZ2   1 
ATOM   7930  C  CZ3   . TRP A 1 2548 ? 240.499 176.067 220.986 1.00 44.92  ? 2548 TRP A CZ3   1 
ATOM   7931  C  CH2   . TRP A 1 2548 ? 240.132 176.710 222.169 1.00 40.17  ? 2548 TRP A CH2   1 
ATOM   7932  N  N     . GLN A 1 2549 ? 246.453 175.259 217.487 1.00 44.18  ? 2549 GLN A N     1 
ATOM   7933  C  CA    . GLN A 1 2549 ? 246.677 174.904 216.092 1.00 38.35  ? 2549 GLN A CA    1 
ATOM   7934  C  C     . GLN A 1 2549 ? 246.201 173.496 215.767 1.00 46.65  ? 2549 GLN A C     1 
ATOM   7935  O  O     . GLN A 1 2549 ? 245.934 173.202 214.598 1.00 57.86  ? 2549 GLN A O     1 
ATOM   7936  C  CB    . GLN A 1 2549 ? 248.156 175.044 215.744 1.00 42.59  ? 2549 GLN A CB    1 
ATOM   7937  C  CG    . GLN A 1 2549 ? 248.417 175.344 214.280 1.00 47.88  ? 2549 GLN A CG    1 
ATOM   7938  C  CD    . GLN A 1 2549 ? 248.114 176.783 213.918 1.00 55.68  ? 2549 GLN A CD    1 
ATOM   7939  O  OE1   . GLN A 1 2549 ? 247.222 177.059 213.118 1.00 54.26  ? 2549 GLN A OE1   1 
ATOM   7940  N  NE2   . GLN A 1 2549 ? 248.858 177.710 214.509 1.00 49.52  ? 2549 GLN A NE2   1 
ATOM   7941  N  N     . ALA A 1 2550 ? 246.097 172.618 216.766 1.00 40.29  ? 2550 ALA A N     1 
ATOM   7942  C  CA    . ALA A 1 2550 ? 245.502 171.309 216.537 1.00 42.36  ? 2550 ALA A CA    1 
ATOM   7943  C  C     . ALA A 1 2550 ? 244.018 171.406 216.216 1.00 43.93  ? 2550 ALA A C     1 
ATOM   7944  O  O     . ALA A 1 2550 ? 243.470 170.493 215.592 1.00 52.79  ? 2550 ALA A O     1 
ATOM   7945  C  CB    . ALA A 1 2550 ? 245.716 170.413 217.756 1.00 42.75  ? 2550 ALA A CB    1 
ATOM   7946  N  N     . LYS A 1 2551 ? 243.362 172.488 216.625 1.00 38.62  ? 2551 LYS A N     1 
ATOM   7947  C  CA    . LYS A 1 2551 ? 241.967 172.741 216.296 1.00 36.18  ? 2551 LYS A CA    1 
ATOM   7948  C  C     . LYS A 1 2551 ? 241.801 173.510 214.994 1.00 44.41  ? 2551 LYS A C     1 
ATOM   7949  O  O     . LYS A 1 2551 ? 240.667 173.821 214.617 1.00 53.72  ? 2551 LYS A O     1 
ATOM   7950  C  CB    . LYS A 1 2551 ? 241.287 173.514 217.430 1.00 47.13  ? 2551 LYS A CB    1 
ATOM   7951  C  CG    . LYS A 1 2551 ? 241.158 172.746 218.733 1.00 47.78  ? 2551 LYS A CG    1 
ATOM   7952  C  CD    . LYS A 1 2551 ? 240.031 171.734 218.665 1.00 49.14  ? 2551 LYS A CD    1 
ATOM   7953  C  CE    . LYS A 1 2551 ? 239.675 171.212 220.045 1.00 51.36  ? 2551 LYS A CE    1 
ATOM   7954  N  NZ    . LYS A 1 2551 ? 239.024 172.260 220.878 1.00 52.07  ? 2551 LYS A NZ    1 
ATOM   7955  N  N     . VAL A 1 2552 ? 242.895 173.825 214.307 1.00 47.35  ? 2552 VAL A N     1 
ATOM   7956  C  CA    . VAL A 1 2552 ? 242.852 174.583 213.059 1.00 46.38  ? 2552 VAL A CA    1 
ATOM   7957  C  C     . VAL A 1 2552 ? 243.225 173.655 211.909 1.00 49.12  ? 2552 VAL A C     1 
ATOM   7958  O  O     . VAL A 1 2552 ? 244.416 173.488 211.609 1.00 50.67  ? 2552 VAL A O     1 
ATOM   7959  C  CB    . VAL A 1 2552 ? 243.787 175.800 213.118 1.00 44.65  ? 2552 VAL A CB    1 
ATOM   7960  C  CG1   . VAL A 1 2552 ? 243.775 176.550 211.800 1.00 46.72  ? 2552 VAL A CG1   1 
ATOM   7961  C  CG2   . VAL A 1 2552 ? 243.385 176.719 214.255 1.00 46.80  ? 2552 VAL A CG2   1 
ATOM   7962  N  N     . PRO A 1 2553 ? 242.255 173.022 211.250 1.00 60.02  ? 2553 PRO A N     1 
ATOM   7963  C  CA    . PRO A 1 2553 ? 242.574 172.153 210.115 1.00 59.46  ? 2553 PRO A CA    1 
ATOM   7964  C  C     . PRO A 1 2553 ? 242.483 172.885 208.786 1.00 62.67  ? 2553 PRO A C     1 
ATOM   7965  O  O     . PRO A 1 2553 ? 241.600 173.713 208.557 1.00 69.49  ? 2553 PRO A O     1 
ATOM   7966  C  CB    . PRO A 1 2553 ? 241.497 171.067 210.216 1.00 58.46  ? 2553 PRO A CB    1 
ATOM   7967  C  CG    . PRO A 1 2553 ? 240.310 171.792 210.780 1.00 57.29  ? 2553 PRO A CG    1 
ATOM   7968  C  CD    . PRO A 1 2553 ? 240.823 172.967 211.591 1.00 55.95  ? 2553 PRO A CD    1 
ATOM   7969  N  N     . GLN A 1 2554 ? 243.421 172.571 207.896 1.00 68.01  ? 2554 GLN A N     1 
ATOM   7970  C  CA    . GLN A 1 2554 ? 243.369 173.095 206.537 1.00 71.20  ? 2554 GLN A CA    1 
ATOM   7971  C  C     . GLN A 1 2554 ? 242.205 172.440 205.806 1.00 73.05  ? 2554 GLN A C     1 
ATOM   7972  O  O     . GLN A 1 2554 ? 242.254 171.248 205.487 1.00 74.17  ? 2554 GLN A O     1 
ATOM   7973  C  CB    . GLN A 1 2554 ? 244.688 172.839 205.815 1.00 71.81  ? 2554 GLN A CB    1 
ATOM   7974  C  CG    . GLN A 1 2554 ? 244.750 173.435 204.417 1.00 74.81  ? 2554 GLN A CG    1 
ATOM   7975  C  CD    . GLN A 1 2554 ? 246.091 173.214 203.749 1.00 76.44  ? 2554 GLN A CD    1 
ATOM   7976  O  OE1   . GLN A 1 2554 ? 246.980 172.578 204.313 1.00 78.59  ? 2554 GLN A OE1   1 
ATOM   7977  N  NE2   . GLN A 1 2554 ? 246.244 173.739 202.539 1.00 72.06  ? 2554 GLN A NE2   1 
ATOM   7978  N  N     . ILE A 1 2555 ? 241.156 173.208 205.545 1.00 70.41  ? 2555 ILE A N     1 
ATOM   7979  C  CA    . ILE A 1 2555 ? 239.940 172.679 204.968 1.00 70.70  ? 2555 ILE A CA    1 
ATOM   7980  C  C     . ILE A 1 2555 ? 239.935 172.942 203.468 1.00 72.46  ? 2555 ILE A C     1 
ATOM   7981  O  O     . ILE A 1 2555 ? 240.754 173.690 202.940 1.00 73.10  ? 2555 ILE A O     1 
ATOM   7982  C  CB    . ILE A 1 2555 ? 238.677 173.275 205.632 1.00 69.66  ? 2555 ILE A CB    1 
ATOM   7983  C  CG1   . ILE A 1 2555 ? 238.623 174.787 205.411 1.00 66.22  ? 2555 ILE A CG1   1 
ATOM   7984  C  CG2   . ILE A 1 2555 ? 238.646 172.942 207.113 1.00 69.45  ? 2555 ILE A CG2   1 
ATOM   7985  C  CD1   . ILE A 1 2555 ? 237.311 175.414 205.820 1.00 68.06  ? 2555 ILE A CD1   1 
ATOM   7986  N  N     . GLU A 1 2556 ? 239.001 172.305 202.768 1.00 72.16  ? 2556 GLU A N     1 
ATOM   7987  C  CA    . GLU A 1 2556 ? 238.747 172.559 201.355 1.00 70.74  ? 2556 GLU A CA    1 
ATOM   7988  C  C     . GLU A 1 2556 ? 237.294 172.992 201.220 1.00 72.79  ? 2556 GLU A C     1 
ATOM   7989  O  O     . GLU A 1 2556 ? 236.380 172.183 201.413 1.00 72.04  ? 2556 GLU A O     1 
ATOM   7990  C  CB    . GLU A 1 2556 ? 239.035 171.321 200.508 1.00 67.92  ? 2556 GLU A CB    1 
ATOM   7991  C  CG    . GLU A 1 2556 ? 240.496 170.913 200.481 1.00 71.14  ? 2556 GLU A CG    1 
ATOM   7992  C  CD    . GLU A 1 2556 ? 241.372 171.929 199.779 1.00 78.29  ? 2556 GLU A CD    1 
ATOM   7993  O  OE1   . GLU A 1 2556 ? 240.883 172.590 198.839 1.00 78.91  ? 2556 GLU A OE1   1 
ATOM   7994  O  OE2   . GLU A 1 2556 ? 242.553 172.065 200.165 1.00 77.77  ? 2556 GLU A OE2   1 
ATOM   7995  N  N     . VAL A 1 2557 ? 237.081 174.267 200.899 1.00 72.19  ? 2557 VAL A N     1 
ATOM   7996  C  CA    . VAL A 1 2557 ? 235.729 174.783 200.740 1.00 67.45  ? 2557 VAL A CA    1 
ATOM   7997  C  C     . VAL A 1 2557 ? 235.130 174.252 199.445 1.00 69.29  ? 2557 VAL A C     1 
ATOM   7998  O  O     . VAL A 1 2557 ? 235.828 174.091 198.435 1.00 73.83  ? 2557 VAL A O     1 
ATOM   7999  C  CB    . VAL A 1 2557 ? 235.736 176.321 200.760 1.00 64.60  ? 2557 VAL A CB    1 
ATOM   8000  C  CG1   . VAL A 1 2557 ? 234.324 176.860 200.894 1.00 67.24  ? 2557 VAL A CG1   1 
ATOM   8001  C  CG2   . VAL A 1 2557 ? 236.608 176.829 201.890 1.00 64.17  ? 2557 VAL A CG2   1 
ATOM   8002  N  N     . GLU A 1 2558 ? 233.833 173.959 199.473 1.00 71.03  ? 2558 GLU A N     1 
ATOM   8003  C  CA    . GLU A 1 2558 ? 233.135 173.600 198.248 1.00 71.17  ? 2558 GLU A CA    1 
ATOM   8004  C  C     . GLU A 1 2558 ? 233.153 174.775 197.280 1.00 73.07  ? 2558 GLU A C     1 
ATOM   8005  O  O     . GLU A 1 2558 ? 233.103 175.940 197.682 1.00 79.92  ? 2558 GLU A O     1 
ATOM   8006  C  CB    . GLU A 1 2558 ? 231.696 173.184 198.548 1.00 72.31  ? 2558 GLU A CB    1 
ATOM   8007  C  CG    . GLU A 1 2558 ? 231.531 172.414 199.844 1.00 76.23  ? 2558 GLU A CG    1 
ATOM   8008  C  CD    . GLU A 1 2558 ? 230.132 171.861 200.017 1.00 79.53  ? 2558 GLU A CD    1 
ATOM   8009  O  OE1   . GLU A 1 2558 ? 229.167 172.547 199.617 1.00 78.87  ? 2558 GLU A OE1   1 
ATOM   8010  O  OE2   . GLU A 1 2558 ? 229.995 170.742 200.552 1.00 79.46  ? 2558 GLU A OE2   1 
ATOM   8011  N  N     . THR A 1 2559 ? 233.235 174.459 195.986 1.00 66.07  ? 2559 THR A N     1 
ATOM   8012  C  CA    . THR A 1 2559 ? 233.402 175.508 194.986 1.00 65.90  ? 2559 THR A CA    1 
ATOM   8013  C  C     . THR A 1 2559 ? 232.194 176.432 194.923 1.00 66.54  ? 2559 THR A C     1 
ATOM   8014  O  O     . THR A 1 2559 ? 232.313 177.574 194.469 1.00 71.96  ? 2559 THR A O     1 
ATOM   8015  C  CB    . THR A 1 2559 ? 233.672 174.889 193.615 1.00 67.79  ? 2559 THR A CB    1 
ATOM   8016  O  OG1   . THR A 1 2559 ? 233.775 175.928 192.634 1.00 67.66  ? 2559 THR A OG1   1 
ATOM   8017  C  CG2   . THR A 1 2559 ? 232.551 173.939 193.231 1.00 66.40  ? 2559 THR A CG2   1 
ATOM   8018  N  N     . HIS A 1 2560 ? 231.029 175.969 195.374 1.00 68.08  ? 2560 HIS A N     1 
ATOM   8019  C  CA    . HIS A 1 2560 ? 229.836 176.804 195.394 1.00 67.67  ? 2560 HIS A CA    1 
ATOM   8020  C  C     . HIS A 1 2560 ? 229.661 177.564 196.702 1.00 69.97  ? 2560 HIS A C     1 
ATOM   8021  O  O     . HIS A 1 2560 ? 228.725 178.362 196.814 1.00 75.13  ? 2560 HIS A O     1 
ATOM   8022  C  CB    . HIS A 1 2560 ? 228.589 175.955 195.122 1.00 69.72  ? 2560 HIS A CB    1 
ATOM   8023  C  CG    . HIS A 1 2560 ? 228.214 175.047 196.250 1.00 71.00  ? 2560 HIS A CG    1 
ATOM   8024  N  ND1   . HIS A 1 2560 ? 227.248 175.371 197.177 1.00 71.97  ? 2560 HIS A ND1   1 
ATOM   8025  C  CD2   . HIS A 1 2560 ? 228.671 173.820 196.597 1.00 70.73  ? 2560 HIS A CD2   1 
ATOM   8026  C  CE1   . HIS A 1 2560 ? 227.127 174.385 198.048 1.00 72.24  ? 2560 HIS A CE1   1 
ATOM   8027  N  NE2   . HIS A 1 2560 ? 227.980 173.432 197.719 1.00 73.96  ? 2560 HIS A NE2   1 
ATOM   8028  N  N     . LYS A 1 2561 ? 230.534 177.343 197.684 1.00 63.50  ? 2561 LYS A N     1 
ATOM   8029  C  CA    . LYS A 1 2561 ? 230.503 178.061 198.952 1.00 63.02  ? 2561 LYS A CA    1 
ATOM   8030  C  C     . LYS A 1 2561 ? 231.675 179.028 199.083 1.00 63.53  ? 2561 LYS A C     1 
ATOM   8031  O  O     . LYS A 1 2561 ? 232.083 179.372 200.193 1.00 67.95  ? 2561 LYS A O     1 
ATOM   8032  C  CB    . LYS A 1 2561 ? 230.492 177.082 200.124 1.00 64.15  ? 2561 LYS A CB    1 
ATOM   8033  C  CG    . LYS A 1 2561 ? 229.272 176.187 200.170 1.00 67.96  ? 2561 LYS A CG    1 
ATOM   8034  C  CD    . LYS A 1 2561 ? 228.013 177.005 200.388 1.00 68.16  ? 2561 LYS A CD    1 
ATOM   8035  C  CE    . LYS A 1 2561 ? 227.958 177.564 201.798 1.00 68.98  ? 2561 LYS A CE    1 
ATOM   8036  N  NZ    . LYS A 1 2561 ? 226.691 178.304 202.046 1.00 67.51  ? 2561 LYS A NZ    1 
ATOM   8037  N  N     . VAL A 1 2562 ? 232.220 179.474 197.956 1.00 55.21  ? 2562 VAL A N     1 
ATOM   8038  C  CA    . VAL A 1 2562 ? 233.412 180.315 197.951 1.00 50.72  ? 2562 VAL A CA    1 
ATOM   8039  C  C     . VAL A 1 2562 ? 233.038 181.706 198.441 1.00 56.21  ? 2562 VAL A C     1 
ATOM   8040  O  O     . VAL A 1 2562 ? 232.181 182.371 197.851 1.00 58.53  ? 2562 VAL A O     1 
ATOM   8041  C  CB    . VAL A 1 2562 ? 234.033 180.376 196.550 1.00 50.12  ? 2562 VAL A CB    1 
ATOM   8042  C  CG1   . VAL A 1 2562 ? 235.049 181.490 196.475 1.00 52.50  ? 2562 VAL A CG1   1 
ATOM   8043  C  CG2   . VAL A 1 2562 ? 234.664 179.052 196.196 1.00 53.41  ? 2562 VAL A CG2   1 
ATOM   8044  N  N     . ALA A 1 2563 ? 233.689 182.150 199.518 1.00 56.94  ? 2563 ALA A N     1 
ATOM   8045  C  CA    . ALA A 1 2563 ? 233.460 183.472 200.103 1.00 52.52  ? 2563 ALA A CA    1 
ATOM   8046  C  C     . ALA A 1 2563 ? 231.989 183.698 200.443 1.00 56.48  ? 2563 ALA A C     1 
ATOM   8047  O  O     . ALA A 1 2563 ? 231.468 184.804 200.287 1.00 54.31  ? 2563 ALA A O     1 
ATOM   8048  C  CB    . ALA A 1 2563 ? 233.974 184.584 199.186 1.00 42.46  ? 2563 ALA A CB    1 
ATOM   8049  N  N     . ALA A 1 2564 ? 231.312 182.651 200.904 1.00 65.50  ? 2564 ALA A N     1 
ATOM   8050  C  CA    . ALA A 1 2564 ? 229.921 182.779 201.298 1.00 66.08  ? 2564 ALA A CA    1 
ATOM   8051  C  C     . ALA A 1 2564 ? 229.819 183.497 202.643 1.00 70.96  ? 2564 ALA A C     1 
ATOM   8052  O  O     . ALA A 1 2564 ? 230.763 183.478 203.437 1.00 70.58  ? 2564 ALA A O     1 
ATOM   8053  C  CB    . ALA A 1 2564 ? 229.262 181.406 201.383 1.00 64.35  ? 2564 ALA A CB    1 
ATOM   8054  N  N     . PRO A 1 2565 ? 228.688 184.156 202.915 1.00 71.43  ? 2565 PRO A N     1 
ATOM   8055  C  CA    . PRO A 1 2565 ? 228.556 184.876 204.192 1.00 70.38  ? 2565 PRO A CA    1 
ATOM   8056  C  C     . PRO A 1 2565 ? 228.663 183.983 205.417 1.00 72.16  ? 2565 PRO A C     1 
ATOM   8057  O  O     . PRO A 1 2565 ? 229.141 184.441 206.462 1.00 72.13  ? 2565 PRO A O     1 
ATOM   8058  C  CB    . PRO A 1 2565 ? 227.169 185.527 204.086 1.00 69.53  ? 2565 PRO A CB    1 
ATOM   8059  C  CG    . PRO A 1 2565 ? 226.463 184.782 203.002 1.00 71.54  ? 2565 PRO A CG    1 
ATOM   8060  C  CD    . PRO A 1 2565 ? 227.521 184.360 202.043 1.00 69.29  ? 2565 PRO A CD    1 
ATOM   8061  N  N     . ASP A 1 2566 ? 228.267 182.715 205.293 1.00 63.62  ? 2566 ASP A N     1 
ATOM   8062  C  CA    . ASP A 1 2566 ? 228.263 181.810 206.474 1.00 63.97  ? 2566 ASP A CA    1 
ATOM   8063  C  C     . ASP A 1 2566 ? 229.515 180.928 206.478 1.00 66.52  ? 2566 ASP A C     1 
ATOM   8064  O  O     . ASP A 1 2566 ? 229.546 179.968 207.268 1.00 65.63  ? 2566 ASP A O     1 
ATOM   8065  C  CB    . ASP A 1 2566 ? 227.004 180.942 206.492 1.00 69.13  ? 2566 ASP A CB    1 
ATOM   8066  C  CG    . ASP A 1 2566 ? 226.867 180.074 205.253 1.00 73.69  ? 2566 ASP A CG    1 
ATOM   8067  O  OD1   . ASP A 1 2566 ? 226.805 180.642 204.145 1.00 75.44  ? 2566 ASP A OD1   1 
ATOM   8068  O  OD2   . ASP A 1 2566 ? 226.829 178.837 205.406 1.00 68.22  ? 2566 ASP A OD2   1 
ATOM   8069  N  N     . VAL A 1 2567 ? 230.503 181.237 205.634 1.00 61.68  ? 2567 VAL A N     1 
ATOM   8070  C  CA    . VAL A 1 2567 ? 231.716 180.373 205.525 1.00 62.51  ? 2567 VAL A CA    1 
ATOM   8071  C  C     . VAL A 1 2567 ? 232.866 181.031 206.292 1.00 58.20  ? 2567 VAL A C     1 
ATOM   8072  O  O     . VAL A 1 2567 ? 233.153 182.210 206.019 1.00 58.55  ? 2567 VAL A O     1 
ATOM   8073  C  CB    . VAL A 1 2567 ? 232.095 180.110 204.056 1.00 60.50  ? 2567 VAL A CB    1 
ATOM   8074  C  CG1   . VAL A 1 2567 ? 233.447 179.425 203.937 1.00 56.54  ? 2567 VAL A CG1   1 
ATOM   8075  C  CG2   . VAL A 1 2567 ? 231.024 179.306 203.338 1.00 59.70  ? 2567 VAL A CG2   1 
ATOM   8076  N  N     . VAL A 1 2568 ? 233.491 180.291 207.212 1.00 42.73  ? 2568 VAL A N     1 
ATOM   8077  C  CA    . VAL A 1 2568 ? 234.611 180.842 208.028 1.00 44.64  ? 2568 VAL A CA    1 
ATOM   8078  C  C     . VAL A 1 2568 ? 235.810 179.898 207.921 1.00 45.52  ? 2568 VAL A C     1 
ATOM   8079  O  O     . VAL A 1 2568 ? 235.766 178.824 208.543 1.00 50.41  ? 2568 VAL A O     1 
ATOM   8080  C  CB    . VAL A 1 2568 ? 234.190 181.035 209.496 1.00 43.69  ? 2568 VAL A CB    1 
ATOM   8081  C  CG1   . VAL A 1 2568 ? 235.310 181.640 210.328 1.00 39.53  ? 2568 VAL A CG1   1 
ATOM   8082  C  CG2   . VAL A 1 2568 ? 232.923 181.866 209.616 1.00 45.88  ? 2568 VAL A CG2   1 
ATOM   8083  N  N     . VAL A 1 2569 ? 236.840 180.288 207.167 1.00 39.48  ? 2569 VAL A N     1 
ATOM   8084  C  CA    . VAL A 1 2569 ? 238.077 179.456 207.099 1.00 36.05  ? 2569 VAL A CA    1 
ATOM   8085  C  C     . VAL A 1 2569 ? 238.666 179.396 208.510 1.00 44.45  ? 2569 VAL A C     1 
ATOM   8086  O  O     . VAL A 1 2569 ? 238.859 180.470 209.108 1.00 47.54  ? 2569 VAL A O     1 
ATOM   8087  C  CB    . VAL A 1 2569 ? 239.083 180.026 206.082 1.00 30.75  ? 2569 VAL A CB    1 
ATOM   8088  C  CG1   . VAL A 1 2569 ? 240.415 179.296 206.132 1.00 39.51  ? 2569 VAL A CG1   1 
ATOM   8089  C  CG2   . VAL A 1 2569 ? 238.518 180.026 204.671 1.00 29.82  ? 2569 VAL A CG2   1 
ATOM   8090  N  N     . PRO A 1 2570 ? 238.960 178.202 209.067 1.00 45.23  ? 2570 PRO A N     1 
ATOM   8091  C  CA    . PRO A 1 2570 ? 239.443 178.090 210.446 1.00 41.23  ? 2570 PRO A CA    1 
ATOM   8092  C  C     . PRO A 1 2570 ? 240.825 178.728 210.628 1.00 46.79  ? 2570 PRO A C     1 
ATOM   8093  O  O     . PRO A 1 2570 ? 241.753 178.287 209.985 1.00 49.05  ? 2570 PRO A O     1 
ATOM   8094  C  CB    . PRO A 1 2570 ? 239.549 176.576 210.665 1.00 43.06  ? 2570 PRO A CB    1 
ATOM   8095  C  CG    . PRO A 1 2570 ? 239.710 176.007 209.275 1.00 43.45  ? 2570 PRO A CG    1 
ATOM   8096  C  CD    . PRO A 1 2570 ? 238.863 176.905 208.400 1.00 47.04  ? 2570 PRO A CD    1 
ATOM   8097  N  N     . THR A 1 2571 ? 240.922 179.731 211.502 1.00 35.43  ? 2571 THR A N     1 
ATOM   8098  C  CA    . THR A 1 2571 ? 242.222 180.395 211.781 1.00 35.25  ? 2571 THR A CA    1 
ATOM   8099  C  C     . THR A 1 2571 ? 242.463 180.368 213.292 1.00 42.93  ? 2571 THR A C     1 
ATOM   8100  O  O     . THR A 1 2571 ? 241.475 180.252 214.036 1.00 53.82  ? 2571 THR A O     1 
ATOM   8101  C  CB    . THR A 1 2571 ? 242.241 181.827 211.235 1.00 40.89  ? 2571 THR A CB    1 
ATOM   8102  O  OG1   . THR A 1 2571 ? 241.326 182.608 212.003 1.00 50.24  ? 2571 THR A OG1   1 
ATOM   8103  C  CG2   . THR A 1 2571 ? 241.877 181.903 209.769 1.00 38.72  ? 2571 THR A CG2   1 
ATOM   8104  N  N     . LEU A 1 2572 ? 243.720 180.478 213.726 1.00 42.05  ? 2572 LEU A N     1 
ATOM   8105  C  CA    . LEU A 1 2572 ? 244.034 180.376 215.176 1.00 37.70  ? 2572 LEU A CA    1 
ATOM   8106  C  C     . LEU A 1 2572 ? 243.175 181.379 215.950 1.00 39.44  ? 2572 LEU A C     1 
ATOM   8107  O  O     . LEU A 1 2572 ? 242.622 180.994 216.990 1.00 43.91  ? 2572 LEU A O     1 
ATOM   8108  C  CB    . LEU A 1 2572 ? 245.526 180.656 215.383 1.00 41.49  ? 2572 LEU A CB    1 
ATOM   8109  C  CG    . LEU A 1 2572 ? 246.037 180.499 216.813 1.00 39.66  ? 2572 LEU A CG    1 
ATOM   8110  C  CD1   . LEU A 1 2572 ? 246.303 179.037 217.132 1.00 44.07  ? 2572 LEU A CD1   1 
ATOM   8111  C  CD2   . LEU A 1 2572 ? 247.294 181.325 217.029 1.00 40.67  ? 2572 LEU A CD2   1 
ATOM   8112  N  N     . ASP A 1 2573 ? 243.059 182.609 215.449 1.00 34.21  ? 2573 ASP A N     1 
ATOM   8113  C  CA    . ASP A 1 2573 ? 242.293 183.663 216.168 1.00 33.25  ? 2573 ASP A CA    1 
ATOM   8114  C  C     . ASP A 1 2573 ? 240.805 183.303 216.177 1.00 34.99  ? 2573 ASP A C     1 
ATOM   8115  O  O     . ASP A 1 2573 ? 240.147 183.563 217.196 1.00 48.98  ? 2573 ASP A O     1 
ATOM   8116  C  CB    . ASP A 1 2573 ? 242.556 185.042 215.560 1.00 44.61  ? 2573 ASP A CB    1 
ATOM   8117  C  CG    . ASP A 1 2573 ? 243.998 185.491 215.708 1.00 53.96  ? 2573 ASP A CG    1 
ATOM   8118  O  OD1   . ASP A 1 2573 ? 244.884 184.803 215.164 1.00 48.72  ? 2573 ASP A OD1   1 
ATOM   8119  O  OD2   . ASP A 1 2573 ? 244.225 186.521 216.374 1.00 58.50  ? 2573 ASP A OD2   1 
ATOM   8120  N  N     . THR A 1 2574 ? 240.298 182.740 215.079 1.00 28.46  ? 2574 THR A N     1 
ATOM   8121  C  CA    . THR A 1 2574 ? 238.871 182.331 215.003 1.00 31.74  ? 2574 THR A CA    1 
ATOM   8122  C  C     . THR A 1 2574 ? 238.598 181.230 216.032 1.00 38.50  ? 2574 THR A C     1 
ATOM   8123  O  O     . THR A 1 2574 ? 237.582 181.333 216.737 1.00 40.90  ? 2574 THR A O     1 
ATOM   8124  C  CB    . THR A 1 2574 ? 238.513 181.874 213.584 1.00 37.16  ? 2574 THR A CB    1 
ATOM   8125  O  OG1   . THR A 1 2574 ? 238.750 182.966 212.696 1.00 46.80  ? 2574 THR A OG1   1 
ATOM   8126  C  CG2   . THR A 1 2574 ? 237.078 181.416 213.456 1.00 37.81  ? 2574 THR A CG2   1 
ATOM   8127  N  N     . VAL A 1 2575 ? 239.478 180.228 216.120 1.00 36.65  ? 2575 VAL A N     1 
ATOM   8128  C  CA    . VAL A 1 2575 ? 239.255 179.080 217.048 1.00 32.66  ? 2575 VAL A CA    1 
ATOM   8129  C  C     . VAL A 1 2575 ? 239.397 179.571 218.492 1.00 33.41  ? 2575 VAL A C     1 
ATOM   8130  O  O     . VAL A 1 2575 ? 238.693 179.034 219.362 1.00 43.61  ? 2575 VAL A O     1 
ATOM   8131  C  CB    . VAL A 1 2575 ? 240.211 177.909 216.745 1.00 34.42  ? 2575 VAL A CB    1 
ATOM   8132  C  CG1   . VAL A 1 2575 ? 240.138 177.490 215.285 1.00 39.89  ? 2575 VAL A CG1   1 
ATOM   8133  C  CG2   . VAL A 1 2575 ? 241.644 178.217 217.144 1.00 37.73  ? 2575 VAL A CG2   1 
ATOM   8134  N  N     . ARG A 1 2576 ? 240.259 180.563 218.727 1.00 33.31  ? 2576 ARG A N     1 
ATOM   8135  C  CA    . ARG A 1 2576 ? 240.432 181.112 220.069 1.00 24.62  ? 2576 ARG A CA    1 
ATOM   8136  C  C     . ARG A 1 2576 ? 239.259 182.003 220.462 1.00 38.52  ? 2576 ARG A C     1 
ATOM   8137  O  O     . ARG A 1 2576 ? 238.699 181.863 221.559 1.00 51.87  ? 2576 ARG A O     1 
ATOM   8138  C  CB    . ARG A 1 2576 ? 241.742 181.890 220.146 1.00 30.55  ? 2576 ARG A CB    1 
ATOM   8139  C  CG    . ARG A 1 2576 ? 242.967 181.019 220.004 1.00 42.11  ? 2576 ARG A CG    1 
ATOM   8140  C  CD    . ARG A 1 2576 ? 244.233 181.755 220.378 1.00 36.22  ? 2576 ARG A CD    1 
ATOM   8141  N  NE    . ARG A 1 2576 ? 244.232 183.127 219.893 1.00 34.16  ? 2576 ARG A NE    1 
ATOM   8142  C  CZ    . ARG A 1 2576 ? 245.321 183.790 219.534 1.00 43.43  ? 2576 ARG A CZ    1 
ATOM   8143  N  NH1   . ARG A 1 2576 ? 246.519 183.236 219.599 1.00 40.13  ? 2576 ARG A NH1   1 
ATOM   8144  N  NH2   . ARG A 1 2576 ? 245.205 185.040 219.098 1.00 48.46  ? 2576 ARG A NH2   1 
ATOM   8145  N  N     . HIS A 1 2577 ? 238.863 182.915 219.571 1.00 35.04  ? 2577 HIS A N     1 
ATOM   8146  C  CA    . HIS A 1 2577 ? 237.759 183.814 219.868 1.00 24.73  ? 2577 HIS A CA    1 
ATOM   8147  C  C     . HIS A 1 2577 ? 236.434 183.071 219.931 1.00 32.45  ? 2577 HIS A C     1 
ATOM   8148  O  O     . HIS A 1 2577 ? 235.569 183.433 220.732 1.00 43.52  ? 2577 HIS A O     1 
ATOM   8149  C  CB    . HIS A 1 2577 ? 237.704 184.929 218.827 1.00 30.41  ? 2577 HIS A CB    1 
ATOM   8150  C  CG    . HIS A 1 2577 ? 238.905 185.822 218.839 1.00 41.77  ? 2577 HIS A CG    1 
ATOM   8151  N  ND1   . HIS A 1 2577 ? 239.288 186.570 217.747 1.00 42.46  ? 2577 HIS A ND1   1 
ATOM   8152  C  CD2   . HIS A 1 2577 ? 239.810 186.085 219.810 1.00 42.73  ? 2577 HIS A CD2   1 
ATOM   8153  C  CE1   . HIS A 1 2577 ? 240.376 187.256 218.046 1.00 41.92  ? 2577 HIS A CE1   1 
ATOM   8154  N  NE2   . HIS A 1 2577 ? 240.714 186.978 219.292 1.00 38.95  ? 2577 HIS A NE2   1 
ATOM   8155  N  N     . GLU A 1 2578 ? 236.252 182.035 219.109 1.00 31.74  ? 2578 GLU A N     1 
ATOM   8156  C  CA    . GLU A 1 2578 ? 235.038 181.233 219.200 1.00 32.48  ? 2578 GLU A CA    1 
ATOM   8157  C  C     . GLU A 1 2578 ? 234.939 180.543 220.551 1.00 34.89  ? 2578 GLU A C     1 
ATOM   8158  O  O     . GLU A 1 2578 ? 233.864 180.510 221.158 1.00 45.65  ? 2578 GLU A O     1 
ATOM   8159  C  CB    . GLU A 1 2578 ? 234.998 180.201 218.077 1.00 34.12  ? 2578 GLU A CB    1 
ATOM   8160  C  CG    . GLU A 1 2578 ? 234.521 180.734 216.744 1.00 36.85  ? 2578 GLU A CG    1 
ATOM   8161  C  CD    . GLU A 1 2578 ? 234.669 179.714 215.636 1.00 52.18  ? 2578 GLU A CD    1 
ATOM   8162  O  OE1   . GLU A 1 2578 ? 234.922 178.531 215.949 1.00 47.75  ? 2578 GLU A OE1   1 
ATOM   8163  O  OE2   . GLU A 1 2578 ? 234.538 180.090 214.454 1.00 52.04  ? 2578 GLU A OE2   1 
ATOM   8164  N  N     . ALA A 1 2579 ? 236.048 179.984 221.040 1.00 28.17  ? 2579 ALA A N     1 
ATOM   8165  C  CA    . ALA A 1 2579 ? 236.024 179.341 222.350 1.00 23.63  ? 2579 ALA A CA    1 
ATOM   8166  C  C     . ALA A 1 2579 ? 235.736 180.347 223.457 1.00 32.16  ? 2579 ALA A C     1 
ATOM   8167  O  O     . ALA A 1 2579 ? 234.939 180.072 224.365 1.00 35.85  ? 2579 ALA A O     1 
ATOM   8168  C  CB    . ALA A 1 2579 ? 237.348 178.628 222.608 1.00 21.84  ? 2579 ALA A CB    1 
ATOM   8169  N  N     . LEU A 1 2580 ? 236.370 181.519 223.397 1.00 41.82  ? 2580 LEU A N     1 
ATOM   8170  C  CA    . LEU A 1 2580 ? 236.122 182.539 224.412 1.00 33.62  ? 2580 LEU A CA    1 
ATOM   8171  C  C     . LEU A 1 2580 ? 234.667 182.999 224.392 1.00 33.42  ? 2580 LEU A C     1 
ATOM   8172  O  O     . LEU A 1 2580 ? 234.034 183.147 225.448 1.00 38.67  ? 2580 LEU A O     1 
ATOM   8173  C  CB    . LEU A 1 2580 ? 237.069 183.718 224.196 1.00 23.08  ? 2580 LEU A CB    1 
ATOM   8174  C  CG    . LEU A 1 2580 ? 237.049 184.848 225.219 1.00 33.49  ? 2580 LEU A CG    1 
ATOM   8175  C  CD1   . LEU A 1 2580 ? 237.478 184.336 226.576 1.00 40.92  ? 2580 LEU A CD1   1 
ATOM   8176  C  CD2   . LEU A 1 2580 ? 237.949 185.979 224.761 1.00 31.82  ? 2580 LEU A CD2   1 
ATOM   8177  N  N     . LEU A 1 2581 ? 234.115 183.219 223.197 1.00 31.35  ? 2581 LEU A N     1 
ATOM   8178  C  CA    . LEU A 1 2581 ? 232.730 183.657 223.087 1.00 25.64  ? 2581 LEU A CA    1 
ATOM   8179  C  C     . LEU A 1 2581 ? 231.767 182.571 223.539 1.00 29.46  ? 2581 LEU A C     1 
ATOM   8180  O  O     . LEU A 1 2581 ? 230.727 182.873 224.125 1.00 38.56  ? 2581 LEU A O     1 
ATOM   8181  C  CB    . LEU A 1 2581 ? 232.420 184.085 221.654 1.00 33.89  ? 2581 LEU A CB    1 
ATOM   8182  C  CG    . LEU A 1 2581 ? 233.052 185.390 221.174 1.00 31.26  ? 2581 LEU A CG    1 
ATOM   8183  C  CD1   . LEU A 1 2581 ? 232.372 185.868 219.909 1.00 39.82  ? 2581 LEU A CD1   1 
ATOM   8184  C  CD2   . LEU A 1 2581 ? 232.983 186.451 222.253 1.00 38.15  ? 2581 LEU A CD2   1 
ATOM   8185  N  N     . TYR A 1 2582 ? 232.085 181.303 223.272 1.00 29.23  ? 2582 TYR A N     1 
ATOM   8186  C  CA    . TYR A 1 2582 ? 231.258 180.220 223.791 1.00 25.11  ? 2582 TYR A CA    1 
ATOM   8187  C  C     . TYR A 1 2582 ? 231.268 180.215 225.312 1.00 32.84  ? 2582 TYR A C     1 
ATOM   8188  O  O     . TYR A 1 2582 ? 230.222 180.043 225.948 1.00 38.42  ? 2582 TYR A O     1 
ATOM   8189  C  CB    . TYR A 1 2582 ? 231.741 178.876 223.246 1.00 29.87  ? 2582 TYR A CB    1 
ATOM   8190  C  CG    . TYR A 1 2582 ? 230.831 177.705 223.561 1.00 40.23  ? 2582 TYR A CG    1 
ATOM   8191  C  CD1   . TYR A 1 2582 ? 230.845 177.101 224.813 1.00 38.87  ? 2582 TYR A CD1   1 
ATOM   8192  C  CD2   . TYR A 1 2582 ? 229.967 177.198 222.603 1.00 44.21  ? 2582 TYR A CD2   1 
ATOM   8193  C  CE1   . TYR A 1 2582 ? 230.017 176.037 225.102 1.00 40.45  ? 2582 TYR A CE1   1 
ATOM   8194  C  CE2   . TYR A 1 2582 ? 229.140 176.129 222.883 1.00 42.50  ? 2582 TYR A CE2   1 
ATOM   8195  C  CZ    . TYR A 1 2582 ? 229.167 175.555 224.134 1.00 45.52  ? 2582 TYR A CZ    1 
ATOM   8196  O  OH    . TYR A 1 2582 ? 228.342 174.491 224.416 1.00 46.79  ? 2582 TYR A OH    1 
ATOM   8197  N  N     . THR A 1 2583 ? 232.444 180.410 225.912 1.00 40.10  ? 2583 THR A N     1 
ATOM   8198  C  CA    . THR A 1 2583 ? 232.529 180.445 227.368 1.00 24.83  ? 2583 THR A CA    1 
ATOM   8199  C  C     . THR A 1 2583 ? 231.692 181.580 227.942 1.00 31.56  ? 2583 THR A C     1 
ATOM   8200  O  O     . THR A 1 2583 ? 230.980 181.397 228.936 1.00 43.42  ? 2583 THR A O     1 
ATOM   8201  C  CB    . THR A 1 2583 ? 233.988 180.579 227.806 1.00 30.73  ? 2583 THR A CB    1 
ATOM   8202  O  OG1   . THR A 1 2583 ? 234.667 179.334 227.603 1.00 42.76  ? 2583 THR A OG1   1 
ATOM   8203  C  CG2   . THR A 1 2583 ? 234.074 180.954 229.269 1.00 35.39  ? 2583 THR A CG2   1 
ATOM   8204  N  N     . TRP A 1 2584 ? 231.749 182.759 227.320 1.00 38.99  ? 2584 TRP A N     1 
ATOM   8205  C  CA    . TRP A 1 2584 ? 231.008 183.895 227.863 1.00 28.48  ? 2584 TRP A CA    1 
ATOM   8206  C  C     . TRP A 1 2584 ? 229.512 183.804 227.576 1.00 25.38  ? 2584 TRP A C     1 
ATOM   8207  O  O     . TRP A 1 2584 ? 228.698 184.256 228.387 1.00 37.67  ? 2584 TRP A O     1 
ATOM   8208  C  CB    . TRP A 1 2584 ? 231.571 185.205 227.319 1.00 33.01  ? 2584 TRP A CB    1 
ATOM   8209  C  CG    . TRP A 1 2584 ? 232.881 185.583 227.919 1.00 36.68  ? 2584 TRP A CG    1 
ATOM   8210  C  CD1   . TRP A 1 2584 ? 233.406 185.134 229.092 1.00 22.98  ? 2584 TRP A CD1   1 
ATOM   8211  C  CD2   . TRP A 1 2584 ? 233.834 186.502 227.379 1.00 33.24  ? 2584 TRP A CD2   1 
ATOM   8212  N  NE1   . TRP A 1 2584 ? 234.631 185.708 229.314 1.00 28.05  ? 2584 TRP A NE1   1 
ATOM   8213  C  CE2   . TRP A 1 2584 ? 234.917 186.554 228.275 1.00 33.95  ? 2584 TRP A CE2   1 
ATOM   8214  C  CE3   . TRP A 1 2584 ? 233.878 187.284 226.222 1.00 28.01  ? 2584 TRP A CE3   1 
ATOM   8215  C  CZ2   . TRP A 1 2584 ? 236.030 187.357 228.053 1.00 32.31  ? 2584 TRP A CZ2   1 
ATOM   8216  C  CZ3   . TRP A 1 2584 ? 234.982 188.078 226.003 1.00 37.24  ? 2584 TRP A CZ3   1 
ATOM   8217  C  CH2   . TRP A 1 2584 ? 236.044 188.110 226.913 1.00 38.66  ? 2584 TRP A CH2   1 
ATOM   8218  N  N     . LEU A 1 2585 ? 229.126 183.234 226.432 1.00 36.46  ? 2585 LEU A N     1 
ATOM   8219  C  CA    . LEU A 1 2585 ? 227.714 183.148 226.077 1.00 33.05  ? 2585 LEU A CA    1 
ATOM   8220  C  C     . LEU A 1 2585 ? 227.009 182.049 226.856 1.00 38.91  ? 2585 LEU A C     1 
ATOM   8221  O  O     . LEU A 1 2585 ? 225.851 182.212 227.254 1.00 46.41  ? 2585 LEU A O     1 
ATOM   8222  C  CB    . LEU A 1 2585 ? 227.563 182.908 224.575 1.00 31.00  ? 2585 LEU A CB    1 
ATOM   8223  C  CG    . LEU A 1 2585 ? 227.815 184.070 223.614 1.00 34.71  ? 2585 LEU A CG    1 
ATOM   8224  C  CD1   . LEU A 1 2585 ? 228.037 183.548 222.208 1.00 29.97  ? 2585 LEU A CD1   1 
ATOM   8225  C  CD2   . LEU A 1 2585 ? 226.661 185.048 223.639 1.00 36.91  ? 2585 LEU A CD2   1 
ATOM   8226  N  N     . ALA A 1 2586 ? 227.687 180.918 227.079 1.00 39.63  ? 2586 ALA A N     1 
ATOM   8227  C  CA    . ALA A 1 2586 ? 227.068 179.810 227.798 1.00 37.51  ? 2586 ALA A CA    1 
ATOM   8228  C  C     . ALA A 1 2586 ? 226.671 180.207 229.213 1.00 45.24  ? 2586 ALA A C     1 
ATOM   8229  O  O     . ALA A 1 2586 ? 225.741 179.625 229.781 1.00 48.11  ? 2586 ALA A O     1 
ATOM   8230  C  CB    . ALA A 1 2586 ? 228.013 178.612 227.828 1.00 37.28  ? 2586 ALA A CB    1 
ATOM   8231  N  N     . GLU A 1 2587 ? 227.360 181.186 229.794 1.00 41.46  ? 2587 GLU A N     1 
ATOM   8232  C  CA    . GLU A 1 2587 ? 226.982 181.740 231.085 1.00 40.74  ? 2587 GLU A CA    1 
ATOM   8233  C  C     . GLU A 1 2587 ? 225.940 182.842 230.966 1.00 39.04  ? 2587 GLU A C     1 
ATOM   8234  O  O     . GLU A 1 2587 ? 225.542 183.405 231.991 1.00 48.05  ? 2587 GLU A O     1 
ATOM   8235  C  CB    . GLU A 1 2587 ? 228.219 182.281 231.807 1.00 38.44  ? 2587 GLU A CB    1 
ATOM   8236  C  CG    . GLU A 1 2587 ? 229.293 181.240 232.063 1.00 43.36  ? 2587 GLU A CG    1 
ATOM   8237  C  CD    . GLU A 1 2587 ? 228.818 180.126 232.974 1.00 58.46  ? 2587 GLU A CD    1 
ATOM   8238  O  OE1   . GLU A 1 2587 ? 228.146 180.426 233.983 1.00 54.65  ? 2587 GLU A OE1   1 
ATOM   8239  O  OE2   . GLU A 1 2587 ? 229.118 178.950 232.682 1.00 55.32  ? 2587 GLU A OE2   1 
ATOM   8240  N  N     . HIS A 1 2588 ? 225.506 183.165 229.746 1.00 34.74  ? 2588 HIS A N     1 
ATOM   8241  C  CA    . HIS A 1 2588 ? 224.550 184.243 229.487 1.00 39.57  ? 2588 HIS A CA    1 
ATOM   8242  C  C     . HIS A 1 2588 ? 225.080 185.589 229.967 1.00 42.66  ? 2588 HIS A C     1 
ATOM   8243  O  O     . HIS A 1 2588 ? 224.310 186.486 230.314 1.00 40.22  ? 2588 HIS A O     1 
ATOM   8244  C  CB    . HIS A 1 2588 ? 223.186 183.940 230.113 1.00 32.65  ? 2588 HIS A CB    1 
ATOM   8245  C  CG    . HIS A 1 2588 ? 222.695 182.555 229.836 1.00 39.49  ? 2588 HIS A CG    1 
ATOM   8246  N  ND1   . HIS A 1 2588 ? 222.684 182.008 228.572 1.00 41.94  ? 2588 HIS A ND1   1 
ATOM   8247  C  CD2   . HIS A 1 2588 ? 222.208 181.600 230.662 1.00 44.18  ? 2588 HIS A CD2   1 
ATOM   8248  C  CE1   . HIS A 1 2588 ? 222.208 180.778 228.630 1.00 41.53  ? 2588 HIS A CE1   1 
ATOM   8249  N  NE2   . HIS A 1 2588 ? 221.910 180.506 229.887 1.00 48.38  ? 2588 HIS A NE2   1 
ATOM   8250  N  N     . LYS A 1 2589 ? 226.394 185.730 229.982 1.00 32.32  ? 2589 LYS A N     1 
ATOM   8251  C  CA    . LYS A 1 2589 ? 227.033 186.978 230.374 1.00 32.15  ? 2589 LYS A CA    1 
ATOM   8252  C  C     . LYS A 1 2589 ? 227.034 187.949 229.199 1.00 28.52  ? 2589 LYS A C     1 
ATOM   8253  O  O     . LYS A 1 2589 ? 227.321 187.543 228.069 1.00 35.61  ? 2589 LYS A O     1 
ATOM   8254  C  CB    . LYS A 1 2589 ? 228.463 186.711 230.839 1.00 31.49  ? 2589 LYS A CB    1 
ATOM   8255  C  CG    . LYS A 1 2589 ? 229.237 187.946 231.251 1.00 31.07  ? 2589 LYS A CG    1 
ATOM   8256  C  CD    . LYS A 1 2589 ? 229.223 188.125 232.757 1.00 38.64  ? 2589 LYS A CD    1 
ATOM   8257  C  CE    . LYS A 1 2589 ? 230.305 189.087 233.208 1.00 38.49  ? 2589 LYS A CE    1 
ATOM   8258  N  NZ    . LYS A 1 2589 ? 230.032 189.627 234.567 1.00 35.88  ? 2589 LYS A NZ    1 
ATOM   8259  N  N     . PRO A 1 2590 ? 226.704 189.221 229.416 1.00 27.03  ? 2590 PRO A N     1 
ATOM   8260  C  CA    . PRO A 1 2590 ? 226.836 190.204 228.337 1.00 21.46  ? 2590 PRO A CA    1 
ATOM   8261  C  C     . PRO A 1 2590 ? 228.294 190.372 227.945 1.00 30.69  ? 2590 PRO A C     1 
ATOM   8262  O  O     . PRO A 1 2590 ? 229.200 190.211 228.761 1.00 41.66  ? 2590 PRO A O     1 
ATOM   8263  C  CB    . PRO A 1 2590 ? 226.267 191.486 228.952 1.00 23.84  ? 2590 PRO A CB    1 
ATOM   8264  C  CG    . PRO A 1 2590 ? 226.394 191.287 230.418 1.00 30.61  ? 2590 PRO A CG    1 
ATOM   8265  C  CD    . PRO A 1 2590 ? 226.175 189.826 230.648 1.00 31.09  ? 2590 PRO A CD    1 
ATOM   8266  N  N     . LEU A 1 2591 ? 228.519 190.687 226.673 1.00 22.70  ? 2591 LEU A N     1 
ATOM   8267  C  CA    . LEU A 1 2591 ? 229.879 190.796 226.173 1.00 17.90  ? 2591 LEU A CA    1 
ATOM   8268  C  C     . LEU A 1 2591 ? 229.914 191.799 225.032 1.00 20.30  ? 2591 LEU A C     1 
ATOM   8269  O  O     . LEU A 1 2591 ? 228.894 192.097 224.408 1.00 29.02  ? 2591 LEU A O     1 
ATOM   8270  C  CB    . LEU A 1 2591 ? 230.420 189.426 225.739 1.00 24.61  ? 2591 LEU A CB    1 
ATOM   8271  C  CG    . LEU A 1 2591 ? 229.748 188.658 224.597 1.00 22.64  ? 2591 LEU A CG    1 
ATOM   8272  C  CD1   . LEU A 1 2591 ? 230.331 189.033 223.251 1.00 27.95  ? 2591 LEU A CD1   1 
ATOM   8273  C  CD2   . LEU A 1 2591 ? 229.848 187.165 224.820 1.00 26.39  ? 2591 LEU A CD2   1 
ATOM   8274  N  N     . VAL A 1 2592 ? 231.107 192.325 224.775 1.00 25.01  ? 2592 VAL A N     1 
ATOM   8275  C  CA    . VAL A 1 2592 ? 231.330 193.311 223.727 1.00 26.31  ? 2592 VAL A CA    1 
ATOM   8276  C  C     . VAL A 1 2592 ? 232.523 192.864 222.896 1.00 31.92  ? 2592 VAL A C     1 
ATOM   8277  O  O     . VAL A 1 2592 ? 233.570 192.509 223.447 1.00 39.01  ? 2592 VAL A O     1 
ATOM   8278  C  CB    . VAL A 1 2592 ? 231.565 194.718 224.309 1.00 27.30  ? 2592 VAL A CB    1 
ATOM   8279  C  CG1   . VAL A 1 2592 ? 232.236 195.612 223.290 1.00 21.64  ? 2592 VAL A CG1   1 
ATOM   8280  C  CG2   . VAL A 1 2592 ? 230.252 195.330 224.761 1.00 30.15  ? 2592 VAL A CG2   1 
ATOM   8281  N  N     . LEU A 1 2593 ? 232.361 192.866 221.576 1.00 36.10  ? 2593 LEU A N     1 
ATOM   8282  C  CA    . LEU A 1 2593 ? 233.459 192.614 220.654 1.00 22.63  ? 2593 LEU A CA    1 
ATOM   8283  C  C     . LEU A 1 2593 ? 233.942 193.953 220.117 1.00 28.36  ? 2593 LEU A C     1 
ATOM   8284  O  O     . LEU A 1 2593 ? 233.163 194.705 219.527 1.00 44.91  ? 2593 LEU A O     1 
ATOM   8285  C  CB    . LEU A 1 2593 ? 233.029 191.704 219.504 1.00 23.36  ? 2593 LEU A CB    1 
ATOM   8286  C  CG    . LEU A 1 2593 ? 232.623 190.265 219.811 1.00 29.18  ? 2593 LEU A CG    1 
ATOM   8287  C  CD1   . LEU A 1 2593 ? 231.118 190.167 219.945 1.00 28.28  ? 2593 LEU A CD1   1 
ATOM   8288  C  CD2   . LEU A 1 2593 ? 233.128 189.327 218.736 1.00 29.80  ? 2593 LEU A CD2   1 
ATOM   8289  N  N     . CYS A 1 2594 ? 235.217 194.250 220.324 1.00 28.78  ? 2594 CYS A N     1 
ATOM   8290  C  CA    . CYS A 1 2594 ? 235.807 195.500 219.877 1.00 21.06  ? 2594 CYS A CA    1 
ATOM   8291  C  C     . CYS A 1 2594 ? 236.856 195.221 218.812 1.00 35.08  ? 2594 CYS A C     1 
ATOM   8292  O  O     . CYS A 1 2594 ? 237.533 194.192 218.838 1.00 49.11  ? 2594 CYS A O     1 
ATOM   8293  C  CB    . CYS A 1 2594 ? 236.435 196.263 221.046 1.00 28.44  ? 2594 CYS A CB    1 
ATOM   8294  S  SG    . CYS A 1 2594 ? 236.643 198.032 220.762 1.00 52.09  ? 2594 CYS A SG    1 
ATOM   8295  N  N     . GLY A 1 2595 ? 236.973 196.127 217.846 1.00 26.72  ? 2595 GLY A N     1 
ATOM   8296  C  CA    . GLY A 1 2595 ? 238.003 195.952 216.810 1.00 19.18  ? 2595 GLY A CA    1 
ATOM   8297  C  C     . GLY A 1 2595 ? 237.728 196.799 215.586 1.00 29.67  ? 2595 GLY A C     1 
ATOM   8298  O  O     . GLY A 1 2595 ? 236.636 197.383 215.498 1.00 41.64  ? 2595 GLY A O     1 
ATOM   8299  N  N     . PRO A 1 2596 ? 238.676 196.878 214.631 1.00 37.63  ? 2596 PRO A N     1 
ATOM   8300  C  CA    . PRO A 1 2596 ? 238.502 197.703 213.444 1.00 26.96  ? 2596 PRO A CA    1 
ATOM   8301  C  C     . PRO A 1 2596 ? 237.296 197.197 212.646 1.00 34.11  ? 2596 PRO A C     1 
ATOM   8302  O  O     . PRO A 1 2596 ? 236.951 196.043 212.792 1.00 47.29  ? 2596 PRO A O     1 
ATOM   8303  C  CB    . PRO A 1 2596 ? 239.787 197.445 212.654 1.00 22.12  ? 2596 PRO A CB    1 
ATOM   8304  C  CG    . PRO A 1 2596 ? 240.786 196.975 213.683 1.00 29.16  ? 2596 PRO A CG    1 
ATOM   8305  C  CD    . PRO A 1 2596 ? 239.957 196.173 214.659 1.00 37.76  ? 2596 PRO A CD    1 
ATOM   8306  N  N     . PRO A 1 2597 ? 236.640 198.033 211.815 1.00 31.74  ? 2597 PRO A N     1 
ATOM   8307  C  CA    . PRO A 1 2597 ? 235.537 197.561 210.977 1.00 31.41  ? 2597 PRO A CA    1 
ATOM   8308  C  C     . PRO A 1 2597 ? 236.026 196.512 209.969 1.00 31.99  ? 2597 PRO A C     1 
ATOM   8309  O  O     . PRO A 1 2597 ? 237.012 196.764 209.314 1.00 43.19  ? 2597 PRO A O     1 
ATOM   8310  C  CB    . PRO A 1 2597 ? 235.065 198.835 210.263 1.00 31.05  ? 2597 PRO A CB    1 
ATOM   8311  C  CG    . PRO A 1 2597 ? 236.253 199.768 210.324 1.00 28.52  ? 2597 PRO A CG    1 
ATOM   8312  C  CD    . PRO A 1 2597 ? 236.921 199.458 211.645 1.00 37.58  ? 2597 PRO A CD    1 
ATOM   8313  N  N     . GLY A 1 2598 ? 235.329 195.377 209.868 1.00 22.26  ? 2598 GLY A N     1 
ATOM   8314  C  CA    . GLY A 1 2598 ? 235.733 194.301 208.942 1.00 22.77  ? 2598 GLY A CA    1 
ATOM   8315  C  C     . GLY A 1 2598 ? 236.678 193.312 209.599 1.00 33.41  ? 2598 GLY A C     1 
ATOM   8316  O  O     . GLY A 1 2598 ? 237.107 192.368 208.913 1.00 37.73  ? 2598 GLY A O     1 
ATOM   8317  N  N     . SER A 1 2599 ? 236.984 193.513 210.883 1.00 32.95  ? 2599 SER A N     1 
ATOM   8318  C  CA    . SER A 1 2599 ? 237.916 192.619 211.616 1.00 23.29  ? 2599 SER A CA    1 
ATOM   8319  C  C     . SER A 1 2599 ? 237.354 191.195 211.658 1.00 32.58  ? 2599 SER A C     1 
ATOM   8320  O  O     . SER A 1 2599 ? 238.159 190.247 211.641 1.00 40.19  ? 2599 SER A O     1 
ATOM   8321  C  CB    . SER A 1 2599 ? 238.179 193.148 212.997 1.00 24.16  ? 2599 SER A CB    1 
ATOM   8322  O  OG    . SER A 1 2599 ? 236.963 193.322 213.708 1.00 31.43  ? 2599 SER A OG    1 
ATOM   8323  N  N     . GLY A 1 2600 ? 236.027 191.056 211.713 1.00 36.16  ? 2600 GLY A N     1 
ATOM   8324  C  CA    . GLY A 1 2600 ? 235.394 189.725 211.755 1.00 23.21  ? 2600 GLY A CA    1 
ATOM   8325  C  C     . GLY A 1 2600 ? 234.693 189.484 213.077 1.00 27.84  ? 2600 GLY A C     1 
ATOM   8326  O  O     . GLY A 1 2600 ? 234.648 188.323 213.513 1.00 37.52  ? 2600 GLY A O     1 
ATOM   8327  N  N     . LYS A 1 2601 ? 234.176 190.545 213.699 1.00 24.86  ? 2601 LYS A N     1 
ATOM   8328  C  CA    . LYS A 1 2601 ? 233.502 190.423 215.017 1.00 18.12  ? 2601 LYS A CA    1 
ATOM   8329  C  C     . LYS A 1 2601 ? 232.173 189.684 214.843 1.00 27.50  ? 2601 LYS A C     1 
ATOM   8330  O  O     . LYS A 1 2601 ? 231.926 188.737 215.608 1.00 43.43  ? 2601 LYS A O     1 
ATOM   8331  C  CB    . LYS A 1 2601 ? 233.297 191.814 215.623 1.00 24.48  ? 2601 LYS A CB    1 
ATOM   8332  C  CG    . LYS A 1 2601 ? 234.574 192.567 215.968 1.00 30.60  ? 2601 LYS A CG    1 
ATOM   8333  C  CD    . LYS A 1 2601 ? 234.320 193.968 216.478 1.00 28.42  ? 2601 LYS A CD    1 
ATOM   8334  C  CE    . LYS A 1 2601 ? 233.802 194.904 215.406 1.00 22.83  ? 2601 LYS A CE    1 
ATOM   8335  N  NZ    . LYS A 1 2601 ? 234.797 195.099 214.326 1.00 32.25  ? 2601 LYS A NZ    1 
ATOM   8336  N  N     . THR A 1 2602 ? 231.362 190.092 213.865 1.00 35.91  ? 2602 THR A N     1 
ATOM   8337  C  CA    . THR A 1 2602 ? 230.043 189.449 213.615 1.00 27.39  ? 2602 THR A CA    1 
ATOM   8338  C  C     . THR A 1 2602 ? 230.249 188.022 213.100 1.00 27.37  ? 2602 THR A C     1 
ATOM   8339  O  O     . THR A 1 2602 ? 229.483 187.136 213.511 1.00 42.50  ? 2602 THR A O     1 
ATOM   8340  C  CB    . THR A 1 2602 ? 229.203 190.269 212.629 1.00 30.23  ? 2602 THR A CB    1 
ATOM   8341  O  OG1   . THR A 1 2602 ? 229.128 191.608 213.119 1.00 42.61  ? 2602 THR A OG1   1 
ATOM   8342  C  CG2   . THR A 1 2602 ? 227.810 189.712 212.438 1.00 33.94  ? 2602 THR A CG2   1 
ATOM   8343  N  N     . MET A 1 2603 ? 231.242 187.814 212.235 1.00 32.25  ? 2603 MET A N     1 
ATOM   8344  C  CA    . MET A 1 2603 ? 231.542 186.445 211.746 1.00 34.14  ? 2603 MET A CA    1 
ATOM   8345  C  C     . MET A 1 2603 ? 231.867 185.563 212.953 1.00 34.72  ? 2603 MET A C     1 
ATOM   8346  O  O     . MET A 1 2603 ? 231.340 184.440 213.021 1.00 37.06  ? 2603 MET A O     1 
ATOM   8347  C  CB    . MET A 1 2603 ? 232.740 186.454 210.793 1.00 31.94  ? 2603 MET A CB    1 
ATOM   8348  C  CG    . MET A 1 2603 ? 233.488 185.140 210.761 1.00 32.58  ? 2603 MET A CG    1 
ATOM   8349  S  SD    . MET A 1 2603 ? 235.084 185.285 209.931 1.00 51.55  ? 2603 MET A SD    1 
ATOM   8350  C  CE    . MET A 1 2603 ? 236.144 185.654 211.327 1.00 37.45  ? 2603 MET A CE    1 
ATOM   8351  N  N     . THR A 1 2604 ? 232.695 186.069 213.870 1.00 35.63  ? 2604 THR A N     1 
ATOM   8352  C  CA    . THR A 1 2604 ? 233.073 185.293 215.081 1.00 30.80  ? 2604 THR A CA    1 
ATOM   8353  C  C     . THR A 1 2604 ? 231.824 185.054 215.934 1.00 28.84  ? 2604 THR A C     1 
ATOM   8354  O  O     . THR A 1 2604 ? 231.632 183.909 216.378 1.00 44.33  ? 2604 THR A O     1 
ATOM   8355  C  CB    . THR A 1 2604 ? 234.176 186.000 215.875 1.00 33.57  ? 2604 THR A CB    1 
ATOM   8356  O  OG1   . THR A 1 2604 ? 235.301 186.173 215.013 1.00 37.75  ? 2604 THR A OG1   1 
ATOM   8357  C  CG2   . THR A 1 2604 ? 234.593 185.231 217.109 1.00 32.92  ? 2604 THR A CG2   1 
ATOM   8358  N  N     . LEU A 1 2605 ? 231.013 186.091 216.152 1.00 30.97  ? 2605 LEU A N     1 
ATOM   8359  C  CA    . LEU A 1 2605 ? 229.843 185.902 217.004 1.00 30.04  ? 2605 LEU A CA    1 
ATOM   8360  C  C     . LEU A 1 2605 ? 228.875 184.892 216.402 1.00 36.03  ? 2605 LEU A C     1 
ATOM   8361  O  O     . LEU A 1 2605 ? 228.343 184.032 217.112 1.00 43.20  ? 2605 LEU A O     1 
ATOM   8362  C  CB    . LEU A 1 2605 ? 229.139 187.236 217.242 1.00 28.19  ? 2605 LEU A CB    1 
ATOM   8363  C  CG    . LEU A 1 2605 ? 227.784 187.110 217.941 1.00 33.87  ? 2605 LEU A CG    1 
ATOM   8364  C  CD1   . LEU A 1 2605 ? 227.968 186.764 219.408 1.00 30.57  ? 2605 LEU A CD1   1 
ATOM   8365  C  CD2   . LEU A 1 2605 ? 226.971 188.377 217.782 1.00 38.31  ? 2605 LEU A CD2   1 
ATOM   8366  N  N     . PHE A 1 2606 ? 228.636 184.975 215.092 1.00 28.84  ? 2606 PHE A N     1 
ATOM   8367  C  CA    . PHE A 1 2606 ? 227.713 184.045 214.453 1.00 14.75  ? 2606 PHE A CA    1 
ATOM   8368  C  C     . PHE A 1 2606 ? 228.303 182.646 214.353 1.00 31.98  ? 2606 PHE A C     1 
ATOM   8369  O  O     . PHE A 1 2606 ? 227.557 181.663 214.321 1.00 38.48  ? 2606 PHE A O     1 
ATOM   8370  C  CB    . PHE A 1 2606 ? 227.318 184.557 213.069 1.00 33.00  ? 2606 PHE A CB    1 
ATOM   8371  C  CG    . PHE A 1 2606 ? 226.352 185.710 213.095 1.00 33.29  ? 2606 PHE A CG    1 
ATOM   8372  C  CD1   . PHE A 1 2606 ? 226.118 186.420 214.258 1.00 36.24  ? 2606 PHE A CD1   1 
ATOM   8373  C  CD2   . PHE A 1 2606 ? 225.680 186.085 211.947 1.00 40.33  ? 2606 PHE A CD2   1 
ATOM   8374  C  CE1   . PHE A 1 2606 ? 225.233 187.476 214.278 1.00 32.75  ? 2606 PHE A CE1   1 
ATOM   8375  C  CE2   . PHE A 1 2606 ? 224.794 187.142 211.961 1.00 43.87  ? 2606 PHE A CE2   1 
ATOM   8376  C  CZ    . PHE A 1 2606 ? 224.571 187.837 213.129 1.00 37.69  ? 2606 PHE A CZ    1 
ATOM   8377  N  N     . SER A 1 2607 ? 229.632 182.535 214.293 1.00 39.64  ? 2607 SER A N     1 
ATOM   8378  C  CA    . SER A 1 2607 ? 230.264 181.221 214.296 1.00 33.75  ? 2607 SER A CA    1 
ATOM   8379  C  C     . SER A 1 2607 ? 230.198 180.582 215.675 1.00 30.64  ? 2607 SER A C     1 
ATOM   8380  O  O     . SER A 1 2607 ? 230.049 179.361 215.796 1.00 36.32  ? 2607 SER A O     1 
ATOM   8381  C  CB    . SER A 1 2607 ? 231.713 181.342 213.829 1.00 36.74  ? 2607 SER A CB    1 
ATOM   8382  O  OG    . SER A 1 2607 ? 232.302 180.066 213.660 1.00 46.42  ? 2607 SER A OG    1 
ATOM   8383  N  N     . ALA A 1 2608 ? 230.319 181.390 216.730 1.00 40.63  ? 2608 ALA A N     1 
ATOM   8384  C  CA    . ALA A 1 2608 ? 230.215 180.859 218.084 1.00 34.69  ? 2608 ALA A CA    1 
ATOM   8385  C  C     . ALA A 1 2608 ? 228.771 180.527 218.437 1.00 30.99  ? 2608 ALA A C     1 
ATOM   8386  O  O     . ALA A 1 2608 ? 228.510 179.566 219.168 1.00 39.98  ? 2608 ALA A O     1 
ATOM   8387  C  CB    . ALA A 1 2608 ? 230.798 181.855 219.084 1.00 25.45  ? 2608 ALA A CB    1 
ATOM   8388  N  N     . LEU A 1 2609 ? 227.820 181.313 217.930 1.00 30.72  ? 2609 LEU A N     1 
ATOM   8389  C  CA    . LEU A 1 2609 ? 226.412 181.055 218.201 1.00 33.99  ? 2609 LEU A CA    1 
ATOM   8390  C  C     . LEU A 1 2609 ? 225.899 179.819 217.479 1.00 41.17  ? 2609 LEU A C     1 
ATOM   8391  O  O     . LEU A 1 2609 ? 224.855 179.283 217.862 1.00 44.72  ? 2609 LEU A O     1 
ATOM   8392  C  CB    . LEU A 1 2609 ? 225.571 182.269 217.809 1.00 33.17  ? 2609 LEU A CB    1 
ATOM   8393  C  CG    . LEU A 1 2609 ? 225.403 183.346 218.878 1.00 31.84  ? 2609 LEU A CG    1 
ATOM   8394  C  CD1   . LEU A 1 2609 ? 224.726 184.564 218.294 1.00 27.88  ? 2609 LEU A CD1   1 
ATOM   8395  C  CD2   . LEU A 1 2609 ? 224.609 182.809 220.052 1.00 39.89  ? 2609 LEU A CD2   1 
ATOM   8396  N  N     . ARG A 1 2610 ? 226.598 179.362 216.438 1.00 45.11  ? 2610 ARG A N     1 
ATOM   8397  C  CA    . ARG A 1 2610 ? 226.190 178.137 215.760 1.00 39.98  ? 2610 ARG A CA    1 
ATOM   8398  C  C     . ARG A 1 2610 ? 226.373 176.919 216.654 1.00 45.43  ? 2610 ARG A C     1 
ATOM   8399  O  O     . ARG A 1 2610 ? 225.640 175.934 216.514 1.00 47.07  ? 2610 ARG A O     1 
ATOM   8400  C  CB    . ARG A 1 2610 ? 226.974 177.969 214.459 1.00 41.98  ? 2610 ARG A CB    1 
ATOM   8401  C  CG    . ARG A 1 2610 ? 226.421 178.775 213.295 1.00 45.85  ? 2610 ARG A CG    1 
ATOM   8402  C  CD    . ARG A 1 2610 ? 227.018 178.321 211.973 1.00 44.85  ? 2610 ARG A CD    1 
ATOM   8403  N  NE    . ARG A 1 2610 ? 228.152 179.144 211.565 1.00 48.91  ? 2610 ARG A NE    1 
ATOM   8404  C  CZ    . ARG A 1 2610 ? 228.047 180.325 210.973 1.00 48.84  ? 2610 ARG A CZ    1 
ATOM   8405  N  NH1   . ARG A 1 2610 ? 226.868 180.860 210.701 1.00 46.08  ? 2610 ARG A NH1   1 
ATOM   8406  N  NH2   . ARG A 1 2610 ? 229.152 180.986 210.642 1.00 41.69  ? 2610 ARG A NH2   1 
ATOM   8407  N  N     . ALA A 1 2611 ? 227.336 176.967 217.575 1.00 47.90  ? 2611 ALA A N     1 
ATOM   8408  C  CA    . ALA A 1 2611 ? 227.549 175.880 218.520 1.00 49.10  ? 2611 ALA A CA    1 
ATOM   8409  C  C     . ALA A 1 2611 ? 226.576 175.916 219.689 1.00 51.53  ? 2611 ALA A C     1 
ATOM   8410  O  O     . ALA A 1 2611 ? 226.581 174.991 220.508 1.00 52.01  ? 2611 ALA A O     1 
ATOM   8411  C  CB    . ALA A 1 2611 ? 228.985 175.915 219.047 1.00 46.57  ? 2611 ALA A CB    1 
ATOM   8412  N  N     . LEU A 1 2612 ? 225.754 176.958 219.788 1.00 46.48  ? 2612 LEU A N     1 
ATOM   8413  C  CA    . LEU A 1 2612 ? 224.734 177.082 220.823 1.00 43.66  ? 2612 LEU A CA    1 
ATOM   8414  C  C     . LEU A 1 2612 ? 223.365 177.057 220.160 1.00 51.22  ? 2612 LEU A C     1 
ATOM   8415  O  O     . LEU A 1 2612 ? 222.908 178.086 219.640 1.00 56.42  ? 2612 LEU A O     1 
ATOM   8416  C  CB    . LEU A 1 2612 ? 224.931 178.377 221.614 1.00 42.91  ? 2612 LEU A CB    1 
ATOM   8417  C  CG    . LEU A 1 2612 ? 226.181 178.401 222.494 1.00 46.26  ? 2612 LEU A CG    1 
ATOM   8418  C  CD1   . LEU A 1 2612 ? 226.445 179.786 223.030 1.00 45.34  ? 2612 LEU A CD1   1 
ATOM   8419  C  CD2   . LEU A 1 2612 ? 226.002 177.432 223.642 1.00 52.78  ? 2612 LEU A CD2   1 
ATOM   8420  N  N     . PRO A 1 2613 ? 222.668 175.916 220.150 1.00 55.18  ? 2613 PRO A N     1 
ATOM   8421  C  CA    . PRO A 1 2613 ? 221.443 175.805 219.348 1.00 53.43  ? 2613 PRO A CA    1 
ATOM   8422  C  C     . PRO A 1 2613 ? 220.207 176.404 219.993 1.00 51.18  ? 2613 PRO A C     1 
ATOM   8423  O  O     . PRO A 1 2613 ? 219.200 176.587 219.296 1.00 49.87  ? 2613 PRO A O     1 
ATOM   8424  C  CB    . PRO A 1 2613 ? 221.281 174.288 219.168 1.00 50.30  ? 2613 PRO A CB    1 
ATOM   8425  C  CG    . PRO A 1 2613 ? 222.115 173.652 220.248 1.00 50.34  ? 2613 PRO A CG    1 
ATOM   8426  C  CD    . PRO A 1 2613 ? 222.935 174.703 220.937 1.00 45.67  ? 2613 PRO A CD    1 
ATOM   8427  N  N     . ASP A 1 2614 ? 220.243 176.719 221.284 1.00 52.48  ? 2614 ASP A N     1 
ATOM   8428  C  CA    . ASP A 1 2614 ? 219.087 177.262 221.982 1.00 49.51  ? 2614 ASP A CA    1 
ATOM   8429  C  C     . ASP A 1 2614 ? 219.105 178.782 222.061 1.00 47.92  ? 2614 ASP A C     1 
ATOM   8430  O  O     . ASP A 1 2614 ? 218.257 179.364 222.742 1.00 55.19  ? 2614 ASP A O     1 
ATOM   8431  C  CB    . ASP A 1 2614 ? 218.994 176.667 223.388 1.00 49.33  ? 2614 ASP A CB    1 
ATOM   8432  C  CG    . ASP A 1 2614 ? 218.478 175.242 223.381 1.00 61.67  ? 2614 ASP A CG    1 
ATOM   8433  O  OD1   . ASP A 1 2614 ? 217.274 175.048 223.115 1.00 60.30  ? 2614 ASP A OD1   1 
ATOM   8434  O  OD2   . ASP A 1 2614 ? 219.276 174.316 223.638 1.00 61.74  ? 2614 ASP A OD2   1 
ATOM   8435  N  N     . MET A 1 2615 ? 220.044 179.433 221.384 1.00 48.87  ? 2615 MET A N     1 
ATOM   8436  C  CA    . MET A 1 2615 ? 220.158 180.884 221.386 1.00 43.42  ? 2615 MET A CA    1 
ATOM   8437  C  C     . MET A 1 2615 ? 219.886 181.409 219.986 1.00 49.59  ? 2615 MET A C     1 
ATOM   8438  O  O     . MET A 1 2615 ? 220.486 180.937 219.015 1.00 55.64  ? 2615 MET A O     1 
ATOM   8439  C  CB    . MET A 1 2615 ? 221.548 181.322 221.847 1.00 44.82  ? 2615 MET A CB    1 
ATOM   8440  C  CG    . MET A 1 2615 ? 221.839 181.012 223.297 1.00 44.57  ? 2615 MET A CG    1 
ATOM   8441  S  SD    . MET A 1 2615 ? 223.484 181.538 223.788 1.00 65.12  ? 2615 MET A SD    1 
ATOM   8442  C  CE    . MET A 1 2615 ? 223.522 180.939 225.471 1.00 50.72  ? 2615 MET A CE    1 
ATOM   8443  N  N     . GLU A 1 2616 ? 218.986 182.380 219.883 1.00 42.05  ? 2616 GLU A N     1 
ATOM   8444  C  CA    . GLU A 1 2616 ? 218.677 183.035 218.620 1.00 45.37  ? 2616 GLU A CA    1 
ATOM   8445  C  C     . GLU A 1 2616 ? 219.091 184.495 218.709 1.00 49.56  ? 2616 GLU A C     1 
ATOM   8446  O  O     . GLU A 1 2616 ? 218.706 185.196 219.650 1.00 55.34  ? 2616 GLU A O     1 
ATOM   8447  C  CB    . GLU A 1 2616 ? 217.193 182.915 218.281 1.00 44.87  ? 2616 GLU A CB    1 
ATOM   8448  C  CG    . GLU A 1 2616 ? 216.743 181.500 217.981 1.00 55.58  ? 2616 GLU A CG    1 
ATOM   8449  C  CD    . GLU A 1 2616 ? 215.268 181.429 217.668 1.00 61.82  ? 2616 GLU A CD    1 
ATOM   8450  O  OE1   . GLU A 1 2616 ? 214.590 182.467 217.812 1.00 62.88  ? 2616 GLU A OE1   1 
ATOM   8451  O  OE2   . GLU A 1 2616 ? 214.788 180.344 217.278 1.00 59.07  ? 2616 GLU A OE2   1 
ATOM   8452  N  N     . VAL A 1 2617 ? 219.865 184.947 217.736 1.00 38.75  ? 2617 VAL A N     1 
ATOM   8453  C  CA    . VAL A 1 2617 ? 220.397 186.303 217.729 1.00 36.52  ? 2617 VAL A CA    1 
ATOM   8454  C  C     . VAL A 1 2617 ? 219.451 187.215 216.962 1.00 40.09  ? 2617 VAL A C     1 
ATOM   8455  O  O     . VAL A 1 2617 ? 218.835 186.812 215.970 1.00 46.44  ? 2617 VAL A O     1 
ATOM   8456  C  CB    . VAL A 1 2617 ? 221.818 186.326 217.133 1.00 36.00  ? 2617 VAL A CB    1 
ATOM   8457  C  CG1   . VAL A 1 2617 ? 221.797 185.927 215.670 1.00 44.40  ? 2617 VAL A CG1   1 
ATOM   8458  C  CG2   . VAL A 1 2617 ? 222.451 187.690 217.310 1.00 45.35  ? 2617 VAL A CG2   1 
ATOM   8459  N  N     . VAL A 1 2618 ? 219.318 188.448 217.443 1.00 39.32  ? 2618 VAL A N     1 
ATOM   8460  C  CA    . VAL A 1 2618 ? 218.532 189.484 216.787 1.00 41.80  ? 2618 VAL A CA    1 
ATOM   8461  C  C     . VAL A 1 2618 ? 219.436 190.687 216.570 1.00 45.20  ? 2618 VAL A C     1 
ATOM   8462  O  O     . VAL A 1 2618 ? 220.035 191.196 217.523 1.00 53.21  ? 2618 VAL A O     1 
ATOM   8463  C  CB    . VAL A 1 2618 ? 217.295 189.875 217.616 1.00 36.74  ? 2618 VAL A CB    1 
ATOM   8464  C  CG1   . VAL A 1 2618 ? 216.701 191.170 217.103 1.00 41.98  ? 2618 VAL A CG1   1 
ATOM   8465  C  CG2   . VAL A 1 2618 ? 216.269 188.764 217.579 1.00 37.18  ? 2618 VAL A CG2   1 
ATOM   8466  N  N     . GLY A 1 2619 ? 219.537 191.138 215.321 1.00 37.05  ? 2619 GLY A N     1 
ATOM   8467  C  CA    . GLY A 1 2619 ? 220.448 192.212 214.975 1.00 31.48  ? 2619 GLY A CA    1 
ATOM   8468  C  C     . GLY A 1 2619 ? 219.854 193.577 215.251 1.00 41.27  ? 2619 GLY A C     1 
ATOM   8469  O  O     . GLY A 1 2619 ? 218.772 193.907 214.759 1.00 53.11  ? 2619 GLY A O     1 
ATOM   8470  N  N     . LEU A 1 2620 ? 220.569 194.369 216.045 1.00 40.28  ? 2620 LEU A N     1 
ATOM   8471  C  CA    . LEU A 1 2620 ? 220.220 195.757 216.312 1.00 31.35  ? 2620 LEU A CA    1 
ATOM   8472  C  C     . LEU A 1 2620 ? 221.386 196.635 215.887 1.00 38.84  ? 2620 LEU A C     1 
ATOM   8473  O  O     . LEU A 1 2620 ? 222.526 196.395 216.294 1.00 53.44  ? 2620 LEU A O     1 
ATOM   8474  C  CB    . LEU A 1 2620 ? 219.904 195.981 217.791 1.00 37.00  ? 2620 LEU A CB    1 
ATOM   8475  C  CG    . LEU A 1 2620 ? 218.572 195.455 218.319 1.00 42.54  ? 2620 LEU A CG    1 
ATOM   8476  C  CD1   . LEU A 1 2620 ? 218.711 194.012 218.757 1.00 43.16  ? 2620 LEU A CD1   1 
ATOM   8477  C  CD2   . LEU A 1 2620 ? 218.090 196.317 219.467 1.00 42.54  ? 2620 LEU A CD2   1 
ATOM   8478  N  N     . ASN A 1 2621 ? 221.104 197.643 215.071 1.00 42.24  ? 2621 ASN A N     1 
ATOM   8479  C  CA    . ASN A 1 2621 ? 222.128 198.548 214.562 1.00 37.01  ? 2621 ASN A CA    1 
ATOM   8480  C  C     . ASN A 1 2621 ? 221.922 199.913 215.201 1.00 43.48  ? 2621 ASN A C     1 
ATOM   8481  O  O     . ASN A 1 2621 ? 220.950 200.610 214.894 1.00 49.88  ? 2621 ASN A O     1 
ATOM   8482  C  CB    . ASN A 1 2621 ? 222.070 198.634 213.040 1.00 37.02  ? 2621 ASN A CB    1 
ATOM   8483  C  CG    . ASN A 1 2621 ? 222.096 197.275 212.387 1.00 46.67  ? 2621 ASN A CG    1 
ATOM   8484  O  OD1   . ASN A 1 2621 ? 221.051 196.675 212.138 1.00 47.22  ? 2621 ASN A OD1   1 
ATOM   8485  N  ND2   . ASN A 1 2621 ? 223.293 196.777 212.101 1.00 46.27  ? 2621 ASN A ND2   1 
ATOM   8486  N  N     . PHE A 1 2622 ? 222.836 200.289 216.086 1.00 45.77  ? 2622 PHE A N     1 
ATOM   8487  C  CA    . PHE A 1 2622 ? 222.744 201.566 216.770 1.00 42.11  ? 2622 PHE A CA    1 
ATOM   8488  C  C     . PHE A 1 2622 ? 223.365 202.667 215.922 1.00 42.65  ? 2622 PHE A C     1 
ATOM   8489  O  O     . PHE A 1 2622 ? 224.366 202.461 215.232 1.00 51.68  ? 2622 PHE A O     1 
ATOM   8490  C  CB    . PHE A 1 2622 ? 223.450 201.512 218.127 1.00 38.64  ? 2622 PHE A CB    1 
ATOM   8491  C  CG    . PHE A 1 2622 ? 222.745 200.681 219.162 1.00 36.58  ? 2622 PHE A CG    1 
ATOM   8492  C  CD1   . PHE A 1 2622 ? 221.642 199.913 218.838 1.00 41.85  ? 2622 PHE A CD1   1 
ATOM   8493  C  CD2   . PHE A 1 2622 ? 223.198 200.668 220.468 1.00 36.42  ? 2622 PHE A CD2   1 
ATOM   8494  C  CE1   . PHE A 1 2622 ? 221.005 199.152 219.796 1.00 40.59  ? 2622 PHE A CE1   1 
ATOM   8495  C  CE2   . PHE A 1 2622 ? 222.565 199.912 221.428 1.00 40.01  ? 2622 PHE A CE2   1 
ATOM   8496  C  CZ    . PHE A 1 2622 ? 221.467 199.153 221.091 1.00 40.20  ? 2622 PHE A CZ    1 
ATOM   8497  N  N     . SER A 1 2623 ? 222.756 203.846 215.975 1.00 41.02  ? 2623 SER A N     1 
ATOM   8498  C  CA    . SER A 1 2623 ? 223.300 205.041 215.354 1.00 44.03  ? 2623 SER A CA    1 
ATOM   8499  C  C     . SER A 1 2623 ? 223.367 206.139 216.407 1.00 44.02  ? 2623 SER A C     1 
ATOM   8500  O  O     . SER A 1 2623 ? 223.080 205.914 217.586 1.00 55.34  ? 2623 SER A O     1 
ATOM   8501  C  CB    . SER A 1 2623 ? 222.462 205.475 214.146 1.00 42.75  ? 2623 SER A CB    1 
ATOM   8502  O  OG    . SER A 1 2623 ? 221.173 205.903 214.539 1.00 51.78  ? 2623 SER A OG    1 
ATOM   8503  N  N     . SER A 1 2624 ? 223.751 207.341 215.979 1.00 35.44  ? 2624 SER A N     1 
ATOM   8504  C  CA    . SER A 1 2624 ? 223.870 208.450 216.917 1.00 34.62  ? 2624 SER A CA    1 
ATOM   8505  C  C     . SER A 1 2624 ? 222.529 208.854 217.514 1.00 43.95  ? 2624 SER A C     1 
ATOM   8506  O  O     . SER A 1 2624 ? 222.504 209.490 218.572 1.00 53.60  ? 2624 SER A O     1 
ATOM   8507  C  CB    . SER A 1 2624 ? 224.520 209.650 216.231 1.00 44.85  ? 2624 SER A CB    1 
ATOM   8508  O  OG    . SER A 1 2624 ? 223.633 210.247 215.303 1.00 54.70  ? 2624 SER A OG    1 
ATOM   8509  N  N     . ALA A 1 2625 ? 221.421 208.499 216.869 1.00 44.78  ? 2625 ALA A N     1 
ATOM   8510  C  CA    . ALA A 1 2625 ? 220.089 208.847 217.342 1.00 44.01  ? 2625 ALA A CA    1 
ATOM   8511  C  C     . ALA A 1 2625 ? 219.399 207.694 218.057 1.00 44.30  ? 2625 ALA A C     1 
ATOM   8512  O  O     . ALA A 1 2625 ? 218.183 207.742 218.257 1.00 48.09  ? 2625 ALA A O     1 
ATOM   8513  C  CB    . ALA A 1 2625 ? 219.226 209.328 216.176 1.00 45.73  ? 2625 ALA A CB    1 
ATOM   8514  N  N     . THR A 1 2626 ? 220.143 206.661 218.439 1.00 46.52  ? 2626 THR A N     1 
ATOM   8515  C  CA    . THR A 1 2626 ? 219.544 205.503 219.085 1.00 38.54  ? 2626 THR A CA    1 
ATOM   8516  C  C     . THR A 1 2626 ? 219.087 205.843 220.498 1.00 46.78  ? 2626 THR A C     1 
ATOM   8517  O  O     . THR A 1 2626 ? 219.793 206.513 221.256 1.00 50.94  ? 2626 THR A O     1 
ATOM   8518  C  CB    . THR A 1 2626 ? 220.538 204.344 219.121 1.00 37.58  ? 2626 THR A CB    1 
ATOM   8519  O  OG1   . THR A 1 2626 ? 220.987 204.065 217.791 1.00 43.05  ? 2626 THR A OG1   1 
ATOM   8520  C  CG2   . THR A 1 2626 ? 219.888 203.098 219.694 1.00 40.31  ? 2626 THR A CG2   1 
ATOM   8521  N  N     . THR A 1 2627 ? 217.897 205.377 220.841 1.00 48.19  ? 2627 THR A N     1 
ATOM   8522  C  CA    . THR A 1 2627 ? 217.288 205.527 222.154 1.00 43.04  ? 2627 THR A CA    1 
ATOM   8523  C  C     . THR A 1 2627 ? 216.825 204.161 222.622 1.00 45.86  ? 2627 THR A C     1 
ATOM   8524  O  O     . THR A 1 2627 ? 216.840 203.194 221.854 1.00 55.13  ? 2627 THR A O     1 
ATOM   8525  C  CB    . THR A 1 2627 ? 216.104 206.508 222.093 1.00 46.14  ? 2627 THR A CB    1 
ATOM   8526  O  OG1   . THR A 1 2627 ? 215.149 206.046 221.131 1.00 49.32  ? 2627 THR A OG1   1 
ATOM   8527  C  CG2   . THR A 1 2627 ? 216.575 207.901 221.711 1.00 49.01  ? 2627 THR A CG2   1 
ATOM   8528  N  N     . PRO A 1 2628 ? 216.419 204.032 223.890 1.00 38.29  ? 2628 PRO A N     1 
ATOM   8529  C  CA    . PRO A 1 2628 ? 215.824 202.763 224.341 1.00 38.30  ? 2628 PRO A CA    1 
ATOM   8530  C  C     . PRO A 1 2628 ? 214.586 202.352 223.563 1.00 40.86  ? 2628 PRO A C     1 
ATOM   8531  O  O     . PRO A 1 2628 ? 214.146 201.204 223.708 1.00 51.48  ? 2628 PRO A O     1 
ATOM   8532  C  CB    . PRO A 1 2628 ? 215.484 203.038 225.809 1.00 38.44  ? 2628 PRO A CB    1 
ATOM   8533  C  CG    . PRO A 1 2628 ? 216.463 204.056 226.226 1.00 42.50  ? 2628 PRO A CG    1 
ATOM   8534  C  CD    . PRO A 1 2628 ? 216.723 204.920 225.026 1.00 42.16  ? 2628 PRO A CD    1 
ATOM   8535  N  N     . GLU A 1 2629 ? 214.010 203.243 222.753 1.00 41.83  ? 2629 GLU A N     1 
ATOM   8536  C  CA    . GLU A 1 2629 ? 212.823 202.886 221.985 1.00 37.78  ? 2629 GLU A CA    1 
ATOM   8537  C  C     . GLU A 1 2629 ? 213.116 201.767 220.994 1.00 47.48  ? 2629 GLU A C     1 
ATOM   8538  O  O     . GLU A 1 2629 ? 212.251 200.930 220.727 1.00 61.10  ? 2629 GLU A O     1 
ATOM   8539  C  CB    . GLU A 1 2629 ? 212.274 204.115 221.260 1.00 40.83  ? 2629 GLU A CB    1 
ATOM   8540  C  CG    . GLU A 1 2629 ? 212.129 205.350 222.138 1.00 53.18  ? 2629 GLU A CG    1 
ATOM   8541  C  CD    . GLU A 1 2629 ? 211.547 205.038 223.504 1.00 60.36  ? 2629 GLU A CD    1 
ATOM   8542  O  OE1   . GLU A 1 2629 ? 210.463 204.420 223.567 1.00 57.54  ? 2629 GLU A OE1   1 
ATOM   8543  O  OE2   . GLU A 1 2629 ? 212.173 205.416 224.517 1.00 56.49  ? 2629 GLU A OE2   1 
ATOM   8544  N  N     . LEU A 1 2630 ? 214.328 201.735 220.438 1.00 37.57  ? 2630 LEU A N     1 
ATOM   8545  C  CA    . LEU A 1 2630 ? 214.690 200.654 219.524 1.00 35.45  ? 2630 LEU A CA    1 
ATOM   8546  C  C     . LEU A 1 2630 ? 214.680 199.304 220.234 1.00 44.21  ? 2630 LEU A C     1 
ATOM   8547  O  O     . LEU A 1 2630 ? 214.120 198.323 219.724 1.00 46.47  ? 2630 LEU A O     1 
ATOM   8548  C  CB    . LEU A 1 2630 ? 216.061 200.935 218.910 1.00 39.28  ? 2630 LEU A CB    1 
ATOM   8549  C  CG    . LEU A 1 2630 ? 216.565 199.997 217.812 1.00 43.46  ? 2630 LEU A CG    1 
ATOM   8550  C  CD1   . LEU A 1 2630 ? 215.909 200.331 216.485 1.00 45.47  ? 2630 LEU A CD1   1 
ATOM   8551  C  CD2   . LEU A 1 2630 ? 218.075 200.088 217.696 1.00 41.59  ? 2630 LEU A CD2   1 
ATOM   8552  N  N     . LEU A 1 2631 ? 215.283 199.241 221.423 1.00 38.31  ? 2631 LEU A N     1 
ATOM   8553  C  CA    . LEU A 1 2631 ? 215.261 198.009 222.202 1.00 29.91  ? 2631 LEU A CA    1 
ATOM   8554  C  C     . LEU A 1 2631 ? 213.840 197.637 222.600 1.00 37.71  ? 2631 LEU A C     1 
ATOM   8555  O  O     . LEU A 1 2631 ? 213.486 196.455 222.620 1.00 52.49  ? 2631 LEU A O     1 
ATOM   8556  C  CB    . LEU A 1 2631 ? 216.140 198.153 223.442 1.00 35.64  ? 2631 LEU A CB    1 
ATOM   8557  C  CG    . LEU A 1 2631 ? 217.654 198.152 223.234 1.00 40.05  ? 2631 LEU A CG    1 
ATOM   8558  C  CD1   . LEU A 1 2631 ? 218.315 199.081 224.229 1.00 44.17  ? 2631 LEU A CD1   1 
ATOM   8559  C  CD2   . LEU A 1 2631 ? 218.215 196.753 223.366 1.00 40.98  ? 2631 LEU A CD2   1 
ATOM   8560  N  N     . LEU A 1 2632 ? 213.013 198.632 222.926 1.00 34.77  ? 2632 LEU A N     1 
ATOM   8561  C  CA    . LEU A 1 2632 ? 211.632 198.344 223.298 1.00 33.71  ? 2632 LEU A CA    1 
ATOM   8562  C  C     . LEU A 1 2632 ? 210.837 197.798 222.117 1.00 39.28  ? 2632 LEU A C     1 
ATOM   8563  O  O     . LEU A 1 2632 ? 209.998 196.907 222.287 1.00 41.58  ? 2632 LEU A O     1 
ATOM   8564  C  CB    . LEU A 1 2632 ? 210.971 199.597 223.869 1.00 41.27  ? 2632 LEU A CB    1 
ATOM   8565  C  CG    . LEU A 1 2632 ? 211.539 200.080 225.204 1.00 41.08  ? 2632 LEU A CG    1 
ATOM   8566  C  CD1   . LEU A 1 2632 ? 210.831 201.338 225.672 1.00 44.57  ? 2632 LEU A CD1   1 
ATOM   8567  C  CD2   . LEU A 1 2632 ? 211.441 198.989 226.252 1.00 44.09  ? 2632 LEU A CD2   1 
ATOM   8568  N  N     . LYS A 1 2633 ? 211.081 198.317 220.912 1.00 40.15  ? 2633 LYS A N     1 
ATOM   8569  C  CA    . LYS A 1 2633 ? 210.423 197.771 219.728 1.00 39.15  ? 2633 LYS A CA    1 
ATOM   8570  C  C     . LYS A 1 2633 ? 210.885 196.347 219.450 1.00 44.37  ? 2633 LYS A C     1 
ATOM   8571  O  O     . LYS A 1 2633 ? 210.083 195.489 219.059 1.00 53.64  ? 2633 LYS A O     1 
ATOM   8572  C  CB    . LYS A 1 2633 ? 210.684 198.663 218.515 1.00 38.63  ? 2633 LYS A CB    1 
ATOM   8573  C  CG    . LYS A 1 2633 ? 210.152 200.076 218.653 1.00 42.76  ? 2633 LYS A CG    1 
ATOM   8574  C  CD    . LYS A 1 2633 ? 208.639 200.110 218.650 1.00 50.91  ? 2633 LYS A CD    1 
ATOM   8575  C  CE    . LYS A 1 2633 ? 208.132 201.532 218.796 1.00 49.85  ? 2633 LYS A CE    1 
ATOM   8576  N  NZ    . LYS A 1 2633 ? 208.445 202.353 217.595 1.00 50.81  ? 2633 LYS A NZ    1 
ATOM   8577  N  N     . THR A 1 2634 ? 212.179 196.078 219.642 1.00 44.48  ? 2634 THR A N     1 
ATOM   8578  C  CA    . THR A 1 2634 ? 212.667 194.709 219.506 1.00 39.21  ? 2634 THR A CA    1 
ATOM   8579  C  C     . THR A 1 2634 ? 211.998 193.787 220.520 1.00 33.78  ? 2634 THR A C     1 
ATOM   8580  O  O     . THR A 1 2634 ? 211.628 192.654 220.193 1.00 42.17  ? 2634 THR A O     1 
ATOM   8581  C  CB    . THR A 1 2634 ? 214.187 194.676 219.667 1.00 45.22  ? 2634 THR A CB    1 
ATOM   8582  O  OG1   . THR A 1 2634 ? 214.795 195.386 218.582 1.00 42.22  ? 2634 THR A OG1   1 
ATOM   8583  C  CG2   . THR A 1 2634 ? 214.698 193.245 219.670 1.00 42.53  ? 2634 THR A CG2   1 
ATOM   8584  N  N     . PHE A 1 2635 ? 211.833 194.261 221.756 1.00 36.94  ? 2635 PHE A N     1 
ATOM   8585  C  CA    . PHE A 1 2635 ? 211.142 193.479 222.776 1.00 39.25  ? 2635 PHE A CA    1 
ATOM   8586  C  C     . PHE A 1 2635 ? 209.692 193.224 222.389 1.00 41.54  ? 2635 PHE A C     1 
ATOM   8587  O  O     . PHE A 1 2635 ? 209.170 192.124 222.593 1.00 48.88  ? 2635 PHE A O     1 
ATOM   8588  C  CB    . PHE A 1 2635 ? 211.210 194.199 224.122 1.00 37.82  ? 2635 PHE A CB    1 
ATOM   8589  C  CG    . PHE A 1 2635 ? 212.582 194.233 224.727 1.00 35.61  ? 2635 PHE A CG    1 
ATOM   8590  C  CD1   . PHE A 1 2635 ? 213.504 193.245 224.441 1.00 36.57  ? 2635 PHE A CD1   1 
ATOM   8591  C  CD2   . PHE A 1 2635 ? 212.948 195.256 225.583 1.00 40.12  ? 2635 PHE A CD2   1 
ATOM   8592  C  CE1   . PHE A 1 2635 ? 214.763 193.275 224.999 1.00 38.71  ? 2635 PHE A CE1   1 
ATOM   8593  C  CE2   . PHE A 1 2635 ? 214.207 195.292 226.140 1.00 34.26  ? 2635 PHE A CE2   1 
ATOM   8594  C  CZ    . PHE A 1 2635 ? 215.116 194.300 225.847 1.00 34.02  ? 2635 PHE A CZ    1 
ATOM   8595  N  N     . ASP A 1 2636 ? 209.019 194.238 221.845 1.00 40.95  ? 2636 ASP A N     1 
ATOM   8596  C  CA    . ASP A 1 2636 ? 207.633 194.063 221.423 1.00 38.29  ? 2636 ASP A CA    1 
ATOM   8597  C  C     . ASP A 1 2636 ? 207.524 193.031 220.310 1.00 44.16  ? 2636 ASP A C     1 
ATOM   8598  O  O     . ASP A 1 2636 ? 206.603 192.207 220.304 1.00 52.22  ? 2636 ASP A O     1 
ATOM   8599  C  CB    . ASP A 1 2636 ? 207.049 195.400 220.971 1.00 36.68  ? 2636 ASP A CB    1 
ATOM   8600  C  CG    . ASP A 1 2636 ? 206.551 196.240 222.129 1.00 56.70  ? 2636 ASP A CG    1 
ATOM   8601  O  OD1   . ASP A 1 2636 ? 207.124 197.323 222.370 1.00 52.58  ? 2636 ASP A OD1   1 
ATOM   8602  O  OD2   . ASP A 1 2636 ? 205.586 195.817 222.800 1.00 57.05  ? 2636 ASP A OD2   1 
ATOM   8603  N  N     . HIS A 1 2637 ? 208.455 193.061 219.356 1.00 46.01  ? 2637 HIS A N     1 
ATOM   8604  C  CA    . HIS A 1 2637 ? 208.376 192.138 218.229 1.00 39.63  ? 2637 HIS A CA    1 
ATOM   8605  C  C     . HIS A 1 2637 ? 208.726 190.711 218.637 1.00 44.13  ? 2637 HIS A C     1 
ATOM   8606  O  O     . HIS A 1 2637 ? 208.015 189.767 218.275 1.00 48.54  ? 2637 HIS A O     1 
ATOM   8607  C  CB    . HIS A 1 2637 ? 209.292 192.609 217.101 1.00 43.54  ? 2637 HIS A CB    1 
ATOM   8608  C  CG    . HIS A 1 2637 ? 209.049 191.912 215.799 1.00 49.53  ? 2637 HIS A CG    1 
ATOM   8609  N  ND1   . HIS A 1 2637 ? 209.553 190.660 215.520 1.00 50.93  ? 2637 HIS A ND1   1 
ATOM   8610  C  CD2   . HIS A 1 2637 ? 208.348 192.288 214.705 1.00 53.25  ? 2637 HIS A CD2   1 
ATOM   8611  C  CE1   . HIS A 1 2637 ? 209.177 190.297 214.307 1.00 51.32  ? 2637 HIS A CE1   1 
ATOM   8612  N  NE2   . HIS A 1 2637 ? 208.444 191.266 213.791 1.00 56.75  ? 2637 HIS A NE2   1 
ATOM   8613  N  N     . TYR A 1 2638 ? 209.811 190.528 219.390 1.00 43.33  ? 2638 TYR A N     1 
ATOM   8614  C  CA    . TYR A 1 2638 ? 210.359 189.202 219.637 1.00 38.38  ? 2638 TYR A CA    1 
ATOM   8615  C  C     . TYR A 1 2638 ? 210.051 188.643 221.017 1.00 40.65  ? 2638 TYR A C     1 
ATOM   8616  O  O     . TYR A 1 2638 ? 210.362 187.475 221.271 1.00 45.01  ? 2638 TYR A O     1 
ATOM   8617  C  CB    . TYR A 1 2638 ? 211.881 189.214 219.439 1.00 34.30  ? 2638 TYR A CB    1 
ATOM   8618  C  CG    . TYR A 1 2638 ? 212.307 189.402 218.004 1.00 32.19  ? 2638 TYR A CG    1 
ATOM   8619  C  CD1   . TYR A 1 2638 ? 212.441 188.316 217.153 1.00 36.93  ? 2638 TYR A CD1   1 
ATOM   8620  C  CD2   . TYR A 1 2638 ? 212.571 190.665 217.500 1.00 37.36  ? 2638 TYR A CD2   1 
ATOM   8621  C  CE1   . TYR A 1 2638 ? 212.828 188.483 215.842 1.00 39.60  ? 2638 TYR A CE1   1 
ATOM   8622  C  CE2   . TYR A 1 2638 ? 212.957 190.843 216.190 1.00 43.69  ? 2638 TYR A CE2   1 
ATOM   8623  C  CZ    . TYR A 1 2638 ? 213.085 189.748 215.365 1.00 46.09  ? 2638 TYR A CZ    1 
ATOM   8624  O  OH    . TYR A 1 2638 ? 213.471 189.920 214.057 1.00 53.41  ? 2638 TYR A OH    1 
ATOM   8625  N  N     . CYS A 1 2639 ? 209.461 189.430 221.910 1.00 44.04  ? 2639 CYS A N     1 
ATOM   8626  C  CA    . CYS A 1 2639 ? 209.188 188.999 223.272 1.00 35.83  ? 2639 CYS A CA    1 
ATOM   8627  C  C     . CYS A 1 2639 ? 207.750 189.345 223.631 1.00 41.46  ? 2639 CYS A C     1 
ATOM   8628  O  O     . CYS A 1 2639 ? 207.064 190.076 222.912 1.00 41.98  ? 2639 CYS A O     1 
ATOM   8629  C  CB    . CYS A 1 2639 ? 210.158 189.649 224.267 1.00 37.64  ? 2639 CYS A CB    1 
ATOM   8630  S  SG    . CYS A 1 2639 ? 211.891 189.241 224.006 1.00 52.97  ? 2639 CYS A SG    1 
ATOM   8631  N  N     . GLU A 1 2640 ? 207.294 188.808 224.759 1.00 44.29  ? 2640 GLU A N     1 
ATOM   8632  C  CA    . GLU A 1 2640 ? 205.958 189.088 225.259 1.00 47.42  ? 2640 GLU A CA    1 
ATOM   8633  C  C     . GLU A 1 2640 ? 206.005 189.249 226.771 1.00 46.96  ? 2640 GLU A C     1 
ATOM   8634  O  O     . GLU A 1 2640 ? 206.805 188.605 227.454 1.00 48.70  ? 2640 GLU A O     1 
ATOM   8635  C  CB    . GLU A 1 2640 ? 204.966 187.983 224.871 1.00 43.80  ? 2640 GLU A CB    1 
ATOM   8636  C  CG    . GLU A 1 2640 ? 205.318 186.609 225.408 1.00 48.00  ? 2640 GLU A CG    1 
ATOM   8637  C  CD    . GLU A 1 2640 ? 204.219 185.593 225.167 1.00 58.44  ? 2640 GLU A CD    1 
ATOM   8638  O  OE1   . GLU A 1 2640 ? 203.956 185.267 223.990 1.00 52.57  ? 2640 GLU A OE1   1 
ATOM   8639  O  OE2   . GLU A 1 2640 ? 203.615 185.121 226.154 1.00 56.05  ? 2640 GLU A OE2   1 
ATOM   8640  N  N     . TYR A 1 2641 ? 205.139 190.116 227.286 1.00 45.48  ? 2641 TYR A N     1 
ATOM   8641  C  CA    . TYR A 1 2641 ? 205.038 190.375 228.716 1.00 46.15  ? 2641 TYR A CA    1 
ATOM   8642  C  C     . TYR A 1 2641 ? 203.973 189.472 229.321 1.00 53.58  ? 2641 TYR A C     1 
ATOM   8643  O  O     . TYR A 1 2641 ? 202.842 189.423 228.826 1.00 59.00  ? 2641 TYR A O     1 
ATOM   8644  C  CB    . TYR A 1 2641 ? 204.686 191.837 228.996 1.00 43.51  ? 2641 TYR A CB    1 
ATOM   8645  C  CG    . TYR A 1 2641 ? 205.683 192.856 228.491 1.00 47.40  ? 2641 TYR A CG    1 
ATOM   8646  C  CD1   . TYR A 1 2641 ? 205.738 193.199 227.148 1.00 51.76  ? 2641 TYR A CD1   1 
ATOM   8647  C  CD2   . TYR A 1 2641 ? 206.552 193.492 229.363 1.00 43.92  ? 2641 TYR A CD2   1 
ATOM   8648  C  CE1   . TYR A 1 2641 ? 206.640 194.136 226.687 1.00 50.08  ? 2641 TYR A CE1   1 
ATOM   8649  C  CE2   . TYR A 1 2641 ? 207.455 194.430 228.912 1.00 45.87  ? 2641 TYR A CE2   1 
ATOM   8650  C  CZ    . TYR A 1 2641 ? 207.496 194.748 227.574 1.00 49.99  ? 2641 TYR A CZ    1 
ATOM   8651  O  OH    . TYR A 1 2641 ? 208.396 195.681 227.119 1.00 48.49  ? 2641 TYR A OH    1 
ATOM   8652  N  N     . ARG A 1 2642 ? 204.332 188.766 230.388 1.00 51.20  ? 2642 ARG A N     1 
ATOM   8653  C  CA    . ARG A 1 2642 ? 203.385 187.957 231.138 1.00 49.88  ? 2642 ARG A CA    1 
ATOM   8654  C  C     . ARG A 1 2642 ? 203.465 188.335 232.608 1.00 51.49  ? 2642 ARG A C     1 
ATOM   8655  O  O     . ARG A 1 2642 ? 204.551 188.591 233.134 1.00 55.37  ? 2642 ARG A O     1 
ATOM   8656  C  CB    . ARG A 1 2642 ? 203.647 186.456 230.955 1.00 54.07  ? 2642 ARG A CB    1 
ATOM   8657  C  CG    . ARG A 1 2642 ? 205.041 185.998 231.342 1.00 54.26  ? 2642 ARG A CG    1 
ATOM   8658  C  CD    . ARG A 1 2642 ? 205.141 184.483 231.304 1.00 52.20  ? 2642 ARG A CD    1 
ATOM   8659  N  NE    . ARG A 1 2642 ? 205.949 183.956 232.397 1.00 64.12  ? 2642 ARG A NE    1 
ATOM   8660  C  CZ    . ARG A 1 2642 ? 207.256 183.748 232.331 1.00 60.82  ? 2642 ARG A CZ    1 
ATOM   8661  N  NH1   . ARG A 1 2642 ? 207.943 184.017 231.233 1.00 53.91  ? 2642 ARG A NH1   1 
ATOM   8662  N  NH2   . ARG A 1 2642 ? 207.890 183.255 233.391 1.00 52.22  ? 2642 ARG A NH2   1 
ATOM   8663  N  N     . ARG A 1 2643 ? 202.307 188.378 233.264 1.00 58.70  ? 2643 ARG A N     1 
ATOM   8664  C  CA    . ARG A 1 2643 ? 202.218 188.798 234.661 1.00 58.52  ? 2643 ARG A CA    1 
ATOM   8665  C  C     . ARG A 1 2643 ? 202.305 187.567 235.552 1.00 58.32  ? 2643 ARG A C     1 
ATOM   8666  O  O     . ARG A 1 2643 ? 201.301 186.933 235.875 1.00 64.13  ? 2643 ARG A O     1 
ATOM   8667  C  CB    . ARG A 1 2643 ? 200.934 189.577 234.909 1.00 56.13  ? 2643 ARG A CB    1 
ATOM   8668  C  CG    . ARG A 1 2643 ? 200.983 190.471 236.135 1.00 58.19  ? 2643 ARG A CG    1 
ATOM   8669  C  CD    . ARG A 1 2643 ? 199.780 191.396 236.194 1.00 60.87  ? 2643 ARG A CD    1 
ATOM   8670  N  NE    . ARG A 1 2643 ? 200.052 192.699 235.600 1.00 62.88  ? 2643 ARG A NE    1 
ATOM   8671  C  CZ    . ARG A 1 2643 ? 200.770 193.653 236.178 1.00 63.01  ? 2643 ARG A CZ    1 
ATOM   8672  N  NH1   . ARG A 1 2643 ? 201.315 193.483 237.371 1.00 60.97  ? 2643 ARG A NH1   1 
ATOM   8673  N  NH2   . ARG A 1 2643 ? 200.944 194.808 235.542 1.00 58.16  ? 2643 ARG A NH2   1 
ATOM   8674  N  N     . THR A 1 2644 ? 203.525 187.225 235.950 1.00 61.23  ? 2644 THR A N     1 
ATOM   8675  C  CA    . THR A 1 2644 ? 203.731 186.180 236.932 1.00 64.08  ? 2644 THR A CA    1 
ATOM   8676  C  C     . THR A 1 2644 ? 203.331 186.688 238.316 1.00 66.84  ? 2644 THR A C     1 
ATOM   8677  O  O     . THR A 1 2644 ? 203.231 187.897 238.535 1.00 66.62  ? 2644 THR A O     1 
ATOM   8678  C  CB    . THR A 1 2644 ? 205.191 185.733 236.929 1.00 66.74  ? 2644 THR A CB    1 
ATOM   8679  O  OG1   . THR A 1 2644 ? 206.032 186.839 237.277 1.00 71.32  ? 2644 THR A OG1   1 
ATOM   8680  C  CG2   . THR A 1 2644 ? 205.584 185.219 235.554 1.00 62.27  ? 2644 THR A CG2   1 
ATOM   8681  N  N     . PRO A 1 2645 ? 203.075 185.784 239.267 1.00 78.26  ? 2645 PRO A N     1 
ATOM   8682  C  CA    . PRO A 1 2645 ? 202.763 186.241 240.632 1.00 76.29  ? 2645 PRO A CA    1 
ATOM   8683  C  C     . PRO A 1 2645 ? 203.876 187.051 241.272 1.00 74.25  ? 2645 PRO A C     1 
ATOM   8684  O  O     . PRO A 1 2645 ? 203.595 187.867 242.158 1.00 73.36  ? 2645 PRO A O     1 
ATOM   8685  C  CB    . PRO A 1 2645 ? 202.504 184.936 241.399 1.00 80.05  ? 2645 PRO A CB    1 
ATOM   8686  C  CG    . PRO A 1 2645 ? 203.072 183.849 240.554 1.00 78.02  ? 2645 PRO A CG    1 
ATOM   8687  C  CD    . PRO A 1 2645 ? 202.995 184.319 239.140 1.00 77.11  ? 2645 PRO A CD    1 
ATOM   8688  N  N     . ASN A 1 2646 ? 205.129 186.854 240.859 1.00 76.26  ? 2646 ASN A N     1 
ATOM   8689  C  CA    . ASN A 1 2646 ? 206.232 187.659 241.367 1.00 75.41  ? 2646 ASN A CA    1 
ATOM   8690  C  C     . ASN A 1 2646 ? 206.343 189.017 240.686 1.00 76.56  ? 2646 ASN A C     1 
ATOM   8691  O  O     . ASN A 1 2646 ? 207.042 189.893 241.203 1.00 77.18  ? 2646 ASN A O     1 
ATOM   8692  C  CB    . ASN A 1 2646 ? 207.553 186.904 241.208 1.00 73.72  ? 2646 ASN A CB    1 
ATOM   8693  C  CG    . ASN A 1 2646 ? 207.659 185.716 242.139 1.00 80.20  ? 2646 ASN A CG    1 
ATOM   8694  O  OD1   . ASN A 1 2646 ? 207.282 185.794 243.308 1.00 81.22  ? 2646 ASN A OD1   1 
ATOM   8695  N  ND2   . ASN A 1 2646 ? 208.179 184.606 241.626 1.00 77.63  ? 2646 ASN A ND2   1 
ATOM   8696  N  N     . GLY A 1 2647 ? 205.683 189.211 239.557 1.00 61.24  ? 2647 GLY A N     1 
ATOM   8697  C  CA    . GLY A 1 2647 ? 205.745 190.466 238.842 1.00 55.13  ? 2647 GLY A CA    1 
ATOM   8698  C  C     . GLY A 1 2647 ? 205.596 190.231 237.353 1.00 57.05  ? 2647 GLY A C     1 
ATOM   8699  O  O     . GLY A 1 2647 ? 205.242 189.144 236.909 1.00 61.60  ? 2647 GLY A O     1 
ATOM   8700  N  N     . VAL A 1 2648 ? 205.874 191.282 236.590 1.00 48.42  ? 2648 VAL A N     1 
ATOM   8701  C  CA    . VAL A 1 2648 ? 205.802 191.213 235.136 1.00 45.69  ? 2648 VAL A CA    1 
ATOM   8702  C  C     . VAL A 1 2648 ? 207.140 190.728 234.597 1.00 44.17  ? 2648 VAL A C     1 
ATOM   8703  O  O     . VAL A 1 2648 ? 208.199 191.237 234.980 1.00 55.35  ? 2648 VAL A O     1 
ATOM   8704  C  CB    . VAL A 1 2648 ? 205.424 192.579 234.544 1.00 44.60  ? 2648 VAL A CB    1 
ATOM   8705  C  CG1   . VAL A 1 2648 ? 205.467 192.531 233.029 1.00 44.74  ? 2648 VAL A CG1   1 
ATOM   8706  C  CG2   . VAL A 1 2648 ? 204.047 192.990 235.021 1.00 46.82  ? 2648 VAL A CG2   1 
ATOM   8707  N  N     . VAL A 1 2649 ? 207.095 189.737 233.712 1.00 38.93  ? 2649 VAL A N     1 
ATOM   8708  C  CA    . VAL A 1 2649 ? 208.288 189.104 233.164 1.00 40.95  ? 2649 VAL A CA    1 
ATOM   8709  C  C     . VAL A 1 2649 ? 208.258 189.245 231.650 1.00 46.38  ? 2649 VAL A C     1 
ATOM   8710  O  O     . VAL A 1 2649 ? 207.243 188.943 231.013 1.00 53.03  ? 2649 VAL A O     1 
ATOM   8711  C  CB    . VAL A 1 2649 ? 208.376 187.623 233.573 1.00 40.35  ? 2649 VAL A CB    1 
ATOM   8712  C  CG1   . VAL A 1 2649 ? 209.509 186.936 232.839 1.00 41.65  ? 2649 VAL A CG1   1 
ATOM   8713  C  CG2   . VAL A 1 2649 ? 208.552 187.498 235.075 1.00 43.53  ? 2649 VAL A CG2   1 
ATOM   8714  N  N     . LEU A 1 2650 ? 209.366 189.706 231.078 1.00 36.61  ? 2650 LEU A N     1 
ATOM   8715  C  CA    . LEU A 1 2650 ? 209.528 189.806 229.634 1.00 32.86  ? 2650 LEU A CA    1 
ATOM   8716  C  C     . LEU A 1 2650 ? 210.409 188.659 229.157 1.00 48.59  ? 2650 LEU A C     1 
ATOM   8717  O  O     . LEU A 1 2650 ? 211.591 188.592 229.510 1.00 55.50  ? 2650 LEU A O     1 
ATOM   8718  C  CB    . LEU A 1 2650 ? 210.140 191.150 229.246 1.00 37.18  ? 2650 LEU A CB    1 
ATOM   8719  C  CG    . LEU A 1 2650 ? 210.439 191.359 227.763 1.00 34.12  ? 2650 LEU A CG    1 
ATOM   8720  C  CD1   . LEU A 1 2650 ? 209.175 191.716 227.015 1.00 39.18  ? 2650 LEU A CD1   1 
ATOM   8721  C  CD2   . LEU A 1 2650 ? 211.485 192.436 227.579 1.00 36.90  ? 2650 LEU A CD2   1 
ATOM   8722  N  N     . ALA A 1 2651 ? 209.838 187.767 228.357 1.00 43.35  ? 2651 ALA A N     1 
ATOM   8723  C  CA    . ALA A 1 2651 ? 210.534 186.598 227.849 1.00 29.54  ? 2651 ALA A CA    1 
ATOM   8724  C  C     . ALA A 1 2651 ? 210.291 186.464 226.355 1.00 41.79  ? 2651 ALA A C     1 
ATOM   8725  O  O     . ALA A 1 2651 ? 209.283 186.960 225.843 1.00 49.72  ? 2651 ALA A O     1 
ATOM   8726  C  CB    . ALA A 1 2651 ? 210.066 185.324 228.564 1.00 33.15  ? 2651 ALA A CB    1 
ATOM   8727  N  N     . PRO A 1 2652 ? 211.197 185.809 225.629 1.00 46.52  ? 2652 PRO A N     1 
ATOM   8728  C  CA    . PRO A 1 2652 ? 210.980 185.614 224.192 1.00 41.56  ? 2652 PRO A CA    1 
ATOM   8729  C  C     . PRO A 1 2652 ? 209.728 184.794 223.927 1.00 44.64  ? 2652 PRO A C     1 
ATOM   8730  O  O     . PRO A 1 2652 ? 209.316 183.966 224.741 1.00 46.66  ? 2652 PRO A O     1 
ATOM   8731  C  CB    . PRO A 1 2652 ? 212.243 184.873 223.737 1.00 37.13  ? 2652 PRO A CB    1 
ATOM   8732  C  CG    . PRO A 1 2652 ? 213.254 185.173 224.774 1.00 34.00  ? 2652 PRO A CG    1 
ATOM   8733  C  CD    . PRO A 1 2652 ? 212.507 185.294 226.058 1.00 45.91  ? 2652 PRO A CD    1 
ATOM   8734  N  N     . VAL A 1 2653 ? 209.112 185.049 222.771 1.00 52.10  ? 2653 VAL A N     1 
ATOM   8735  C  CA    . VAL A 1 2653 ? 207.868 184.366 222.425 1.00 49.67  ? 2653 VAL A CA    1 
ATOM   8736  C  C     . VAL A 1 2653 ? 208.095 182.865 222.302 1.00 52.85  ? 2653 VAL A C     1 
ATOM   8737  O  O     . VAL A 1 2653 ? 207.266 182.060 222.744 1.00 57.10  ? 2653 VAL A O     1 
ATOM   8738  C  CB    . VAL A 1 2653 ? 207.272 184.960 221.136 1.00 52.55  ? 2653 VAL A CB    1 
ATOM   8739  C  CG1   . VAL A 1 2653 ? 205.888 184.397 220.889 1.00 52.93  ? 2653 VAL A CG1   1 
ATOM   8740  C  CG2   . VAL A 1 2653 ? 207.213 186.473 221.231 1.00 49.90  ? 2653 VAL A CG2   1 
ATOM   8741  N  N     . GLN A 1 2654 ? 209.219 182.461 221.711 1.00 56.02  ? 2654 GLN A N     1 
ATOM   8742  C  CA    . GLN A 1 2654 ? 209.526 181.042 221.554 1.00 56.26  ? 2654 GLN A CA    1 
ATOM   8743  C  C     . GLN A 1 2654 ? 210.004 180.471 222.881 1.00 54.40  ? 2654 GLN A C     1 
ATOM   8744  O  O     . GLN A 1 2654 ? 211.011 180.920 223.436 1.00 51.20  ? 2654 GLN A O     1 
ATOM   8745  C  CB    . GLN A 1 2654 ? 210.570 180.837 220.463 1.00 53.10  ? 2654 GLN A CB    1 
ATOM   8746  C  CG    . GLN A 1 2654 ? 210.257 181.586 219.192 1.00 57.73  ? 2654 GLN A CG    1 
ATOM   8747  C  CD    . GLN A 1 2654 ? 211.488 182.060 218.466 1.00 62.68  ? 2654 GLN A CD    1 
ATOM   8748  O  OE1   . GLN A 1 2654 ? 212.159 181.280 217.791 1.00 61.20  ? 2654 GLN A OE1   1 
ATOM   8749  N  NE2   . GLN A 1 2654 ? 211.801 183.345 218.596 1.00 63.66  ? 2654 GLN A NE2   1 
ATOM   8750  N  N     . LEU A 1 2655 ? 209.284 179.475 223.384 1.00 56.75  ? 2655 LEU A N     1 
ATOM   8751  C  CA    . LEU A 1 2655 ? 209.606 178.890 224.677 1.00 59.48  ? 2655 LEU A CA    1 
ATOM   8752  C  C     . LEU A 1 2655 ? 210.872 178.050 224.587 1.00 56.64  ? 2655 LEU A C     1 
ATOM   8753  O  O     . LEU A 1 2655 ? 211.100 177.341 223.604 1.00 58.06  ? 2655 LEU A O     1 
ATOM   8754  C  CB    . LEU A 1 2655 ? 208.441 178.034 225.174 1.00 62.00  ? 2655 LEU A CB    1 
ATOM   8755  C  CG    . LEU A 1 2655 ? 207.346 178.725 225.994 1.00 62.29  ? 2655 LEU A CG    1 
ATOM   8756  C  CD1   . LEU A 1 2655 ? 207.919 179.297 227.280 1.00 58.02  ? 2655 LEU A CD1   1 
ATOM   8757  C  CD2   . LEU A 1 2655 ? 206.639 179.807 225.190 1.00 58.42  ? 2655 LEU A CD2   1 
ATOM   8758  N  N     . GLY A 1 2656 ? 211.702 178.137 225.624 1.00 57.08  ? 2656 GLY A N     1 
ATOM   8759  C  CA    . GLY A 1 2656 ? 212.902 177.333 225.716 1.00 54.32  ? 2656 GLY A CA    1 
ATOM   8760  C  C     . GLY A 1 2656 ? 214.104 177.862 224.967 1.00 51.16  ? 2656 GLY A C     1 
ATOM   8761  O  O     . GLY A 1 2656 ? 215.166 177.229 225.015 1.00 49.62  ? 2656 GLY A O     1 
ATOM   8762  N  N     . LYS A 1 2657 ? 213.982 178.994 224.282 1.00 48.47  ? 2657 LYS A N     1 
ATOM   8763  C  CA    . LYS A 1 2657 ? 215.078 179.579 223.526 1.00 46.93  ? 2657 LYS A CA    1 
ATOM   8764  C  C     . LYS A 1 2657 ? 215.507 180.895 224.156 1.00 42.95  ? 2657 LYS A C     1 
ATOM   8765  O  O     . LYS A 1 2657 ? 214.668 181.722 224.523 1.00 50.25  ? 2657 LYS A O     1 
ATOM   8766  C  CB    . LYS A 1 2657 ? 214.682 179.813 222.065 1.00 50.12  ? 2657 LYS A CB    1 
ATOM   8767  C  CG    . LYS A 1 2657 ? 214.349 178.548 221.302 1.00 52.46  ? 2657 LYS A CG    1 
ATOM   8768  C  CD    . LYS A 1 2657 ? 215.585 177.994 220.617 1.00 49.89  ? 2657 LYS A CD    1 
ATOM   8769  C  CE    . LYS A 1 2657 ? 215.264 176.742 219.824 1.00 53.76  ? 2657 LYS A CE    1 
ATOM   8770  N  NZ    . LYS A 1 2657 ? 216.224 175.645 220.127 1.00 51.94  ? 2657 LYS A NZ    1 
ATOM   8771  N  N     . TRP A 1 2658 ? 216.817 181.079 224.278 1.00 40.50  ? 2658 TRP A N     1 
ATOM   8772  C  CA    . TRP A 1 2658 ? 217.386 182.327 224.762 1.00 31.36  ? 2658 TRP A CA    1 
ATOM   8773  C  C     . TRP A 1 2658 ? 217.503 183.309 223.606 1.00 40.53  ? 2658 TRP A C     1 
ATOM   8774  O  O     . TRP A 1 2658 ? 217.852 182.922 222.488 1.00 57.04  ? 2658 TRP A O     1 
ATOM   8775  C  CB    . TRP A 1 2658 ? 218.754 182.084 225.399 1.00 32.59  ? 2658 TRP A CB    1 
ATOM   8776  C  CG    . TRP A 1 2658 ? 218.672 181.739 226.846 1.00 36.89  ? 2658 TRP A CG    1 
ATOM   8777  C  CD1   . TRP A 1 2658 ? 218.309 180.541 227.383 1.00 36.55  ? 2658 TRP A CD1   1 
ATOM   8778  C  CD2   . TRP A 1 2658 ? 218.949 182.606 227.950 1.00 43.24  ? 2658 TRP A CD2   1 
ATOM   8779  N  NE1   . TRP A 1 2658 ? 218.345 180.606 228.754 1.00 38.79  ? 2658 TRP A NE1   1 
ATOM   8780  C  CE2   . TRP A 1 2658 ? 218.736 181.865 229.126 1.00 42.84  ? 2658 TRP A CE2   1 
ATOM   8781  C  CE3   . TRP A 1 2658 ? 219.359 183.937 228.057 1.00 39.07  ? 2658 TRP A CE3   1 
ATOM   8782  C  CZ2   . TRP A 1 2658 ? 218.916 182.410 230.392 1.00 41.47  ? 2658 TRP A CZ2   1 
ATOM   8783  C  CZ3   . TRP A 1 2658 ? 219.538 184.475 229.314 1.00 39.23  ? 2658 TRP A CZ3   1 
ATOM   8784  C  CH2   . TRP A 1 2658 ? 219.318 183.714 230.465 1.00 37.10  ? 2658 TRP A CH2   1 
ATOM   8785  N  N     . LEU A 1 2659 ? 217.198 184.573 223.873 1.00 40.17  ? 2659 LEU A N     1 
ATOM   8786  C  CA    . LEU A 1 2659 ? 217.273 185.623 222.869 1.00 36.00  ? 2659 LEU A CA    1 
ATOM   8787  C  C     . LEU A 1 2659 ? 218.541 186.436 223.078 1.00 33.74  ? 2659 LEU A C     1 
ATOM   8788  O  O     . LEU A 1 2659 ? 218.798 186.920 224.184 1.00 50.91  ? 2659 LEU A O     1 
ATOM   8789  C  CB    . LEU A 1 2659 ? 216.047 186.534 222.934 1.00 37.65  ? 2659 LEU A CB    1 
ATOM   8790  C  CG    . LEU A 1 2659 ? 215.826 187.465 221.742 1.00 40.46  ? 2659 LEU A CG    1 
ATOM   8791  C  CD1   . LEU A 1 2659 ? 215.312 186.688 220.546 1.00 42.65  ? 2659 LEU A CD1   1 
ATOM   8792  C  CD2   . LEU A 1 2659 ? 214.865 188.577 222.108 1.00 36.70  ? 2659 LEU A CD2   1 
ATOM   8793  N  N     . VAL A 1 2660 ? 219.327 186.581 222.018 1.00 27.69  ? 2660 VAL A N     1 
ATOM   8794  C  CA    . VAL A 1 2660 ? 220.538 187.390 222.034 1.00 25.42  ? 2660 VAL A CA    1 
ATOM   8795  C  C     . VAL A 1 2660 ? 220.256 188.654 221.237 1.00 30.00  ? 2660 VAL A C     1 
ATOM   8796  O  O     . VAL A 1 2660 ? 219.939 188.586 220.044 1.00 38.76  ? 2660 VAL A O     1 
ATOM   8797  C  CB    . VAL A 1 2660 ? 221.739 186.629 221.453 1.00 29.15  ? 2660 VAL A CB    1 
ATOM   8798  C  CG1   . VAL A 1 2660 ? 222.997 187.473 221.545 1.00 25.06  ? 2660 VAL A CG1   1 
ATOM   8799  C  CG2   . VAL A 1 2660 ? 221.928 185.306 222.172 1.00 32.39  ? 2660 VAL A CG2   1 
ATOM   8800  N  N     . LEU A 1 2661 ? 220.357 189.806 221.895 1.00 32.97  ? 2661 LEU A N     1 
ATOM   8801  C  CA    . LEU A 1 2661 ? 220.211 191.094 221.221 1.00 32.00  ? 2661 LEU A CA    1 
ATOM   8802  C  C     . LEU A 1 2661 ? 221.600 191.579 220.839 1.00 34.55  ? 2661 LEU A C     1 
ATOM   8803  O  O     . LEU A 1 2661 ? 222.357 192.059 221.684 1.00 41.95  ? 2661 LEU A O     1 
ATOM   8804  C  CB    . LEU A 1 2661 ? 219.492 192.108 222.103 1.00 36.13  ? 2661 LEU A CB    1 
ATOM   8805  C  CG    . LEU A 1 2661 ? 217.971 192.003 222.220 1.00 38.93  ? 2661 LEU A CG    1 
ATOM   8806  C  CD1   . LEU A 1 2661 ? 217.552 190.816 223.063 1.00 38.35  ? 2661 LEU A CD1   1 
ATOM   8807  C  CD2   . LEU A 1 2661 ? 217.401 193.288 222.774 1.00 37.40  ? 2661 LEU A CD2   1 
ATOM   8808  N  N     . PHE A 1 2662 ? 221.935 191.457 219.560 1.00 29.10  ? 2662 PHE A N     1 
ATOM   8809  C  CA    . PHE A 1 2662 ? 223.235 191.875 219.059 1.00 28.13  ? 2662 PHE A CA    1 
ATOM   8810  C  C     . PHE A 1 2662 ? 223.164 193.340 218.650 1.00 32.10  ? 2662 PHE A C     1 
ATOM   8811  O  O     . PHE A 1 2662 ? 222.442 193.693 217.712 1.00 44.54  ? 2662 PHE A O     1 
ATOM   8812  C  CB    . PHE A 1 2662 ? 223.665 191.000 217.884 1.00 33.92  ? 2662 PHE A CB    1 
ATOM   8813  C  CG    . PHE A 1 2662 ? 224.982 191.394 217.286 1.00 34.91  ? 2662 PHE A CG    1 
ATOM   8814  C  CD1   . PHE A 1 2662 ? 226.043 191.755 218.095 1.00 26.44  ? 2662 PHE A CD1   1 
ATOM   8815  C  CD2   . PHE A 1 2662 ? 225.160 191.398 215.916 1.00 36.70  ? 2662 PHE A CD2   1 
ATOM   8816  C  CE1   . PHE A 1 2662 ? 227.253 192.115 217.550 1.00 33.63  ? 2662 PHE A CE1   1 
ATOM   8817  C  CE2   . PHE A 1 2662 ? 226.371 191.759 215.366 1.00 40.18  ? 2662 PHE A CE2   1 
ATOM   8818  C  CZ    . PHE A 1 2662 ? 227.417 192.118 216.184 1.00 37.00  ? 2662 PHE A CZ    1 
ATOM   8819  N  N     . CYS A 1 2663 ? 223.909 194.186 219.352 1.00 31.11  ? 2663 CYS A N     1 
ATOM   8820  C  CA    . CYS A 1 2663 ? 223.993 195.607 219.043 1.00 29.49  ? 2663 CYS A CA    1 
ATOM   8821  C  C     . CYS A 1 2663 ? 225.255 195.846 218.224 1.00 32.41  ? 2663 CYS A C     1 
ATOM   8822  O  O     . CYS A 1 2663 ? 226.366 195.599 218.704 1.00 40.77  ? 2663 CYS A O     1 
ATOM   8823  C  CB    . CYS A 1 2663 ? 224.000 196.440 220.323 1.00 37.79  ? 2663 CYS A CB    1 
ATOM   8824  S  SG    . CYS A 1 2663 ? 222.822 195.869 221.569 1.00 47.80  ? 2663 CYS A SG    1 
ATOM   8825  N  N     . ASP A 1 2664 ? 225.079 196.327 216.993 1.00 33.95  ? 2664 ASP A N     1 
ATOM   8826  C  CA    . ASP A 1 2664 ? 226.181 196.336 216.036 1.00 37.16  ? 2664 ASP A CA    1 
ATOM   8827  C  C     . ASP A 1 2664 ? 227.203 197.420 216.352 1.00 49.28  ? 2664 ASP A C     1 
ATOM   8828  O  O     . ASP A 1 2664 ? 228.412 197.186 216.240 1.00 54.36  ? 2664 ASP A O     1 
ATOM   8829  C  CB    . ASP A 1 2664 ? 225.645 196.513 214.619 1.00 43.27  ? 2664 ASP A CB    1 
ATOM   8830  C  CG    . ASP A 1 2664 ? 226.710 196.296 213.566 1.00 52.76  ? 2664 ASP A CG    1 
ATOM   8831  O  OD1   . ASP A 1 2664 ? 227.733 195.650 213.878 1.00 52.27  ? 2664 ASP A OD1   1 
ATOM   8832  O  OD2   . ASP A 1 2664 ? 226.527 196.774 212.428 1.00 56.22  ? 2664 ASP A OD2   1 
ATOM   8833  N  N     . GLU A 1 2665 ? 226.747 198.618 216.716 1.00 42.93  ? 2665 GLU A N     1 
ATOM   8834  C  CA    . GLU A 1 2665 ? 227.635 199.747 216.998 1.00 34.08  ? 2665 GLU A CA    1 
ATOM   8835  C  C     . GLU A 1 2665 ? 227.224 200.331 218.344 1.00 38.22  ? 2665 GLU A C     1 
ATOM   8836  O  O     . GLU A 1 2665 ? 226.489 201.318 218.402 1.00 49.65  ? 2665 GLU A O     1 
ATOM   8837  C  CB    . GLU A 1 2665 ? 227.562 200.788 215.892 1.00 42.21  ? 2665 GLU A CB    1 
ATOM   8838  C  CG    . GLU A 1 2665 ? 227.793 200.246 214.493 1.00 49.02  ? 2665 GLU A CG    1 
ATOM   8839  C  CD    . GLU A 1 2665 ? 229.256 200.243 214.106 1.00 53.65  ? 2665 GLU A CD    1 
ATOM   8840  O  OE1   . GLU A 1 2665 ? 230.101 200.564 214.967 1.00 54.94  ? 2665 GLU A OE1   1 
ATOM   8841  O  OE2   . GLU A 1 2665 ? 229.561 199.927 212.937 1.00 54.27  ? 2665 GLU A OE2   1 
ATOM   8842  N  N     . ILE A 1 2666 ? 227.737 199.749 219.427 1.00 42.61  ? 2666 ILE A N     1 
ATOM   8843  C  CA    . ILE A 1 2666 ? 227.201 200.054 220.747 1.00 35.33  ? 2666 ILE A CA    1 
ATOM   8844  C  C     . ILE A 1 2666 ? 227.686 201.391 221.295 1.00 38.33  ? 2666 ILE A C     1 
ATOM   8845  O  O     . ILE A 1 2666 ? 227.079 201.918 222.235 1.00 43.61  ? 2666 ILE A O     1 
ATOM   8846  C  CB    . ILE A 1 2666 ? 227.535 198.912 221.722 1.00 30.25  ? 2666 ILE A CB    1 
ATOM   8847  C  CG1   . ILE A 1 2666 ? 226.525 198.873 222.868 1.00 37.42  ? 2666 ILE A CG1   1 
ATOM   8848  C  CG2   . ILE A 1 2666 ? 228.953 199.046 222.247 1.00 32.15  ? 2666 ILE A CG2   1 
ATOM   8849  C  CD1   . ILE A 1 2666 ? 226.474 197.553 223.587 1.00 44.51  ? 2666 ILE A CD1   1 
ATOM   8850  N  N     . ASN A 1 2667 ? 228.747 201.969 220.735 1.00 34.76  ? 2667 ASN A N     1 
ATOM   8851  C  CA    . ASN A 1 2667 ? 229.315 203.201 221.265 1.00 32.70  ? 2667 ASN A CA    1 
ATOM   8852  C  C     . ASN A 1 2667 ? 229.068 204.414 220.373 1.00 46.21  ? 2667 ASN A C     1 
ATOM   8853  O  O     . ASN A 1 2667 ? 229.665 205.469 220.605 1.00 47.84  ? 2667 ASN A O     1 
ATOM   8854  C  CB    . ASN A 1 2667 ? 230.813 203.024 221.516 1.00 31.03  ? 2667 ASN A CB    1 
ATOM   8855  C  CG    . ASN A 1 2667 ? 231.566 202.593 220.280 1.00 31.15  ? 2667 ASN A CG    1 
ATOM   8856  O  OD1   . ASN A 1 2667 ? 230.978 202.369 219.225 1.00 45.93  ? 2667 ASN A OD1   1 
ATOM   8857  N  ND2   . ASN A 1 2667 ? 232.880 202.473 220.405 1.00 34.51  ? 2667 ASN A ND2   1 
ATOM   8858  N  N     . LEU A 1 2668 ? 228.209 204.292 219.364 1.00 46.57  ? 2668 LEU A N     1 
ATOM   8859  C  CA    . LEU A 1 2668 ? 227.807 205.424 218.533 1.00 39.54  ? 2668 LEU A CA    1 
ATOM   8860  C  C     . LEU A 1 2668 ? 226.785 206.375 219.154 1.00 40.74  ? 2668 LEU A C     1 
ATOM   8861  O  O     . LEU A 1 2668 ? 226.881 207.583 218.907 1.00 50.04  ? 2668 LEU A O     1 
ATOM   8862  C  CB    . LEU A 1 2668 ? 227.256 204.945 217.189 1.00 43.15  ? 2668 LEU A CB    1 
ATOM   8863  C  CG    . LEU A 1 2668 ? 228.286 204.590 216.124 1.00 41.97  ? 2668 LEU A CG    1 
ATOM   8864  C  CD1   . LEU A 1 2668 ? 227.583 204.126 214.874 1.00 46.28  ? 2668 LEU A CD1   1 
ATOM   8865  C  CD2   . LEU A 1 2668 ? 229.141 205.799 215.824 1.00 44.72  ? 2668 LEU A CD2   1 
ATOM   8866  N  N     . PRO A 1 2669 ? 225.789 205.908 219.920 1.00 34.76  ? 2669 PRO A N     1 
ATOM   8867  C  CA    . PRO A 1 2669 ? 224.718 206.816 220.354 1.00 36.72  ? 2669 PRO A CA    1 
ATOM   8868  C  C     . PRO A 1 2669 ? 225.253 208.064 221.041 1.00 36.71  ? 2669 PRO A C     1 
ATOM   8869  O  O     . PRO A 1 2669 ? 226.203 208.013 221.824 1.00 40.97  ? 2669 PRO A O     1 
ATOM   8870  C  CB    . PRO A 1 2669 ? 223.896 205.955 221.314 1.00 37.96  ? 2669 PRO A CB    1 
ATOM   8871  C  CG    . PRO A 1 2669 ? 224.075 204.596 220.807 1.00 37.44  ? 2669 PRO A CG    1 
ATOM   8872  C  CD    . PRO A 1 2669 ? 225.482 204.519 220.311 1.00 31.08  ? 2669 PRO A CD    1 
ATOM   8873  N  N     . ASP A 1 2670 ? 224.633 209.196 220.720 1.00 40.59  ? 2670 ASP A N     1 
ATOM   8874  C  CA    . ASP A 1 2670 ? 225.158 210.493 221.121 1.00 41.03  ? 2670 ASP A CA    1 
ATOM   8875  C  C     . ASP A 1 2670 ? 225.140 210.659 222.633 1.00 46.81  ? 2670 ASP A C     1 
ATOM   8876  O  O     . ASP A 1 2670 ? 224.168 210.306 223.306 1.00 51.17  ? 2670 ASP A O     1 
ATOM   8877  C  CB    . ASP A 1 2670 ? 224.349 211.613 220.470 1.00 43.09  ? 2670 ASP A CB    1 
ATOM   8878  C  CG    . ASP A 1 2670 ? 224.964 212.100 219.175 1.00 56.02  ? 2670 ASP A CG    1 
ATOM   8879  O  OD1   . ASP A 1 2670 ? 226.118 211.724 218.886 1.00 56.98  ? 2670 ASP A OD1   1 
ATOM   8880  O  OD2   . ASP A 1 2670 ? 224.295 212.862 218.447 1.00 52.16  ? 2670 ASP A OD2   1 
ATOM   8881  N  N     . MET A 1 2671 ? 226.229 211.203 223.162 1.00 50.38  ? 2671 MET A N     1 
ATOM   8882  C  CA    . MET A 1 2671 ? 226.292 211.628 224.551 1.00 43.90  ? 2671 MET A CA    1 
ATOM   8883  C  C     . MET A 1 2671 ? 225.688 213.020 224.664 1.00 48.66  ? 2671 MET A C     1 
ATOM   8884  O  O     . MET A 1 2671 ? 226.027 213.912 223.880 1.00 55.84  ? 2671 MET A O     1 
ATOM   8885  C  CB    . MET A 1 2671 ? 227.739 211.637 225.046 1.00 38.90  ? 2671 MET A CB    1 
ATOM   8886  C  CG    . MET A 1 2671 ? 228.199 210.324 225.642 1.00 47.38  ? 2671 MET A CG    1 
ATOM   8887  S  SD    . MET A 1 2671 ? 229.551 210.524 226.812 1.00 68.21  ? 2671 MET A SD    1 
ATOM   8888  C  CE    . MET A 1 2671 ? 230.253 208.879 226.797 1.00 53.35  ? 2671 MET A CE    1 
ATOM   8889  N  N     . ASP A 1 2672 ? 224.794 213.205 225.630 1.00 47.01  ? 2672 ASP A N     1 
ATOM   8890  C  CA    . ASP A 1 2672 ? 224.237 214.528 225.854 1.00 48.92  ? 2672 ASP A CA    1 
ATOM   8891  C  C     . ASP A 1 2672 ? 225.312 215.443 226.438 1.00 51.77  ? 2672 ASP A C     1 
ATOM   8892  O  O     . ASP A 1 2672 ? 226.456 215.040 226.666 1.00 55.34  ? 2672 ASP A O     1 
ATOM   8893  C  CB    . ASP A 1 2672 ? 223.012 214.448 226.763 1.00 50.15  ? 2672 ASP A CB    1 
ATOM   8894  C  CG    . ASP A 1 2672 ? 223.294 213.732 228.064 1.00 54.76  ? 2672 ASP A CG    1 
ATOM   8895  O  OD1   . ASP A 1 2672 ? 224.367 213.108 228.182 1.00 56.36  ? 2672 ASP A OD1   1 
ATOM   8896  O  OD2   . ASP A 1 2672 ? 222.438 213.792 228.971 1.00 56.41  ? 2672 ASP A OD2   1 
ATOM   8897  N  N     . LYS A 1 2673 ? 224.941 216.696 226.693 1.00 46.24  ? 2673 LYS A N     1 
ATOM   8898  C  CA    . LYS A 1 2673 ? 225.919 217.653 227.197 1.00 48.16  ? 2673 LYS A CA    1 
ATOM   8899  C  C     . LYS A 1 2673 ? 226.402 217.324 228.602 1.00 51.26  ? 2673 LYS A C     1 
ATOM   8900  O  O     . LYS A 1 2673 ? 227.206 218.083 229.153 1.00 56.13  ? 2673 LYS A O     1 
ATOM   8901  C  CB    . LYS A 1 2673 ? 225.340 219.067 227.161 1.00 44.76  ? 2673 LYS A CB    1 
ATOM   8902  C  CG    . LYS A 1 2673 ? 224.133 219.264 228.047 1.00 49.01  ? 2673 LYS A CG    1 
ATOM   8903  C  CD    . LYS A 1 2673 ? 223.633 220.695 227.990 1.00 51.92  ? 2673 LYS A CD    1 
ATOM   8904  C  CE    . LYS A 1 2673 ? 222.711 220.905 226.806 1.00 54.79  ? 2673 LYS A CE    1 
ATOM   8905  N  NZ    . LYS A 1 2673 ? 221.419 220.189 226.987 1.00 55.94  ? 2673 LYS A NZ    1 
ATOM   8906  N  N     . TYR A 1 2674 ? 225.941 216.218 229.189 1.00 44.48  ? 2674 TYR A N     1 
ATOM   8907  C  CA    . TYR A 1 2674 ? 226.364 215.790 230.516 1.00 45.22  ? 2674 TYR A CA    1 
ATOM   8908  C  C     . TYR A 1 2674 ? 227.008 214.409 230.496 1.00 42.88  ? 2674 TYR A C     1 
ATOM   8909  O  O     . TYR A 1 2674 ? 227.031 213.725 231.523 1.00 47.80  ? 2674 TYR A O     1 
ATOM   8910  C  CB    . TYR A 1 2674 ? 225.177 215.817 231.477 1.00 40.74  ? 2674 TYR A CB    1 
ATOM   8911  C  CG    . TYR A 1 2674 ? 224.448 217.138 231.476 1.00 43.27  ? 2674 TYR A CG    1 
ATOM   8912  C  CD1   . TYR A 1 2674 ? 225.043 218.281 231.988 1.00 46.68  ? 2674 TYR A CD1   1 
ATOM   8913  C  CD2   . TYR A 1 2674 ? 223.167 217.244 230.958 1.00 42.83  ? 2674 TYR A CD2   1 
ATOM   8914  C  CE1   . TYR A 1 2674 ? 224.383 219.490 231.988 1.00 44.55  ? 2674 TYR A CE1   1 
ATOM   8915  C  CE2   . TYR A 1 2674 ? 222.499 218.447 230.957 1.00 48.15  ? 2674 TYR A CE2   1 
ATOM   8916  C  CZ    . TYR A 1 2674 ? 223.111 219.567 231.470 1.00 50.67  ? 2674 TYR A CZ    1 
ATOM   8917  O  OH    . TYR A 1 2674 ? 222.445 220.770 231.467 1.00 44.70  ? 2674 TYR A OH    1 
ATOM   8918  N  N     . GLY A 1 2675 ? 227.528 213.986 229.346 1.00 41.98  ? 2675 GLY A N     1 
ATOM   8919  C  CA    . GLY A 1 2675 ? 228.296 212.760 229.249 1.00 41.83  ? 2675 GLY A CA    1 
ATOM   8920  C  C     . GLY A 1 2675 ? 227.545 211.484 229.565 1.00 44.30  ? 2675 GLY A C     1 
ATOM   8921  O  O     . GLY A 1 2675 ? 228.051 210.634 230.303 1.00 48.01  ? 2675 GLY A O     1 
ATOM   8922  N  N     . THR A 1 2676 ? 226.342 211.330 229.017 1.00 39.18  ? 2676 THR A N     1 
ATOM   8923  C  CA    . THR A 1 2676 ? 225.530 210.146 229.263 1.00 35.04  ? 2676 THR A CA    1 
ATOM   8924  C  C     . THR A 1 2676 ? 224.886 209.679 227.968 1.00 43.86  ? 2676 THR A C     1 
ATOM   8925  O  O     . THR A 1 2676 ? 224.317 210.487 227.229 1.00 50.77  ? 2676 THR A O     1 
ATOM   8926  C  CB    . THR A 1 2676 ? 224.448 210.429 230.312 1.00 39.62  ? 2676 THR A CB    1 
ATOM   8927  O  OG1   . THR A 1 2676 ? 225.046 210.503 231.611 1.00 56.59  ? 2676 THR A OG1   1 
ATOM   8928  C  CG2   . THR A 1 2676 ? 223.393 209.334 230.311 1.00 36.03  ? 2676 THR A CG2   1 
ATOM   8929  N  N     . GLN A 1 2677 ? 224.983 208.381 227.694 1.00 41.71  ? 2677 GLN A N     1 
ATOM   8930  C  CA    . GLN A 1 2677 ? 224.237 207.745 226.616 1.00 33.75  ? 2677 GLN A CA    1 
ATOM   8931  C  C     . GLN A 1 2677 ? 223.022 207.054 227.221 1.00 42.22  ? 2677 GLN A C     1 
ATOM   8932  O  O     . GLN A 1 2677 ? 223.169 206.133 228.031 1.00 49.68  ? 2677 GLN A O     1 
ATOM   8933  C  CB    . GLN A 1 2677 ? 225.110 206.747 225.857 1.00 26.08  ? 2677 GLN A CB    1 
ATOM   8934  C  CG    . GLN A 1 2677 ? 226.154 207.393 224.969 1.00 36.22  ? 2677 GLN A CG    1 
ATOM   8935  C  CD    . GLN A 1 2677 ? 227.330 206.484 224.687 1.00 39.52  ? 2677 GLN A CD    1 
ATOM   8936  O  OE1   . GLN A 1 2677 ? 227.994 206.005 225.604 1.00 47.20  ? 2677 GLN A OE1   1 
ATOM   8937  N  NE2   . GLN A 1 2677 ? 227.597 206.244 223.411 1.00 40.28  ? 2677 GLN A NE2   1 
ATOM   8938  N  N     . ARG A 1 2678 ? 221.827 207.502 226.831 1.00 34.12  ? 2678 ARG A N     1 
ATOM   8939  C  CA    . ARG A 1 2678 ? 220.606 206.996 227.451 1.00 22.24  ? 2678 ARG A CA    1 
ATOM   8940  C  C     . ARG A 1 2678 ? 220.416 205.508 227.187 1.00 29.72  ? 2678 ARG A C     1 
ATOM   8941  O  O     . ARG A 1 2678 ? 220.000 204.761 228.080 1.00 39.06  ? 2678 ARG A O     1 
ATOM   8942  C  CB    . ARG A 1 2678 ? 219.397 207.786 226.952 1.00 28.69  ? 2678 ARG A CB    1 
ATOM   8943  C  CG    . ARG A 1 2678 ? 218.074 207.292 227.501 1.00 33.17  ? 2678 ARG A CG    1 
ATOM   8944  C  CD    . ARG A 1 2678 ? 216.898 207.986 226.842 1.00 33.85  ? 2678 ARG A CD    1 
ATOM   8945  N  NE    . ARG A 1 2678 ? 216.743 209.364 227.288 1.00 40.35  ? 2678 ARG A NE    1 
ATOM   8946  C  CZ    . ARG A 1 2678 ? 215.891 210.228 226.755 1.00 40.73  ? 2678 ARG A CZ    1 
ATOM   8947  N  NH1   . ARG A 1 2678 ? 215.106 209.889 225.746 1.00 32.64  ? 2678 ARG A NH1   1 
ATOM   8948  N  NH2   . ARG A 1 2678 ? 215.825 211.461 227.246 1.00 41.37  ? 2678 ARG A NH2   1 
ATOM   8949  N  N     . VAL A 1 2679 ? 220.706 205.059 225.966 1.00 40.26  ? 2679 VAL A N     1 
ATOM   8950  C  CA    . VAL A 1 2679 ? 220.532 203.647 225.640 1.00 33.34  ? 2679 VAL A CA    1 
ATOM   8951  C  C     . VAL A 1 2679 ? 221.545 202.792 226.393 1.00 38.52  ? 2679 VAL A C     1 
ATOM   8952  O  O     . VAL A 1 2679 ? 221.237 201.673 226.822 1.00 39.27  ? 2679 VAL A O     1 
ATOM   8953  C  CB    . VAL A 1 2679 ? 220.617 203.437 224.116 1.00 28.40  ? 2679 VAL A CB    1 
ATOM   8954  C  CG1   . VAL A 1 2679 ? 221.943 203.928 223.577 1.00 32.39  ? 2679 VAL A CG1   1 
ATOM   8955  C  CG2   . VAL A 1 2679 ? 220.403 201.980 223.766 1.00 30.60  ? 2679 VAL A CG2   1 
ATOM   8956  N  N     . ILE A 1 2680 ? 222.767 203.299 226.572 1.00 32.36  ? 2680 ILE A N     1 
ATOM   8957  C  CA    . ILE A 1 2680 ? 223.767 202.558 227.332 1.00 22.80  ? 2680 ILE A CA    1 
ATOM   8958  C  C     . ILE A 1 2680 ? 223.357 202.462 228.795 1.00 30.29  ? 2680 ILE A C     1 
ATOM   8959  O  O     . ILE A 1 2680 ? 223.552 201.427 229.439 1.00 40.68  ? 2680 ILE A O     1 
ATOM   8960  C  CB    . ILE A 1 2680 ? 225.153 203.204 227.163 1.00 26.67  ? 2680 ILE A CB    1 
ATOM   8961  C  CG1   . ILE A 1 2680 ? 225.637 203.030 225.725 1.00 35.16  ? 2680 ILE A CG1   1 
ATOM   8962  C  CG2   . ILE A 1 2680 ? 226.153 202.592 228.123 1.00 29.19  ? 2680 ILE A CG2   1 
ATOM   8963  C  CD1   . ILE A 1 2680 ? 225.687 201.592 225.277 1.00 30.86  ? 2680 ILE A CD1   1 
ATOM   8964  N  N     . SER A 1 2681 ? 222.763 203.528 229.338 1.00 31.83  ? 2681 SER A N     1 
ATOM   8965  C  CA    . SER A 1 2681 ? 222.220 203.462 230.691 1.00 22.80  ? 2681 SER A CA    1 
ATOM   8966  C  C     . SER A 1 2681 ? 221.071 202.467 230.784 1.00 28.11  ? 2681 SER A C     1 
ATOM   8967  O  O     . SER A 1 2681 ? 220.950 201.752 231.783 1.00 31.03  ? 2681 SER A O     1 
ATOM   8968  C  CB    . SER A 1 2681 ? 221.761 204.846 231.143 1.00 26.31  ? 2681 SER A CB    1 
ATOM   8969  O  OG    . SER A 1 2681 ? 222.868 205.697 231.376 1.00 38.09  ? 2681 SER A OG    1 
ATOM   8970  N  N     . PHE A 1 2682 ? 220.222 202.406 229.757 1.00 30.46  ? 2682 PHE A N     1 
ATOM   8971  C  CA    . PHE A 1 2682 ? 219.134 201.432 229.731 1.00 20.65  ? 2682 PHE A CA    1 
ATOM   8972  C  C     . PHE A 1 2682 ? 219.668 200.004 229.736 1.00 33.58  ? 2682 PHE A C     1 
ATOM   8973  O  O     . PHE A 1 2682 ? 219.174 199.145 230.478 1.00 40.84  ? 2682 PHE A O     1 
ATOM   8974  C  CB    . PHE A 1 2682 ? 218.266 201.685 228.498 1.00 22.27  ? 2682 PHE A CB    1 
ATOM   8975  C  CG    . PHE A 1 2682 ? 216.998 200.885 228.459 1.00 29.46  ? 2682 PHE A CG    1 
ATOM   8976  C  CD1   . PHE A 1 2682 ? 216.023 201.057 229.421 1.00 36.63  ? 2682 PHE A CD1   1 
ATOM   8977  C  CD2   . PHE A 1 2682 ? 216.771 199.979 227.440 1.00 30.38  ? 2682 PHE A CD2   1 
ATOM   8978  C  CE1   . PHE A 1 2682 ? 214.853 200.329 229.376 1.00 36.02  ? 2682 PHE A CE1   1 
ATOM   8979  C  CE2   . PHE A 1 2682 ? 215.603 199.248 227.392 1.00 30.43  ? 2682 PHE A CE2   1 
ATOM   8980  C  CZ    . PHE A 1 2682 ? 214.644 199.423 228.360 1.00 35.25  ? 2682 PHE A CZ    1 
ATOM   8981  N  N     . ILE A 1 2683 ? 220.688 199.734 228.920 1.00 28.40  ? 2683 ILE A N     1 
ATOM   8982  C  CA    . ILE A 1 2683 ? 221.261 198.392 228.862 1.00 18.12  ? 2683 ILE A CA    1 
ATOM   8983  C  C     . ILE A 1 2683 ? 221.977 198.058 230.164 1.00 26.68  ? 2683 ILE A C     1 
ATOM   8984  O  O     . ILE A 1 2683 ? 221.927 196.919 230.643 1.00 41.01  ? 2683 ILE A O     1 
ATOM   8985  C  CB    . ILE A 1 2683 ? 222.196 198.263 227.647 1.00 26.16  ? 2683 ILE A CB    1 
ATOM   8986  C  CG1   . ILE A 1 2683 ? 221.410 198.445 226.350 1.00 30.30  ? 2683 ILE A CG1   1 
ATOM   8987  C  CG2   . ILE A 1 2683 ? 222.889 196.913 227.646 1.00 32.07  ? 2683 ILE A CG2   1 
ATOM   8988  C  CD1   . ILE A 1 2683 ? 222.277 198.484 225.118 1.00 27.08  ? 2683 ILE A CD1   1 
ATOM   8989  N  N     . ARG A 1 2684 ? 222.653 199.041 230.761 1.00 30.31  ? 2684 ARG A N     1 
ATOM   8990  C  CA    . ARG A 1 2684 ? 223.310 198.816 232.042 1.00 24.91  ? 2684 ARG A CA    1 
ATOM   8991  C  C     . ARG A 1 2684 ? 222.291 198.541 233.139 1.00 29.96  ? 2684 ARG A C     1 
ATOM   8992  O  O     . ARG A 1 2684 ? 222.553 197.757 234.055 1.00 30.36  ? 2684 ARG A O     1 
ATOM   8993  C  CB    . ARG A 1 2684 ? 224.188 200.017 232.392 1.00 24.62  ? 2684 ARG A CB    1 
ATOM   8994  C  CG    . ARG A 1 2684 ? 225.031 199.841 233.639 1.00 34.44  ? 2684 ARG A CG    1 
ATOM   8995  C  CD    . ARG A 1 2684 ? 224.426 200.557 234.825 1.00 35.59  ? 2684 ARG A CD    1 
ATOM   8996  N  NE    . ARG A 1 2684 ? 225.264 200.440 236.010 1.00 44.51  ? 2684 ARG A NE    1 
ATOM   8997  C  CZ    . ARG A 1 2684 ? 224.915 200.858 237.218 1.00 44.06  ? 2684 ARG A CZ    1 
ATOM   8998  N  NH1   . ARG A 1 2684 ? 223.759 201.463 237.431 1.00 31.11  ? 2684 ARG A NH1   1 
ATOM   8999  N  NH2   . ARG A 1 2684 ? 225.746 200.665 238.236 1.00 48.65  ? 2684 ARG A NH2   1 
ATOM   9000  N  N     . GLN A 1 2685 ? 221.126 199.187 233.069 1.00 38.43  ? 2685 GLN A N     1 
ATOM   9001  C  CA    . GLN A 1 2685 ? 220.053 198.882 234.009 1.00 22.31  ? 2685 GLN A CA    1 
ATOM   9002  C  C     . GLN A 1 2685 ? 219.525 197.469 233.803 1.00 25.70  ? 2685 GLN A C     1 
ATOM   9003  O  O     . GLN A 1 2685 ? 219.269 196.747 234.772 1.00 31.02  ? 2685 GLN A O     1 
ATOM   9004  C  CB    . GLN A 1 2685 ? 218.922 199.898 233.863 1.00 23.55  ? 2685 GLN A CB    1 
ATOM   9005  C  CG    . GLN A 1 2685 ? 217.656 199.515 234.603 1.00 28.75  ? 2685 GLN A CG    1 
ATOM   9006  C  CD    . GLN A 1 2685 ? 216.622 200.618 234.604 1.00 38.78  ? 2685 GLN A CD    1 
ATOM   9007  O  OE1   . GLN A 1 2685 ? 216.248 201.134 233.553 1.00 35.74  ? 2685 GLN A OE1   1 
ATOM   9008  N  NE2   . GLN A 1 2685 ? 216.152 200.985 235.788 1.00 36.91  ? 2685 GLN A NE2   1 
ATOM   9009  N  N     . MET A 1 2686 ? 219.347 197.060 232.547 1.00 34.34  ? 2686 MET A N     1 
ATOM   9010  C  CA    . MET A 1 2686 ? 218.860 195.717 232.256 1.00 25.86  ? 2686 MET A CA    1 
ATOM   9011  C  C     . MET A 1 2686 ? 219.863 194.626 232.603 1.00 31.75  ? 2686 MET A C     1 
ATOM   9012  O  O     . MET A 1 2686 ? 219.455 193.486 232.836 1.00 38.91  ? 2686 MET A O     1 
ATOM   9013  C  CB    . MET A 1 2686 ? 218.474 195.600 230.781 1.00 23.20  ? 2686 MET A CB    1 
ATOM   9014  C  CG    . MET A 1 2686 ? 217.256 196.415 230.397 1.00 33.41  ? 2686 MET A CG    1 
ATOM   9015  S  SD    . MET A 1 2686 ? 216.630 195.984 228.768 1.00 61.85  ? 2686 MET A SD    1 
ATOM   9016  C  CE    . MET A 1 2686 ? 217.941 196.622 227.735 1.00 33.55  ? 2686 MET A CE    1 
ATOM   9017  N  N     . VAL A 1 2687 ? 221.153 194.936 232.627 1.00 34.09  ? 2687 VAL A N     1 
ATOM   9018  C  CA    . VAL A 1 2687 ? 222.183 193.962 232.974 1.00 29.38  ? 2687 VAL A CA    1 
ATOM   9019  C  C     . VAL A 1 2687 ? 222.433 193.924 234.478 1.00 30.12  ? 2687 VAL A C     1 
ATOM   9020  O  O     . VAL A 1 2687 ? 222.544 192.850 235.069 1.00 36.34  ? 2687 VAL A O     1 
ATOM   9021  C  CB    . VAL A 1 2687 ? 223.482 194.262 232.194 1.00 24.70  ? 2687 VAL A CB    1 
ATOM   9022  C  CG1   . VAL A 1 2687 ? 224.632 193.477 232.773 1.00 35.10  ? 2687 VAL A CG1   1 
ATOM   9023  C  CG2   . VAL A 1 2687 ? 223.303 193.936 230.724 1.00 22.09  ? 2687 VAL A CG2   1 
ATOM   9024  N  N     . GLU A 1 2688 ? 222.520 195.095 235.112 1.00 33.81  ? 2688 GLU A N     1 
ATOM   9025  C  CA    . GLU A 1 2688 ? 222.713 195.165 236.557 1.00 25.31  ? 2688 GLU A CA    1 
ATOM   9026  C  C     . GLU A 1 2688 ? 221.521 194.590 237.309 1.00 35.79  ? 2688 GLU A C     1 
ATOM   9027  O  O     . GLU A 1 2688 ? 221.662 193.631 238.076 1.00 47.91  ? 2688 GLU A O     1 
ATOM   9028  C  CB    . GLU A 1 2688 ? 222.960 196.616 236.973 1.00 31.41  ? 2688 GLU A CB    1 
ATOM   9029  C  CG    . GLU A 1 2688 ? 223.212 196.838 238.462 1.00 42.87  ? 2688 GLU A CG    1 
ATOM   9030  C  CD    . GLU A 1 2688 ? 224.482 196.197 238.969 1.00 50.92  ? 2688 GLU A CD    1 
ATOM   9031  O  OE1   . GLU A 1 2688 ? 225.413 196.001 238.166 1.00 56.72  ? 2688 GLU A OE1   1 
ATOM   9032  O  OE2   . GLU A 1 2688 ? 224.553 195.892 240.177 1.00 50.79  ? 2688 GLU A OE2   1 
ATOM   9033  N  N     . HIS A 1 2689 ? 220.340 195.165 237.108 1.00 31.20  ? 2689 HIS A N     1 
ATOM   9034  C  CA    . HIS A 1 2689 ? 219.159 194.801 237.875 1.00 31.66  ? 2689 HIS A CA    1 
ATOM   9035  C  C     . HIS A 1 2689 ? 218.295 193.754 237.190 1.00 34.13  ? 2689 HIS A C     1 
ATOM   9036  O  O     . HIS A 1 2689 ? 217.266 193.361 237.747 1.00 40.45  ? 2689 HIS A O     1 
ATOM   9037  C  CB    . HIS A 1 2689 ? 218.330 196.053 238.172 1.00 28.47  ? 2689 HIS A CB    1 
ATOM   9038  C  CG    . HIS A 1 2689 ? 219.094 197.117 238.894 1.00 40.13  ? 2689 HIS A CG    1 
ATOM   9039  N  ND1   . HIS A 1 2689 ? 219.290 198.377 238.373 1.00 42.41  ? 2689 HIS A ND1   1 
ATOM   9040  C  CD2   . HIS A 1 2689 ? 219.724 197.104 240.092 1.00 35.57  ? 2689 HIS A CD2   1 
ATOM   9041  C  CE1   . HIS A 1 2689 ? 220.002 199.097 239.222 1.00 32.94  ? 2689 HIS A CE1   1 
ATOM   9042  N  NE2   . HIS A 1 2689 ? 220.278 198.347 240.273 1.00 39.01  ? 2689 HIS A NE2   1 
ATOM   9043  N  N     . GLY A 1 2690 ? 218.685 193.288 236.008 1.00 33.45  ? 2690 GLY A N     1 
ATOM   9044  C  CA    . GLY A 1 2690 ? 217.934 192.239 235.338 1.00 35.84  ? 2690 GLY A CA    1 
ATOM   9045  C  C     . GLY A 1 2690 ? 216.533 192.638 234.934 1.00 30.56  ? 2690 GLY A C     1 
ATOM   9046  O  O     . GLY A 1 2690 ? 215.609 191.820 235.020 1.00 38.61  ? 2690 GLY A O     1 
ATOM   9047  N  N     . GLY A 1 2691 ? 216.352 193.874 234.492 1.00 30.61  ? 2691 GLY A N     1 
ATOM   9048  C  CA    . GLY A 1 2691 ? 215.047 194.321 234.056 1.00 26.21  ? 2691 GLY A CA    1 
ATOM   9049  C  C     . GLY A 1 2691 ? 215.040 195.813 233.815 1.00 37.97  ? 2691 GLY A C     1 
ATOM   9050  O  O     . GLY A 1 2691 ? 216.080 196.476 233.827 1.00 51.46  ? 2691 GLY A O     1 
ATOM   9051  N  N     . PHE A 1 2692 ? 213.834 196.331 233.595 1.00 35.36  ? 2692 PHE A N     1 
ATOM   9052  C  CA    . PHE A 1 2692 ? 213.637 197.753 233.354 1.00 32.73  ? 2692 PHE A CA    1 
ATOM   9053  C  C     . PHE A 1 2692 ? 212.246 198.141 233.834 1.00 31.19  ? 2692 PHE A C     1 
ATOM   9054  O  O     . PHE A 1 2692 ? 211.472 197.304 234.302 1.00 38.59  ? 2692 PHE A O     1 
ATOM   9055  C  CB    . PHE A 1 2692 ? 213.837 198.097 231.874 1.00 39.27  ? 2692 PHE A CB    1 
ATOM   9056  C  CG    . PHE A 1 2692 ? 212.844 197.444 230.953 1.00 39.98  ? 2692 PHE A CG    1 
ATOM   9057  C  CD1   . PHE A 1 2692 ? 213.058 196.164 230.474 1.00 37.09  ? 2692 PHE A CD1   1 
ATOM   9058  C  CD2   . PHE A 1 2692 ? 211.702 198.116 230.558 1.00 37.33  ? 2692 PHE A CD2   1 
ATOM   9059  C  CE1   . PHE A 1 2692 ? 212.150 195.568 229.630 1.00 34.48  ? 2692 PHE A CE1   1 
ATOM   9060  C  CE2   . PHE A 1 2692 ? 210.791 197.522 229.714 1.00 36.82  ? 2692 PHE A CE2   1 
ATOM   9061  C  CZ    . PHE A 1 2692 ? 211.016 196.248 229.249 1.00 32.84  ? 2692 PHE A CZ    1 
ATOM   9062  N  N     . TYR A 1 2693 ? 211.933 199.428 233.715 1.00 39.85  ? 2693 TYR A N     1 
ATOM   9063  C  CA    . TYR A 1 2693 ? 210.644 199.976 234.115 1.00 35.24  ? 2693 TYR A CA    1 
ATOM   9064  C  C     . TYR A 1 2693 ? 209.794 200.219 232.878 1.00 42.56  ? 2693 TYR A C     1 
ATOM   9065  O  O     . TYR A 1 2693 ? 210.229 200.905 231.948 1.00 44.89  ? 2693 TYR A O     1 
ATOM   9066  C  CB    . TYR A 1 2693 ? 210.819 201.285 234.887 1.00 31.39  ? 2693 TYR A CB    1 
ATOM   9067  C  CG    . TYR A 1 2693 ? 210.997 201.114 236.376 1.00 35.39  ? 2693 TYR A CG    1 
ATOM   9068  C  CD1   . TYR A 1 2693 ? 209.941 200.714 237.180 1.00 40.04  ? 2693 TYR A CD1   1 
ATOM   9069  C  CD2   . TYR A 1 2693 ? 212.222 201.358 236.979 1.00 34.78  ? 2693 TYR A CD2   1 
ATOM   9070  C  CE1   . TYR A 1 2693 ? 210.101 200.558 238.539 1.00 36.68  ? 2693 TYR A CE1   1 
ATOM   9071  C  CE2   . TYR A 1 2693 ? 212.390 201.205 238.336 1.00 38.26  ? 2693 TYR A CE2   1 
ATOM   9072  C  CZ    . TYR A 1 2693 ? 211.327 200.805 239.112 1.00 38.11  ? 2693 TYR A CZ    1 
ATOM   9073  O  OH    . TYR A 1 2693 ? 211.492 200.651 240.467 1.00 39.36  ? 2693 TYR A OH    1 
ATOM   9074  N  N     . ARG A 1 2694 ? 208.588 199.658 232.868 1.00 45.51  ? 2694 ARG A N     1 
ATOM   9075  C  CA    . ARG A 1 2694 ? 207.641 199.909 231.788 1.00 41.97  ? 2694 ARG A CA    1 
ATOM   9076  C  C     . ARG A 1 2694 ? 206.932 201.227 232.067 1.00 44.35  ? 2694 ARG A C     1 
ATOM   9077  O  O     . ARG A 1 2694 ? 206.144 201.329 233.013 1.00 47.46  ? 2694 ARG A O     1 
ATOM   9078  C  CB    . ARG A 1 2694 ? 206.644 198.763 231.661 1.00 41.65  ? 2694 ARG A CB    1 
ATOM   9079  C  CG    . ARG A 1 2694 ? 205.676 198.929 230.503 1.00 47.12  ? 2694 ARG A CG    1 
ATOM   9080  C  CD    . ARG A 1 2694 ? 204.895 197.658 230.237 1.00 48.16  ? 2694 ARG A CD    1 
ATOM   9081  N  NE    . ARG A 1 2694 ? 204.243 197.150 231.437 1.00 49.49  ? 2694 ARG A NE    1 
ATOM   9082  C  CZ    . ARG A 1 2694 ? 203.557 196.017 231.489 1.00 46.71  ? 2694 ARG A CZ    1 
ATOM   9083  N  NH1   . ARG A 1 2694 ? 203.412 195.250 230.423 1.00 44.99  ? 2694 ARG A NH1   1 
ATOM   9084  N  NH2   . ARG A 1 2694 ? 203.002 195.647 232.638 1.00 44.05  ? 2694 ARG A NH2   1 
ATOM   9085  N  N     . THR A 1 2695 ? 207.205 202.235 231.240 1.00 46.97  ? 2695 THR A N     1 
ATOM   9086  C  CA    . THR A 1 2695 ? 206.673 203.572 231.467 1.00 44.29  ? 2695 THR A CA    1 
ATOM   9087  C  C     . THR A 1 2695 ? 205.173 203.667 231.220 1.00 47.91  ? 2695 THR A C     1 
ATOM   9088  O  O     . THR A 1 2695 ? 204.579 204.703 231.534 1.00 50.40  ? 2695 THR A O     1 
ATOM   9089  C  CB    . THR A 1 2695 ? 207.407 204.579 230.582 1.00 50.57  ? 2695 THR A CB    1 
ATOM   9090  O  OG1   . THR A 1 2695 ? 207.351 204.146 229.218 1.00 51.25  ? 2695 THR A OG1   1 
ATOM   9091  C  CG2   . THR A 1 2695 ? 208.860 204.692 231.009 1.00 46.14  ? 2695 THR A CG2   1 
ATOM   9092  N  N     . SER A 1 2696 ? 204.554 202.627 230.660 1.00 53.74  ? 2696 SER A N     1 
ATOM   9093  C  CA    . SER A 1 2696 ? 203.111 202.653 230.448 1.00 52.38  ? 2696 SER A CA    1 
ATOM   9094  C  C     . SER A 1 2696 ? 202.358 202.706 231.771 1.00 53.50  ? 2696 SER A C     1 
ATOM   9095  O  O     . SER A 1 2696 ? 201.386 203.457 231.912 1.00 57.03  ? 2696 SER A O     1 
ATOM   9096  C  CB    . SER A 1 2696 ? 202.680 201.433 229.636 1.00 49.47  ? 2696 SER A CB    1 
ATOM   9097  O  OG    . SER A 1 2696 ? 203.339 201.399 228.382 1.00 54.40  ? 2696 SER A OG    1 
ATOM   9098  N  N     . ASP A 1 2697 ? 202.794 201.918 232.757 1.00 39.97  ? 2697 ASP A N     1 
ATOM   9099  C  CA    . ASP A 1 2697 ? 202.126 201.863 234.052 1.00 39.63  ? 2697 ASP A CA    1 
ATOM   9100  C  C     . ASP A 1 2697 ? 203.117 201.836 235.210 1.00 47.71  ? 2697 ASP A C     1 
ATOM   9101  O  O     . ASP A 1 2697 ? 202.754 201.421 236.316 1.00 46.44  ? 2697 ASP A O     1 
ATOM   9102  C  CB    . ASP A 1 2697 ? 201.192 200.653 234.126 1.00 44.23  ? 2697 ASP A CB    1 
ATOM   9103  C  CG    . ASP A 1 2697 ? 201.913 199.346 233.883 1.00 53.53  ? 2697 ASP A CG    1 
ATOM   9104  O  OD1   . ASP A 1 2697 ? 202.820 199.317 233.026 1.00 54.90  ? 2697 ASP A OD1   1 
ATOM   9105  O  OD2   . ASP A 1 2697 ? 201.571 198.346 234.546 1.00 56.39  ? 2697 ASP A OD2   1 
ATOM   9106  N  N     . GLN A 1 2698 ? 204.357 202.271 234.976 1.00 41.10  ? 2698 GLN A N     1 
ATOM   9107  C  CA    . GLN A 1 2698 ? 205.381 202.379 236.018 1.00 40.57  ? 2698 GLN A CA    1 
ATOM   9108  C  C     . GLN A 1 2698 ? 205.583 201.052 236.749 1.00 43.37  ? 2698 GLN A C     1 
ATOM   9109  O  O     . GLN A 1 2698 ? 205.679 200.999 237.976 1.00 52.15  ? 2698 GLN A O     1 
ATOM   9110  C  CB    . GLN A 1 2698 ? 205.041 203.498 237.004 1.00 37.90  ? 2698 GLN A CB    1 
ATOM   9111  C  CG    . GLN A 1 2698 ? 205.351 204.889 236.492 1.00 40.19  ? 2698 GLN A CG    1 
ATOM   9112  C  CD    . GLN A 1 2698 ? 204.306 205.406 235.530 1.00 43.87  ? 2698 GLN A CD    1 
ATOM   9113  O  OE1   . GLN A 1 2698 ? 204.600 205.684 234.369 1.00 52.02  ? 2698 GLN A OE1   1 
ATOM   9114  N  NE2   . GLN A 1 2698 ? 203.079 205.550 236.012 1.00 38.18  ? 2698 GLN A NE2   1 
ATOM   9115  N  N     . THR A 1 2699 ? 205.654 199.971 235.980 1.00 40.82  ? 2699 THR A N     1 
ATOM   9116  C  CA    . THR A 1 2699 ? 205.789 198.627 236.522 1.00 42.46  ? 2699 THR A CA    1 
ATOM   9117  C  C     . THR A 1 2699 ? 207.176 198.087 236.207 1.00 44.30  ? 2699 THR A C     1 
ATOM   9118  O  O     . THR A 1 2699 ? 207.624 198.149 235.058 1.00 46.12  ? 2699 THR A O     1 
ATOM   9119  C  CB    . THR A 1 2699 ? 204.717 197.696 235.952 1.00 45.44  ? 2699 THR A CB    1 
ATOM   9120  O  OG1   . THR A 1 2699 ? 203.432 198.081 236.455 1.00 45.37  ? 2699 THR A OG1   1 
ATOM   9121  C  CG2   . THR A 1 2699 ? 204.989 196.260 236.353 1.00 43.45  ? 2699 THR A CG2   1 
ATOM   9122  N  N     . TRP A 1 2700 ? 207.851 197.565 237.227 1.00 40.68  ? 2700 TRP A N     1 
ATOM   9123  C  CA    . TRP A 1 2700 ? 209.156 196.952 237.030 1.00 34.03  ? 2700 TRP A CA    1 
ATOM   9124  C  C     . TRP A 1 2700 ? 208.999 195.650 236.255 1.00 41.36  ? 2700 TRP A C     1 
ATOM   9125  O  O     . TRP A 1 2700 ? 208.320 194.725 236.712 1.00 49.37  ? 2700 TRP A O     1 
ATOM   9126  C  CB    . TRP A 1 2700 ? 209.830 196.700 238.375 1.00 29.20  ? 2700 TRP A CB    1 
ATOM   9127  C  CG    . TRP A 1 2700 ? 211.118 195.953 238.263 1.00 38.01  ? 2700 TRP A CG    1 
ATOM   9128  C  CD1   . TRP A 1 2700 ? 211.329 194.639 238.550 1.00 41.16  ? 2700 TRP A CD1   1 
ATOM   9129  C  CD2   . TRP A 1 2700 ? 212.376 196.475 237.827 1.00 36.11  ? 2700 TRP A CD2   1 
ATOM   9130  N  NE1   . TRP A 1 2700 ? 212.641 194.309 238.322 1.00 35.15  ? 2700 TRP A NE1   1 
ATOM   9131  C  CE2   . TRP A 1 2700 ? 213.305 195.421 237.877 1.00 37.87  ? 2700 TRP A CE2   1 
ATOM   9132  C  CE3   . TRP A 1 2700 ? 212.807 197.733 237.398 1.00 30.61  ? 2700 TRP A CE3   1 
ATOM   9133  C  CZ2   . TRP A 1 2700 ? 214.635 195.585 237.516 1.00 45.09  ? 2700 TRP A CZ2   1 
ATOM   9134  C  CZ3   . TRP A 1 2700 ? 214.126 197.894 237.044 1.00 33.97  ? 2700 TRP A CZ3   1 
ATOM   9135  C  CH2   . TRP A 1 2700 ? 215.026 196.827 237.104 1.00 41.49  ? 2700 TRP A CH2   1 
ATOM   9136  N  N     . VAL A 1 2701 ? 209.625 195.580 235.085 1.00 34.92  ? 2701 VAL A N     1 
ATOM   9137  C  CA    . VAL A 1 2701 ? 209.572 194.410 234.217 1.00 28.66  ? 2701 VAL A CA    1 
ATOM   9138  C  C     . VAL A 1 2701 ? 210.884 193.657 234.360 1.00 36.23  ? 2701 VAL A C     1 
ATOM   9139  O  O     . VAL A 1 2701 ? 211.960 194.241 234.194 1.00 48.08  ? 2701 VAL A O     1 
ATOM   9140  C  CB    . VAL A 1 2701 ? 209.327 194.807 232.752 1.00 31.75  ? 2701 VAL A CB    1 
ATOM   9141  C  CG1   . VAL A 1 2701 ? 209.449 193.597 231.850 1.00 34.43  ? 2701 VAL A CG1   1 
ATOM   9142  C  CG2   . VAL A 1 2701 ? 207.965 195.454 232.602 1.00 40.79  ? 2701 VAL A CG2   1 
ATOM   9143  N  N     . LYS A 1 2702 ? 210.798 192.366 234.661 1.00 34.80  ? 2702 LYS A N     1 
ATOM   9144  C  CA    . LYS A 1 2702 ? 211.973 191.526 234.850 1.00 27.03  ? 2702 LYS A CA    1 
ATOM   9145  C  C     . LYS A 1 2702 ? 212.275 190.759 233.571 1.00 40.20  ? 2702 LYS A C     1 
ATOM   9146  O  O     . LYS A 1 2702 ? 211.402 190.073 233.031 1.00 49.08  ? 2702 LYS A O     1 
ATOM   9147  C  CB    . LYS A 1 2702 ? 211.767 190.553 236.010 1.00 28.65  ? 2702 LYS A CB    1 
ATOM   9148  C  CG    . LYS A 1 2702 ? 212.964 189.659 236.279 1.00 42.51  ? 2702 LYS A CG    1 
ATOM   9149  C  CD    . LYS A 1 2702 ? 212.750 188.797 237.511 1.00 46.87  ? 2702 LYS A CD    1 
ATOM   9150  C  CE    . LYS A 1 2702 ? 211.862 187.604 237.203 1.00 47.13  ? 2702 LYS A CE    1 
ATOM   9151  N  NZ    . LYS A 1 2702 ? 212.560 186.600 236.355 1.00 48.65  ? 2702 LYS A NZ    1 
ATOM   9152  N  N     . LEU A 1 2703 ? 213.511 190.875 233.092 1.00 45.37  ? 2703 LEU A N     1 
ATOM   9153  C  CA    . LEU A 1 2703 ? 213.934 190.138 231.911 1.00 33.76  ? 2703 LEU A CA    1 
ATOM   9154  C  C     . LEU A 1 2703 ? 214.083 188.655 232.224 1.00 37.66  ? 2703 LEU A C     1 
ATOM   9155  O  O     . LEU A 1 2703 ? 214.467 188.264 233.329 1.00 48.64  ? 2703 LEU A O     1 
ATOM   9156  C  CB    . LEU A 1 2703 ? 215.263 190.677 231.385 1.00 38.38  ? 2703 LEU A CB    1 
ATOM   9157  C  CG    . LEU A 1 2703 ? 215.333 192.118 230.886 1.00 37.71  ? 2703 LEU A CG    1 
ATOM   9158  C  CD1   . LEU A 1 2703 ? 216.558 192.293 230.015 1.00 33.99  ? 2703 LEU A CD1   1 
ATOM   9159  C  CD2   . LEU A 1 2703 ? 214.078 192.493 230.129 1.00 35.99  ? 2703 LEU A CD2   1 
ATOM   9160  N  N     . GLU A 1 2704 ? 213.775 187.824 231.233 1.00 44.35  ? 2704 GLU A N     1 
ATOM   9161  C  CA    . GLU A 1 2704 ? 213.996 186.388 231.333 1.00 42.68  ? 2704 GLU A CA    1 
ATOM   9162  C  C     . GLU A 1 2704 ? 214.383 185.854 229.965 1.00 42.69  ? 2704 GLU A C     1 
ATOM   9163  O  O     . GLU A 1 2704 ? 213.756 186.204 228.962 1.00 52.57  ? 2704 GLU A O     1 
ATOM   9164  C  CB    . GLU A 1 2704 ? 212.752 185.662 231.854 1.00 44.71  ? 2704 GLU A CB    1 
ATOM   9165  C  CG    . GLU A 1 2704 ? 212.939 184.162 232.009 1.00 52.91  ? 2704 GLU A CG    1 
ATOM   9166  C  CD    . GLU A 1 2704 ? 211.696 183.373 231.645 1.00 60.81  ? 2704 GLU A CD    1 
ATOM   9167  O  OE1   . GLU A 1 2704 ? 211.779 182.129 231.574 1.00 51.86  ? 2704 GLU A OE1   1 
ATOM   9168  O  OE2   . GLU A 1 2704 ? 210.635 183.996 231.438 1.00 59.80  ? 2704 GLU A OE2   1 
ATOM   9169  N  N     . ARG A 1 2705 ? 215.417 185.013 229.935 1.00 37.24  ? 2705 ARG A N     1 
ATOM   9170  C  CA    . ARG A 1 2705 ? 215.896 184.376 228.707 1.00 32.27  ? 2705 ARG A CA    1 
ATOM   9171  C  C     . ARG A 1 2705 ? 216.297 185.406 227.654 1.00 31.08  ? 2705 ARG A C     1 
ATOM   9172  O  O     . ARG A 1 2705 ? 216.103 185.202 226.455 1.00 38.88  ? 2705 ARG A O     1 
ATOM   9173  C  CB    . ARG A 1 2705 ? 214.854 183.407 228.146 1.00 32.87  ? 2705 ARG A CB    1 
ATOM   9174  C  CG    . ARG A 1 2705 ? 214.787 182.080 228.874 1.00 31.77  ? 2705 ARG A CG    1 
ATOM   9175  C  CD    . ARG A 1 2705 ? 213.892 181.100 228.142 1.00 34.41  ? 2705 ARG A CD    1 
ATOM   9176  N  NE    . ARG A 1 2705 ? 212.495 181.515 228.150 1.00 36.83  ? 2705 ARG A NE    1 
ATOM   9177  C  CZ    . ARG A 1 2705 ? 211.786 181.775 227.061 1.00 40.13  ? 2705 ARG A CZ    1 
ATOM   9178  N  NH1   . ARG A 1 2705 ? 212.319 181.700 225.855 1.00 43.49  ? 2705 ARG A NH1   1 
ATOM   9179  N  NH2   . ARG A 1 2705 ? 210.508 182.119 227.187 1.00 40.62  ? 2705 ARG A NH2   1 
ATOM   9180  N  N     . ILE A 1 2706 ? 216.870 186.520 228.102 1.00 32.47  ? 2706 ILE A N     1 
ATOM   9181  C  CA    . ILE A 1 2706 ? 217.327 187.587 227.220 1.00 30.91  ? 2706 ILE A CA    1 
ATOM   9182  C  C     . ILE A 1 2706 ? 218.749 187.957 227.611 1.00 40.40  ? 2706 ILE A C     1 
ATOM   9183  O  O     . ILE A 1 2706 ? 219.031 188.189 228.791 1.00 47.81  ? 2706 ILE A O     1 
ATOM   9184  C  CB    . ILE A 1 2706 ? 216.411 188.823 227.293 1.00 36.40  ? 2706 ILE A CB    1 
ATOM   9185  C  CG1   . ILE A 1 2706 ? 215.042 188.517 226.689 1.00 37.35  ? 2706 ILE A CG1   1 
ATOM   9186  C  CG2   . ILE A 1 2706 ? 217.047 189.999 226.581 1.00 34.38  ? 2706 ILE A CG2   1 
ATOM   9187  C  CD1   . ILE A 1 2706 ? 214.023 189.591 226.936 1.00 29.04  ? 2706 ILE A CD1   1 
ATOM   9188  N  N     . GLN A 1 2707 ? 219.640 188.014 226.624 1.00 35.29  ? 2707 GLN A N     1 
ATOM   9189  C  CA    . GLN A 1 2707 ? 221.023 188.407 226.846 1.00 28.26  ? 2707 GLN A CA    1 
ATOM   9190  C  C     . GLN A 1 2707 ? 221.451 189.366 225.747 1.00 28.88  ? 2707 GLN A C     1 
ATOM   9191  O  O     . GLN A 1 2707 ? 220.820 189.456 224.692 1.00 37.80  ? 2707 GLN A O     1 
ATOM   9192  C  CB    . GLN A 1 2707 ? 221.957 187.195 226.895 1.00 26.28  ? 2707 GLN A CB    1 
ATOM   9193  C  CG    . GLN A 1 2707 ? 221.794 186.245 225.735 1.00 33.02  ? 2707 GLN A CG    1 
ATOM   9194  C  CD    . GLN A 1 2707 ? 222.853 185.173 225.725 1.00 42.13  ? 2707 GLN A CD    1 
ATOM   9195  O  OE1   . GLN A 1 2707 ? 222.547 183.985 225.762 1.00 41.22  ? 2707 GLN A OE1   1 
ATOM   9196  N  NE2   . GLN A 1 2707 ? 224.111 185.586 225.682 1.00 44.22  ? 2707 GLN A NE2   1 
ATOM   9197  N  N     . PHE A 1 2708 ? 222.538 190.086 226.007 1.00 27.15  ? 2708 PHE A N     1 
ATOM   9198  C  CA    . PHE A 1 2708 ? 223.004 191.147 225.128 1.00 25.78  ? 2708 PHE A CA    1 
ATOM   9199  C  C     . PHE A 1 2708 ? 224.432 190.879 224.681 1.00 31.42  ? 2708 PHE A C     1 
ATOM   9200  O  O     . PHE A 1 2708 ? 225.278 190.466 225.479 1.00 44.76  ? 2708 PHE A O     1 
ATOM   9201  C  CB    . PHE A 1 2708 ? 222.931 192.511 225.821 1.00 27.19  ? 2708 PHE A CB    1 
ATOM   9202  C  CG    . PHE A 1 2708 ? 221.607 192.792 226.463 1.00 37.97  ? 2708 PHE A CG    1 
ATOM   9203  C  CD1   . PHE A 1 2708 ? 220.614 193.456 225.767 1.00 35.54  ? 2708 PHE A CD1   1 
ATOM   9204  C  CD2   . PHE A 1 2708 ? 221.353 192.392 227.763 1.00 38.52  ? 2708 PHE A CD2   1 
ATOM   9205  C  CE1   . PHE A 1 2708 ? 219.395 193.713 226.353 1.00 36.31  ? 2708 PHE A CE1   1 
ATOM   9206  C  CE2   . PHE A 1 2708 ? 220.134 192.646 228.353 1.00 36.33  ? 2708 PHE A CE2   1 
ATOM   9207  C  CZ    . PHE A 1 2708 ? 219.155 193.308 227.648 1.00 34.51  ? 2708 PHE A CZ    1 
ATOM   9208  N  N     . VAL A 1 2709 ? 224.685 191.108 223.398 1.00 23.46  ? 2709 VAL A N     1 
ATOM   9209  C  CA    . VAL A 1 2709 ? 226.025 191.090 222.828 1.00 16.56  ? 2709 VAL A CA    1 
ATOM   9210  C  C     . VAL A 1 2709 ? 226.204 192.380 222.044 1.00 30.65  ? 2709 VAL A C     1 
ATOM   9211  O  O     . VAL A 1 2709 ? 225.338 192.748 221.246 1.00 42.98  ? 2709 VAL A O     1 
ATOM   9212  C  CB    . VAL A 1 2709 ? 226.251 189.865 221.923 1.00 24.18  ? 2709 VAL A CB    1 
ATOM   9213  C  CG1   . VAL A 1 2709 ? 227.543 190.010 221.145 1.00 26.45  ? 2709 VAL A CG1   1 
ATOM   9214  C  CG2   . VAL A 1 2709 ? 226.272 188.598 222.750 1.00 35.63  ? 2709 VAL A CG2   1 
ATOM   9215  N  N     . GLY A 1 2710 ? 227.313 193.071 222.280 1.00 28.78  ? 2710 GLY A N     1 
ATOM   9216  C  CA    . GLY A 1 2710 ? 227.601 194.326 221.615 1.00 20.91  ? 2710 GLY A CA    1 
ATOM   9217  C  C     . GLY A 1 2710 ? 228.846 194.217 220.758 1.00 30.12  ? 2710 GLY A C     1 
ATOM   9218  O  O     . GLY A 1 2710 ? 229.725 193.395 221.018 1.00 42.04  ? 2710 GLY A O     1 
ATOM   9219  N  N     . ALA A 1 2711 ? 228.905 195.042 219.720 1.00 27.90  ? 2711 ALA A N     1 
ATOM   9220  C  CA    . ALA A 1 2711 ? 230.092 195.188 218.895 1.00 19.08  ? 2711 ALA A CA    1 
ATOM   9221  C  C     . ALA A 1 2711 ? 230.347 196.670 218.683 1.00 28.92  ? 2711 ALA A C     1 
ATOM   9222  O  O     . ALA A 1 2711 ? 229.422 197.483 218.736 1.00 45.56  ? 2711 ALA A O     1 
ATOM   9223  C  CB    . ALA A 1 2711 ? 229.944 194.475 217.547 1.00 20.25  ? 2711 ALA A CB    1 
ATOM   9224  N  N     . CYS A 1 2712 ? 231.609 197.022 218.461 1.00 24.28  ? 2712 CYS A N     1 
ATOM   9225  C  CA    . CYS A 1 2712 ? 231.950 198.424 218.276 1.00 29.53  ? 2712 CYS A CA    1 
ATOM   9226  C  C     . CYS A 1 2712 ? 233.357 198.535 217.715 1.00 39.59  ? 2712 CYS A C     1 
ATOM   9227  O  O     . CYS A 1 2712 ? 234.178 197.625 217.855 1.00 40.38  ? 2712 CYS A O     1 
ATOM   9228  C  CB    . CYS A 1 2712 ? 231.845 199.207 219.589 1.00 35.07  ? 2712 CYS A CB    1 
ATOM   9229  S  SG    . CYS A 1 2712 ? 232.625 198.406 221.001 1.00 47.33  ? 2712 CYS A SG    1 
ATOM   9230  N  N     . ASN A 1 2713 ? 233.615 199.663 217.070 1.00 43.04  ? 2713 ASN A N     1 
ATOM   9231  C  CA    . ASN A 1 2713 ? 234.963 200.067 216.725 1.00 31.39  ? 2713 ASN A CA    1 
ATOM   9232  C  C     . ASN A 1 2713 ? 235.632 200.678 217.952 1.00 38.85  ? 2713 ASN A C     1 
ATOM   9233  O  O     . ASN A 1 2713 ? 234.951 201.072 218.902 1.00 45.77  ? 2713 ASN A O     1 
ATOM   9234  C  CB    . ASN A 1 2713 ? 234.928 201.062 215.570 1.00 39.09  ? 2713 ASN A CB    1 
ATOM   9235  C  CG    . ASN A 1 2713 ? 234.212 200.514 214.354 1.00 42.87  ? 2713 ASN A CG    1 
ATOM   9236  O  OD1   . ASN A 1 2713 ? 233.824 199.348 214.319 1.00 41.77  ? 2713 ASN A OD1   1 
ATOM   9237  N  ND2   . ASN A 1 2713 ? 234.033 201.356 213.347 1.00 47.74  ? 2713 ASN A ND2   1 
ATOM   9238  N  N     . PRO A 1 2714 ? 236.961 200.754 217.972 1.00 40.70  ? 2714 PRO A N     1 
ATOM   9239  C  CA    . PRO A 1 2714 ? 237.653 201.297 219.146 1.00 40.22  ? 2714 PRO A CA    1 
ATOM   9240  C  C     . PRO A 1 2714 ? 237.182 202.705 219.457 1.00 40.49  ? 2714 PRO A C     1 
ATOM   9241  O  O     . PRO A 1 2714 ? 236.909 203.494 218.541 1.00 46.16  ? 2714 PRO A O     1 
ATOM   9242  C  CB    . PRO A 1 2714 ? 239.128 201.284 218.723 1.00 38.65  ? 2714 PRO A CB    1 
ATOM   9243  C  CG    . PRO A 1 2714 ? 239.213 200.200 217.723 1.00 41.30  ? 2714 PRO A CG    1 
ATOM   9244  C  CD    . PRO A 1 2714 ? 237.911 200.219 216.981 1.00 40.81  ? 2714 PRO A CD    1 
ATOM   9245  N  N     . PRO A 1 2715 ? 237.067 203.057 220.741 1.00 41.89  ? 2715 PRO A N     1 
ATOM   9246  C  CA    . PRO A 1 2715 ? 236.532 204.381 221.100 1.00 45.35  ? 2715 PRO A CA    1 
ATOM   9247  C  C     . PRO A 1 2715 ? 237.401 205.545 220.658 1.00 44.97  ? 2715 PRO A C     1 
ATOM   9248  O  O     . PRO A 1 2715 ? 237.018 206.697 220.892 1.00 47.29  ? 2715 PRO A O     1 
ATOM   9249  C  CB    . PRO A 1 2715 ? 236.429 204.318 222.630 1.00 45.96  ? 2715 PRO A CB    1 
ATOM   9250  C  CG    . PRO A 1 2715 ? 237.350 203.220 223.035 1.00 42.46  ? 2715 PRO A CG    1 
ATOM   9251  C  CD    . PRO A 1 2715 ? 237.320 202.222 221.926 1.00 39.93  ? 2715 PRO A CD    1 
ATOM   9252  N  N     . THR A 1 2716 ? 238.553 205.289 220.042 1.00 42.41  ? 2716 THR A N     1 
ATOM   9253  C  CA    . THR A 1 2716 ? 239.365 206.355 219.474 1.00 41.75  ? 2716 THR A CA    1 
ATOM   9254  C  C     . THR A 1 2716 ? 239.018 206.648 218.022 1.00 46.57  ? 2716 THR A C     1 
ATOM   9255  O  O     . THR A 1 2716 ? 239.568 207.593 217.449 1.00 53.22  ? 2716 THR A O     1 
ATOM   9256  C  CB    . THR A 1 2716 ? 240.848 206.001 219.586 1.00 50.56  ? 2716 THR A CB    1 
ATOM   9257  O  OG1   . THR A 1 2716 ? 241.111 204.804 218.846 1.00 53.78  ? 2716 THR A OG1   1 
ATOM   9258  C  CG2   . THR A 1 2716 ? 241.229 205.785 221.038 1.00 45.24  ? 2716 THR A CG2   1 
ATOM   9259  N  N     . ASP A 1 2717 ? 238.130 205.863 217.417 1.00 49.37  ? 2717 ASP A N     1 
ATOM   9260  C  CA    . ASP A 1 2717 ? 237.690 206.139 216.061 1.00 41.66  ? 2717 ASP A CA    1 
ATOM   9261  C  C     . ASP A 1 2717 ? 236.726 207.324 216.054 1.00 42.85  ? 2717 ASP A C     1 
ATOM   9262  O  O     . ASP A 1 2717 ? 236.029 207.571 217.041 1.00 50.06  ? 2717 ASP A O     1 
ATOM   9263  C  CB    . ASP A 1 2717 ? 237.014 204.910 215.461 1.00 44.08  ? 2717 ASP A CB    1 
ATOM   9264  C  CG    . ASP A 1 2717 ? 238.010 203.877 214.976 1.00 56.13  ? 2717 ASP A CG    1 
ATOM   9265  O  OD1   . ASP A 1 2717 ? 239.215 204.031 215.264 1.00 49.78  ? 2717 ASP A OD1   1 
ATOM   9266  O  OD2   . ASP A 1 2717 ? 237.590 202.913 214.305 1.00 57.49  ? 2717 ASP A OD2   1 
ATOM   9267  N  N     . PRO A 1 2718 ? 236.679 208.083 214.959 1.00 44.61  ? 2718 PRO A N     1 
ATOM   9268  C  CA    . PRO A 1 2718 ? 235.802 209.259 214.919 1.00 42.52  ? 2718 PRO A CA    1 
ATOM   9269  C  C     . PRO A 1 2718 ? 234.337 208.874 215.060 1.00 41.95  ? 2718 PRO A C     1 
ATOM   9270  O  O     . PRO A 1 2718 ? 233.848 207.953 214.405 1.00 48.77  ? 2718 PRO A O     1 
ATOM   9271  C  CB    . PRO A 1 2718 ? 236.093 209.875 213.546 1.00 44.27  ? 2718 PRO A CB    1 
ATOM   9272  C  CG    . PRO A 1 2718 ? 236.748 208.792 212.759 1.00 48.99  ? 2718 PRO A CG    1 
ATOM   9273  C  CD    . PRO A 1 2718 ? 237.494 207.959 213.740 1.00 47.49  ? 2718 PRO A CD    1 
ATOM   9274  N  N     . GLY A 1 2719 ? 233.634 209.604 215.923 1.00 35.43  ? 2719 GLY A N     1 
ATOM   9275  C  CA    . GLY A 1 2719 ? 232.237 209.345 216.190 1.00 36.44  ? 2719 GLY A CA    1 
ATOM   9276  C  C     . GLY A 1 2719 ? 231.966 208.320 217.267 1.00 44.97  ? 2719 GLY A C     1 
ATOM   9277  O  O     . GLY A 1 2719 ? 230.801 208.136 217.640 1.00 49.42  ? 2719 GLY A O     1 
ATOM   9278  N  N     . ARG A 1 2720 ? 232.994 207.653 217.782 1.00 43.44  ? 2720 ARG A N     1 
ATOM   9279  C  CA    . ARG A 1 2720 ? 232.842 206.631 218.807 1.00 36.33  ? 2720 ARG A CA    1 
ATOM   9280  C  C     . ARG A 1 2720 ? 233.111 207.239 220.176 1.00 43.34  ? 2720 ARG A C     1 
ATOM   9281  O  O     . ARG A 1 2720 ? 234.121 207.923 220.368 1.00 43.20  ? 2720 ARG A O     1 
ATOM   9282  C  CB    . ARG A 1 2720 ? 233.792 205.459 218.557 1.00 39.23  ? 2720 ARG A CB    1 
ATOM   9283  C  CG    . ARG A 1 2720 ? 233.749 204.911 217.142 1.00 40.90  ? 2720 ARG A CG    1 
ATOM   9284  C  CD    . ARG A 1 2720 ? 232.333 204.552 216.752 1.00 48.58  ? 2720 ARG A CD    1 
ATOM   9285  N  NE    . ARG A 1 2720 ? 232.257 203.838 215.483 1.00 53.52  ? 2720 ARG A NE    1 
ATOM   9286  C  CZ    . ARG A 1 2720 ? 232.177 204.424 214.297 1.00 49.45  ? 2720 ARG A CZ    1 
ATOM   9287  N  NH1   . ARG A 1 2720 ? 232.186 205.740 214.173 1.00 45.42  ? 2720 ARG A NH1   1 
ATOM   9288  N  NH2   . ARG A 1 2720 ? 232.080 203.670 213.206 1.00 45.90  ? 2720 ARG A NH2   1 
ATOM   9289  N  N     . LYS A 1 2721 ? 232.208 206.991 221.118 1.00 47.68  ? 2721 LYS A N     1 
ATOM   9290  C  CA    . LYS A 1 2721 ? 232.277 207.484 222.485 1.00 42.41  ? 2721 LYS A CA    1 
ATOM   9291  C  C     . LYS A 1 2721 ? 232.727 206.381 223.432 1.00 46.30  ? 2721 LYS A C     1 
ATOM   9292  O  O     . LYS A 1 2721 ? 232.265 205.241 223.318 1.00 54.37  ? 2721 LYS A O     1 
ATOM   9293  C  CB    . LYS A 1 2721 ? 230.914 208.009 222.939 1.00 43.66  ? 2721 LYS A CB    1 
ATOM   9294  C  CG    . LYS A 1 2721 ? 230.698 209.490 222.692 1.00 46.61  ? 2721 LYS A CG    1 
ATOM   9295  C  CD    . LYS A 1 2721 ? 230.387 209.772 221.236 1.00 45.85  ? 2721 LYS A CD    1 
ATOM   9296  C  CE    . LYS A 1 2721 ? 229.152 209.026 220.780 1.00 45.06  ? 2721 LYS A CE    1 
ATOM   9297  N  NZ    . LYS A 1 2721 ? 228.859 209.287 219.345 1.00 44.69  ? 2721 LYS A NZ    1 
ATOM   9298  N  N     . PRO A 1 2722 ? 233.628 206.675 224.367 1.00 49.25  ? 2722 PRO A N     1 
ATOM   9299  C  CA    . PRO A 1 2722 ? 234.029 205.655 225.341 1.00 46.57  ? 2722 PRO A CA    1 
ATOM   9300  C  C     . PRO A 1 2722 ? 232.862 205.253 226.231 1.00 45.79  ? 2722 PRO A C     1 
ATOM   9301  O  O     . PRO A 1 2722 ? 232.111 206.097 226.724 1.00 39.74  ? 2722 PRO A O     1 
ATOM   9302  C  CB    . PRO A 1 2722 ? 235.142 206.342 226.140 1.00 40.57  ? 2722 PRO A CB    1 
ATOM   9303  C  CG    . PRO A 1 2722 ? 234.918 207.796 225.937 1.00 41.51  ? 2722 PRO A CG    1 
ATOM   9304  C  CD    . PRO A 1 2722 ? 234.345 207.944 224.564 1.00 45.40  ? 2722 PRO A CD    1 
ATOM   9305  N  N     . LEU A 1 2723 ? 232.719 203.948 226.436 1.00 40.94  ? 2723 LEU A N     1 
ATOM   9306  C  CA    . LEU A 1 2723 ? 231.610 203.426 227.219 1.00 34.10  ? 2723 LEU A CA    1 
ATOM   9307  C  C     . LEU A 1 2723 ? 231.813 203.715 228.701 1.00 35.15  ? 2723 LEU A C     1 
ATOM   9308  O  O     . LEU A 1 2723 ? 232.940 203.860 229.181 1.00 44.43  ? 2723 LEU A O     1 
ATOM   9309  C  CB    . LEU A 1 2723 ? 231.459 201.923 226.991 1.00 36.36  ? 2723 LEU A CB    1 
ATOM   9310  C  CG    . LEU A 1 2723 ? 230.835 201.512 225.656 1.00 38.62  ? 2723 LEU A CG    1 
ATOM   9311  C  CD1   . LEU A 1 2723 ? 231.165 200.068 225.330 1.00 38.56  ? 2723 LEU A CD1   1 
ATOM   9312  C  CD2   . LEU A 1 2723 ? 229.337 201.727 225.680 1.00 31.57  ? 2723 LEU A CD2   1 
ATOM   9313  N  N     . SER A 1 2724 ? 230.702 203.799 229.426 1.00 26.93  ? 2724 SER A N     1 
ATOM   9314  C  CA    . SER A 1 2724 ? 230.752 204.127 230.842 1.00 27.27  ? 2724 SER A CA    1 
ATOM   9315  C  C     . SER A 1 2724 ? 231.429 203.014 231.630 1.00 32.06  ? 2724 SER A C     1 
ATOM   9316  O  O     . SER A 1 2724 ? 231.356 201.836 231.276 1.00 43.65  ? 2724 SER A O     1 
ATOM   9317  C  CB    . SER A 1 2724 ? 229.344 204.368 231.382 1.00 35.12  ? 2724 SER A CB    1 
ATOM   9318  O  OG    . SER A 1 2724 ? 229.379 204.775 232.737 1.00 38.27  ? 2724 SER A OG    1 
ATOM   9319  N  N     . HIS A 1 2725 ? 232.105 203.404 232.712 1.00 37.76  ? 2725 HIS A N     1 
ATOM   9320  C  CA    . HIS A 1 2725 ? 232.790 202.422 233.543 1.00 31.74  ? 2725 HIS A CA    1 
ATOM   9321  C  C     . HIS A 1 2725 ? 231.807 201.560 234.321 1.00 29.71  ? 2725 HIS A C     1 
ATOM   9322  O  O     . HIS A 1 2725 ? 232.138 200.431 234.696 1.00 36.52  ? 2725 HIS A O     1 
ATOM   9323  C  CB    . HIS A 1 2725 ? 233.754 203.121 234.497 1.00 41.17  ? 2725 HIS A CB    1 
ATOM   9324  C  CG    . HIS A 1 2725 ? 235.066 203.477 233.873 1.00 38.26  ? 2725 HIS A CG    1 
ATOM   9325  N  ND1   . HIS A 1 2725 ? 236.097 204.050 234.585 1.00 46.31  ? 2725 HIS A ND1   1 
ATOM   9326  C  CD2   . HIS A 1 2725 ? 235.516 203.340 232.604 1.00 42.86  ? 2725 HIS A CD2   1 
ATOM   9327  C  CE1   . HIS A 1 2725 ? 237.126 204.250 233.781 1.00 46.75  ? 2725 HIS A CE1   1 
ATOM   9328  N  NE2   . HIS A 1 2725 ? 236.799 203.828 232.574 1.00 46.27  ? 2725 HIS A NE2   1 
ATOM   9329  N  N     . ARG A 1 2726 ? 230.604 202.073 234.583 1.00 29.87  ? 2726 ARG A N     1 
ATOM   9330  C  CA    . ARG A 1 2726 ? 229.589 201.259 235.239 1.00 25.35  ? 2726 ARG A CA    1 
ATOM   9331  C  C     . ARG A 1 2726 ? 228.991 200.239 234.282 1.00 34.32  ? 2726 ARG A C     1 
ATOM   9332  O  O     . ARG A 1 2726 ? 228.622 199.138 234.703 1.00 43.22  ? 2726 ARG A O     1 
ATOM   9333  C  CB    . ARG A 1 2726 ? 228.495 202.151 235.823 1.00 23.72  ? 2726 ARG A CB    1 
ATOM   9334  C  CG    . ARG A 1 2726 ? 229.020 203.261 236.710 1.00 31.03  ? 2726 ARG A CG    1 
ATOM   9335  C  CD    . ARG A 1 2726 ? 227.887 204.042 237.344 1.00 31.17  ? 2726 ARG A CD    1 
ATOM   9336  N  NE    . ARG A 1 2726 ? 227.651 203.635 238.722 1.00 28.49  ? 2726 ARG A NE    1 
ATOM   9337  C  CZ    . ARG A 1 2726 ? 226.619 204.031 239.453 1.00 24.56  ? 2726 ARG A CZ    1 
ATOM   9338  N  NH1   . ARG A 1 2726 ? 225.702 204.848 238.967 1.00 28.74  ? 2726 ARG A NH1   1 
ATOM   9339  N  NH2   . ARG A 1 2726 ? 226.505 203.595 240.703 1.00 33.29  ? 2726 ARG A NH2   1 
ATOM   9340  N  N     . PHE A 1 2727 ? 228.876 200.588 233.000 1.00 40.19  ? 2727 PHE A N     1 
ATOM   9341  C  CA    . PHE A 1 2727 ? 228.422 199.630 232.000 1.00 30.56  ? 2727 PHE A CA    1 
ATOM   9342  C  C     . PHE A 1 2727 ? 229.509 198.617 231.666 1.00 33.24  ? 2727 PHE A C     1 
ATOM   9343  O  O     . PHE A 1 2727 ? 229.226 197.424 231.522 1.00 43.78  ? 2727 PHE A O     1 
ATOM   9344  C  CB    . PHE A 1 2727 ? 227.976 200.363 230.736 1.00 37.81  ? 2727 PHE A CB    1 
ATOM   9345  C  CG    . PHE A 1 2727 ? 227.684 199.454 229.577 1.00 43.38  ? 2727 PHE A CG    1 
ATOM   9346  C  CD1   . PHE A 1 2727 ? 226.502 198.739 229.523 1.00 40.96  ? 2727 PHE A CD1   1 
ATOM   9347  C  CD2   . PHE A 1 2727 ? 228.591 199.318 228.541 1.00 36.88  ? 2727 PHE A CD2   1 
ATOM   9348  C  CE1   . PHE A 1 2727 ? 226.232 197.904 228.461 1.00 28.11  ? 2727 PHE A CE1   1 
ATOM   9349  C  CE2   . PHE A 1 2727 ? 228.324 198.484 227.479 1.00 37.79  ? 2727 PHE A CE2   1 
ATOM   9350  C  CZ    . PHE A 1 2727 ? 227.143 197.778 227.438 1.00 34.81  ? 2727 PHE A CZ    1 
ATOM   9351  N  N     . LEU A 1 2728 ? 230.755 199.076 231.541 1.00 37.30  ? 2728 LEU A N     1 
ATOM   9352  C  CA    . LEU A 1 2728 ? 231.856 198.184 231.205 1.00 38.01  ? 2728 LEU A CA    1 
ATOM   9353  C  C     . LEU A 1 2728 ? 232.176 197.205 232.324 1.00 38.47  ? 2728 LEU A C     1 
ATOM   9354  O  O     . LEU A 1 2728 ? 232.903 196.236 232.091 1.00 47.83  ? 2728 LEU A O     1 
ATOM   9355  C  CB    . LEU A 1 2728 ? 233.102 198.996 230.859 1.00 46.78  ? 2728 LEU A CB    1 
ATOM   9356  C  CG    . LEU A 1 2728 ? 233.209 199.495 229.419 1.00 41.72  ? 2728 LEU A CG    1 
ATOM   9357  C  CD1   . LEU A 1 2728 ? 234.525 200.219 229.210 1.00 43.60  ? 2728 LEU A CD1   1 
ATOM   9358  C  CD2   . LEU A 1 2728 ? 233.068 198.340 228.447 1.00 41.43  ? 2728 LEU A CD2   1 
ATOM   9359  N  N     . ARG A 1 2729 ? 231.654 197.433 233.528 1.00 33.18  ? 2729 ARG A N     1 
ATOM   9360  C  CA    . ARG A 1 2729 ? 231.937 196.531 234.638 1.00 28.74  ? 2729 ARG A CA    1 
ATOM   9361  C  C     . ARG A 1 2729 ? 231.332 195.152 234.410 1.00 33.02  ? 2729 ARG A C     1 
ATOM   9362  O  O     . ARG A 1 2729 ? 231.901 194.144 234.845 1.00 43.71  ? 2729 ARG A O     1 
ATOM   9363  C  CB    . ARG A 1 2729 ? 231.422 197.140 235.941 1.00 26.23  ? 2729 ARG A CB    1 
ATOM   9364  C  CG    . ARG A 1 2729 ? 231.266 196.155 237.074 1.00 34.80  ? 2729 ARG A CG    1 
ATOM   9365  C  CD    . ARG A 1 2729 ? 230.776 196.831 238.334 1.00 32.26  ? 2729 ARG A CD    1 
ATOM   9366  N  NE    . ARG A 1 2729 ? 230.306 195.854 239.306 1.00 24.22  ? 2729 ARG A NE    1 
ATOM   9367  C  CZ    . ARG A 1 2729 ? 229.108 195.878 239.868 1.00 28.79  ? 2729 ARG A CZ    1 
ATOM   9368  N  NH1   . ARG A 1 2729 ? 228.234 196.829 239.588 1.00 39.83  ? 2729 ARG A NH1   1 
ATOM   9369  N  NH2   . ARG A 1 2729 ? 228.776 194.923 240.730 1.00 34.64  ? 2729 ARG A NH2   1 
ATOM   9370  N  N     . HIS A 1 2730 ? 230.196 195.080 233.719 1.00 44.02  ? 2730 HIS A N     1 
ATOM   9371  C  CA    . HIS A 1 2730 ? 229.504 193.813 233.530 1.00 41.85  ? 2730 HIS A CA    1 
ATOM   9372  C  C     . HIS A 1 2730 ? 229.771 193.163 232.181 1.00 38.26  ? 2730 HIS A C     1 
ATOM   9373  O  O     . HIS A 1 2730 ? 229.438 191.987 232.006 1.00 50.01  ? 2730 HIS A O     1 
ATOM   9374  C  CB    . HIS A 1 2730 ? 227.994 194.001 233.677 1.00 45.78  ? 2730 HIS A CB    1 
ATOM   9375  C  CG    . HIS A 1 2730 ? 227.600 194.901 234.802 1.00 43.00  ? 2730 HIS A CG    1 
ATOM   9376  N  ND1   . HIS A 1 2730 ? 227.405 196.255 234.638 1.00 44.44  ? 2730 HIS A ND1   1 
ATOM   9377  C  CD2   . HIS A 1 2730 ? 227.350 194.640 236.106 1.00 39.95  ? 2730 HIS A CD2   1 
ATOM   9378  C  CE1   . HIS A 1 2730 ? 227.061 196.791 235.794 1.00 47.28  ? 2730 HIS A CE1   1 
ATOM   9379  N  NE2   . HIS A 1 2730 ? 227.021 195.833 236.701 1.00 48.98  ? 2730 HIS A NE2   1 
ATOM   9380  N  N     . VAL A 1 2731 ? 230.346 193.884 231.226 1.00 33.71  ? 2731 VAL A N     1 
ATOM   9381  C  CA    . VAL A 1 2731 ? 230.521 193.365 229.875 1.00 29.39  ? 2731 VAL A CA    1 
ATOM   9382  C  C     . VAL A 1 2731 ? 232.011 193.111 229.646 1.00 36.60  ? 2731 VAL A C     1 
ATOM   9383  O  O     . VAL A 1 2731 ? 232.803 194.061 229.568 1.00 36.12  ? 2731 VAL A O     1 
ATOM   9384  C  CB    . VAL A 1 2731 ? 229.924 194.309 228.819 1.00 24.35  ? 2731 VAL A CB    1 
ATOM   9385  C  CG1   . VAL A 1 2731 ? 228.425 194.398 229.000 1.00 38.70  ? 2731 VAL A CG1   1 
ATOM   9386  C  CG2   . VAL A 1 2731 ? 230.499 195.706 228.921 1.00 38.61  ? 2731 VAL A CG2   1 
ATOM   9387  N  N     . PRO A 1 2732 ? 232.447 191.854 229.586 1.00 36.83  ? 2732 PRO A N     1 
ATOM   9388  C  CA    . PRO A 1 2732 ? 233.797 191.570 229.095 1.00 26.58  ? 2732 PRO A CA    1 
ATOM   9389  C  C     . PRO A 1 2732 ? 233.969 192.036 227.659 1.00 27.56  ? 2732 PRO A C     1 
ATOM   9390  O  O     . PRO A 1 2732 ? 233.043 191.984 226.848 1.00 34.65  ? 2732 PRO A O     1 
ATOM   9391  C  CB    . PRO A 1 2732 ? 233.904 190.043 229.203 1.00 24.38  ? 2732 PRO A CB    1 
ATOM   9392  C  CG    . PRO A 1 2732 ? 232.520 189.558 229.531 1.00 26.97  ? 2732 PRO A CG    1 
ATOM   9393  C  CD    . PRO A 1 2732 ? 231.853 190.679 230.236 1.00 28.04  ? 2732 PRO A CD    1 
ATOM   9394  N  N     . VAL A 1 2733 ? 235.177 192.494 227.348 1.00 33.14  ? 2733 VAL A N     1 
ATOM   9395  C  CA    . VAL A 1 2733 ? 235.513 193.010 226.027 1.00 31.42  ? 2733 VAL A CA    1 
ATOM   9396  C  C     . VAL A 1 2733 ? 236.597 192.128 225.428 1.00 35.30  ? 2733 VAL A C     1 
ATOM   9397  O  O     . VAL A 1 2733 ? 237.619 191.869 226.072 1.00 39.99  ? 2733 VAL A O     1 
ATOM   9398  C  CB    . VAL A 1 2733 ? 235.976 194.476 226.089 1.00 23.10  ? 2733 VAL A CB    1 
ATOM   9399  C  CG1   . VAL A 1 2733 ? 236.244 195.004 224.694 1.00 26.81  ? 2733 VAL A CG1   1 
ATOM   9400  C  CG2   . VAL A 1 2733 ? 234.939 195.328 226.795 1.00 30.49  ? 2733 VAL A CG2   1 
ATOM   9401  N  N     . VAL A 1 2734 ? 236.371 191.666 224.202 1.00 27.65  ? 2734 VAL A N     1 
ATOM   9402  C  CA    . VAL A 1 2734 ? 237.364 190.921 223.440 1.00 26.94  ? 2734 VAL A CA    1 
ATOM   9403  C  C     . VAL A 1 2734 ? 237.735 191.747 222.217 1.00 25.90  ? 2734 VAL A C     1 
ATOM   9404  O  O     . VAL A 1 2734 ? 236.856 192.231 221.496 1.00 36.53  ? 2734 VAL A O     1 
ATOM   9405  C  CB    . VAL A 1 2734 ? 236.856 189.520 223.044 1.00 30.06  ? 2734 VAL A CB    1 
ATOM   9406  C  CG1   . VAL A 1 2734 ? 235.545 189.603 222.282 1.00 33.72  ? 2734 VAL A CG1   1 
ATOM   9407  C  CG2   . VAL A 1 2734 ? 237.904 188.788 222.223 1.00 22.38  ? 2734 VAL A CG2   1 
ATOM   9408  N  N     . TYR A 1 2735 ? 239.032 191.935 222.005 1.00 26.77  ? 2735 TYR A N     1 
ATOM   9409  C  CA    . TYR A 1 2735 ? 239.527 192.741 220.897 1.00 20.19  ? 2735 TYR A CA    1 
ATOM   9410  C  C     . TYR A 1 2735 ? 239.764 191.833 219.697 1.00 40.54  ? 2735 TYR A C     1 
ATOM   9411  O  O     . TYR A 1 2735 ? 240.649 190.972 219.725 1.00 50.72  ? 2735 TYR A O     1 
ATOM   9412  C  CB    . TYR A 1 2735 ? 240.803 193.475 221.293 1.00 26.86  ? 2735 TYR A CB    1 
ATOM   9413  C  CG    . TYR A 1 2735 ? 241.350 194.373 220.212 1.00 37.52  ? 2735 TYR A CG    1 
ATOM   9414  C  CD1   . TYR A 1 2735 ? 240.581 195.396 219.681 1.00 35.98  ? 2735 TYR A CD1   1 
ATOM   9415  C  CD2   . TYR A 1 2735 ? 242.635 194.200 219.723 1.00 36.31  ? 2735 TYR A CD2   1 
ATOM   9416  C  CE1   . TYR A 1 2735 ? 241.075 196.218 218.694 1.00 40.14  ? 2735 TYR A CE1   1 
ATOM   9417  C  CE2   . TYR A 1 2735 ? 243.137 195.018 218.736 1.00 31.95  ? 2735 TYR A CE2   1 
ATOM   9418  C  CZ    . TYR A 1 2735 ? 242.353 196.025 218.226 1.00 41.71  ? 2735 TYR A CZ    1 
ATOM   9419  O  OH    . TYR A 1 2735 ? 242.848 196.846 217.241 1.00 48.67  ? 2735 TYR A OH    1 
ATOM   9420  N  N     . VAL A 1 2736 ? 238.975 192.023 218.646 1.00 31.52  ? 2736 VAL A N     1 
ATOM   9421  C  CA    . VAL A 1 2736 ? 239.137 191.294 217.395 1.00 20.29  ? 2736 VAL A CA    1 
ATOM   9422  C  C     . VAL A 1 2736 ? 239.847 192.223 216.421 1.00 32.79  ? 2736 VAL A C     1 
ATOM   9423  O  O     . VAL A 1 2736 ? 239.268 193.210 215.957 1.00 44.48  ? 2736 VAL A O     1 
ATOM   9424  C  CB    . VAL A 1 2736 ? 237.790 190.818 216.837 1.00 24.43  ? 2736 VAL A CB    1 
ATOM   9425  C  CG1   . VAL A 1 2736 ? 238.003 189.966 215.602 1.00 34.73  ? 2736 VAL A CG1   1 
ATOM   9426  C  CG2   . VAL A 1 2736 ? 237.025 190.042 217.891 1.00 33.67  ? 2736 VAL A CG2   1 
ATOM   9427  N  N     . ASP A 1 2737 ? 241.098 191.915 216.111 1.00 33.13  ? 2737 ASP A N     1 
ATOM   9428  C  CA    . ASP A 1 2737 ? 241.911 192.739 215.232 1.00 32.11  ? 2737 ASP A CA    1 
ATOM   9429  C  C     . ASP A 1 2737 ? 241.882 192.192 213.810 1.00 35.44  ? 2737 ASP A C     1 
ATOM   9430  O  O     . ASP A 1 2737 ? 241.380 191.098 213.543 1.00 38.37  ? 2737 ASP A O     1 
ATOM   9431  C  CB    . ASP A 1 2737 ? 243.351 192.814 215.753 1.00 40.74  ? 2737 ASP A CB    1 
ATOM   9432  C  CG    . ASP A 1 2737 ? 244.103 194.018 215.225 1.00 49.60  ? 2737 ASP A CG    1 
ATOM   9433  O  OD1   . ASP A 1 2737 ? 243.462 194.902 214.619 1.00 46.74  ? 2737 ASP A OD1   1 
ATOM   9434  O  OD2   . ASP A 1 2737 ? 245.335 194.081 215.413 1.00 43.35  ? 2737 ASP A OD2   1 
ATOM   9435  N  N     . TYR A 1 2738 ? 242.409 192.979 212.871 1.00 36.66  ? 2738 TYR A N     1 
ATOM   9436  C  CA    . TYR A 1 2738 ? 242.409 192.553 211.450 1.00 31.74  ? 2738 TYR A CA    1 
ATOM   9437  C  C     . TYR A 1 2738 ? 243.306 191.327 211.279 1.00 39.50  ? 2738 TYR A C     1 
ATOM   9438  O  O     . TYR A 1 2738 ? 244.405 191.305 211.861 1.00 37.52  ? 2738 TYR A O     1 
ATOM   9439  C  CB    . TYR A 1 2738 ? 242.924 193.668 210.539 1.00 33.12  ? 2738 TYR A CB    1 
ATOM   9440  C  CG    . TYR A 1 2738 ? 241.938 194.753 210.195 1.00 33.72  ? 2738 TYR A CG    1 
ATOM   9441  C  CD1   . TYR A 1 2738 ? 240.671 194.451 209.727 1.00 34.43  ? 2738 TYR A CD1   1 
ATOM   9442  C  CD2   . TYR A 1 2738 ? 242.294 196.087 210.282 1.00 28.24  ? 2738 TYR A CD2   1 
ATOM   9443  C  CE1   . TYR A 1 2738 ? 239.769 195.447 209.394 1.00 33.63  ? 2738 TYR A CE1   1 
ATOM   9444  C  CE2   . TYR A 1 2738 ? 241.408 197.095 209.944 1.00 30.52  ? 2738 TYR A CE2   1 
ATOM   9445  C  CZ    . TYR A 1 2738 ? 240.140 196.774 209.500 1.00 30.83  ? 2738 TYR A CZ    1 
ATOM   9446  O  OH    . TYR A 1 2738 ? 239.263 197.778 209.171 1.00 37.02  ? 2738 TYR A OH    1 
ATOM   9447  N  N     . PRO A 1 2739 ? 242.894 190.305 210.499 1.00 43.17  ? 2739 PRO A N     1 
ATOM   9448  C  CA    . PRO A 1 2739 ? 243.763 189.162 210.227 1.00 35.98  ? 2739 PRO A CA    1 
ATOM   9449  C  C     . PRO A 1 2739 ? 245.063 189.654 209.576 1.00 39.57  ? 2739 PRO A C     1 
ATOM   9450  O  O     . PRO A 1 2739 ? 244.984 190.471 208.683 1.00 37.82  ? 2739 PRO A O     1 
ATOM   9451  C  CB    . PRO A 1 2739 ? 242.949 188.334 209.227 1.00 32.46  ? 2739 PRO A CB    1 
ATOM   9452  C  CG    . PRO A 1 2739 ? 241.513 188.725 209.491 1.00 26.50  ? 2739 PRO A CG    1 
ATOM   9453  C  CD    . PRO A 1 2739 ? 241.578 190.189 209.869 1.00 36.87  ? 2739 PRO A CD    1 
ATOM   9454  N  N     . GLY A 1 2740 ? 246.214 189.151 210.030 1.00 42.81  ? 2740 GLY A N     1 
ATOM   9455  C  CA    . GLY A 1 2740 ? 247.516 189.593 209.494 1.00 40.88  ? 2740 GLY A CA    1 
ATOM   9456  C  C     . GLY A 1 2740 ? 247.805 188.974 208.140 1.00 44.09  ? 2740 GLY A C     1 
ATOM   9457  O  O     . GLY A 1 2740 ? 246.993 188.147 207.690 1.00 49.05  ? 2740 GLY A O     1 
ATOM   9458  N  N     . PRO A 1 2741 ? 248.916 189.328 207.457 1.00 48.47  ? 2741 PRO A N     1 
ATOM   9459  C  CA    . PRO A 1 2741 ? 249.181 188.825 206.099 1.00 38.76  ? 2741 PRO A CA    1 
ATOM   9460  C  C     . PRO A 1 2741 ? 249.217 187.310 206.018 1.00 40.43  ? 2741 PRO A C     1 
ATOM   9461  O  O     . PRO A 1 2741 ? 248.779 186.741 205.013 1.00 48.13  ? 2741 PRO A O     1 
ATOM   9462  C  CB    . PRO A 1 2741 ? 250.539 189.452 205.756 1.00 39.06  ? 2741 PRO A CB    1 
ATOM   9463  C  CG    . PRO A 1 2741 ? 250.631 190.654 206.632 1.00 44.72  ? 2741 PRO A CG    1 
ATOM   9464  C  CD    . PRO A 1 2741 ? 249.946 190.277 207.908 1.00 47.68  ? 2741 PRO A CD    1 
ATOM   9465  N  N     . ALA A 1 2742 ? 249.718 186.635 207.055 1.00 35.26  ? 2742 ALA A N     1 
ATOM   9466  C  CA    . ALA A 1 2742 ? 249.702 185.176 207.057 1.00 36.80  ? 2742 ALA A CA    1 
ATOM   9467  C  C     . ALA A 1 2742 ? 248.281 184.638 207.177 1.00 39.43  ? 2742 ALA A C     1 
ATOM   9468  O  O     . ALA A 1 2742 ? 247.897 183.713 206.453 1.00 45.78  ? 2742 ALA A O     1 
ATOM   9469  C  CB    . ALA A 1 2742 ? 250.576 184.644 208.190 1.00 42.55  ? 2742 ALA A CB    1 
ATOM   9470  N  N     . SER A 1 2743 ? 247.484 185.208 208.084 1.00 41.56  ? 2743 SER A N     1 
ATOM   9471  C  CA    . SER A 1 2743 ? 246.104 184.761 208.241 1.00 36.96  ? 2743 SER A CA    1 
ATOM   9472  C  C     . SER A 1 2743 ? 245.265 185.113 207.019 1.00 35.40  ? 2743 SER A C     1 
ATOM   9473  O  O     . SER A 1 2743 ? 244.419 184.319 206.590 1.00 37.91  ? 2743 SER A O     1 
ATOM   9474  C  CB    . SER A 1 2743 ? 245.500 185.368 209.506 1.00 39.10  ? 2743 SER A CB    1 
ATOM   9475  O  OG    . SER A 1 2743 ? 244.099 185.173 209.548 1.00 55.87  ? 2743 SER A OG    1 
ATOM   9476  N  N     . LEU A 1 2744 ? 245.480 186.301 206.449 1.00 37.29  ? 2744 LEU A N     1 
ATOM   9477  C  CA    . LEU A 1 2744 ? 244.797 186.664 205.213 1.00 31.91  ? 2744 LEU A CA    1 
ATOM   9478  C  C     . LEU A 1 2744 ? 245.169 185.711 204.088 1.00 30.00  ? 2744 LEU A C     1 
ATOM   9479  O  O     . LEU A 1 2744 ? 244.305 185.280 203.313 1.00 36.03  ? 2744 LEU A O     1 
ATOM   9480  C  CB    . LEU A 1 2744 ? 245.144 188.099 204.822 1.00 27.33  ? 2744 LEU A CB    1 
ATOM   9481  C  CG    . LEU A 1 2744 ? 244.418 189.235 205.537 1.00 35.03  ? 2744 LEU A CG    1 
ATOM   9482  C  CD1   . LEU A 1 2744 ? 244.966 190.559 205.059 1.00 40.59  ? 2744 LEU A CD1   1 
ATOM   9483  C  CD2   . LEU A 1 2744 ? 242.926 189.156 205.300 1.00 38.05  ? 2744 LEU A CD2   1 
ATOM   9484  N  N     . THR A 1 2745 ? 246.457 185.375 203.983 1.00 33.19  ? 2745 THR A N     1 
ATOM   9485  C  CA    . THR A 1 2745 ? 246.894 184.424 202.972 1.00 36.44  ? 2745 THR A CA    1 
ATOM   9486  C  C     . THR A 1 2745 ? 246.219 183.078 203.167 1.00 38.93  ? 2745 THR A C     1 
ATOM   9487  O  O     . THR A 1 2745 ? 245.723 182.490 202.208 1.00 55.29  ? 2745 THR A O     1 
ATOM   9488  C  CB    . THR A 1 2745 ? 248.413 184.273 203.007 1.00 36.49  ? 2745 THR A CB    1 
ATOM   9489  O  OG1   . THR A 1 2745 ? 249.025 185.525 202.675 1.00 45.16  ? 2745 THR A OG1   1 
ATOM   9490  C  CG2   . THR A 1 2745 ? 248.864 183.219 202.016 1.00 34.99  ? 2745 THR A CG2   1 
ATOM   9491  N  N     . GLN A 1 2746 ? 246.099 182.637 204.419 1.00 35.97  ? 2746 GLN A N     1 
ATOM   9492  C  CA    . GLN A 1 2746 ? 245.420 181.347 204.718 1.00 32.41  ? 2746 GLN A CA    1 
ATOM   9493  C  C     . GLN A 1 2746 ? 243.932 181.419 204.360 1.00 35.23  ? 2746 GLN A C     1 
ATOM   9494  O  O     . GLN A 1 2746 ? 243.465 180.512 203.649 1.00 42.04  ? 2746 GLN A O     1 
ATOM   9495  C  CB    . GLN A 1 2746 ? 245.575 181.000 206.198 1.00 39.16  ? 2746 GLN A CB    1 
ATOM   9496  C  CG    . GLN A 1 2746 ? 244.917 179.686 206.587 1.00 49.96  ? 2746 GLN A CG    1 
ATOM   9497  C  CD    . GLN A 1 2746 ? 244.698 179.588 208.076 1.00 53.19  ? 2746 GLN A CD    1 
ATOM   9498  O  OE1   . GLN A 1 2746 ? 245.632 179.671 208.869 1.00 48.18  ? 2746 GLN A OE1   1 
ATOM   9499  N  NE2   . GLN A 1 2746 ? 243.446 179.418 208.467 1.00 48.04  ? 2746 GLN A NE2   1 
ATOM   9500  N  N     . ILE A 1 2747 ? 243.215 182.444 204.830 1.00 36.61  ? 2747 ILE A N     1 
ATOM   9501  C  CA    . ILE A 1 2747 ? 241.738 182.532 204.610 1.00 32.50  ? 2747 ILE A CA    1 
ATOM   9502  C  C     . ILE A 1 2747 ? 241.413 182.601 203.116 1.00 31.97  ? 2747 ILE A C     1 
ATOM   9503  O  O     . ILE A 1 2747 ? 240.652 181.736 202.640 1.00 38.41  ? 2747 ILE A O     1 
ATOM   9504  C  CB    . ILE A 1 2747 ? 241.156 183.761 205.337 1.00 30.26  ? 2747 ILE A CB    1 
ATOM   9505  C  CG1   . ILE A 1 2747 ? 241.467 183.740 206.835 1.00 35.55  ? 2747 ILE A CG1   1 
ATOM   9506  C  CG2   . ILE A 1 2747 ? 239.665 183.890 205.070 1.00 34.30  ? 2747 ILE A CG2   1 
ATOM   9507  C  CD1   . ILE A 1 2747 ? 241.263 185.071 207.517 1.00 30.38  ? 2747 ILE A CD1   1 
ATOM   9508  N  N     . TYR A 1 2748 ? 241.984 183.568 202.399 1.00 38.21  ? 2748 TYR A N     1 
ATOM   9509  C  CA    . TYR A 1 2748 ? 241.608 183.774 200.974 1.00 34.37  ? 2748 TYR A CA    1 
ATOM   9510  C  C     . TYR A 1 2748 ? 242.335 182.769 200.077 1.00 36.21  ? 2748 TYR A C     1 
ATOM   9511  O  O     . TYR A 1 2748 ? 241.870 182.556 198.946 1.00 52.41  ? 2748 TYR A O     1 
ATOM   9512  C  CB    . TYR A 1 2748 ? 241.789 185.254 200.627 1.00 31.32  ? 2748 TYR A CB    1 
ATOM   9513  C  CG    . TYR A 1 2748 ? 240.883 186.126 201.457 1.00 35.85  ? 2748 TYR A CG    1 
ATOM   9514  C  CD1   . TYR A 1 2748 ? 239.509 186.065 201.302 1.00 35.51  ? 2748 TYR A CD1   1 
ATOM   9515  C  CD2   . TYR A 1 2748 ? 241.385 186.940 202.458 1.00 38.95  ? 2748 TYR A CD2   1 
ATOM   9516  C  CE1   . TYR A 1 2748 ? 238.658 186.831 202.079 1.00 34.62  ? 2748 TYR A CE1   1 
ATOM   9517  C  CE2   . TYR A 1 2748 ? 240.548 187.713 203.245 1.00 34.08  ? 2748 TYR A CE2   1 
ATOM   9518  C  CZ    . TYR A 1 2748 ? 239.180 187.658 203.056 1.00 35.74  ? 2748 TYR A CZ    1 
ATOM   9519  O  OH    . TYR A 1 2748 ? 238.340 188.418 203.829 1.00 39.71  ? 2748 TYR A OH    1 
ATOM   9520  N  N     . GLY A 1 2749 ? 243.421 182.166 200.560 1.00 27.88  ? 2749 GLY A N     1 
ATOM   9521  C  CA    . GLY A 1 2749 ? 244.075 181.099 199.780 1.00 26.86  ? 2749 GLY A CA    1 
ATOM   9522  C  C     . GLY A 1 2749 ? 243.134 179.916 199.658 1.00 34.16  ? 2749 GLY A C     1 
ATOM   9523  O  O     . GLY A 1 2749 ? 243.065 179.329 198.566 1.00 43.77  ? 2749 GLY A O     1 
ATOM   9524  N  N     . THR A 1 2750 ? 242.421 179.589 200.739 1.00 37.90  ? 2750 THR A N     1 
ATOM   9525  C  CA    . THR A 1 2750 ? 241.427 178.483 200.712 1.00 39.36  ? 2750 THR A CA    1 
ATOM   9526  C  C     . THR A 1 2750 ? 240.284 178.868 199.772 1.00 41.92  ? 2750 THR A C     1 
ATOM   9527  O  O     . THR A 1 2750 ? 239.841 177.999 199.001 1.00 50.06  ? 2750 THR A O     1 
ATOM   9528  C  CB    . THR A 1 2750 ? 240.904 178.187 202.121 1.00 37.07  ? 2750 THR A CB    1 
ATOM   9529  O  OG1   . THR A 1 2750 ? 242.029 178.109 202.996 1.00 43.81  ? 2750 THR A OG1   1 
ATOM   9530  C  CG2   . THR A 1 2750 ? 240.100 176.908 202.196 1.00 35.72  ? 2750 THR A CG2   1 
ATOM   9531  N  N     . PHE A 1 2751 ? 239.833 180.122 199.840 1.00 40.44  ? 2751 PHE A N     1 
ATOM   9532  C  CA    . PHE A 1 2751 ? 238.719 180.600 198.983 1.00 27.62  ? 2751 PHE A CA    1 
ATOM   9533  C  C     . PHE A 1 2751 ? 239.145 180.563 197.513 1.00 36.81  ? 2751 PHE A C     1 
ATOM   9534  O  O     . PHE A 1 2751 ? 238.322 180.175 196.669 1.00 47.08  ? 2751 PHE A O     1 
ATOM   9535  C  CB    . PHE A 1 2751 ? 238.311 182.010 199.410 1.00 34.16  ? 2751 PHE A CB    1 
ATOM   9536  C  CG    . PHE A 1 2751 ? 237.408 182.071 200.616 1.00 40.21  ? 2751 PHE A CG    1 
ATOM   9537  C  CD1   . PHE A 1 2751 ? 236.868 180.918 201.158 1.00 40.05  ? 2751 PHE A CD1   1 
ATOM   9538  C  CD2   . PHE A 1 2751 ? 237.115 183.282 201.220 1.00 46.09  ? 2751 PHE A CD2   1 
ATOM   9539  C  CE1   . PHE A 1 2751 ? 236.039 180.976 202.267 1.00 40.44  ? 2751 PHE A CE1   1 
ATOM   9540  C  CE2   . PHE A 1 2751 ? 236.290 183.339 202.332 1.00 43.02  ? 2751 PHE A CE2   1 
ATOM   9541  C  CZ    . PHE A 1 2751 ? 235.754 182.186 202.854 1.00 43.69  ? 2751 PHE A CZ    1 
ATOM   9542  N  N     . ASN A 1 2752 ? 240.386 180.962 197.223 1.00 40.19  ? 2752 ASN A N     1 
ATOM   9543  C  CA    . ASN A 1 2752 ? 240.879 180.988 195.820 1.00 30.86  ? 2752 ASN A CA    1 
ATOM   9544  C  C     . ASN A 1 2752 ? 241.073 179.549 195.340 1.00 39.49  ? 2752 ASN A C     1 
ATOM   9545  O  O     . ASN A 1 2752 ? 240.694 179.263 194.192 1.00 48.32  ? 2752 ASN A O     1 
ATOM   9546  C  CB    . ASN A 1 2752 ? 242.151 181.825 195.669 1.00 32.94  ? 2752 ASN A CB    1 
ATOM   9547  C  CG    . ASN A 1 2752 ? 241.918 183.304 195.889 1.00 37.60  ? 2752 ASN A CG    1 
ATOM   9548  O  OD1   . ASN A 1 2752 ? 240.800 183.725 196.172 1.00 40.18  ? 2752 ASN A OD1   1 
ATOM   9549  N  ND2   . ASN A 1 2752 ? 242.968 184.099 195.761 1.00 41.62  ? 2752 ASN A ND2   1 
ATOM   9550  N  N     . ARG A 1 2753 ? 241.634 178.678 196.184 1.00 42.03  ? 2753 ARG A N     1 
ATOM   9551  C  CA    . ARG A 1 2753 ? 241.764 177.279 195.800 1.00 43.31  ? 2753 ARG A CA    1 
ATOM   9552  C  C     . ARG A 1 2753 ? 240.404 176.656 195.537 1.00 44.63  ? 2753 ARG A C     1 
ATOM   9553  O  O     . ARG A 1 2753 ? 240.237 175.898 194.576 1.00 55.62  ? 2753 ARG A O     1 
ATOM   9554  C  CB    . ARG A 1 2753 ? 242.514 176.503 196.880 1.00 47.42  ? 2753 ARG A CB    1 
ATOM   9555  C  CG    . ARG A 1 2753 ? 244.021 176.655 196.814 1.00 49.28  ? 2753 ARG A CG    1 
ATOM   9556  C  CD    . ARG A 1 2753 ? 244.719 175.529 197.552 1.00 48.53  ? 2753 ARG A CD    1 
ATOM   9557  N  NE    . ARG A 1 2753 ? 243.874 174.952 198.590 1.00 48.69  ? 2753 ARG A NE    1 
ATOM   9558  C  CZ    . ARG A 1 2753 ? 243.856 175.357 199.852 1.00 55.40  ? 2753 ARG A CZ    1 
ATOM   9559  N  NH1   . ARG A 1 2753 ? 244.630 176.344 200.272 1.00 43.14  ? 2753 ARG A NH1   1 
ATOM   9560  N  NH2   . ARG A 1 2753 ? 243.040 174.757 200.714 1.00 57.49  ? 2753 ARG A NH2   1 
ATOM   9561  N  N     . ALA A 1 2754 ? 239.418 176.959 196.382 1.00 45.46  ? 2754 ALA A N     1 
ATOM   9562  C  CA    . ALA A 1 2754 ? 238.067 176.487 196.107 1.00 45.24  ? 2754 ALA A CA    1 
ATOM   9563  C  C     . ALA A 1 2754 ? 237.527 177.093 194.816 1.00 52.09  ? 2754 ALA A C     1 
ATOM   9564  O  O     . ALA A 1 2754 ? 236.839 176.416 194.044 1.00 60.64  ? 2754 ALA A O     1 
ATOM   9565  C  CB    . ALA A 1 2754 ? 237.153 176.810 197.285 1.00 48.78  ? 2754 ALA A CB    1 
ATOM   9566  N  N     . MET A 1 2755 ? 237.832 178.369 194.569 1.00 47.32  ? 2755 MET A N     1 
ATOM   9567  C  CA    . MET A 1 2755 ? 237.328 179.056 193.384 1.00 44.44  ? 2755 MET A CA    1 
ATOM   9568  C  C     . MET A 1 2755 ? 237.962 178.524 192.105 1.00 51.79  ? 2755 MET A C     1 
ATOM   9569  O  O     . MET A 1 2755 ? 237.259 178.229 191.132 1.00 54.27  ? 2755 MET A O     1 
ATOM   9570  C  CB    . MET A 1 2755 ? 237.588 180.554 193.516 1.00 42.14  ? 2755 MET A CB    1 
ATOM   9571  C  CG    . MET A 1 2755 ? 237.069 181.392 192.373 1.00 46.54  ? 2755 MET A CG    1 
ATOM   9572  S  SD    . MET A 1 2755 ? 237.417 183.134 192.657 1.00 63.46  ? 2755 MET A SD    1 
ATOM   9573  C  CE    . MET A 1 2755 ? 239.187 183.158 192.401 1.00 43.70  ? 2755 MET A CE    1 
ATOM   9574  N  N     . LEU A 1 2756 ? 239.290 178.396 192.084 1.00 55.05  ? 2756 LEU A N     1 
ATOM   9575  C  CA    . LEU A 1 2756 ? 239.992 178.060 190.851 1.00 51.82  ? 2756 LEU A CA    1 
ATOM   9576  C  C     . LEU A 1 2756 ? 239.805 176.609 190.432 1.00 55.66  ? 2756 LEU A C     1 
ATOM   9577  O  O     . LEU A 1 2756 ? 240.329 176.215 189.386 1.00 59.55  ? 2756 LEU A O     1 
ATOM   9578  C  CB    . LEU A 1 2756 ? 241.482 178.376 190.991 1.00 48.52  ? 2756 LEU A CB    1 
ATOM   9579  C  CG    . LEU A 1 2756 ? 241.832 179.863 190.919 1.00 50.29  ? 2756 LEU A CG    1 
ATOM   9580  C  CD1   . LEU A 1 2756 ? 243.315 180.060 190.706 1.00 53.36  ? 2756 LEU A CD1   1 
ATOM   9581  C  CD2   . LEU A 1 2756 ? 241.046 180.543 189.812 1.00 51.27  ? 2756 LEU A CD2   1 
ATOM   9582  N  N     . ARG A 1 2757 ? 239.086 175.809 191.218 1.00 59.92  ? 2757 ARG A N     1 
ATOM   9583  C  CA    . ARG A 1 2757 ? 238.700 174.475 190.781 1.00 59.54  ? 2757 ARG A CA    1 
ATOM   9584  C  C     . ARG A 1 2757 ? 237.668 174.507 189.662 1.00 62.05  ? 2757 ARG A C     1 
ATOM   9585  O  O     . ARG A 1 2757 ? 237.438 173.473 189.026 1.00 61.71  ? 2757 ARG A O     1 
ATOM   9586  C  CB    . ARG A 1 2757 ? 238.165 173.672 191.967 1.00 59.55  ? 2757 ARG A CB    1 
ATOM   9587  C  CG    . ARG A 1 2757 ? 239.253 173.012 192.792 1.00 58.26  ? 2757 ARG A CG    1 
ATOM   9588  C  CD    . ARG A 1 2757 ? 238.704 171.912 193.678 1.00 58.38  ? 2757 ARG A CD    1 
ATOM   9589  N  NE    . ARG A 1 2757 ? 237.682 172.406 194.591 1.00 65.39  ? 2757 ARG A NE    1 
ATOM   9590  C  CZ    . ARG A 1 2757 ? 237.874 172.603 195.888 1.00 66.23  ? 2757 ARG A CZ    1 
ATOM   9591  N  NH1   . ARG A 1 2757 ? 239.048 172.378 196.455 1.00 60.94  ? 2757 ARG A NH1   1 
ATOM   9592  N  NH2   . ARG A 1 2757 ? 236.864 173.040 196.634 1.00 60.69  ? 2757 ARG A NH2   1 
ATOM   9593  N  N     . LEU A 1 2758 ? 237.038 175.659 189.418 1.00 62.20  ? 2758 LEU A N     1 
ATOM   9594  C  CA    . LEU A 1 2758 ? 236.128 175.785 188.285 1.00 61.53  ? 2758 LEU A CA    1 
ATOM   9595  C  C     . LEU A 1 2758 ? 236.864 175.596 186.966 1.00 66.23  ? 2758 LEU A C     1 
ATOM   9596  O  O     . LEU A 1 2758 ? 236.359 174.937 186.051 1.00 70.46  ? 2758 LEU A O     1 
ATOM   9597  C  CB    . LEU A 1 2758 ? 235.440 177.149 188.314 1.00 59.04  ? 2758 LEU A CB    1 
ATOM   9598  C  CG    . LEU A 1 2758 ? 234.359 177.385 189.367 1.00 63.87  ? 2758 LEU A CG    1 
ATOM   9599  C  CD1   . LEU A 1 2758 ? 234.035 178.863 189.437 1.00 59.99  ? 2758 LEU A CD1   1 
ATOM   9600  C  CD2   . LEU A 1 2758 ? 233.111 176.575 189.062 1.00 62.54  ? 2758 LEU A CD2   1 
ATOM   9601  N  N     . ILE A 1 2759 ? 238.057 176.171 186.849 1.00 62.79  ? 2759 ILE A N     1 
ATOM   9602  C  CA    . ILE A 1 2759 ? 238.864 176.061 185.638 1.00 63.31  ? 2759 ILE A CA    1 
ATOM   9603  C  C     . ILE A 1 2759 ? 240.140 175.303 185.978 1.00 63.94  ? 2759 ILE A C     1 
ATOM   9604  O  O     . ILE A 1 2759 ? 241.085 175.894 186.520 1.00 61.95  ? 2759 ILE A O     1 
ATOM   9605  C  CB    . ILE A 1 2759 ? 239.175 177.444 185.048 1.00 60.67  ? 2759 ILE A CB    1 
ATOM   9606  C  CG1   . ILE A 1 2759 ? 237.914 178.309 185.034 1.00 58.94  ? 2759 ILE A CG1   1 
ATOM   9607  C  CG2   . ILE A 1 2759 ? 239.732 177.308 183.646 1.00 64.09  ? 2759 ILE A CG2   1 
ATOM   9608  C  CD1   . ILE A 1 2759 ? 238.080 179.621 184.310 1.00 61.56  ? 2759 ILE A CD1   1 
ATOM   9609  N  N     . PRO A 1 2760 ? 240.212 174.003 185.684 1.00 65.93  ? 2760 PRO A N     1 
ATOM   9610  C  CA    . PRO A 1 2760 ? 241.402 173.227 186.073 1.00 64.63  ? 2760 PRO A CA    1 
ATOM   9611  C  C     . PRO A 1 2760 ? 242.691 173.716 185.436 1.00 61.21  ? 2760 PRO A C     1 
ATOM   9612  O  O     . PRO A 1 2760 ? 243.771 173.453 185.977 1.00 65.61  ? 2760 PRO A O     1 
ATOM   9613  C  CB    . PRO A 1 2760 ? 241.059 171.801 185.620 1.00 63.24  ? 2760 PRO A CB    1 
ATOM   9614  C  CG    . PRO A 1 2760 ? 239.579 171.776 185.465 1.00 62.07  ? 2760 PRO A CG    1 
ATOM   9615  C  CD    . PRO A 1 2760 ? 239.148 173.162 185.113 1.00 59.44  ? 2760 PRO A CD    1 
ATOM   9616  N  N     . SER A 1 2761 ? 242.618 174.413 184.301 1.00 54.98  ? 2761 SER A N     1 
ATOM   9617  C  CA    . SER A 1 2761 ? 243.830 174.922 183.672 1.00 58.37  ? 2761 SER A CA    1 
ATOM   9618  C  C     . SER A 1 2761 ? 244.459 176.060 184.464 1.00 60.77  ? 2761 SER A C     1 
ATOM   9619  O  O     . SER A 1 2761 ? 245.656 176.322 184.304 1.00 58.03  ? 2761 SER A O     1 
ATOM   9620  C  CB    . SER A 1 2761 ? 243.531 175.382 182.245 1.00 59.02  ? 2761 SER A CB    1 
ATOM   9621  O  OG    . SER A 1 2761 ? 242.466 176.314 182.220 1.00 60.40  ? 2761 SER A OG    1 
ATOM   9622  N  N     . LEU A 1 2762 ? 243.686 176.735 185.312 1.00 62.72  ? 2762 LEU A N     1 
ATOM   9623  C  CA    . LEU A 1 2762 ? 244.178 177.819 186.151 1.00 56.30  ? 2762 LEU A CA    1 
ATOM   9624  C  C     . LEU A 1 2762 ? 244.535 177.347 187.552 1.00 58.33  ? 2762 LEU A C     1 
ATOM   9625  O  O     . LEU A 1 2762 ? 244.706 178.175 188.451 1.00 59.43  ? 2762 LEU A O     1 
ATOM   9626  C  CB    . LEU A 1 2762 ? 243.137 178.936 186.229 1.00 57.64  ? 2762 LEU A CB    1 
ATOM   9627  C  CG    . LEU A 1 2762 ? 243.001 179.839 185.003 1.00 58.71  ? 2762 LEU A CG    1 
ATOM   9628  C  CD1   . LEU A 1 2762 ? 241.890 180.850 185.210 1.00 55.20  ? 2762 LEU A CD1   1 
ATOM   9629  C  CD2   . LEU A 1 2762 ? 244.316 180.538 184.706 1.00 60.18  ? 2762 LEU A CD2   1 
ATOM   9630  N  N     . ARG A 1 2763 ? 244.650 176.032 187.753 1.00 64.34  ? 2763 ARG A N     1 
ATOM   9631  C  CA    . ARG A 1 2763 ? 244.851 175.481 189.089 1.00 59.10  ? 2763 ARG A CA    1 
ATOM   9632  C  C     . ARG A 1 2763 ? 246.172 175.927 189.705 1.00 57.69  ? 2763 ARG A C     1 
ATOM   9633  O  O     . ARG A 1 2763 ? 246.276 176.040 190.932 1.00 55.84  ? 2763 ARG A O     1 
ATOM   9634  C  CB    . ARG A 1 2763 ? 244.766 173.953 189.026 1.00 58.33  ? 2763 ARG A CB    1 
ATOM   9635  C  CG    . ARG A 1 2763 ? 244.999 173.233 190.344 1.00 62.18  ? 2763 ARG A CG    1 
ATOM   9636  C  CD    . ARG A 1 2763 ? 243.846 173.457 191.299 1.00 67.49  ? 2763 ARG A CD    1 
ATOM   9637  N  NE    . ARG A 1 2763 ? 244.044 174.702 192.026 1.00 72.15  ? 2763 ARG A NE    1 
ATOM   9638  C  CZ    . ARG A 1 2763 ? 243.152 175.272 192.821 1.00 64.26  ? 2763 ARG A CZ    1 
ATOM   9639  N  NH1   . ARG A 1 2763 ? 241.982 174.708 193.066 1.00 56.97  ? 2763 ARG A NH1   1 
ATOM   9640  N  NH2   . ARG A 1 2763 ? 243.440 176.442 193.377 1.00 64.18  ? 2763 ARG A NH2   1 
ATOM   9641  N  N     . THR A 1 2764 ? 247.183 176.200 188.883 1.00 56.46  ? 2764 THR A N     1 
ATOM   9642  C  CA    . THR A 1 2764 ? 248.511 176.508 189.399 1.00 57.48  ? 2764 THR A CA    1 
ATOM   9643  C  C     . THR A 1 2764 ? 248.691 177.968 189.795 1.00 57.68  ? 2764 THR A C     1 
ATOM   9644  O  O     . THR A 1 2764 ? 249.766 178.324 190.288 1.00 57.87  ? 2764 THR A O     1 
ATOM   9645  C  CB    . THR A 1 2764 ? 249.576 176.139 188.364 1.00 56.37  ? 2764 THR A CB    1 
ATOM   9646  O  OG1   . THR A 1 2764 ? 250.868 176.516 188.853 1.00 56.14  ? 2764 THR A OG1   1 
ATOM   9647  C  CG2   . THR A 1 2764 ? 249.313 176.854 187.049 1.00 52.66  ? 2764 THR A CG2   1 
ATOM   9648  N  N     . TYR A 1 2765 ? 247.686 178.819 189.594 1.00 52.26  ? 2765 TYR A N     1 
ATOM   9649  C  CA    . TYR A 1 2765 ? 247.832 180.251 189.816 1.00 51.03  ? 2765 TYR A CA    1 
ATOM   9650  C  C     . TYR A 1 2765 ? 247.179 180.732 191.106 1.00 49.04  ? 2765 TYR A C     1 
ATOM   9651  O  O     . TYR A 1 2765 ? 247.117 181.942 191.335 1.00 47.97  ? 2765 TYR A O     1 
ATOM   9652  C  CB    . TYR A 1 2765 ? 247.263 181.028 188.628 1.00 51.98  ? 2765 TYR A CB    1 
ATOM   9653  C  CG    . TYR A 1 2765 ? 248.089 180.901 187.373 1.00 54.36  ? 2765 TYR A CG    1 
ATOM   9654  C  CD1   . TYR A 1 2765 ? 249.283 181.594 187.234 1.00 52.36  ? 2765 TYR A CD1   1 
ATOM   9655  C  CD2   . TYR A 1 2765 ? 247.676 180.093 186.326 1.00 53.48  ? 2765 TYR A CD2   1 
ATOM   9656  C  CE1   . TYR A 1 2765 ? 250.044 181.480 186.089 1.00 52.05  ? 2765 TYR A CE1   1 
ATOM   9657  C  CE2   . TYR A 1 2765 ? 248.430 179.973 185.177 1.00 53.25  ? 2765 TYR A CE2   1 
ATOM   9658  C  CZ    . TYR A 1 2765 ? 249.612 180.669 185.064 1.00 56.40  ? 2765 TYR A CZ    1 
ATOM   9659  O  OH    . TYR A 1 2765 ? 250.366 180.554 183.920 1.00 56.82  ? 2765 TYR A OH    1 
ATOM   9660  N  N     . ALA A 1 2766 ? 246.692 179.820 191.951 1.00 54.17  ? 2766 ALA A N     1 
ATOM   9661  C  CA    . ALA A 1 2766 ? 245.993 180.238 193.163 1.00 46.98  ? 2766 ALA A CA    1 
ATOM   9662  C  C     . ALA A 1 2766 ? 246.923 180.962 194.130 1.00 54.81  ? 2766 ALA A C     1 
ATOM   9663  O  O     . ALA A 1 2766 ? 246.556 182.001 194.692 1.00 61.61  ? 2766 ALA A O     1 
ATOM   9664  C  CB    . ALA A 1 2766 ? 245.354 179.030 193.841 1.00 42.37  ? 2766 ALA A CB    1 
ATOM   9665  N  N     . GLU A 1 2767 ? 248.128 180.424 194.347 1.00 52.21  ? 2767 GLU A N     1 
ATOM   9666  C  CA    . GLU A 1 2767 ? 249.044 181.057 195.296 1.00 47.21  ? 2767 GLU A CA    1 
ATOM   9667  C  C     . GLU A 1 2767 ? 249.488 182.444 194.844 1.00 53.35  ? 2767 GLU A C     1 
ATOM   9668  O  O     . GLU A 1 2767 ? 249.392 183.388 195.648 1.00 52.24  ? 2767 GLU A O     1 
ATOM   9669  C  CB    . GLU A 1 2767 ? 250.237 180.133 195.565 1.00 50.41  ? 2767 GLU A CB    1 
ATOM   9670  C  CG    . GLU A 1 2767 ? 249.959 179.025 196.568 1.00 56.10  ? 2767 GLU A CG    1 
ATOM   9671  C  CD    . GLU A 1 2767 ? 249.055 177.943 196.009 1.00 64.89  ? 2767 GLU A CD    1 
ATOM   9672  O  OE1   . GLU A 1 2767 ? 249.224 177.575 194.828 1.00 60.65  ? 2767 GLU A OE1   1 
ATOM   9673  O  OE2   . GLU A 1 2767 ? 248.174 177.460 196.753 1.00 59.74  ? 2767 GLU A OE2   1 
ATOM   9674  N  N     . PRO A 1 2768 ? 249.990 182.649 193.617 1.00 52.27  ? 2768 PRO A N     1 
ATOM   9675  C  CA    . PRO A 1 2768 ? 250.337 184.020 193.210 1.00 45.45  ? 2768 PRO A CA    1 
ATOM   9676  C  C     . PRO A 1 2768 ? 249.143 184.955 193.154 1.00 45.73  ? 2768 PRO A C     1 
ATOM   9677  O  O     . PRO A 1 2768 ? 249.293 186.148 193.444 1.00 53.29  ? 2768 PRO A O     1 
ATOM   9678  C  CB    . PRO A 1 2768 ? 250.977 183.827 191.829 1.00 43.67  ? 2768 PRO A CB    1 
ATOM   9679  C  CG    . PRO A 1 2768 ? 250.446 182.544 191.340 1.00 48.97  ? 2768 PRO A CG    1 
ATOM   9680  C  CD    . PRO A 1 2768 ? 250.301 181.680 192.550 1.00 50.33  ? 2768 PRO A CD    1 
ATOM   9681  N  N     . LEU A 1 2769 ? 247.959 184.455 192.793 1.00 30.70  ? 2769 LEU A N     1 
ATOM   9682  C  CA    . LEU A 1 2769 ? 246.775 185.309 192.788 1.00 35.04  ? 2769 LEU A CA    1 
ATOM   9683  C  C     . LEU A 1 2769 ? 246.436 185.784 194.194 1.00 44.97  ? 2769 LEU A C     1 
ATOM   9684  O  O     . LEU A 1 2769 ? 246.148 186.969 194.404 1.00 53.09  ? 2769 LEU A O     1 
ATOM   9685  C  CB    . LEU A 1 2769 ? 245.592 184.564 192.173 1.00 38.24  ? 2769 LEU A CB    1 
ATOM   9686  C  CG    . LEU A 1 2769 ? 244.255 185.304 192.143 1.00 37.61  ? 2769 LEU A CG    1 
ATOM   9687  C  CD1   . LEU A 1 2769 ? 244.196 186.246 190.958 1.00 43.12  ? 2769 LEU A CD1   1 
ATOM   9688  C  CD2   . LEU A 1 2769 ? 243.099 184.321 192.107 1.00 41.19  ? 2769 LEU A CD2   1 
ATOM   9689  N  N     . THR A 1 2770 ? 246.475 184.876 195.171 1.00 43.79  ? 2770 THR A N     1 
ATOM   9690  C  CA    . THR A 1 2770 ? 246.213 185.266 196.552 1.00 33.44  ? 2770 THR A CA    1 
ATOM   9691  C  C     . THR A 1 2770 ? 247.280 186.223 197.064 1.00 43.36  ? 2770 THR A C     1 
ATOM   9692  O  O     . THR A 1 2770 ? 246.972 187.176 197.791 1.00 46.43  ? 2770 THR A O     1 
ATOM   9693  C  CB    . THR A 1 2770 ? 246.135 184.027 197.440 1.00 38.72  ? 2770 THR A CB    1 
ATOM   9694  O  OG1   . THR A 1 2770 ? 245.195 183.102 196.882 1.00 46.34  ? 2770 THR A OG1   1 
ATOM   9695  C  CG2   . THR A 1 2770 ? 245.691 184.406 198.839 1.00 39.54  ? 2770 THR A CG2   1 
ATOM   9696  N  N     . ALA A 1 2771 ? 248.541 185.986 196.696 1.00 38.98  ? 2771 ALA A N     1 
ATOM   9697  C  CA    . ALA A 1 2771 ? 249.609 186.891 197.105 1.00 31.69  ? 2771 ALA A CA    1 
ATOM   9698  C  C     . ALA A 1 2771 ? 249.395 188.287 196.539 1.00 40.86  ? 2771 ALA A C     1 
ATOM   9699  O  O     . ALA A 1 2771 ? 249.574 189.284 197.247 1.00 49.70  ? 2771 ALA A O     1 
ATOM   9700  C  CB    . ALA A 1 2771 ? 250.962 186.335 196.670 1.00 37.59  ? 2771 ALA A CB    1 
ATOM   9701  N  N     . ALA A 1 2772 ? 249.009 188.379 195.264 1.00 41.05  ? 2772 ALA A N     1 
ATOM   9702  C  CA    . ALA A 1 2772 ? 248.746 189.680 194.659 1.00 40.05  ? 2772 ALA A CA    1 
ATOM   9703  C  C     . ALA A 1 2772 ? 247.570 190.373 195.333 1.00 38.22  ? 2772 ALA A C     1 
ATOM   9704  O  O     . ALA A 1 2772 ? 247.624 191.579 195.608 1.00 51.85  ? 2772 ALA A O     1 
ATOM   9705  C  CB    . ALA A 1 2772 ? 248.486 189.519 193.162 1.00 31.78  ? 2772 ALA A CB    1 
ATOM   9706  N  N     . MET A 1 2773 ? 246.500 189.623 195.606 1.00 24.50  ? 2773 MET A N     1 
ATOM   9707  C  CA    . MET A 1 2773 ? 245.350 190.187 196.304 1.00 24.35  ? 2773 MET A CA    1 
ATOM   9708  C  C     . MET A 1 2773 ? 245.763 190.768 197.650 1.00 36.25  ? 2773 MET A C     1 
ATOM   9709  O  O     . MET A 1 2773 ? 245.437 191.917 197.973 1.00 38.32  ? 2773 MET A O     1 
ATOM   9710  C  CB    . MET A 1 2773 ? 244.280 189.111 196.494 1.00 30.74  ? 2773 MET A CB    1 
ATOM   9711  C  CG    . MET A 1 2773 ? 243.598 188.665 195.214 1.00 36.60  ? 2773 MET A CG    1 
ATOM   9712  S  SD    . MET A 1 2773 ? 242.145 187.644 195.513 1.00 47.68  ? 2773 MET A SD    1 
ATOM   9713  C  CE    . MET A 1 2773 ? 241.320 188.608 196.771 1.00 32.97  ? 2773 MET A CE    1 
ATOM   9714  N  N     . VAL A 1 2774 ? 246.501 189.986 198.440 1.00 46.52  ? 2774 VAL A N     1 
ATOM   9715  C  CA    . VAL A 1 2774 ? 246.888 190.420 199.778 1.00 40.90  ? 2774 VAL A CA    1 
ATOM   9716  C  C     . VAL A 1 2774 ? 247.815 191.626 199.708 1.00 47.74  ? 2774 VAL A C     1 
ATOM   9717  O  O     . VAL A 1 2774 ? 247.668 192.581 200.479 1.00 52.98  ? 2774 VAL A O     1 
ATOM   9718  C  CB    . VAL A 1 2774 ? 247.530 189.254 200.551 1.00 36.54  ? 2774 VAL A CB    1 
ATOM   9719  C  CG1   . VAL A 1 2774 ? 248.163 189.753 201.835 1.00 42.82  ? 2774 VAL A CG1   1 
ATOM   9720  C  CG2   . VAL A 1 2774 ? 246.495 188.187 200.849 1.00 39.29  ? 2774 VAL A CG2   1 
ATOM   9721  N  N     . GLU A 1 2775 ? 248.783 191.606 198.791 1.00 42.92  ? 2775 GLU A N     1 
ATOM   9722  C  CA    . GLU A 1 2775 ? 249.730 192.711 198.686 1.00 33.27  ? 2775 GLU A CA    1 
ATOM   9723  C  C     . GLU A 1 2775 ? 249.030 194.006 198.293 1.00 38.75  ? 2775 GLU A C     1 
ATOM   9724  O  O     . GLU A 1 2775 ? 249.277 195.065 198.887 1.00 54.72  ? 2775 GLU A O     1 
ATOM   9725  C  CB    . GLU A 1 2775 ? 250.821 192.363 197.677 1.00 35.18  ? 2775 GLU A CB    1 
ATOM   9726  C  CG    . GLU A 1 2775 ? 251.570 193.561 197.142 1.00 43.21  ? 2775 GLU A CG    1 
ATOM   9727  C  CD    . GLU A 1 2775 ? 252.872 193.176 196.477 1.00 55.49  ? 2775 GLU A CD    1 
ATOM   9728  O  OE1   . GLU A 1 2775 ? 252.877 192.186 195.717 1.00 58.61  ? 2775 GLU A OE1   1 
ATOM   9729  O  OE2   . GLU A 1 2775 ? 253.890 193.859 196.715 1.00 51.94  ? 2775 GLU A OE2   1 
ATOM   9730  N  N     . PHE A 1 2776 ? 248.148 193.945 197.291 1.00 35.47  ? 2776 PHE A N     1 
ATOM   9731  C  CA    . PHE A 1 2776 ? 247.453 195.160 196.881 1.00 32.28  ? 2776 PHE A CA    1 
ATOM   9732  C  C     . PHE A 1 2776 ? 246.521 195.660 197.973 1.00 32.70  ? 2776 PHE A C     1 
ATOM   9733  O  O     . PHE A 1 2776 ? 246.418 196.871 198.196 1.00 43.00  ? 2776 PHE A O     1 
ATOM   9734  C  CB    . PHE A 1 2776 ? 246.674 194.942 195.588 1.00 35.80  ? 2776 PHE A CB    1 
ATOM   9735  C  CG    . PHE A 1 2776 ? 246.016 196.191 195.084 1.00 42.43  ? 2776 PHE A CG    1 
ATOM   9736  C  CD1   . PHE A 1 2776 ? 246.777 197.287 194.717 1.00 41.25  ? 2776 PHE A CD1   1 
ATOM   9737  C  CD2   . PHE A 1 2776 ? 244.639 196.289 195.021 1.00 43.61  ? 2776 PHE A CD2   1 
ATOM   9738  C  CE1   . PHE A 1 2776 ? 246.178 198.444 194.274 1.00 35.82  ? 2776 PHE A CE1   1 
ATOM   9739  C  CE2   . PHE A 1 2776 ? 244.036 197.445 194.576 1.00 39.25  ? 2776 PHE A CE2   1 
ATOM   9740  C  CZ    . PHE A 1 2776 ? 244.806 198.524 194.207 1.00 39.84  ? 2776 PHE A CZ    1 
ATOM   9741  N  N     . TYR A 1 2777 ? 245.833 194.750 198.666 1.00 32.53  ? 2777 TYR A N     1 
ATOM   9742  C  CA    . TYR A 1 2777 ? 244.970 195.172 199.762 1.00 34.47  ? 2777 TYR A CA    1 
ATOM   9743  C  C     . TYR A 1 2777 ? 245.777 195.837 200.868 1.00 42.70  ? 2777 TYR A C     1 
ATOM   9744  O  O     . TYR A 1 2777 ? 245.354 196.853 201.432 1.00 46.29  ? 2777 TYR A O     1 
ATOM   9745  C  CB    . TYR A 1 2777 ? 244.194 193.973 200.302 1.00 38.32  ? 2777 TYR A CB    1 
ATOM   9746  C  CG    . TYR A 1 2777 ? 243.684 194.139 201.714 1.00 41.10  ? 2777 TYR A CG    1 
ATOM   9747  C  CD1   . TYR A 1 2777 ? 242.521 194.847 201.973 1.00 34.69  ? 2777 TYR A CD1   1 
ATOM   9748  C  CD2   . TYR A 1 2777 ? 244.359 193.576 202.786 1.00 43.39  ? 2777 TYR A CD2   1 
ATOM   9749  C  CE1   . TYR A 1 2777 ? 242.050 194.996 203.258 1.00 34.40  ? 2777 TYR A CE1   1 
ATOM   9750  C  CE2   . TYR A 1 2777 ? 243.897 193.724 204.073 1.00 42.08  ? 2777 TYR A CE2   1 
ATOM   9751  C  CZ    . TYR A 1 2777 ? 242.743 194.433 204.304 1.00 41.35  ? 2777 TYR A CZ    1 
ATOM   9752  O  OH    . TYR A 1 2777 ? 242.281 194.577 205.590 1.00 38.02  ? 2777 TYR A OH    1 
ATOM   9753  N  N     . THR A 1 2778 ? 246.950 195.284 201.186 1.00 46.49  ? 2778 THR A N     1 
ATOM   9754  C  CA    . THR A 1 2778 ? 247.784 195.865 202.230 1.00 37.10  ? 2778 THR A CA    1 
ATOM   9755  C  C     . THR A 1 2778 ? 248.268 197.257 201.844 1.00 44.21  ? 2778 THR A C     1 
ATOM   9756  O  O     . THR A 1 2778 ? 248.224 198.186 202.662 1.00 47.13  ? 2778 THR A O     1 
ATOM   9757  C  CB    . THR A 1 2778 ? 248.970 194.947 202.519 1.00 37.56  ? 2778 THR A CB    1 
ATOM   9758  O  OG1   . THR A 1 2778 ? 248.490 193.671 202.957 1.00 41.66  ? 2778 THR A OG1   1 
ATOM   9759  C  CG2   . THR A 1 2778 ? 249.853 195.541 203.599 1.00 49.28  ? 2778 THR A CG2   1 
ATOM   9760  N  N     . MET A 1 2779 ? 248.727 197.430 200.600 1.00 41.98  ? 2779 MET A N     1 
ATOM   9761  C  CA    . MET A 1 2779 ? 249.172 198.761 200.196 1.00 36.80  ? 2779 MET A CA    1 
ATOM   9762  C  C     . MET A 1 2779 ? 248.016 199.749 200.153 1.00 41.46  ? 2779 MET A C     1 
ATOM   9763  O  O     . MET A 1 2779 ? 248.193 200.922 200.490 1.00 52.64  ? 2779 MET A O     1 
ATOM   9764  C  CB    . MET A 1 2779 ? 249.882 198.742 198.846 1.00 36.31  ? 2779 MET A CB    1 
ATOM   9765  C  CG    . MET A 1 2779 ? 251.197 198.004 198.830 1.00 48.08  ? 2779 MET A CG    1 
ATOM   9766  S  SD    . MET A 1 2779 ? 251.930 198.154 197.199 1.00 71.25  ? 2779 MET A SD    1 
ATOM   9767  C  CE    . MET A 1 2779 ? 250.873 197.052 196.299 1.00 44.77  ? 2779 MET A CE    1 
ATOM   9768  N  N     . SER A 1 2780 ? 246.837 199.313 199.708 1.00 41.73  ? 2780 SER A N     1 
ATOM   9769  C  CA    . SER A 1 2780 ? 245.687 200.209 199.699 1.00 37.43  ? 2780 SER A CA    1 
ATOM   9770  C  C     . SER A 1 2780 ? 245.312 200.627 201.113 1.00 40.14  ? 2780 SER A C     1 
ATOM   9771  O  O     . SER A 1 2780 ? 244.958 201.786 201.354 1.00 46.71  ? 2780 SER A O     1 
ATOM   9772  C  CB    . SER A 1 2780 ? 244.501 199.540 199.006 1.00 39.21  ? 2780 SER A CB    1 
ATOM   9773  O  OG    . SER A 1 2780 ? 244.842 199.131 197.694 1.00 50.71  ? 2780 SER A OG    1 
ATOM   9774  N  N     . GLN A 1 2781 ? 245.379 199.690 202.060 1.00 39.75  ? 2781 GLN A N     1 
ATOM   9775  C  CA    . GLN A 1 2781 ? 245.073 200.011 203.448 1.00 40.31  ? 2781 GLN A CA    1 
ATOM   9776  C  C     . GLN A 1 2781 ? 246.085 200.990 204.028 1.00 41.86  ? 2781 GLN A C     1 
ATOM   9777  O  O     . GLN A 1 2781 ? 245.717 201.905 204.774 1.00 47.42  ? 2781 GLN A O     1 
ATOM   9778  C  CB    . GLN A 1 2781 ? 245.032 198.727 204.272 1.00 40.05  ? 2781 GLN A CB    1 
ATOM   9779  C  CG    . GLN A 1 2781 ? 244.159 198.802 205.501 1.00 41.93  ? 2781 GLN A CG    1 
ATOM   9780  C  CD    . GLN A 1 2781 ? 244.130 197.495 206.253 1.00 47.41  ? 2781 GLN A CD    1 
ATOM   9781  O  OE1   . GLN A 1 2781 ? 244.946 196.609 206.006 1.00 51.00  ? 2781 GLN A OE1   1 
ATOM   9782  N  NE2   . GLN A 1 2781 ? 243.183 197.359 207.169 1.00 48.09  ? 2781 GLN A NE2   1 
ATOM   9783  N  N     . GLU A 1 2782 ? 247.369 200.808 203.709 1.00 49.10  ? 2782 GLU A N     1 
ATOM   9784  C  CA    . GLU A 1 2782 ? 248.387 201.719 204.226 1.00 41.74  ? 2782 GLU A CA    1 
ATOM   9785  C  C     . GLU A 1 2782 ? 248.286 203.096 203.578 1.00 50.54  ? 2782 GLU A C     1 
ATOM   9786  O  O     . GLU A 1 2782 ? 248.457 204.119 204.249 1.00 52.68  ? 2782 GLU A O     1 
ATOM   9787  C  CB    . GLU A 1 2782 ? 249.780 201.131 204.008 1.00 43.21  ? 2782 GLU A CB    1 
ATOM   9788  C  CG    . GLU A 1 2782 ? 250.073 199.894 204.839 1.00 53.72  ? 2782 GLU A CG    1 
ATOM   9789  C  CD    . GLU A 1 2782 ? 251.521 199.451 204.733 1.00 59.33  ? 2782 GLU A CD    1 
ATOM   9790  O  OE1   . GLU A 1 2782 ? 252.100 199.052 205.765 1.00 57.29  ? 2782 GLU A OE1   1 
ATOM   9791  O  OE2   . GLU A 1 2782 ? 252.079 199.501 203.616 1.00 56.70  ? 2782 GLU A OE2   1 
ATOM   9792  N  N     . ARG A 1 2783 ? 248.012 203.138 202.273 1.00 49.37  ? 2783 ARG A N     1 
ATOM   9793  C  CA    . ARG A 1 2783 ? 248.009 204.398 201.538 1.00 45.22  ? 2783 ARG A CA    1 
ATOM   9794  C  C     . ARG A 1 2783 ? 246.787 205.243 201.872 1.00 52.63  ? 2783 ARG A C     1 
ATOM   9795  O  O     . ARG A 1 2783 ? 246.905 206.453 202.095 1.00 56.08  ? 2783 ARG A O     1 
ATOM   9796  C  CB    . ARG A 1 2783 ? 248.071 204.114 200.039 1.00 42.06  ? 2783 ARG A CB    1 
ATOM   9797  C  CG    . ARG A 1 2783 ? 247.893 205.329 199.151 1.00 49.74  ? 2783 ARG A CG    1 
ATOM   9798  C  CD    . ARG A 1 2783 ? 249.146 206.182 199.112 1.00 50.77  ? 2783 ARG A CD    1 
ATOM   9799  N  NE    . ARG A 1 2783 ? 249.213 206.987 197.899 1.00 54.93  ? 2783 ARG A NE    1 
ATOM   9800  C  CZ    . ARG A 1 2783 ? 248.506 208.089 197.687 1.00 59.53  ? 2783 ARG A CZ    1 
ATOM   9801  N  NH1   . ARG A 1 2783 ? 247.669 208.560 198.596 1.00 54.73  ? 2783 ARG A NH1   1 
ATOM   9802  N  NH2   . ARG A 1 2783 ? 248.644 208.735 196.532 1.00 56.79  ? 2783 ARG A NH2   1 
ATOM   9803  N  N     . PHE A 1 2784 ? 245.608 204.630 201.910 1.00 49.95  ? 2784 PHE A N     1 
ATOM   9804  C  CA    . PHE A 1 2784 ? 244.350 205.341 202.111 1.00 46.06  ? 2784 PHE A CA    1 
ATOM   9805  C  C     . PHE A 1 2784 ? 243.834 205.029 203.508 1.00 50.47  ? 2784 PHE A C     1 
ATOM   9806  O  O     . PHE A 1 2784 ? 243.357 203.919 203.767 1.00 55.54  ? 2784 PHE A O     1 
ATOM   9807  C  CB    . PHE A 1 2784 ? 243.327 204.949 201.049 1.00 48.70  ? 2784 PHE A CB    1 
ATOM   9808  C  CG    . PHE A 1 2784 ? 243.849 205.035 199.646 1.00 43.34  ? 2784 PHE A CG    1 
ATOM   9809  C  CD1   . PHE A 1 2784 ? 244.197 206.255 199.098 1.00 44.90  ? 2784 PHE A CD1   1 
ATOM   9810  C  CD2   . PHE A 1 2784 ? 243.987 203.897 198.875 1.00 46.71  ? 2784 PHE A CD2   1 
ATOM   9811  C  CE1   . PHE A 1 2784 ? 244.678 206.337 197.811 1.00 47.90  ? 2784 PHE A CE1   1 
ATOM   9812  C  CE2   . PHE A 1 2784 ? 244.466 203.974 197.586 1.00 49.59  ? 2784 PHE A CE2   1 
ATOM   9813  C  CZ    . PHE A 1 2784 ? 244.812 205.196 197.054 1.00 48.34  ? 2784 PHE A CZ    1 
ATOM   9814  N  N     . THR A 1 2785 ? 243.923 206.007 204.401 1.00 50.71  ? 2785 THR A N     1 
ATOM   9815  C  CA    . THR A 1 2785 ? 243.454 205.871 205.769 1.00 54.33  ? 2785 THR A CA    1 
ATOM   9816  C  C     . THR A 1 2785 ? 242.325 206.859 206.026 1.00 50.22  ? 2785 THR A C     1 
ATOM   9817  O  O     . THR A 1 2785 ? 242.036 207.740 205.213 1.00 52.22  ? 2785 THR A O     1 
ATOM   9818  C  CB    . THR A 1 2785 ? 244.593 206.091 206.772 1.00 58.08  ? 2785 THR A CB    1 
ATOM   9819  O  OG1   . THR A 1 2785 ? 245.124 207.411 206.614 1.00 60.17  ? 2785 THR A OG1   1 
ATOM   9820  C  CG2   . THR A 1 2785 ? 245.700 205.073 206.549 1.00 55.29  ? 2785 THR A CG2   1 
ATOM   9821  N  N     . GLN A 1 2786 ? 241.683 206.700 207.183 1.00 55.24  ? 2786 GLN A N     1 
ATOM   9822  C  CA    . GLN A 1 2786 ? 240.566 207.557 207.556 1.00 56.60  ? 2786 GLN A CA    1 
ATOM   9823  C  C     . GLN A 1 2786 ? 240.994 208.984 207.866 1.00 59.96  ? 2786 GLN A C     1 
ATOM   9824  O  O     . GLN A 1 2786 ? 240.126 209.848 208.031 1.00 60.22  ? 2786 GLN A O     1 
ATOM   9825  C  CB    . GLN A 1 2786 ? 239.833 206.960 208.757 1.00 56.83  ? 2786 GLN A CB    1 
ATOM   9826  C  CG    . GLN A 1 2786 ? 238.339 207.205 208.754 1.00 57.44  ? 2786 GLN A CG    1 
ATOM   9827  C  CD    . GLN A 1 2786 ? 237.617 206.390 209.803 1.00 64.16  ? 2786 GLN A CD    1 
ATOM   9828  O  OE1   . GLN A 1 2786 ? 238.235 205.639 210.557 1.00 63.37  ? 2786 GLN A OE1   1 
ATOM   9829  N  NE2   . GLN A 1 2786 ? 236.299 206.536 209.862 1.00 63.09  ? 2786 GLN A NE2   1 
ATOM   9830  N  N     . ASP A 1 2787 ? 242.298 209.248 207.968 1.00 67.28  ? 2787 ASP A N     1 
ATOM   9831  C  CA    . ASP A 1 2787 ? 242.763 210.620 208.134 1.00 66.77  ? 2787 ASP A CA    1 
ATOM   9832  C  C     . ASP A 1 2787 ? 242.434 211.462 206.908 1.00 69.40  ? 2787 ASP A C     1 
ATOM   9833  O  O     . ASP A 1 2787 ? 242.024 212.622 207.033 1.00 68.95  ? 2787 ASP A O     1 
ATOM   9834  C  CB    . ASP A 1 2787 ? 244.267 210.637 208.407 1.00 66.88  ? 2787 ASP A CB    1 
ATOM   9835  C  CG    . ASP A 1 2787 ? 244.653 209.777 209.594 1.00 75.38  ? 2787 ASP A CG    1 
ATOM   9836  O  OD1   . ASP A 1 2787 ? 243.754 209.403 210.375 1.00 72.42  ? 2787 ASP A OD1   1 
ATOM   9837  O  OD2   . ASP A 1 2787 ? 245.856 209.478 209.748 1.00 75.59  ? 2787 ASP A OD2   1 
ATOM   9838  N  N     . THR A 1 2788 ? 242.605 210.894 205.713 1.00 64.07  ? 2788 THR A N     1 
ATOM   9839  C  CA    . THR A 1 2788 ? 242.319 211.633 204.488 1.00 58.61  ? 2788 THR A CA    1 
ATOM   9840  C  C     . THR A 1 2788 ? 240.819 211.830 204.304 1.00 61.31  ? 2788 THR A C     1 
ATOM   9841  O  O     . THR A 1 2788 ? 240.328 212.964 204.279 1.00 65.82  ? 2788 THR A O     1 
ATOM   9842  C  CB    . THR A 1 2788 ? 242.918 210.902 203.284 1.00 59.17  ? 2788 THR A CB    1 
ATOM   9843  O  OG1   . THR A 1 2788 ? 244.266 210.519 203.578 1.00 67.48  ? 2788 THR A OG1   1 
ATOM   9844  C  CG2   . THR A 1 2788 ? 242.908 211.800 202.060 1.00 60.41  ? 2788 THR A CG2   1 
ATOM   9845  N  N     . GLN A 1 2789 ? 240.076 210.736 204.173 1.00 51.21  ? 2789 GLN A N     1 
ATOM   9846  C  CA    . GLN A 1 2789 ? 238.635 210.783 203.998 1.00 47.10  ? 2789 GLN A CA    1 
ATOM   9847  C  C     . GLN A 1 2789 ? 237.965 209.799 204.943 1.00 53.30  ? 2789 GLN A C     1 
ATOM   9848  O  O     . GLN A 1 2789 ? 238.528 208.743 205.247 1.00 59.40  ? 2789 GLN A O     1 
ATOM   9849  C  CB    . GLN A 1 2789 ? 238.241 210.457 202.551 1.00 48.57  ? 2789 GLN A CB    1 
ATOM   9850  C  CG    . GLN A 1 2789 ? 238.849 211.385 201.517 1.00 54.83  ? 2789 GLN A CG    1 
ATOM   9851  C  CD    . GLN A 1 2789 ? 238.079 212.680 201.376 1.00 58.44  ? 2789 GLN A CD    1 
ATOM   9852  O  OE1   . GLN A 1 2789 ? 236.923 212.775 201.784 1.00 55.65  ? 2789 GLN A OE1   1 
ATOM   9853  N  NE2   . GLN A 1 2789 ? 238.718 213.688 200.796 1.00 58.91  ? 2789 GLN A NE2   1 
ATOM   9854  N  N     . PRO A 1 2790 ? 236.764 210.124 205.428 1.00 55.70  ? 2790 PRO A N     1 
ATOM   9855  C  CA    . PRO A 1 2790 ? 236.099 209.232 206.393 1.00 49.72  ? 2790 PRO A CA    1 
ATOM   9856  C  C     . PRO A 1 2790 ? 235.798 207.849 205.849 1.00 52.92  ? 2790 PRO A C     1 
ATOM   9857  O  O     . PRO A 1 2790 ? 235.825 206.876 206.613 1.00 58.35  ? 2790 PRO A O     1 
ATOM   9858  C  CB    . PRO A 1 2790 ? 234.811 209.993 206.736 1.00 52.49  ? 2790 PRO A CB    1 
ATOM   9859  C  CG    . PRO A 1 2790 ? 234.585 210.897 205.578 1.00 54.60  ? 2790 PRO A CG    1 
ATOM   9860  C  CD    . PRO A 1 2790 ? 235.946 211.308 205.120 1.00 53.92  ? 2790 PRO A CD    1 
ATOM   9861  N  N     . HIS A 1 2791 ? 235.512 207.726 204.558 1.00 49.34  ? 2791 HIS A N     1 
ATOM   9862  C  CA    . HIS A 1 2791 ? 235.090 206.462 203.974 1.00 46.79  ? 2791 HIS A CA    1 
ATOM   9863  C  C     . HIS A 1 2791 ? 236.251 205.614 203.474 1.00 50.45  ? 2791 HIS A C     1 
ATOM   9864  O  O     . HIS A 1 2791 ? 236.014 204.573 202.854 1.00 53.18  ? 2791 HIS A O     1 
ATOM   9865  C  CB    . HIS A 1 2791 ? 234.108 206.715 202.827 1.00 42.24  ? 2791 HIS A CB    1 
ATOM   9866  C  CG    . HIS A 1 2791 ? 234.673 207.546 201.719 1.00 43.87  ? 2791 HIS A CG    1 
ATOM   9867  N  ND1   . HIS A 1 2791 ? 234.870 208.905 201.832 1.00 45.49  ? 2791 HIS A ND1   1 
ATOM   9868  C  CD2   . HIS A 1 2791 ? 235.073 207.212 200.470 1.00 40.62  ? 2791 HIS A CD2   1 
ATOM   9869  C  CE1   . HIS A 1 2791 ? 235.372 209.371 200.704 1.00 43.24  ? 2791 HIS A CE1   1 
ATOM   9870  N  NE2   . HIS A 1 2791 ? 235.506 208.363 199.861 1.00 40.94  ? 2791 HIS A NE2   1 
ATOM   9871  N  N     . TYR A 1 2792 ? 237.494 206.027 203.721 1.00 39.49  ? 2792 TYR A N     1 
ATOM   9872  C  CA    . TYR A 1 2792 ? 238.662 205.256 203.299 1.00 39.75  ? 2792 TYR A CA    1 
ATOM   9873  C  C     . TYR A 1 2792 ? 238.936 204.160 204.330 1.00 49.61  ? 2792 TYR A C     1 
ATOM   9874  O  O     . TYR A 1 2792 ? 239.943 204.152 205.040 1.00 57.47  ? 2792 TYR A O     1 
ATOM   9875  C  CB    . TYR A 1 2792 ? 239.871 206.162 203.116 1.00 44.20  ? 2792 TYR A CB    1 
ATOM   9876  C  CG    . TYR A 1 2792 ? 239.839 207.012 201.867 1.00 40.97  ? 2792 TYR A CG    1 
ATOM   9877  C  CD1   . TYR A 1 2792 ? 238.730 207.028 201.037 1.00 44.91  ? 2792 TYR A CD1   1 
ATOM   9878  C  CD2   . TYR A 1 2792 ? 240.925 207.798 201.518 1.00 44.85  ? 2792 TYR A CD2   1 
ATOM   9879  C  CE1   . TYR A 1 2792 ? 238.702 207.803 199.901 1.00 45.41  ? 2792 TYR A CE1   1 
ATOM   9880  C  CE2   . TYR A 1 2792 ? 240.906 208.575 200.384 1.00 48.37  ? 2792 TYR A CE2   1 
ATOM   9881  C  CZ    . TYR A 1 2792 ? 239.793 208.575 199.579 1.00 48.19  ? 2792 TYR A CZ    1 
ATOM   9882  O  OH    . TYR A 1 2792 ? 239.773 209.352 198.447 1.00 57.49  ? 2792 TYR A OH    1 
ATOM   9883  N  N     . ILE A 1 2793 ? 238.004 203.216 204.401 1.00 44.70  ? 2793 ILE A N     1 
ATOM   9884  C  CA    . ILE A 1 2793 ? 238.086 202.087 205.318 1.00 38.70  ? 2793 ILE A CA    1 
ATOM   9885  C  C     . ILE A 1 2793 ? 238.221 200.822 204.487 1.00 37.64  ? 2793 ILE A C     1 
ATOM   9886  O  O     . ILE A 1 2793 ? 237.314 200.479 203.718 1.00 43.27  ? 2793 ILE A O     1 
ATOM   9887  C  CB    . ILE A 1 2793 ? 236.861 202.011 206.241 1.00 42.22  ? 2793 ILE A CB    1 
ATOM   9888  C  CG1   . ILE A 1 2793 ? 236.879 203.166 207.241 1.00 46.30  ? 2793 ILE A CG1   1 
ATOM   9889  C  CG2   . ILE A 1 2793 ? 236.821 200.677 206.964 1.00 45.81  ? 2793 ILE A CG2   1 
ATOM   9890  C  CD1   . ILE A 1 2793 ? 235.523 203.496 207.812 1.00 45.49  ? 2793 ILE A CD1   1 
ATOM   9891  N  N     . TYR A 1 2794 ? 239.347 200.133 204.638 1.00 37.46  ? 2794 TYR A N     1 
ATOM   9892  C  CA    . TYR A 1 2794 ? 239.630 198.907 203.908 1.00 37.07  ? 2794 TYR A CA    1 
ATOM   9893  C  C     . TYR A 1 2794 ? 239.781 197.766 204.900 1.00 40.32  ? 2794 TYR A C     1 
ATOM   9894  O  O     . TYR A 1 2794 ? 240.536 197.878 205.871 1.00 43.23  ? 2794 TYR A O     1 
ATOM   9895  C  CB    . TYR A 1 2794 ? 240.890 199.056 203.055 1.00 33.89  ? 2794 TYR A CB    1 
ATOM   9896  C  CG    . TYR A 1 2794 ? 240.725 200.037 201.921 1.00 38.56  ? 2794 TYR A CG    1 
ATOM   9897  C  CD1   . TYR A 1 2794 ? 240.108 199.663 200.739 1.00 37.55  ? 2794 TYR A CD1   1 
ATOM   9898  C  CD2   . TYR A 1 2794 ? 241.176 201.343 202.038 1.00 42.70  ? 2794 TYR A CD2   1 
ATOM   9899  C  CE1   . TYR A 1 2794 ? 239.949 200.557 199.705 1.00 33.80  ? 2794 TYR A CE1   1 
ATOM   9900  C  CE2   . TYR A 1 2794 ? 241.021 202.243 201.008 1.00 35.36  ? 2794 TYR A CE2   1 
ATOM   9901  C  CZ    . TYR A 1 2794 ? 240.409 201.845 199.844 1.00 40.37  ? 2794 TYR A CZ    1 
ATOM   9902  O  OH    . TYR A 1 2794 ? 240.252 202.739 198.812 1.00 50.68  ? 2794 TYR A OH    1 
ATOM   9903  N  N     . SER A 1 2795 ? 239.018 196.695 204.675 1.00 29.60  ? 2795 SER A N     1 
ATOM   9904  C  CA    . SER A 1 2795 ? 239.011 195.557 205.624 1.00 33.09  ? 2795 SER A CA    1 
ATOM   9905  C  C     . SER A 1 2795 ? 238.973 194.241 204.846 1.00 39.91  ? 2795 SER A C     1 
ATOM   9906  O  O     . SER A 1 2795 ? 238.805 194.289 203.615 1.00 46.44  ? 2795 SER A O     1 
ATOM   9907  C  CB    . SER A 1 2795 ? 237.823 195.668 206.527 1.00 35.51  ? 2795 SER A CB    1 
ATOM   9908  O  OG    . SER A 1 2795 ? 236.619 195.658 205.778 1.00 36.63  ? 2795 SER A OG    1 
ATOM   9909  N  N     . PRO A 1 2796 ? 239.106 193.072 205.506 1.00 33.61  ? 2796 PRO A N     1 
ATOM   9910  C  CA    . PRO A 1 2796 ? 238.992 191.790 204.814 1.00 27.30  ? 2796 PRO A CA    1 
ATOM   9911  C  C     . PRO A 1 2796 ? 237.651 191.654 204.077 1.00 34.96  ? 2796 PRO A C     1 
ATOM   9912  O  O     . PRO A 1 2796 ? 237.529 190.756 203.273 1.00 45.61  ? 2796 PRO A O     1 
ATOM   9913  C  CB    . PRO A 1 2796 ? 239.070 190.777 205.963 1.00 26.77  ? 2796 PRO A CB    1 
ATOM   9914  C  CG    . PRO A 1 2796 ? 239.883 191.483 207.020 1.00 29.59  ? 2796 PRO A CG    1 
ATOM   9915  C  CD    . PRO A 1 2796 ? 239.436 192.925 206.924 1.00 29.39  ? 2796 PRO A CD    1 
ATOM   9916  N  N     . ARG A 1 2797 ? 236.685 192.528 204.372 1.00 31.37  ? 2797 ARG A N     1 
ATOM   9917  C  CA    . ARG A 1 2797 ? 235.366 192.493 203.684 1.00 25.10  ? 2797 ARG A CA    1 
ATOM   9918  C  C     . ARG A 1 2797 ? 235.566 192.752 202.187 1.00 32.51  ? 2797 ARG A C     1 
ATOM   9919  O  O     . ARG A 1 2797 ? 234.916 192.062 201.385 1.00 47.96  ? 2797 ARG A O     1 
ATOM   9920  C  CB    . ARG A 1 2797 ? 234.409 193.509 204.311 1.00 32.52  ? 2797 ARG A CB    1 
ATOM   9921  C  CG    . ARG A 1 2797 ? 233.970 193.155 205.724 1.00 43.18  ? 2797 ARG A CG    1 
ATOM   9922  C  CD    . ARG A 1 2797 ? 232.672 193.834 206.117 1.00 31.68  ? 2797 ARG A CD    1 
ATOM   9923  N  NE    . ARG A 1 2797 ? 232.780 195.284 206.127 1.00 34.44  ? 2797 ARG A NE    1 
ATOM   9924  C  CZ    . ARG A 1 2797 ? 232.570 196.044 207.195 1.00 46.56  ? 2797 ARG A CZ    1 
ATOM   9925  N  NH1   . ARG A 1 2797 ? 232.148 195.500 208.322 1.00 36.45  ? 2797 ARG A NH1   1 
ATOM   9926  N  NH2   . ARG A 1 2797 ? 232.782 197.348 207.132 1.00 45.85  ? 2797 ARG A NH2   1 
ATOM   9927  N  N     . GLU A 1 2798 ? 236.431 193.703 201.831 1.00 39.68  ? 2798 GLU A N     1 
ATOM   9928  C  CA    . GLU A 1 2798 ? 236.741 193.982 200.403 1.00 29.50  ? 2798 GLU A CA    1 
ATOM   9929  C  C     . GLU A 1 2798 ? 237.459 192.768 199.813 1.00 35.79  ? 2798 GLU A C     1 
ATOM   9930  O  O     . GLU A 1 2798 ? 237.182 192.428 198.651 1.00 47.41  ? 2798 GLU A O     1 
ATOM   9931  C  CB    . GLU A 1 2798 ? 237.630 195.220 200.287 1.00 29.93  ? 2798 GLU A CB    1 
ATOM   9932  C  CG    . GLU A 1 2798 ? 237.396 196.243 201.384 1.00 41.86  ? 2798 GLU A CG    1 
ATOM   9933  C  CD    . GLU A 1 2798 ? 236.097 197.021 201.271 1.00 50.88  ? 2798 GLU A CD    1 
ATOM   9934  O  OE1   . GLU A 1 2798 ? 235.366 196.808 200.285 1.00 53.27  ? 2798 GLU A OE1   1 
ATOM   9935  O  OE2   . GLU A 1 2798 ? 235.818 197.836 202.173 1.00 45.00  ? 2798 GLU A OE2   1 
ATOM   9936  N  N     . MET A 1 2799 ? 238.347 192.147 200.591 1.00 33.20  ? 2799 MET A N     1 
ATOM   9937  C  CA    . MET A 1 2799 ? 239.084 190.943 200.130 1.00 28.01  ? 2799 MET A CA    1 
ATOM   9938  C  C     . MET A 1 2799 ? 238.077 189.832 199.823 1.00 33.55  ? 2799 MET A C     1 
ATOM   9939  O  O     . MET A 1 2799 ? 238.328 189.056 198.887 1.00 44.42  ? 2799 MET A O     1 
ATOM   9940  C  CB    . MET A 1 2799 ? 240.053 190.467 201.215 1.00 29.81  ? 2799 MET A CB    1 
ATOM   9941  C  CG    . MET A 1 2799 ? 241.307 191.308 201.327 1.00 31.66  ? 2799 MET A CG    1 
ATOM   9942  S  SD    . MET A 1 2799 ? 242.541 190.891 200.074 1.00 56.56  ? 2799 MET A SD    1 
ATOM   9943  C  CE    . MET A 1 2799 ? 242.454 189.103 200.102 1.00 36.77  ? 2799 MET A CE    1 
ATOM   9944  N  N     . THR A 1 2800 ? 236.989 189.757 200.593 1.00 28.98  ? 2800 THR A N     1 
ATOM   9945  C  CA    . THR A 1 2800 ? 235.936 188.732 200.365 1.00 26.46  ? 2800 THR A CA    1 
ATOM   9946  C  C     . THR A 1 2800 ? 235.124 189.107 199.124 1.00 34.37  ? 2800 THR A C     1 
ATOM   9947  O  O     . THR A 1 2800 ? 234.845 188.208 198.315 1.00 48.84  ? 2800 THR A O     1 
ATOM   9948  C  CB    . THR A 1 2800 ? 235.027 188.601 201.591 1.00 30.12  ? 2800 THR A CB    1 
ATOM   9949  O  OG1   . THR A 1 2800 ? 235.857 188.341 202.723 1.00 41.72  ? 2800 THR A OG1   1 
ATOM   9950  C  CG2   . THR A 1 2800 ? 233.994 187.506 201.447 1.00 35.81  ? 2800 THR A CG2   1 
ATOM   9951  N  N     . ARG A 1 2801 ? 234.760 190.385 198.991 1.00 31.32  ? 2801 ARG A N     1 
ATOM   9952  C  CA    . ARG A 1 2801 ? 234.007 190.859 197.801 1.00 29.38  ? 2801 ARG A CA    1 
ATOM   9953  C  C     . ARG A 1 2801 ? 234.876 190.644 196.561 1.00 33.83  ? 2801 ARG A C     1 
ATOM   9954  O  O     . ARG A 1 2801 ? 234.309 190.382 195.488 1.00 47.41  ? 2801 ARG A O     1 
ATOM   9955  C  CB    . ARG A 1 2801 ? 233.630 192.332 197.967 1.00 29.74  ? 2801 ARG A CB    1 
ATOM   9956  C  CG    . ARG A 1 2801 ? 232.799 192.620 199.209 1.00 39.92  ? 2801 ARG A CG    1 
ATOM   9957  C  CD    . ARG A 1 2801 ? 232.527 194.100 199.396 1.00 49.03  ? 2801 ARG A CD    1 
ATOM   9958  N  NE    . ARG A 1 2801 ? 231.740 194.357 200.593 1.00 49.90  ? 2801 ARG A NE    1 
ATOM   9959  C  CZ    . ARG A 1 2801 ? 232.142 195.108 201.611 1.00 47.04  ? 2801 ARG A CZ    1 
ATOM   9960  N  NH1   . ARG A 1 2801 ? 233.271 195.787 201.525 1.00 36.19  ? 2801 ARG A NH1   1 
ATOM   9961  N  NH2   . ARG A 1 2801 ? 231.413 195.178 202.711 1.00 44.83  ? 2801 ARG A NH2   1 
ATOM   9962  N  N     . TRP A 1 2802 ? 236.198 190.754 196.705 1.00 19.85  ? 2802 TRP A N     1 
ATOM   9963  C  CA    . TRP A 1 2802 ? 237.096 190.481 195.589 1.00 24.20  ? 2802 TRP A CA    1 
ATOM   9964  C  C     . TRP A 1 2802 ? 236.992 189.029 195.146 1.00 29.73  ? 2802 TRP A C     1 
ATOM   9965  O  O     . TRP A 1 2802 ? 236.820 188.734 193.954 1.00 39.80  ? 2802 TRP A O     1 
ATOM   9966  C  CB    . TRP A 1 2802 ? 238.523 190.816 196.020 1.00 27.63  ? 2802 TRP A CB    1 
ATOM   9967  C  CG    . TRP A 1 2802 ? 239.470 191.163 194.931 1.00 24.81  ? 2802 TRP A CG    1 
ATOM   9968  C  CD1   . TRP A 1 2802 ? 239.306 190.956 193.599 1.00 30.41  ? 2802 TRP A CD1   1 
ATOM   9969  C  CD2   . TRP A 1 2802 ? 240.743 191.793 195.088 1.00 30.90  ? 2802 TRP A CD2   1 
ATOM   9970  N  NE1   . TRP A 1 2802 ? 240.402 191.416 192.912 1.00 28.42  ? 2802 TRP A NE1   1 
ATOM   9971  C  CE2   . TRP A 1 2802 ? 241.298 191.935 193.806 1.00 25.66  ? 2802 TRP A CE2   1 
ATOM   9972  C  CE3   . TRP A 1 2802 ? 241.469 192.249 196.191 1.00 31.18  ? 2802 TRP A CE3   1 
ATOM   9973  C  CZ2   . TRP A 1 2802 ? 242.543 192.512 193.596 1.00 24.91  ? 2802 TRP A CZ2   1 
ATOM   9974  C  CZ3   . TRP A 1 2802 ? 242.703 192.823 195.980 1.00 29.04  ? 2802 TRP A CZ3   1 
ATOM   9975  C  CH2   . TRP A 1 2802 ? 243.228 192.951 194.693 1.00 29.52  ? 2802 TRP A CH2   1 
ATOM   9976  N  N     . VAL A 1 2803 ? 237.095 188.106 196.102 1.00 37.06  ? 2803 VAL A N     1 
ATOM   9977  C  CA    . VAL A 1 2803 ? 237.025 186.684 195.781 1.00 33.11  ? 2803 VAL A CA    1 
ATOM   9978  C  C     . VAL A 1 2803 ? 235.656 186.338 195.207 1.00 36.36  ? 2803 VAL A C     1 
ATOM   9979  O  O     . VAL A 1 2803 ? 235.545 185.600 194.222 1.00 46.11  ? 2803 VAL A O     1 
ATOM   9980  C  CB    . VAL A 1 2803 ? 237.353 185.837 197.023 1.00 37.48  ? 2803 VAL A CB    1 
ATOM   9981  C  CG1   . VAL A 1 2803 ? 237.097 184.375 196.747 1.00 36.91  ? 2803 VAL A CG1   1 
ATOM   9982  C  CG2   . VAL A 1 2803 ? 238.793 186.050 197.438 1.00 41.86  ? 2803 VAL A CG2   1 
ATOM   9983  N  N     . ARG A 1 2804 ? 234.591 186.879 195.807 1.00 35.41  ? 2804 ARG A N     1 
ATOM   9984  C  CA    . ARG A 1 2804 ? 233.243 186.620 195.310 1.00 35.08  ? 2804 ARG A CA    1 
ATOM   9985  C  C     . ARG A 1 2804 ? 233.046 187.167 193.900 1.00 37.92  ? 2804 ARG A C     1 
ATOM   9986  O  O     . ARG A 1 2804 ? 232.403 186.523 193.065 1.00 47.57  ? 2804 ARG A O     1 
ATOM   9987  C  CB    . ARG A 1 2804 ? 232.212 187.210 196.272 1.00 36.78  ? 2804 ARG A CB    1 
ATOM   9988  C  CG    . ARG A 1 2804 ? 230.781 187.182 195.759 1.00 43.81  ? 2804 ARG A CG    1 
ATOM   9989  C  CD    . ARG A 1 2804 ? 230.252 185.773 195.529 1.00 46.88  ? 2804 ARG A CD    1 
ATOM   9990  N  NE    . ARG A 1 2804 ? 230.075 185.015 196.761 1.00 55.74  ? 2804 ARG A NE    1 
ATOM   9991  C  CZ    . ARG A 1 2804 ? 229.800 183.719 196.805 1.00 53.96  ? 2804 ARG A CZ    1 
ATOM   9992  N  NH1   . ARG A 1 2804 ? 229.658 183.005 195.701 1.00 43.71  ? 2804 ARG A NH1   1 
ATOM   9993  N  NH2   . ARG A 1 2804 ? 229.662 183.124 197.986 1.00 49.14  ? 2804 ARG A NH2   1 
ATOM   9994  N  N     . GLY A 1 2805 ? 233.587 188.351 193.613 1.00 34.58  ? 2805 GLY A N     1 
ATOM   9995  C  CA    . GLY A 1 2805 ? 233.447 188.912 192.280 1.00 29.34  ? 2805 GLY A CA    1 
ATOM   9996  C  C     . GLY A 1 2805 ? 234.185 188.108 191.229 1.00 33.21  ? 2805 GLY A C     1 
ATOM   9997  O  O     . GLY A 1 2805 ? 233.661 187.855 190.140 1.00 50.97  ? 2805 GLY A O     1 
ATOM   9998  N  N     . ILE A 1 2806 ? 235.415 187.691 191.540 1.00 32.15  ? 2806 ILE A N     1 
ATOM   9999  C  CA    . ILE A 1 2806 ? 236.150 186.855 190.594 1.00 26.92  ? 2806 ILE A CA    1 
ATOM   10000 C  C     . ILE A 1 2806 ? 235.437 185.522 190.402 1.00 32.31  ? 2806 ILE A C     1 
ATOM   10001 O  O     . ILE A 1 2806 ? 235.384 184.985 189.290 1.00 47.67  ? 2806 ILE A O     1 
ATOM   10002 C  CB    . ILE A 1 2806 ? 237.608 186.661 191.047 1.00 27.00  ? 2806 ILE A CB    1 
ATOM   10003 C  CG1   . ILE A 1 2806 ? 238.303 188.010 191.203 1.00 33.30  ? 2806 ILE A CG1   1 
ATOM   10004 C  CG2   . ILE A 1 2806 ? 238.365 185.821 190.041 1.00 31.70  ? 2806 ILE A CG2   1 
ATOM   10005 C  CD1   . ILE A 1 2806 ? 239.715 187.904 191.711 1.00 29.44  ? 2806 ILE A CD1   1 
ATOM   10006 N  N     . PHE A 1 2807 ? 234.867 184.973 191.476 1.00 35.64  ? 2807 PHE A N     1 
ATOM   10007 C  CA    . PHE A 1 2807 ? 234.128 183.719 191.367 1.00 33.11  ? 2807 PHE A CA    1 
ATOM   10008 C  C     . PHE A 1 2807 ? 232.896 183.874 190.486 1.00 42.13  ? 2807 PHE A C     1 
ATOM   10009 O  O     . PHE A 1 2807 ? 232.596 182.998 189.667 1.00 57.52  ? 2807 PHE A O     1 
ATOM   10010 C  CB    . PHE A 1 2807 ? 233.738 183.230 192.760 1.00 39.63  ? 2807 PHE A CB    1 
ATOM   10011 C  CG    . PHE A 1 2807 ? 232.784 182.075 192.753 1.00 44.84  ? 2807 PHE A CG    1 
ATOM   10012 C  CD1   . PHE A 1 2807 ? 233.182 180.834 192.298 1.00 44.21  ? 2807 PHE A CD1   1 
ATOM   10013 C  CD2   . PHE A 1 2807 ? 231.487 182.233 193.204 1.00 46.63  ? 2807 PHE A CD2   1 
ATOM   10014 C  CE1   . PHE A 1 2807 ? 232.305 179.774 192.293 1.00 43.45  ? 2807 PHE A CE1   1 
ATOM   10015 C  CE2   . PHE A 1 2807 ? 230.606 181.175 193.200 1.00 49.21  ? 2807 PHE A CE2   1 
ATOM   10016 C  CZ    . PHE A 1 2807 ? 231.016 179.945 192.744 1.00 47.31  ? 2807 PHE A CZ    1 
ATOM   10017 N  N     . GLU A 1 2808 ? 232.164 184.977 190.642 1.00 41.24  ? 2808 GLU A N     1 
ATOM   10018 C  CA    . GLU A 1 2808 ? 230.981 185.200 189.820 1.00 39.55  ? 2808 GLU A CA    1 
ATOM   10019 C  C     . GLU A 1 2808 ? 231.344 185.447 188.363 1.00 41.90  ? 2808 GLU A C     1 
ATOM   10020 O  O     . GLU A 1 2808 ? 230.586 185.064 187.465 1.00 46.43  ? 2808 GLU A O     1 
ATOM   10021 C  CB    . GLU A 1 2808 ? 230.169 186.371 190.370 1.00 36.11  ? 2808 GLU A CB    1 
ATOM   10022 C  CG    . GLU A 1 2808 ? 229.487 186.085 191.696 1.00 42.51  ? 2808 GLU A CG    1 
ATOM   10023 C  CD    . GLU A 1 2808 ? 228.963 187.340 192.361 1.00 55.83  ? 2808 GLU A CD    1 
ATOM   10024 O  OE1   . GLU A 1 2808 ? 229.152 188.438 191.796 1.00 56.48  ? 2808 GLU A OE1   1 
ATOM   10025 O  OE2   . GLU A 1 2808 ? 228.357 187.232 193.447 1.00 53.87  ? 2808 GLU A OE2   1 
ATOM   10026 N  N     . ALA A 1 2809 ? 232.482 186.091 188.105 1.00 42.24  ? 2809 ALA A N     1 
ATOM   10027 C  CA    . ALA A 1 2809 ? 232.916 186.294 186.729 1.00 37.54  ? 2809 ALA A CA    1 
ATOM   10028 C  C     . ALA A 1 2809 ? 233.545 185.048 186.119 1.00 48.89  ? 2809 ALA A C     1 
ATOM   10029 O  O     . ALA A 1 2809 ? 233.660 184.968 184.892 1.00 53.85  ? 2809 ALA A O     1 
ATOM   10030 C  CB    . ALA A 1 2809 ? 233.902 187.460 186.655 1.00 32.67  ? 2809 ALA A CB    1 
ATOM   10031 N  N     . LEU A 1 2810 ? 233.953 184.082 186.942 1.00 51.56  ? 2810 LEU A N     1 
ATOM   10032 C  CA    . LEU A 1 2810 ? 234.552 182.845 186.457 1.00 41.69  ? 2810 LEU A CA    1 
ATOM   10033 C  C     . LEU A 1 2810 ? 233.565 181.691 186.370 1.00 45.82  ? 2810 LEU A C     1 
ATOM   10034 O  O     . LEU A 1 2810 ? 233.827 180.727 185.643 1.00 54.46  ? 2810 LEU A O     1 
ATOM   10035 C  CB    . LEU A 1 2810 ? 235.707 182.420 187.369 1.00 39.39  ? 2810 LEU A CB    1 
ATOM   10036 C  CG    . LEU A 1 2810 ? 237.068 183.084 187.182 1.00 42.07  ? 2810 LEU A CG    1 
ATOM   10037 C  CD1   . LEU A 1 2810 ? 238.134 182.319 187.941 1.00 44.84  ? 2810 LEU A CD1   1 
ATOM   10038 C  CD2   . LEU A 1 2810 ? 237.408 183.150 185.716 1.00 51.39  ? 2810 LEU A CD2   1 
ATOM   10039 N  N     . ARG A 1 2811 ? 232.452 181.762 187.096 1.00 47.79  ? 2811 ARG A N     1 
ATOM   10040 C  CA    . ARG A 1 2811 ? 231.564 180.608 187.226 1.00 45.55  ? 2811 ARG A CA    1 
ATOM   10041 C  C     . ARG A 1 2811 ? 231.000 180.114 185.899 1.00 52.82  ? 2811 ARG A C     1 
ATOM   10042 O  O     . ARG A 1 2811 ? 231.085 178.901 185.637 1.00 57.42  ? 2811 ARG A O     1 
ATOM   10043 C  CB    . ARG A 1 2811 ? 230.447 180.944 188.219 1.00 45.95  ? 2811 ARG A CB    1 
ATOM   10044 C  CG    . ARG A 1 2811 ? 229.747 179.740 188.810 1.00 52.83  ? 2811 ARG A CG    1 
ATOM   10045 C  CD    . ARG A 1 2811 ? 228.294 180.054 189.123 1.00 54.13  ? 2811 ARG A CD    1 
ATOM   10046 N  NE    . ARG A 1 2811 ? 228.157 180.929 190.282 1.00 60.07  ? 2811 ARG A NE    1 
ATOM   10047 C  CZ    . ARG A 1 2811 ? 227.977 182.241 190.216 1.00 60.99  ? 2811 ARG A CZ    1 
ATOM   10048 N  NH1   . ARG A 1 2811 ? 227.908 182.872 189.056 1.00 50.61  ? 2811 ARG A NH1   1 
ATOM   10049 N  NH2   . ARG A 1 2811 ? 227.862 182.937 191.343 1.00 55.97  ? 2811 ARG A NH2   1 
ATOM   10050 N  N     . PRO A 1 2812 ? 230.424 180.953 185.027 1.00 60.74  ? 2812 PRO A N     1 
ATOM   10051 C  CA    . PRO A 1 2812 ? 229.815 180.407 183.804 1.00 55.51  ? 2812 PRO A CA    1 
ATOM   10052 C  C     . PRO A 1 2812 ? 230.809 180.048 182.715 1.00 59.15  ? 2812 PRO A C     1 
ATOM   10053 O  O     . PRO A 1 2812 ? 230.443 179.305 181.795 1.00 61.60  ? 2812 PRO A O     1 
ATOM   10054 C  CB    . PRO A 1 2812 ? 228.885 181.535 183.344 1.00 58.12  ? 2812 PRO A CB    1 
ATOM   10055 C  CG    . PRO A 1 2812 ? 229.553 182.762 183.819 1.00 60.59  ? 2812 PRO A CG    1 
ATOM   10056 C  CD    . PRO A 1 2812 ? 230.226 182.413 185.118 1.00 63.83  ? 2812 PRO A CD    1 
ATOM   10057 N  N     . LEU A 1 2813 ? 232.042 180.542 182.780 1.00 63.46  ? 2813 LEU A N     1 
ATOM   10058 C  CA    . LEU A 1 2813 ? 233.009 180.266 181.728 1.00 63.21  ? 2813 LEU A CA    1 
ATOM   10059 C  C     . LEU A 1 2813 ? 233.496 178.825 181.803 1.00 68.15  ? 2813 LEU A C     1 
ATOM   10060 O  O     . LEU A 1 2813 ? 233.790 178.304 182.882 1.00 67.94  ? 2813 LEU A O     1 
ATOM   10061 C  CB    . LEU A 1 2813 ? 234.195 181.222 181.829 1.00 60.02  ? 2813 LEU A CB    1 
ATOM   10062 C  CG    . LEU A 1 2813 ? 233.862 182.708 181.934 1.00 66.12  ? 2813 LEU A CG    1 
ATOM   10063 C  CD1   . LEU A 1 2813 ? 235.131 183.532 181.854 1.00 62.79  ? 2813 LEU A CD1   1 
ATOM   10064 C  CD2   . LEU A 1 2813 ? 232.884 183.120 180.848 1.00 64.63  ? 2813 LEU A CD2   1 
ATOM   10065 N  N     . GLU A 1 2814 ? 233.580 178.179 180.639 1.00 72.79  ? 2814 GLU A N     1 
ATOM   10066 C  CA    . GLU A 1 2814 ? 234.113 176.824 180.576 1.00 73.50  ? 2814 GLU A CA    1 
ATOM   10067 C  C     . GLU A 1 2814 ? 235.633 176.816 180.684 1.00 71.44  ? 2814 GLU A C     1 
ATOM   10068 O  O     . GLU A 1 2814 ? 236.209 175.912 181.299 1.00 74.19  ? 2814 GLU A O     1 
ATOM   10069 C  CB    . GLU A 1 2814 ? 233.664 176.144 179.283 1.00 74.52  ? 2814 GLU A CB    1 
ATOM   10070 C  CG    . GLU A 1 2814 ? 232.155 175.994 179.155 1.00 74.44  ? 2814 GLU A CG    1 
ATOM   10071 C  CD    . GLU A 1 2814 ? 231.623 174.782 179.895 1.00 78.54  ? 2814 GLU A CD    1 
ATOM   10072 O  OE1   . GLU A 1 2814 ? 231.461 174.861 181.131 1.00 76.06  ? 2814 GLU A OE1   1 
ATOM   10073 O  OE2   . GLU A 1 2814 ? 231.364 173.751 179.240 1.00 76.36  ? 2814 GLU A OE2   1 
ATOM   10074 N  N     . THR A 1 2815 ? 236.297 177.811 180.099 1.00 64.72  ? 2815 THR A N     1 
ATOM   10075 C  CA    . THR A 1 2815 ? 237.750 177.891 180.139 1.00 68.55  ? 2815 THR A CA    1 
ATOM   10076 C  C     . THR A 1 2815 ? 238.171 179.349 180.044 1.00 69.05  ? 2815 THR A C     1 
ATOM   10077 O  O     . THR A 1 2815 ? 237.400 180.213 179.619 1.00 71.42  ? 2815 THR A O     1 
ATOM   10078 C  CB    . THR A 1 2815 ? 238.395 177.073 179.013 1.00 69.83  ? 2815 THR A CB    1 
ATOM   10079 O  OG1   . THR A 1 2815 ? 239.793 176.909 179.281 1.00 69.02  ? 2815 THR A OG1   1 
ATOM   10080 C  CG2   . THR A 1 2815 ? 238.220 177.772 177.674 1.00 65.45  ? 2815 THR A CG2   1 
ATOM   10081 N  N     . LEU A 1 2816 ? 239.411 179.614 180.451 1.00 57.32  ? 2816 LEU A N     1 
ATOM   10082 C  CA    . LEU A 1 2816 ? 239.945 180.969 180.452 1.00 53.95  ? 2816 LEU A CA    1 
ATOM   10083 C  C     . LEU A 1 2816 ? 241.466 180.955 180.544 1.00 56.92  ? 2816 LEU A C     1 
ATOM   10084 O  O     . LEU A 1 2816 ? 242.034 180.193 181.335 1.00 60.46  ? 2816 LEU A O     1 
ATOM   10085 C  CB    . LEU A 1 2816 ? 239.358 181.776 181.610 1.00 56.67  ? 2816 LEU A CB    1 
ATOM   10086 C  CG    . LEU A 1 2816 ? 239.577 183.288 181.560 1.00 60.62  ? 2816 LEU A CG    1 
ATOM   10087 C  CD1   . LEU A 1 2816 ? 238.527 183.967 180.701 1.00 58.69  ? 2816 LEU A CD1   1 
ATOM   10088 C  CD2   . LEU A 1 2816 ? 239.568 183.857 182.960 1.00 55.39  ? 2816 LEU A CD2   1 
ATOM   10089 N  N     . PRO A 1 2817 ? 242.155 181.772 179.753 1.00 53.80  ? 2817 PRO A N     1 
ATOM   10090 C  CA    . PRO A 1 2817 ? 243.609 181.889 179.895 1.00 54.86  ? 2817 PRO A CA    1 
ATOM   10091 C  C     . PRO A 1 2817 ? 243.971 182.694 181.134 1.00 58.00  ? 2817 PRO A C     1 
ATOM   10092 O  O     . PRO A 1 2817 ? 243.126 183.305 181.789 1.00 56.83  ? 2817 PRO A O     1 
ATOM   10093 C  CB    . PRO A 1 2817 ? 244.036 182.607 178.614 1.00 52.34  ? 2817 PRO A CB    1 
ATOM   10094 C  CG    . PRO A 1 2817 ? 242.838 183.384 178.213 1.00 55.65  ? 2817 PRO A CG    1 
ATOM   10095 C  CD    . PRO A 1 2817 ? 241.644 182.570 178.626 1.00 55.13  ? 2817 PRO A CD    1 
ATOM   10096 N  N     . VAL A 1 2818 ? 245.266 182.680 181.455 1.00 53.88  ? 2818 VAL A N     1 
ATOM   10097 C  CA    . VAL A 1 2818 ? 245.743 183.373 182.648 1.00 48.08  ? 2818 VAL A CA    1 
ATOM   10098 C  C     . VAL A 1 2818 ? 245.530 184.877 182.519 1.00 51.14  ? 2818 VAL A C     1 
ATOM   10099 O  O     . VAL A 1 2818 ? 245.201 185.557 183.498 1.00 54.69  ? 2818 VAL A O     1 
ATOM   10100 C  CB    . VAL A 1 2818 ? 247.218 183.022 182.920 1.00 49.23  ? 2818 VAL A CB    1 
ATOM   10101 C  CG1   . VAL A 1 2818 ? 248.082 183.337 181.711 1.00 54.15  ? 2818 VAL A CG1   1 
ATOM   10102 C  CG2   . VAL A 1 2818 ? 247.724 183.760 184.148 1.00 50.77  ? 2818 VAL A CG2   1 
ATOM   10103 N  N     . GLU A 1 2819 ? 245.702 185.419 181.310 1.00 53.20  ? 2819 GLU A N     1 
ATOM   10104 C  CA    . GLU A 1 2819 ? 245.516 186.852 181.114 1.00 49.32  ? 2819 GLU A CA    1 
ATOM   10105 C  C     . GLU A 1 2819 ? 244.075 187.271 181.369 1.00 54.73  ? 2819 GLU A C     1 
ATOM   10106 O  O     . GLU A 1 2819 ? 243.832 188.361 181.895 1.00 57.66  ? 2819 GLU A O     1 
ATOM   10107 C  CB    . GLU A 1 2819 ? 245.951 187.253 179.707 1.00 55.99  ? 2819 GLU A CB    1 
ATOM   10108 C  CG    . GLU A 1 2819 ? 247.451 187.186 179.488 1.00 58.09  ? 2819 GLU A CG    1 
ATOM   10109 C  CD    . GLU A 1 2819 ? 247.905 185.838 178.972 1.00 63.38  ? 2819 GLU A CD    1 
ATOM   10110 O  OE1   . GLU A 1 2819 ? 247.041 185.038 178.555 1.00 58.45  ? 2819 GLU A OE1   1 
ATOM   10111 O  OE2   . GLU A 1 2819 ? 249.125 185.575 178.985 1.00 62.65  ? 2819 GLU A OE2   1 
ATOM   10112 N  N     . GLY A 1 2820 ? 243.109 186.425 181.013 1.00 46.65  ? 2820 GLY A N     1 
ATOM   10113 C  CA    . GLY A 1 2820 ? 241.730 186.711 181.372 1.00 42.69  ? 2820 GLY A CA    1 
ATOM   10114 C  C     . GLY A 1 2820 ? 241.520 186.737 182.873 1.00 48.61  ? 2820 GLY A C     1 
ATOM   10115 O  O     . GLY A 1 2820 ? 240.777 187.576 183.393 1.00 59.77  ? 2820 GLY A O     1 
ATOM   10116 N  N     . LEU A 1 2821 ? 242.170 185.819 183.591 1.00 41.59  ? 2821 LEU A N     1 
ATOM   10117 C  CA    . LEU A 1 2821 ? 242.079 185.817 185.046 1.00 42.66  ? 2821 LEU A CA    1 
ATOM   10118 C  C     . LEU A 1 2821 ? 242.661 187.096 185.633 1.00 44.26  ? 2821 LEU A C     1 
ATOM   10119 O  O     . LEU A 1 2821 ? 242.079 187.684 186.551 1.00 51.24  ? 2821 LEU A O     1 
ATOM   10120 C  CB    . LEU A 1 2821 ? 242.792 184.591 185.614 1.00 45.96  ? 2821 LEU A CB    1 
ATOM   10121 C  CG    . LEU A 1 2821 ? 242.981 184.555 187.131 1.00 43.16  ? 2821 LEU A CG    1 
ATOM   10122 C  CD1   . LEU A 1 2821 ? 241.732 184.024 187.808 1.00 39.46  ? 2821 LEU A CD1   1 
ATOM   10123 C  CD2   . LEU A 1 2821 ? 244.195 183.721 187.502 1.00 40.23  ? 2821 LEU A CD2   1 
ATOM   10124 N  N     . ILE A 1 2822 ? 243.803 187.546 185.111 1.00 40.01  ? 2822 ILE A N     1 
ATOM   10125 C  CA    . ILE A 1 2822 ? 244.396 188.788 185.600 1.00 39.54  ? 2822 ILE A CA    1 
ATOM   10126 C  C     . ILE A 1 2822 ? 243.513 189.979 185.251 1.00 42.30  ? 2822 ILE A C     1 
ATOM   10127 O  O     . ILE A 1 2822 ? 243.437 190.951 186.008 1.00 48.93  ? 2822 ILE A O     1 
ATOM   10128 C  CB    . ILE A 1 2822 ? 245.827 188.967 185.059 1.00 40.30  ? 2822 ILE A CB    1 
ATOM   10129 C  CG1   . ILE A 1 2822 ? 246.626 187.672 185.179 1.00 46.52  ? 2822 ILE A CG1   1 
ATOM   10130 C  CG2   . ILE A 1 2822 ? 246.542 190.057 185.822 1.00 40.43  ? 2822 ILE A CG2   1 
ATOM   10131 C  CD1   . ILE A 1 2822 ? 246.549 187.030 186.543 1.00 49.08  ? 2822 ILE A CD1   1 
ATOM   10132 N  N     . ARG A 1 2823 ? 242.839 189.932 184.100 1.00 40.25  ? 2823 ARG A N     1 
ATOM   10133 C  CA    . ARG A 1 2823 ? 241.926 191.013 183.746 1.00 32.24  ? 2823 ARG A CA    1 
ATOM   10134 C  C     . ARG A 1 2823 ? 240.745 191.080 184.707 1.00 42.53  ? 2823 ARG A C     1 
ATOM   10135 O  O     . ARG A 1 2823 ? 240.348 192.169 185.135 1.00 45.50  ? 2823 ARG A O     1 
ATOM   10136 C  CB    . ARG A 1 2823 ? 241.442 190.847 182.309 1.00 43.80  ? 2823 ARG A CB    1 
ATOM   10137 C  CG    . ARG A 1 2823 ? 240.878 192.120 181.711 1.00 45.84  ? 2823 ARG A CG    1 
ATOM   10138 C  CD    . ARG A 1 2823 ? 240.725 192.010 180.209 1.00 45.01  ? 2823 ARG A CD    1 
ATOM   10139 N  NE    . ARG A 1 2823 ? 240.052 193.176 179.651 1.00 47.55  ? 2823 ARG A NE    1 
ATOM   10140 C  CZ    . ARG A 1 2823 ? 240.646 194.333 179.399 1.00 48.38  ? 2823 ARG A CZ    1 
ATOM   10141 N  NH1   . ARG A 1 2823 ? 241.932 194.517 179.640 1.00 45.41  ? 2823 ARG A NH1   1 
ATOM   10142 N  NH2   . ARG A 1 2823 ? 239.929 195.332 178.892 1.00 53.80  ? 2823 ARG A NH2   1 
ATOM   10143 N  N     . ILE A 1 2824 ? 240.170 189.928 185.058 1.00 48.47  ? 2824 ILE A N     1 
ATOM   10144 C  CA    . ILE A 1 2824 ? 239.091 189.918 186.046 1.00 36.82  ? 2824 ILE A CA    1 
ATOM   10145 C  C     . ILE A 1 2824 ? 239.599 190.412 187.394 1.00 46.03  ? 2824 ILE A C     1 
ATOM   10146 O  O     . ILE A 1 2824 ? 238.920 191.178 188.091 1.00 51.89  ? 2824 ILE A O     1 
ATOM   10147 C  CB    . ILE A 1 2824 ? 238.471 188.515 186.166 1.00 31.49  ? 2824 ILE A CB    1 
ATOM   10148 C  CG1   . ILE A 1 2824 ? 238.015 188.006 184.802 1.00 42.40  ? 2824 ILE A CG1   1 
ATOM   10149 C  CG2   . ILE A 1 2824 ? 237.304 188.540 187.128 1.00 39.29  ? 2824 ILE A CG2   1 
ATOM   10150 C  CD1   . ILE A 1 2824 ? 237.288 186.688 184.865 1.00 46.56  ? 2824 ILE A CD1   1 
ATOM   10151 N  N     . TRP A 1 2825 ? 240.797 189.972 187.784 1.00 38.02  ? 2825 TRP A N     1 
ATOM   10152 C  CA    . TRP A 1 2825 ? 241.395 190.407 189.039 1.00 29.15  ? 2825 TRP A CA    1 
ATOM   10153 C  C     . TRP A 1 2825 ? 241.554 191.923 189.077 1.00 32.68  ? 2825 TRP A C     1 
ATOM   10154 O  O     . TRP A 1 2825 ? 241.176 192.575 190.057 1.00 34.73  ? 2825 TRP A O     1 
ATOM   10155 C  CB    . TRP A 1 2825 ? 242.742 189.704 189.218 1.00 31.33  ? 2825 TRP A CB    1 
ATOM   10156 C  CG    . TRP A 1 2825 ? 243.541 190.153 190.392 1.00 35.23  ? 2825 TRP A CG    1 
ATOM   10157 C  CD1   . TRP A 1 2825 ? 243.489 189.652 191.655 1.00 35.93  ? 2825 TRP A CD1   1 
ATOM   10158 C  CD2   . TRP A 1 2825 ? 244.534 191.184 190.409 1.00 31.20  ? 2825 TRP A CD2   1 
ATOM   10159 N  NE1   . TRP A 1 2825 ? 244.381 190.310 192.461 1.00 35.27  ? 2825 TRP A NE1   1 
ATOM   10160 C  CE2   . TRP A 1 2825 ? 245.034 191.258 191.720 1.00 32.56  ? 2825 TRP A CE2   1 
ATOM   10161 C  CE3   . TRP A 1 2825 ? 245.042 192.056 189.443 1.00 34.41  ? 2825 TRP A CE3   1 
ATOM   10162 C  CZ2   . TRP A 1 2825 ? 246.015 192.169 192.092 1.00 38.87  ? 2825 TRP A CZ2   1 
ATOM   10163 C  CZ3   . TRP A 1 2825 ? 246.017 192.958 189.814 1.00 38.70  ? 2825 TRP A CZ3   1 
ATOM   10164 C  CH2   . TRP A 1 2825 ? 246.494 193.008 191.127 1.00 40.24  ? 2825 TRP A CH2   1 
ATOM   10165 N  N     . ALA A 1 2826 ? 242.087 192.504 188.000 1.00 37.62  ? 2826 ALA A N     1 
ATOM   10166 C  CA    . ALA A 1 2826 ? 242.297 193.946 187.951 1.00 30.87  ? 2826 ALA A CA    1 
ATOM   10167 C  C     . ALA A 1 2826 ? 240.978 194.703 187.906 1.00 31.90  ? 2826 ALA A C     1 
ATOM   10168 O  O     . ALA A 1 2826 ? 240.854 195.775 188.506 1.00 41.79  ? 2826 ALA A O     1 
ATOM   10169 C  CB    . ALA A 1 2826 ? 243.160 194.310 186.745 1.00 32.05  ? 2826 ALA A CB    1 
ATOM   10170 N  N     . HIS A 1 2827 ? 239.984 194.171 187.192 1.00 24.49  ? 2827 HIS A N     1 
ATOM   10171 C  CA    . HIS A 1 2827 ? 238.681 194.824 187.149 1.00 26.83  ? 2827 HIS A CA    1 
ATOM   10172 C  C     . HIS A 1 2827 ? 238.049 194.873 188.531 1.00 34.90  ? 2827 HIS A C     1 
ATOM   10173 O  O     . HIS A 1 2827 ? 237.539 195.918 188.954 1.00 39.55  ? 2827 HIS A O     1 
ATOM   10174 C  CB    . HIS A 1 2827 ? 237.768 194.097 186.164 1.00 32.67  ? 2827 HIS A CB    1 
ATOM   10175 C  CG    . HIS A 1 2827 ? 236.359 194.599 186.161 1.00 28.47  ? 2827 HIS A CG    1 
ATOM   10176 N  ND1   . HIS A 1 2827 ? 236.020 195.861 185.726 1.00 34.50  ? 2827 HIS A ND1   1 
ATOM   10177 C  CD2   . HIS A 1 2827 ? 235.203 194.009 186.542 1.00 26.26  ? 2827 HIS A CD2   1 
ATOM   10178 C  CE1   . HIS A 1 2827 ? 234.715 196.026 185.838 1.00 32.91  ? 2827 HIS A CE1   1 
ATOM   10179 N  NE2   . HIS A 1 2827 ? 234.196 194.917 186.330 1.00 34.31  ? 2827 HIS A NE2   1 
ATOM   10180 N  N     . GLU A 1 2828 ? 238.087 193.756 189.259 1.00 43.37  ? 2828 GLU A N     1 
ATOM   10181 C  CA    . GLU A 1 2828 ? 237.546 193.750 190.614 1.00 26.02  ? 2828 GLU A CA    1 
ATOM   10182 C  C     . GLU A 1 2828 ? 238.354 194.644 191.544 1.00 34.89  ? 2828 GLU A C     1 
ATOM   10183 O  O     . GLU A 1 2828 ? 237.780 195.306 192.416 1.00 42.20  ? 2828 GLU A O     1 
ATOM   10184 C  CB    . GLU A 1 2828 ? 237.494 192.322 191.148 1.00 32.53  ? 2828 GLU A CB    1 
ATOM   10185 C  CG    . GLU A 1 2828 ? 236.463 191.454 190.464 1.00 36.10  ? 2828 GLU A CG    1 
ATOM   10186 C  CD    . GLU A 1 2828 ? 235.077 192.049 190.538 1.00 51.68  ? 2828 GLU A CD    1 
ATOM   10187 O  OE1   . GLU A 1 2828 ? 234.662 192.452 191.644 1.00 47.19  ? 2828 GLU A OE1   1 
ATOM   10188 O  OE2   . GLU A 1 2828 ? 234.401 192.117 189.491 1.00 57.07  ? 2828 GLU A OE2   1 
ATOM   10189 N  N     . ALA A 1 2829 ? 239.678 194.685 191.374 1.00 36.99  ? 2829 ALA A N     1 
ATOM   10190 C  CA    . ALA A 1 2829 ? 240.494 195.590 192.175 1.00 26.64  ? 2829 ALA A CA    1 
ATOM   10191 C  C     . ALA A 1 2829 ? 240.092 197.038 191.944 1.00 36.71  ? 2829 ALA A C     1 
ATOM   10192 O  O     . ALA A 1 2829 ? 239.963 197.812 192.897 1.00 50.79  ? 2829 ALA A O     1 
ATOM   10193 C  CB    . ALA A 1 2829 ? 241.973 195.391 191.854 1.00 23.60  ? 2829 ALA A CB    1 
ATOM   10194 N  N     . LEU A 1 2830 ? 239.892 197.423 190.682 1.00 41.64  ? 2830 LEU A N     1 
ATOM   10195 C  CA    . LEU A 1 2830 ? 239.445 198.780 190.388 1.00 28.36  ? 2830 LEU A CA    1 
ATOM   10196 C  C     . LEU A 1 2830 ? 238.086 199.056 191.012 1.00 28.79  ? 2830 LEU A C     1 
ATOM   10197 O  O     . LEU A 1 2830 ? 237.904 200.073 191.689 1.00 37.38  ? 2830 LEU A O     1 
ATOM   10198 C  CB    . LEU A 1 2830 ? 239.392 199.005 188.878 1.00 31.17  ? 2830 LEU A CB    1 
ATOM   10199 C  CG    . LEU A 1 2830 ? 240.719 199.061 188.122 1.00 32.77  ? 2830 LEU A CG    1 
ATOM   10200 C  CD1   . LEU A 1 2830 ? 240.475 198.970 186.629 1.00 22.13  ? 2830 LEU A CD1   1 
ATOM   10201 C  CD2   . LEU A 1 2830 ? 241.470 200.331 188.464 1.00 37.96  ? 2830 LEU A CD2   1 
ATOM   10202 N  N     . ARG A 1 2831 ? 237.131 198.141 190.830 1.00 34.35  ? 2831 ARG A N     1 
ATOM   10203 C  CA    . ARG A 1 2831 ? 235.785 198.364 191.344 1.00 35.95  ? 2831 ARG A CA    1 
ATOM   10204 C  C     . ARG A 1 2831 ? 235.733 198.414 192.864 1.00 32.59  ? 2831 ARG A C     1 
ATOM   10205 O  O     . ARG A 1 2831 ? 234.838 199.060 193.417 1.00 38.58  ? 2831 ARG A O     1 
ATOM   10206 C  CB    . ARG A 1 2831 ? 234.834 197.281 190.832 1.00 32.00  ? 2831 ARG A CB    1 
ATOM   10207 C  CG    . ARG A 1 2831 ? 234.735 197.196 189.319 1.00 35.75  ? 2831 ARG A CG    1 
ATOM   10208 C  CD    . ARG A 1 2831 ? 233.860 198.295 188.738 1.00 34.27  ? 2831 ARG A CD    1 
ATOM   10209 N  NE    . ARG A 1 2831 ? 234.595 199.540 188.553 1.00 38.95  ? 2831 ARG A NE    1 
ATOM   10210 C  CZ    . ARG A 1 2831 ? 235.474 199.758 187.585 1.00 43.12  ? 2831 ARG A CZ    1 
ATOM   10211 N  NH1   . ARG A 1 2831 ? 235.747 198.837 186.677 1.00 35.93  ? 2831 ARG A NH1   1 
ATOM   10212 N  NH2   . ARG A 1 2831 ? 236.096 200.932 187.527 1.00 40.11  ? 2831 ARG A NH2   1 
ATOM   10213 N  N     . LEU A 1 2832 ? 236.659 197.752 193.554 1.00 27.35  ? 2832 LEU A N     1 
ATOM   10214 C  CA    . LEU A 1 2832 ? 236.624 197.723 195.010 1.00 31.45  ? 2832 LEU A CA    1 
ATOM   10215 C  C     . LEU A 1 2832 ? 237.495 198.777 195.670 1.00 32.74  ? 2832 LEU A C     1 
ATOM   10216 O  O     . LEU A 1 2832 ? 237.174 199.214 196.779 1.00 42.44  ? 2832 LEU A O     1 
ATOM   10217 C  CB    . LEU A 1 2832 ? 237.050 196.347 195.523 1.00 27.63  ? 2832 LEU A CB    1 
ATOM   10218 C  CG    . LEU A 1 2832 ? 236.001 195.249 195.396 1.00 31.52  ? 2832 LEU A CG    1 
ATOM   10219 C  CD1   . LEU A 1 2832 ? 236.623 193.940 195.766 1.00 33.80  ? 2832 LEU A CD1   1 
ATOM   10220 C  CD2   . LEU A 1 2832 ? 234.807 195.545 196.282 1.00 37.67  ? 2832 LEU A CD2   1 
ATOM   10221 N  N     . PHE A 1 2833 ? 238.586 199.199 195.031 1.00 34.97  ? 2833 PHE A N     1 
ATOM   10222 C  CA    . PHE A 1 2833 ? 239.529 200.103 195.666 1.00 34.80  ? 2833 PHE A CA    1 
ATOM   10223 C  C     . PHE A 1 2833 ? 239.568 201.490 195.048 1.00 36.77  ? 2833 PHE A C     1 
ATOM   10224 O  O     . PHE A 1 2833 ? 240.081 202.412 195.688 1.00 53.32  ? 2833 PHE A O     1 
ATOM   10225 C  CB    . PHE A 1 2833 ? 240.941 199.500 195.627 1.00 28.95  ? 2833 PHE A CB    1 
ATOM   10226 C  CG    . PHE A 1 2833 ? 241.069 198.214 196.392 1.00 34.45  ? 2833 PHE A CG    1 
ATOM   10227 C  CD1   . PHE A 1 2833 ? 240.808 197.001 195.783 1.00 32.62  ? 2833 PHE A CD1   1 
ATOM   10228 C  CD2   . PHE A 1 2833 ? 241.448 198.219 197.721 1.00 38.78  ? 2833 PHE A CD2   1 
ATOM   10229 C  CE1   . PHE A 1 2833 ? 240.922 195.821 196.484 1.00 29.80  ? 2833 PHE A CE1   1 
ATOM   10230 C  CE2   . PHE A 1 2833 ? 241.564 197.042 198.426 1.00 33.83  ? 2833 PHE A CE2   1 
ATOM   10231 C  CZ    . PHE A 1 2833 ? 241.301 195.842 197.806 1.00 35.33  ? 2833 PHE A CZ    1 
ATOM   10232 N  N     . GLN A 1 2834 ? 239.039 201.669 193.837 1.00 31.29  ? 2834 GLN A N     1 
ATOM   10233 C  CA    . GLN A 1 2834 ? 239.142 202.939 193.138 1.00 31.46  ? 2834 GLN A CA    1 
ATOM   10234 C  C     . GLN A 1 2834 ? 237.828 203.695 193.033 1.00 38.22  ? 2834 GLN A C     1 
ATOM   10235 O  O     . GLN A 1 2834 ? 237.851 204.898 192.758 1.00 49.16  ? 2834 GLN A O     1 
ATOM   10236 C  CB    . GLN A 1 2834 ? 239.696 202.715 191.725 1.00 37.17  ? 2834 GLN A CB    1 
ATOM   10237 C  CG    . GLN A 1 2834 ? 240.510 203.868 191.184 1.00 36.47  ? 2834 GLN A CG    1 
ATOM   10238 C  CD    . GLN A 1 2834 ? 240.751 203.756 189.696 1.00 36.29  ? 2834 GLN A CD    1 
ATOM   10239 O  OE1   . GLN A 1 2834 ? 239.812 203.638 188.911 1.00 42.72  ? 2834 GLN A OE1   1 
ATOM   10240 N  NE2   . GLN A 1 2834 ? 242.014 203.795 189.298 1.00 44.41  ? 2834 GLN A NE2   1 
ATOM   10241 N  N     . ASP A 1 2835 ? 236.692 203.030 193.242 1.00 30.57  ? 2835 ASP A N     1 
ATOM   10242 C  CA    . ASP A 1 2835 ? 235.406 203.691 193.046 1.00 27.15  ? 2835 ASP A CA    1 
ATOM   10243 C  C     . ASP A 1 2835 ? 235.118 204.713 194.137 1.00 35.77  ? 2835 ASP A C     1 
ATOM   10244 O  O     . ASP A 1 2835 ? 234.410 205.694 193.891 1.00 43.82  ? 2835 ASP A O     1 
ATOM   10245 C  CB    . ASP A 1 2835 ? 234.292 202.650 192.984 1.00 38.80  ? 2835 ASP A CB    1 
ATOM   10246 C  CG    . ASP A 1 2835 ? 234.148 202.035 191.610 1.00 50.06  ? 2835 ASP A CG    1 
ATOM   10247 O  OD1   . ASP A 1 2835 ? 234.939 202.393 190.713 1.00 45.22  ? 2835 ASP A OD1   1 
ATOM   10248 O  OD2   . ASP A 1 2835 ? 233.247 201.192 191.427 1.00 51.87  ? 2835 ASP A OD2   1 
ATOM   10249 N  N     . ARG A 1 2836 ? 235.647 204.501 195.338 1.00 39.66  ? 2836 ARG A N     1 
ATOM   10250 C  CA    . ARG A 1 2836 ? 235.411 205.398 196.459 1.00 35.98  ? 2836 ARG A CA    1 
ATOM   10251 C  C     . ARG A 1 2836 ? 236.395 206.558 196.521 1.00 39.15  ? 2836 ARG A C     1 
ATOM   10252 O  O     . ARG A 1 2836 ? 236.186 207.482 197.313 1.00 45.52  ? 2836 ARG A O     1 
ATOM   10253 C  CB    . ARG A 1 2836 ? 235.473 204.616 197.774 1.00 38.34  ? 2836 ARG A CB    1 
ATOM   10254 C  CG    . ARG A 1 2836 ? 236.883 204.257 198.206 1.00 41.75  ? 2836 ARG A CG    1 
ATOM   10255 C  CD    . ARG A 1 2836 ? 236.881 203.439 199.483 1.00 44.11  ? 2836 ARG A CD    1 
ATOM   10256 N  NE    . ARG A 1 2836 ? 236.643 202.025 199.222 1.00 46.21  ? 2836 ARG A NE    1 
ATOM   10257 C  CZ    . ARG A 1 2836 ? 236.280 201.145 200.145 1.00 45.16  ? 2836 ARG A CZ    1 
ATOM   10258 N  NH1   . ARG A 1 2836 ? 236.095 201.501 201.405 1.00 40.00  ? 2836 ARG A NH1   1 
ATOM   10259 N  NH2   . ARG A 1 2836 ? 236.096 199.876 199.793 1.00 38.35  ? 2836 ARG A NH2   1 
ATOM   10260 N  N     . LEU A 1 2837 ? 237.451 206.536 195.712 1.00 41.15  ? 2837 LEU A N     1 
ATOM   10261 C  CA    . LEU A 1 2837 ? 238.492 207.549 195.808 1.00 38.37  ? 2837 LEU A CA    1 
ATOM   10262 C  C     . LEU A 1 2837 ? 237.999 208.893 195.290 1.00 43.66  ? 2837 LEU A C     1 
ATOM   10263 O  O     . LEU A 1 2837 ? 237.253 208.966 194.310 1.00 53.65  ? 2837 LEU A O     1 
ATOM   10264 C  CB    . LEU A 1 2837 ? 239.730 207.105 195.034 1.00 42.67  ? 2837 LEU A CB    1 
ATOM   10265 C  CG    . LEU A 1 2837 ? 240.385 205.836 195.577 1.00 35.02  ? 2837 LEU A CG    1 
ATOM   10266 C  CD1   . LEU A 1 2837 ? 241.614 205.475 194.772 1.00 40.18  ? 2837 LEU A CD1   1 
ATOM   10267 C  CD2   . LEU A 1 2837 ? 240.729 206.005 197.041 1.00 36.44  ? 2837 LEU A CD2   1 
ATOM   10268 N  N     . VAL A 1 2838 ? 238.434 209.964 195.952 1.00 38.84  ? 2838 VAL A N     1 
ATOM   10269 C  CA    . VAL A 1 2838 ? 237.994 211.316 195.630 1.00 41.67  ? 2838 VAL A CA    1 
ATOM   10270 C  C     . VAL A 1 2838 ? 238.935 211.951 194.616 1.00 54.31  ? 2838 VAL A C     1 
ATOM   10271 O  O     . VAL A 1 2838 ? 238.525 212.298 193.503 1.00 56.72  ? 2838 VAL A O     1 
ATOM   10272 C  CB    . VAL A 1 2838 ? 237.905 212.180 196.900 1.00 38.77  ? 2838 VAL A CB    1 
ATOM   10273 C  CG1   . VAL A 1 2838 ? 237.235 213.502 196.592 1.00 41.57  ? 2838 VAL A CG1   1 
ATOM   10274 C  CG2   . VAL A 1 2838 ? 237.161 211.441 197.990 1.00 40.41  ? 2838 VAL A CG2   1 
ATOM   10275 N  N     . GLU A 1 2839 ? 240.199 212.111 194.995 1.00 54.16  ? 2839 GLU A N     1 
ATOM   10276 C  CA    . GLU A 1 2839 ? 241.152 212.810 194.147 1.00 50.31  ? 2839 GLU A CA    1 
ATOM   10277 C  C     . GLU A 1 2839 ? 241.604 211.930 192.988 1.00 56.42  ? 2839 GLU A C     1 
ATOM   10278 O  O     . GLU A 1 2839 ? 241.574 210.700 193.061 1.00 60.56  ? 2839 GLU A O     1 
ATOM   10279 C  CB    . GLU A 1 2839 ? 242.360 213.259 194.965 1.00 52.62  ? 2839 GLU A CB    1 
ATOM   10280 C  CG    . GLU A 1 2839 ? 242.182 214.604 195.642 1.00 58.36  ? 2839 GLU A CG    1 
ATOM   10281 C  CD    . GLU A 1 2839 ? 241.559 214.487 197.017 1.00 64.09  ? 2839 GLU A CD    1 
ATOM   10282 O  OE1   . GLU A 1 2839 ? 241.882 213.520 197.737 1.00 63.18  ? 2839 GLU A OE1   1 
ATOM   10283 O  OE2   . GLU A 1 2839 ? 240.748 215.365 197.381 1.00 58.60  ? 2839 GLU A OE2   1 
ATOM   10284 N  N     . ASP A 1 2840 ? 242.028 212.584 191.904 1.00 67.40  ? 2840 ASP A N     1 
ATOM   10285 C  CA    . ASP A 1 2840 ? 242.504 211.854 190.733 1.00 66.38  ? 2840 ASP A CA    1 
ATOM   10286 C  C     . ASP A 1 2840 ? 243.888 211.264 190.960 1.00 66.31  ? 2840 ASP A C     1 
ATOM   10287 O  O     . ASP A 1 2840 ? 244.242 210.259 190.332 1.00 64.85  ? 2840 ASP A O     1 
ATOM   10288 C  CB    . ASP A 1 2840 ? 242.513 212.769 189.511 1.00 66.12  ? 2840 ASP A CB    1 
ATOM   10289 C  CG    . ASP A 1 2840 ? 242.864 212.031 188.237 1.00 74.95  ? 2840 ASP A CG    1 
ATOM   10290 O  OD1   . ASP A 1 2840 ? 242.006 211.280 187.728 1.00 77.73  ? 2840 ASP A OD1   1 
ATOM   10291 O  OD2   . ASP A 1 2840 ? 243.998 212.203 187.743 1.00 75.72  ? 2840 ASP A OD2   1 
ATOM   10292 N  N     . GLU A 1 2841 ? 244.685 211.874 191.840 1.00 64.96  ? 2841 GLU A N     1 
ATOM   10293 C  CA    . GLU A 1 2841 ? 245.988 211.308 192.169 1.00 67.91  ? 2841 GLU A CA    1 
ATOM   10294 C  C     . GLU A 1 2841 ? 245.839 209.938 192.815 1.00 74.14  ? 2841 GLU A C     1 
ATOM   10295 O  O     . GLU A 1 2841 ? 246.617 209.019 192.530 1.00 74.75  ? 2841 GLU A O     1 
ATOM   10296 C  CB    . GLU A 1 2841 ? 246.754 212.256 193.090 1.00 68.10  ? 2841 GLU A CB    1 
ATOM   10297 C  CG    . GLU A 1 2841 ? 248.148 211.771 193.457 1.00 75.49  ? 2841 GLU A CG    1 
ATOM   10298 C  CD    . GLU A 1 2841 ? 249.080 211.699 192.263 1.00 76.47  ? 2841 GLU A CD    1 
ATOM   10299 O  OE1   . GLU A 1 2841 ? 248.859 212.444 191.284 1.00 73.44  ? 2841 GLU A OE1   1 
ATOM   10300 O  OE2   . GLU A 1 2841 ? 250.031 210.892 192.302 1.00 72.09  ? 2841 GLU A OE2   1 
ATOM   10301 N  N     . GLU A 1 2842 ? 244.841 209.782 193.686 1.00 64.31  ? 2842 GLU A N     1 
ATOM   10302 C  CA    . GLU A 1 2842 ? 244.588 208.488 194.309 1.00 53.68  ? 2842 GLU A CA    1 
ATOM   10303 C  C     . GLU A 1 2842 ? 244.195 207.442 193.274 1.00 54.52  ? 2842 GLU A C     1 
ATOM   10304 O  O     . GLU A 1 2842 ? 244.656 206.296 193.333 1.00 62.12  ? 2842 GLU A O     1 
ATOM   10305 C  CB    . GLU A 1 2842 ? 243.501 208.631 195.371 1.00 50.88  ? 2842 GLU A CB    1 
ATOM   10306 C  CG    . GLU A 1 2842 ? 243.876 209.572 196.498 1.00 57.34  ? 2842 GLU A CG    1 
ATOM   10307 C  CD    . GLU A 1 2842 ? 242.685 209.978 197.337 1.00 59.38  ? 2842 GLU A CD    1 
ATOM   10308 O  OE1   . GLU A 1 2842 ? 241.563 209.524 197.036 1.00 62.67  ? 2842 GLU A OE1   1 
ATOM   10309 O  OE2   . GLU A 1 2842 ? 242.870 210.753 198.296 1.00 60.62  ? 2842 GLU A OE2   1 
ATOM   10310 N  N     . ARG A 1 2843 ? 243.339 207.816 192.321 1.00 44.07  ? 2843 ARG A N     1 
ATOM   10311 C  CA    . ARG A 1 2843 ? 242.945 206.882 191.270 1.00 48.70  ? 2843 ARG A CA    1 
ATOM   10312 C  C     . ARG A 1 2843 ? 244.138 206.485 190.411 1.00 59.49  ? 2843 ARG A C     1 
ATOM   10313 O  O     . ARG A 1 2843 ? 244.291 205.311 190.048 1.00 67.92  ? 2843 ARG A O     1 
ATOM   10314 C  CB    . ARG A 1 2843 ? 241.848 207.502 190.408 1.00 49.68  ? 2843 ARG A CB    1 
ATOM   10315 C  CG    . ARG A 1 2843 ? 240.730 208.156 191.196 1.00 50.85  ? 2843 ARG A CG    1 
ATOM   10316 C  CD    . ARG A 1 2843 ? 239.433 208.144 190.411 1.00 57.26  ? 2843 ARG A CD    1 
ATOM   10317 N  NE    . ARG A 1 2843 ? 238.370 208.871 191.093 1.00 59.87  ? 2843 ARG A NE    1 
ATOM   10318 C  CZ    . ARG A 1 2843 ? 238.087 210.150 190.888 1.00 63.94  ? 2843 ARG A CZ    1 
ATOM   10319 N  NH1   . ARG A 1 2843 ? 238.773 210.880 190.025 1.00 58.37  ? 2843 ARG A NH1   1 
ATOM   10320 N  NH2   . ARG A 1 2843 ? 237.087 210.709 191.564 1.00 55.52  ? 2843 ARG A NH2   1 
ATOM   10321 N  N     . ARG A 1 2844 ? 244.991 207.453 190.072 1.00 60.93  ? 2844 ARG A N     1 
ATOM   10322 C  CA    . ARG A 1 2844 ? 246.182 207.151 189.287 1.00 60.14  ? 2844 ARG A CA    1 
ATOM   10323 C  C     . ARG A 1 2844 ? 247.114 206.213 190.043 1.00 64.11  ? 2844 ARG A C     1 
ATOM   10324 O  O     . ARG A 1 2844 ? 247.658 205.265 189.463 1.00 70.31  ? 2844 ARG A O     1 
ATOM   10325 C  CB    . ARG A 1 2844 ? 246.898 208.449 188.912 1.00 67.39  ? 2844 ARG A CB    1 
ATOM   10326 C  CG    . ARG A 1 2844 ? 248.397 208.313 188.707 1.00 69.19  ? 2844 ARG A CG    1 
ATOM   10327 C  CD    . ARG A 1 2844 ? 248.980 209.545 188.031 1.00 66.89  ? 2844 ARG A CD    1 
ATOM   10328 N  NE    . ARG A 1 2844 ? 248.712 210.769 188.778 1.00 72.04  ? 2844 ARG A NE    1 
ATOM   10329 C  CZ    . ARG A 1 2844 ? 247.828 211.691 188.418 1.00 70.97  ? 2844 ARG A CZ    1 
ATOM   10330 N  NH1   . ARG A 1 2844 ? 247.102 211.560 187.320 1.00 66.65  ? 2844 ARG A NH1   1 
ATOM   10331 N  NH2   . ARG A 1 2844 ? 247.669 212.770 189.179 1.00 63.78  ? 2844 ARG A NH2   1 
ATOM   10332 N  N     . TRP A 1 2845 ? 247.303 206.457 191.343 1.00 54.26  ? 2845 TRP A N     1 
ATOM   10333 C  CA    . TRP A 1 2845 ? 248.127 205.566 192.152 1.00 52.97  ? 2845 TRP A CA    1 
ATOM   10334 C  C     . TRP A 1 2845 ? 247.548 204.160 192.185 1.00 54.38  ? 2845 TRP A C     1 
ATOM   10335 O  O     . TRP A 1 2845 ? 248.282 203.175 192.037 1.00 59.08  ? 2845 TRP A O     1 
ATOM   10336 C  CB    . TRP A 1 2845 ? 248.260 206.118 193.571 1.00 54.44  ? 2845 TRP A CB    1 
ATOM   10337 C  CG    . TRP A 1 2845 ? 249.096 205.261 194.473 1.00 57.64  ? 2845 TRP A CG    1 
ATOM   10338 C  CD1   . TRP A 1 2845 ? 250.430 205.389 194.716 1.00 60.89  ? 2845 TRP A CD1   1 
ATOM   10339 C  CD2   . TRP A 1 2845 ? 248.651 204.147 195.258 1.00 59.20  ? 2845 TRP A CD2   1 
ATOM   10340 N  NE1   . TRP A 1 2845 ? 250.845 204.423 195.600 1.00 62.09  ? 2845 TRP A NE1   1 
ATOM   10341 C  CE2   . TRP A 1 2845 ? 249.770 203.650 195.950 1.00 55.90  ? 2845 TRP A CE2   1 
ATOM   10342 C  CE3   . TRP A 1 2845 ? 247.414 203.523 195.443 1.00 58.99  ? 2845 TRP A CE3   1 
ATOM   10343 C  CZ2   . TRP A 1 2845 ? 249.692 202.556 196.805 1.00 54.26  ? 2845 TRP A CZ2   1 
ATOM   10344 C  CZ3   . TRP A 1 2845 ? 247.339 202.439 196.293 1.00 55.28  ? 2845 TRP A CZ3   1 
ATOM   10345 C  CH2   . TRP A 1 2845 ? 248.470 201.967 196.964 1.00 56.50  ? 2845 TRP A CH2   1 
ATOM   10346 N  N     . THR A 1 2846 ? 246.232 204.046 192.382 1.00 51.09  ? 2846 THR A N     1 
ATOM   10347 C  CA    . THR A 1 2846 ? 245.603 202.732 192.438 1.00 49.74  ? 2846 THR A CA    1 
ATOM   10348 C  C     . THR A 1 2846 ? 245.788 201.980 191.130 1.00 53.43  ? 2846 THR A C     1 
ATOM   10349 O  O     . THR A 1 2846 ? 246.135 200.794 191.131 1.00 62.42  ? 2846 THR A O     1 
ATOM   10350 C  CB    . THR A 1 2846 ? 244.117 202.875 192.767 1.00 46.03  ? 2846 THR A CB    1 
ATOM   10351 O  OG1   . THR A 1 2846 ? 243.970 203.382 194.097 1.00 51.23  ? 2846 THR A OG1   1 
ATOM   10352 C  CG2   . THR A 1 2846 ? 243.413 201.535 192.664 1.00 51.50  ? 2846 THR A CG2   1 
ATOM   10353 N  N     . ASP A 1 2847 ? 245.585 202.660 190.002 1.00 50.38  ? 2847 ASP A N     1 
ATOM   10354 C  CA    . ASP A 1 2847 ? 245.726 202.007 188.705 1.00 54.01  ? 2847 ASP A CA    1 
ATOM   10355 C  C     . ASP A 1 2847 ? 247.169 201.570 188.457 1.00 60.53  ? 2847 ASP A C     1 
ATOM   10356 O  O     . ASP A 1 2847 ? 247.428 200.422 188.057 1.00 63.26  ? 2847 ASP A O     1 
ATOM   10357 C  CB    . ASP A 1 2847 ? 245.242 202.964 187.619 1.00 54.44  ? 2847 ASP A CB    1 
ATOM   10358 C  CG    . ASP A 1 2847 ? 245.144 202.317 186.259 1.00 70.98  ? 2847 ASP A CG    1 
ATOM   10359 O  OD1   . ASP A 1 2847 ? 245.477 201.121 186.118 1.00 68.74  ? 2847 ASP A OD1   1 
ATOM   10360 O  OD2   . ASP A 1 2847 ? 244.722 203.023 185.324 1.00 72.32  ? 2847 ASP A OD2   1 
ATOM   10361 N  N     . GLU A 1 2848 ? 248.127 202.471 188.705 1.00 59.55  ? 2848 GLU A N     1 
ATOM   10362 C  CA    . GLU A 1 2848 ? 249.530 202.144 188.480 1.00 58.36  ? 2848 GLU A CA    1 
ATOM   10363 C  C     . GLU A 1 2848 ? 249.975 200.983 189.355 1.00 64.26  ? 2848 GLU A C     1 
ATOM   10364 O  O     . GLU A 1 2848 ? 250.683 200.083 188.889 1.00 67.92  ? 2848 GLU A O     1 
ATOM   10365 C  CB    . GLU A 1 2848 ? 250.405 203.369 188.741 1.00 58.86  ? 2848 GLU A CB    1 
ATOM   10366 C  CG    . GLU A 1 2848 ? 250.246 204.484 187.724 1.00 65.68  ? 2848 GLU A CG    1 
ATOM   10367 C  CD    . GLU A 1 2848 ? 250.877 205.780 188.189 1.00 71.49  ? 2848 GLU A CD    1 
ATOM   10368 O  OE1   . GLU A 1 2848 ? 251.296 205.847 189.364 1.00 71.00  ? 2848 GLU A OE1   1 
ATOM   10369 O  OE2   . GLU A 1 2848 ? 250.954 206.731 187.383 1.00 71.80  ? 2848 GLU A OE2   1 
ATOM   10370 N  N     . ASN A 1 2849 ? 249.564 200.973 190.622 1.00 55.17  ? 2849 ASN A N     1 
ATOM   10371 C  CA    . ASN A 1 2849 ? 249.975 199.902 191.514 1.00 45.63  ? 2849 ASN A CA    1 
ATOM   10372 C  C     . ASN A 1 2849 ? 249.243 198.597 191.239 1.00 50.90  ? 2849 ASN A C     1 
ATOM   10373 O  O     . ASN A 1 2849 ? 249.808 197.530 191.487 1.00 61.62  ? 2849 ASN A O     1 
ATOM   10374 C  CB    . ASN A 1 2849 ? 249.789 200.339 192.963 1.00 50.19  ? 2849 ASN A CB    1 
ATOM   10375 C  CG    . ASN A 1 2849 ? 250.926 201.214 193.442 1.00 60.29  ? 2849 ASN A CG    1 
ATOM   10376 O  OD1   . ASN A 1 2849 ? 250.790 202.430 193.534 1.00 57.92  ? 2849 ASN A OD1   1 
ATOM   10377 N  ND2   . ASN A 1 2849 ? 252.060 200.596 193.742 1.00 65.81  ? 2849 ASN A ND2   1 
ATOM   10378 N  N     . ILE A 1 2850 ? 248.022 198.650 190.705 1.00 52.82  ? 2850 ILE A N     1 
ATOM   10379 C  CA    . ILE A 1 2850 ? 247.382 197.433 190.218 1.00 50.07  ? 2850 ILE A CA    1 
ATOM   10380 C  C     . ILE A 1 2850 ? 248.220 196.814 189.110 1.00 48.65  ? 2850 ILE A C     1 
ATOM   10381 O  O     . ILE A 1 2850 ? 248.499 195.606 189.118 1.00 55.19  ? 2850 ILE A O     1 
ATOM   10382 C  CB    . ILE A 1 2850 ? 245.951 197.738 189.740 1.00 48.82  ? 2850 ILE A CB    1 
ATOM   10383 C  CG1   . ILE A 1 2850 ? 244.991 197.775 190.922 1.00 54.02  ? 2850 ILE A CG1   1 
ATOM   10384 C  CG2   . ILE A 1 2850 ? 245.489 196.702 188.735 1.00 50.18  ? 2850 ILE A CG2   1 
ATOM   10385 C  CD1   . ILE A 1 2850 ? 243.653 198.375 190.593 1.00 48.21  ? 2850 ILE A CD1   1 
ATOM   10386 N  N     . ASP A 1 2851 ? 248.654 197.638 188.151 1.00 52.62  ? 2851 ASP A N     1 
ATOM   10387 C  CA    . ASP A 1 2851 ? 249.515 197.126 187.086 1.00 57.66  ? 2851 ASP A CA    1 
ATOM   10388 C  C     . ASP A 1 2851 ? 250.816 196.566 187.652 1.00 57.34  ? 2851 ASP A C     1 
ATOM   10389 O  O     . ASP A 1 2851 ? 251.269 195.484 187.247 1.00 52.92  ? 2851 ASP A O     1 
ATOM   10390 C  CB    . ASP A 1 2851 ? 249.809 198.231 186.072 1.00 59.24  ? 2851 ASP A CB    1 
ATOM   10391 C  CG    . ASP A 1 2851 ? 248.565 198.715 185.358 1.00 62.85  ? 2851 ASP A CG    1 
ATOM   10392 O  OD1   . ASP A 1 2851 ? 247.500 198.087 185.523 1.00 63.73  ? 2851 ASP A OD1   1 
ATOM   10393 O  OD2   . ASP A 1 2851 ? 248.651 199.727 184.632 1.00 64.17  ? 2851 ASP A OD2   1 
ATOM   10394 N  N     . THR A 1 2852 ? 251.419 197.288 188.601 1.00 57.19  ? 2852 THR A N     1 
ATOM   10395 C  CA    . THR A 1 2852 ? 252.682 196.859 189.192 1.00 54.24  ? 2852 THR A CA    1 
ATOM   10396 C  C     . THR A 1 2852 ? 252.546 195.513 189.892 1.00 55.53  ? 2852 THR A C     1 
ATOM   10397 O  O     . THR A 1 2852 ? 253.386 194.630 189.705 1.00 61.47  ? 2852 THR A O     1 
ATOM   10398 C  CB    . THR A 1 2852 ? 253.186 197.916 190.175 1.00 52.81  ? 2852 THR A CB    1 
ATOM   10399 O  OG1   . THR A 1 2852 ? 253.252 199.188 189.520 1.00 54.89  ? 2852 THR A OG1   1 
ATOM   10400 C  CG2   . THR A 1 2852 ? 254.567 197.547 190.689 1.00 56.32  ? 2852 THR A CG2   1 
ATOM   10401 N  N     . VAL A 1 2853 ? 251.499 195.337 190.698 1.00 49.12  ? 2853 VAL A N     1 
ATOM   10402 C  CA    . VAL A 1 2853 ? 251.309 194.079 191.414 1.00 46.15  ? 2853 VAL A CA    1 
ATOM   10403 C  C     . VAL A 1 2853 ? 251.038 192.942 190.440 1.00 47.73  ? 2853 VAL A C     1 
ATOM   10404 O  O     . VAL A 1 2853 ? 251.576 191.836 190.585 1.00 51.51  ? 2853 VAL A O     1 
ATOM   10405 C  CB    . VAL A 1 2853 ? 250.176 194.217 192.441 1.00 45.99  ? 2853 VAL A CB    1 
ATOM   10406 C  CG1   . VAL A 1 2853 ? 249.863 192.875 193.070 1.00 48.19  ? 2853 VAL A CG1   1 
ATOM   10407 C  CG2   . VAL A 1 2853 ? 250.576 195.197 193.490 1.00 47.36  ? 2853 VAL A CG2   1 
ATOM   10408 N  N     . ALA A 1 2854 ? 250.192 193.192 189.437 1.00 48.74  ? 2854 ALA A N     1 
ATOM   10409 C  CA    . ALA A 1 2854 ? 249.863 192.137 188.488 1.00 46.59  ? 2854 ALA A CA    1 
ATOM   10410 C  C     . ALA A 1 2854 ? 251.101 191.665 187.741 1.00 52.10  ? 2854 ALA A C     1 
ATOM   10411 O  O     . ALA A 1 2854 ? 251.264 190.465 187.501 1.00 55.11  ? 2854 ALA A O     1 
ATOM   10412 C  CB    . ALA A 1 2854 ? 248.793 192.620 187.513 1.00 51.38  ? 2854 ALA A CB    1 
ATOM   10413 N  N     . LEU A 1 2855 ? 251.988 192.589 187.366 1.00 55.62  ? 2855 LEU A N     1 
ATOM   10414 C  CA    . LEU A 1 2855 ? 253.203 192.161 186.676 1.00 53.80  ? 2855 LEU A CA    1 
ATOM   10415 C  C     . LEU A 1 2855 ? 254.255 191.622 187.640 1.00 55.21  ? 2855 LEU A C     1 
ATOM   10416 O  O     . LEU A 1 2855 ? 255.133 190.859 187.225 1.00 64.51  ? 2855 LEU A O     1 
ATOM   10417 C  CB    . LEU A 1 2855 ? 253.773 193.302 185.835 1.00 55.66  ? 2855 LEU A CB    1 
ATOM   10418 C  CG    . LEU A 1 2855 ? 253.153 193.491 184.446 1.00 63.70  ? 2855 LEU A CG    1 
ATOM   10419 C  CD1   . LEU A 1 2855 ? 253.432 192.266 183.592 1.00 60.54  ? 2855 LEU A CD1   1 
ATOM   10420 C  CD2   . LEU A 1 2855 ? 251.655 193.774 184.492 1.00 64.57  ? 2855 LEU A CD2   1 
ATOM   10421 N  N     . LYS A 1 2856 ? 254.197 192.006 188.917 1.00 49.15  ? 2856 LYS A N     1 
ATOM   10422 C  CA    . LYS A 1 2856 ? 255.137 191.455 189.886 1.00 48.08  ? 2856 LYS A CA    1 
ATOM   10423 C  C     . LYS A 1 2856 ? 254.835 189.993 190.183 1.00 47.93  ? 2856 LYS A C     1 
ATOM   10424 O  O     . LYS A 1 2856 ? 255.741 189.152 190.169 1.00 54.06  ? 2856 LYS A O     1 
ATOM   10425 C  CB    . LYS A 1 2856 ? 255.108 192.276 191.175 1.00 48.23  ? 2856 LYS A CB    1 
ATOM   10426 C  CG    . LYS A 1 2856 ? 255.742 191.576 192.363 1.00 49.01  ? 2856 LYS A CG    1 
ATOM   10427 C  CD    . LYS A 1 2856 ? 255.636 192.415 193.624 1.00 53.17  ? 2856 LYS A CD    1 
ATOM   10428 C  CE    . LYS A 1 2856 ? 256.229 191.686 194.819 1.00 56.13  ? 2856 LYS A CE    1 
ATOM   10429 N  NZ    . LYS A 1 2856 ? 256.058 192.455 196.082 1.00 52.69  ? 2856 LYS A NZ    1 
ATOM   10430 N  N     . HIS A 1 2857 ? 253.572 189.668 190.450 1.00 50.68  ? 2857 HIS A N     1 
ATOM   10431 C  CA    . HIS A 1 2857 ? 253.215 188.298 190.797 1.00 48.07  ? 2857 HIS A CA    1 
ATOM   10432 C  C     . HIS A 1 2857 ? 252.929 187.425 189.585 1.00 53.30  ? 2857 HIS A C     1 
ATOM   10433 O  O     . HIS A 1 2857 ? 252.890 186.197 189.721 1.00 51.04  ? 2857 HIS A O     1 
ATOM   10434 C  CB    . HIS A 1 2857 ? 252.005 188.290 191.732 1.00 40.76  ? 2857 HIS A CB    1 
ATOM   10435 C  CG    . HIS A 1 2857 ? 252.298 188.823 193.098 1.00 44.11  ? 2857 HIS A CG    1 
ATOM   10436 N  ND1   . HIS A 1 2857 ? 252.949 188.083 194.061 1.00 50.55  ? 2857 HIS A ND1   1 
ATOM   10437 C  CD2   . HIS A 1 2857 ? 252.041 190.027 193.659 1.00 48.05  ? 2857 HIS A CD2   1 
ATOM   10438 C  CE1   . HIS A 1 2857 ? 253.073 188.806 195.159 1.00 52.51  ? 2857 HIS A CE1   1 
ATOM   10439 N  NE2   . HIS A 1 2857 ? 252.529 189.989 194.942 1.00 48.33  ? 2857 HIS A NE2   1 
ATOM   10440 N  N     . PHE A 1 2858 ? 252.735 188.021 188.410 1.00 58.37  ? 2858 PHE A N     1 
ATOM   10441 C  CA    . PHE A 1 2858 ? 252.510 187.287 187.166 1.00 56.49  ? 2858 PHE A CA    1 
ATOM   10442 C  C     . PHE A 1 2858 ? 253.477 187.836 186.127 1.00 59.35  ? 2858 PHE A C     1 
ATOM   10443 O  O     . PHE A 1 2858 ? 253.102 188.666 185.289 1.00 61.84  ? 2858 PHE A O     1 
ATOM   10444 C  CB    . PHE A 1 2858 ? 251.061 187.412 186.697 1.00 50.82  ? 2858 PHE A CB    1 
ATOM   10445 C  CG    . PHE A 1 2858 ? 250.063 186.813 187.643 1.00 52.48  ? 2858 PHE A CG    1 
ATOM   10446 C  CD1   . PHE A 1 2858 ? 249.686 185.488 187.527 1.00 52.12  ? 2858 PHE A CD1   1 
ATOM   10447 C  CD2   . PHE A 1 2858 ? 249.497 187.580 188.646 1.00 50.28  ? 2858 PHE A CD2   1 
ATOM   10448 C  CE1   . PHE A 1 2858 ? 248.767 184.938 188.397 1.00 51.92  ? 2858 PHE A CE1   1 
ATOM   10449 C  CE2   . PHE A 1 2858 ? 248.577 187.036 189.517 1.00 50.13  ? 2858 PHE A CE2   1 
ATOM   10450 C  CZ    . PHE A 1 2858 ? 248.212 185.713 189.392 1.00 52.05  ? 2858 PHE A CZ    1 
ATOM   10451 N  N     . PRO A 1 2859 ? 254.738 187.399 186.156 1.00 65.50  ? 2859 PRO A N     1 
ATOM   10452 C  CA    . PRO A 1 2859 ? 255.725 187.998 185.243 1.00 65.68  ? 2859 PRO A CA    1 
ATOM   10453 C  C     . PRO A 1 2859 ? 255.526 187.600 183.793 1.00 69.78  ? 2859 PRO A C     1 
ATOM   10454 O  O     . PRO A 1 2859 ? 255.640 188.451 182.902 1.00 67.48  ? 2859 PRO A O     1 
ATOM   10455 C  CB    . PRO A 1 2859 ? 257.068 187.491 185.794 1.00 66.71  ? 2859 PRO A CB    1 
ATOM   10456 C  CG    . PRO A 1 2859 ? 256.755 186.877 187.137 1.00 66.83  ? 2859 PRO A CG    1 
ATOM   10457 C  CD    . PRO A 1 2859 ? 255.348 186.398 187.041 1.00 63.10  ? 2859 PRO A CD    1 
ATOM   10458 N  N     . ASN A 1 2860 ? 255.229 186.331 183.525 1.00 75.04  ? 2860 ASN A N     1 
ATOM   10459 C  CA    . ASN A 1 2860 ? 255.160 185.828 182.155 1.00 72.65  ? 2860 ASN A CA    1 
ATOM   10460 C  C     . ASN A 1 2860 ? 253.715 185.843 181.659 1.00 78.28  ? 2860 ASN A C     1 
ATOM   10461 O  O     . ASN A 1 2860 ? 253.105 184.813 181.371 1.00 80.90  ? 2860 ASN A O     1 
ATOM   10462 C  CB    . ASN A 1 2860 ? 255.767 184.431 182.077 1.00 73.61  ? 2860 ASN A CB    1 
ATOM   10463 C  CG    . ASN A 1 2860 ? 256.967 184.270 182.984 1.00 76.82  ? 2860 ASN A CG    1 
ATOM   10464 O  OD1   . ASN A 1 2860 ? 257.918 185.047 182.917 1.00 74.89  ? 2860 ASN A OD1   1 
ATOM   10465 N  ND2   . ASN A 1 2860 ? 256.928 183.258 183.842 1.00 77.03  ? 2860 ASN A ND2   1 
ATOM   10466 N  N     . ILE A 1 2861 ? 253.170 187.055 181.561 1.00 78.66  ? 2861 ILE A N     1 
ATOM   10467 C  CA    . ILE A 1 2861 ? 251.857 187.280 180.973 1.00 76.05  ? 2861 ILE A CA    1 
ATOM   10468 C  C     . ILE A 1 2861 ? 251.969 188.422 179.975 1.00 76.49  ? 2861 ILE A C     1 
ATOM   10469 O  O     . ILE A 1 2861 ? 252.910 189.218 180.004 1.00 78.40  ? 2861 ILE A O     1 
ATOM   10470 C  CB    . ILE A 1 2861 ? 250.769 187.599 182.022 1.00 74.06  ? 2861 ILE A CB    1 
ATOM   10471 C  CG1   . ILE A 1 2861 ? 251.107 188.893 182.764 1.00 73.73  ? 2861 ILE A CG1   1 
ATOM   10472 C  CG2   . ILE A 1 2861 ? 250.593 186.440 182.988 1.00 72.64  ? 2861 ILE A CG2   1 
ATOM   10473 C  CD1   . ILE A 1 2861 ? 249.964 189.442 183.584 1.00 73.46  ? 2861 ILE A CD1   1 
ATOM   10474 N  N     . ASP A 1 2862 ? 250.987 188.493 179.081 1.00 80.69  ? 2862 ASP A N     1 
ATOM   10475 C  CA    . ASP A 1 2862 ? 250.909 189.581 178.115 1.00 77.69  ? 2862 ASP A CA    1 
ATOM   10476 C  C     . ASP A 1 2862 ? 250.333 190.804 178.817 1.00 79.66  ? 2862 ASP A C     1 
ATOM   10477 O  O     . ASP A 1 2862 ? 249.170 190.800 179.231 1.00 81.65  ? 2862 ASP A O     1 
ATOM   10478 C  CB    . ASP A 1 2862 ? 250.057 189.174 176.917 1.00 75.66  ? 2862 ASP A CB    1 
ATOM   10479 C  CG    . ASP A 1 2862 ? 250.191 190.136 175.757 1.00 82.81  ? 2862 ASP A CG    1 
ATOM   10480 O  OD1   . ASP A 1 2862 ? 251.241 190.804 175.657 1.00 82.61  ? 2862 ASP A OD1   1 
ATOM   10481 O  OD2   . ASP A 1 2862 ? 249.250 190.222 174.940 1.00 87.05  ? 2862 ASP A OD2   1 
ATOM   10482 N  N     . ARG A 1 2863 ? 251.151 191.849 178.958 1.00 75.52  ? 2863 ARG A N     1 
ATOM   10483 C  CA    . ARG A 1 2863 ? 250.715 193.044 179.674 1.00 76.24  ? 2863 ARG A CA    1 
ATOM   10484 C  C     . ARG A 1 2863 ? 249.508 193.687 179.005 1.00 79.05  ? 2863 ARG A C     1 
ATOM   10485 O  O     . ARG A 1 2863 ? 248.549 194.074 179.682 1.00 78.41  ? 2863 ARG A O     1 
ATOM   10486 C  CB    . ARG A 1 2863 ? 251.865 194.047 179.766 1.00 76.00  ? 2863 ARG A CB    1 
ATOM   10487 C  CG    . ARG A 1 2863 ? 251.544 195.297 180.570 1.00 76.62  ? 2863 ARG A CG    1 
ATOM   10488 C  CD    . ARG A 1 2863 ? 252.762 196.200 180.692 1.00 74.65  ? 2863 ARG A CD    1 
ATOM   10489 N  NE    . ARG A 1 2863 ? 252.460 197.448 181.384 1.00 77.90  ? 2863 ARG A NE    1 
ATOM   10490 C  CZ    . ARG A 1 2863 ? 252.498 197.609 182.700 1.00 81.71  ? 2863 ARG A CZ    1 
ATOM   10491 N  NH1   . ARG A 1 2863 ? 252.846 196.623 183.507 1.00 80.18  ? 2863 ARG A NH1   1 
ATOM   10492 N  NH2   . ARG A 1 2863 ? 252.187 198.794 183.217 1.00 76.96  ? 2863 ARG A NH2   1 
ATOM   10493 N  N     . GLU A 1 2864 ? 249.531 193.805 177.677 1.00 81.12  ? 2864 GLU A N     1 
ATOM   10494 C  CA    . GLU A 1 2864 ? 248.477 194.542 176.989 1.00 81.13  ? 2864 GLU A CA    1 
ATOM   10495 C  C     . GLU A 1 2864 ? 247.153 193.786 177.010 1.00 80.19  ? 2864 GLU A C     1 
ATOM   10496 O  O     . GLU A 1 2864 ? 246.092 194.390 177.206 1.00 79.60  ? 2864 GLU A O     1 
ATOM   10497 C  CB    . GLU A 1 2864 ? 248.902 194.843 175.553 1.00 78.86  ? 2864 GLU A CB    1 
ATOM   10498 C  CG    . GLU A 1 2864 ? 247.885 195.651 174.763 1.00 82.58  ? 2864 GLU A CG    1 
ATOM   10499 C  CD    . GLU A 1 2864 ? 247.689 197.050 175.320 1.00 86.46  ? 2864 GLU A CD    1 
ATOM   10500 O  OE1   . GLU A 1 2864 ? 248.622 197.576 175.963 1.00 83.43  ? 2864 GLU A OE1   1 
ATOM   10501 O  OE2   . GLU A 1 2864 ? 246.600 197.624 175.115 1.00 85.16  ? 2864 GLU A OE2   1 
ATOM   10502 N  N     . LYS A 1 2865 ? 247.191 192.468 176.812 1.00 73.20  ? 2865 LYS A N     1 
ATOM   10503 C  CA    . LYS A 1 2865 ? 245.955 191.701 176.715 1.00 72.32  ? 2865 LYS A CA    1 
ATOM   10504 C  C     . LYS A 1 2865 ? 245.260 191.558 178.064 1.00 75.92  ? 2865 LYS A C     1 
ATOM   10505 O  O     . LYS A 1 2865 ? 244.067 191.239 178.107 1.00 75.75  ? 2865 LYS A O     1 
ATOM   10506 C  CB    . LYS A 1 2865 ? 246.252 190.329 176.099 1.00 73.71  ? 2865 LYS A CB    1 
ATOM   10507 C  CG    . LYS A 1 2865 ? 245.042 189.431 175.894 1.00 75.95  ? 2865 LYS A CG    1 
ATOM   10508 C  CD    . LYS A 1 2865 ? 245.413 188.153 175.157 1.00 77.78  ? 2865 LYS A CD    1 
ATOM   10509 C  CE    . LYS A 1 2865 ? 246.192 187.199 176.043 1.00 78.78  ? 2865 LYS A CE    1 
ATOM   10510 N  NZ    . LYS A 1 2865 ? 246.451 185.903 175.358 1.00 75.89  ? 2865 LYS A NZ    1 
ATOM   10511 N  N     . ALA A 1 2866 ? 245.966 191.819 179.164 1.00 72.64  ? 2866 ALA A N     1 
ATOM   10512 C  CA    . ALA A 1 2866 ? 245.380 191.746 180.492 1.00 65.81  ? 2866 ALA A CA    1 
ATOM   10513 C  C     . ALA A 1 2866 ? 245.233 193.097 181.175 1.00 67.09  ? 2866 ALA A C     1 
ATOM   10514 O  O     . ALA A 1 2866 ? 244.415 193.216 182.093 1.00 69.30  ? 2866 ALA A O     1 
ATOM   10515 C  CB    . ALA A 1 2866 ? 246.214 190.824 181.396 1.00 63.81  ? 2866 ALA A CB    1 
ATOM   10516 N  N     . MET A 1 2867 ? 245.986 194.117 180.756 1.00 71.86  ? 2867 MET A N     1 
ATOM   10517 C  CA    . MET A 1 2867 ? 245.964 195.411 181.427 1.00 68.09  ? 2867 MET A CA    1 
ATOM   10518 C  C     . MET A 1 2867 ? 245.498 196.533 180.506 1.00 69.73  ? 2867 MET A C     1 
ATOM   10519 O  O     . MET A 1 2867 ? 245.767 197.704 180.791 1.00 72.64  ? 2867 MET A O     1 
ATOM   10520 C  CB    . MET A 1 2867 ? 247.344 195.747 182.000 1.00 72.16  ? 2867 MET A CB    1 
ATOM   10521 C  CG    . MET A 1 2867 ? 247.708 194.964 183.249 1.00 71.04  ? 2867 MET A CG    1 
ATOM   10522 S  SD    . MET A 1 2867 ? 246.559 195.252 184.601 1.00 83.09  ? 2867 MET A SD    1 
ATOM   10523 C  CE    . MET A 1 2867 ? 246.291 193.577 185.153 1.00 68.72  ? 2867 MET A CE    1 
ATOM   10524 N  N     . SER A 1 2868 ? 244.829 196.205 179.402 1.00 68.88  ? 2868 SER A N     1 
ATOM   10525 C  CA    . SER A 1 2868 ? 244.241 197.213 178.529 1.00 67.28  ? 2868 SER A CA    1 
ATOM   10526 C  C     . SER A 1 2868 ? 243.360 198.155 179.333 1.00 71.92  ? 2868 SER A C     1 
ATOM   10527 O  O     . SER A 1 2868 ? 242.370 197.732 179.935 1.00 75.31  ? 2868 SER A O     1 
ATOM   10528 C  CB    . SER A 1 2868 ? 243.426 196.540 177.424 1.00 70.95  ? 2868 SER A CB    1 
ATOM   10529 O  OG    . SER A 1 2868 ? 244.228 195.647 176.673 1.00 74.43  ? 2868 SER A OG    1 
ATOM   10530 N  N     . ARG A 1 2869 ? 243.718 199.439 179.325 1.00 69.04  ? 2869 ARG A N     1 
ATOM   10531 C  CA    . ARG A 1 2869 ? 243.242 200.378 180.342 1.00 69.29  ? 2869 ARG A CA    1 
ATOM   10532 C  C     . ARG A 1 2869 ? 241.726 200.436 180.485 1.00 76.76  ? 2869 ARG A C     1 
ATOM   10533 O  O     . ARG A 1 2869 ? 241.241 200.392 181.627 1.00 78.40  ? 2869 ARG A O     1 
ATOM   10534 C  CB    . ARG A 1 2869 ? 243.824 201.768 180.056 1.00 72.09  ? 2869 ARG A CB    1 
ATOM   10535 C  CG    . ARG A 1 2869 ? 243.598 202.760 181.178 1.00 73.82  ? 2869 ARG A CG    1 
ATOM   10536 C  CD    . ARG A 1 2869 ? 243.869 202.111 182.525 1.00 71.27  ? 2869 ARG A CD    1 
ATOM   10537 N  NE    . ARG A 1 2869 ? 245.262 201.704 182.683 1.00 78.64  ? 2869 ARG A NE    1 
ATOM   10538 C  CZ    . ARG A 1 2869 ? 246.281 202.541 182.833 1.00 77.49  ? 2869 ARG A CZ    1 
ATOM   10539 N  NH1   . ARG A 1 2869 ? 246.101 203.851 182.878 1.00 72.91  ? 2869 ARG A NH1   1 
ATOM   10540 N  NH2   . ARG A 1 2869 ? 247.511 202.049 182.951 1.00 69.38  ? 2869 ARG A NH2   1 
ATOM   10541 N  N     . PRO A 1 2870 ? 240.924 200.532 179.416 1.00 64.45  ? 2870 PRO A N     1 
ATOM   10542 C  CA    . PRO A 1 2870 ? 239.470 200.485 179.620 1.00 58.04  ? 2870 PRO A CA    1 
ATOM   10543 C  C     . PRO A 1 2870 ? 239.001 199.087 179.984 1.00 59.88  ? 2870 PRO A C     1 
ATOM   10544 O  O     . PRO A 1 2870 ? 238.411 198.390 179.153 1.00 65.17  ? 2870 PRO A O     1 
ATOM   10545 C  CB    . PRO A 1 2870 ? 238.901 200.938 178.267 1.00 55.79  ? 2870 PRO A CB    1 
ATOM   10546 C  CG    . PRO A 1 2870 ? 240.049 201.543 177.533 1.00 62.21  ? 2870 PRO A CG    1 
ATOM   10547 C  CD    . PRO A 1 2870 ? 241.256 200.811 178.010 1.00 60.26  ? 2870 PRO A CD    1 
ATOM   10548 N  N     . ILE A 1 2871 ? 239.263 198.661 181.219 1.00 44.76  ? 2871 ILE A N     1 
ATOM   10549 C  CA    . ILE A 1 2871 ? 238.845 197.340 181.684 1.00 46.35  ? 2871 ILE A CA    1 
ATOM   10550 C  C     . ILE A 1 2871 ? 237.344 197.413 181.945 1.00 45.71  ? 2871 ILE A C     1 
ATOM   10551 O  O     . ILE A 1 2871 ? 236.905 197.905 182.985 1.00 43.04  ? 2871 ILE A O     1 
ATOM   10552 C  CB    . ILE A 1 2871 ? 239.613 196.894 182.930 1.00 42.62  ? 2871 ILE A CB    1 
ATOM   10553 C  CG1   . ILE A 1 2871 ? 241.104 197.176 182.776 1.00 42.20  ? 2871 ILE A CG1   1 
ATOM   10554 C  CG2   . ILE A 1 2871 ? 239.398 195.417 183.179 1.00 47.59  ? 2871 ILE A CG2   1 
ATOM   10555 C  CD1   . ILE A 1 2871 ? 241.924 196.747 183.964 1.00 46.31  ? 2871 ILE A CD1   1 
ATOM   10556 N  N     . LEU A 1 2872 ? 236.552 196.920 180.999 1.00 39.87  ? 2872 LEU A N     1 
ATOM   10557 C  CA    . LEU A 1 2872 ? 235.101 196.972 181.075 1.00 40.17  ? 2872 LEU A CA    1 
ATOM   10558 C  C     . LEU A 1 2872 ? 234.544 195.562 180.985 1.00 39.05  ? 2872 LEU A C     1 
ATOM   10559 O  O     . LEU A 1 2872 ? 234.936 194.793 180.103 1.00 46.91  ? 2872 LEU A O     1 
ATOM   10560 C  CB    . LEU A 1 2872 ? 234.526 197.842 179.955 1.00 49.26  ? 2872 LEU A CB    1 
ATOM   10561 C  CG    . LEU A 1 2872 ? 234.938 199.314 179.966 1.00 44.36  ? 2872 LEU A CG    1 
ATOM   10562 C  CD1   . LEU A 1 2872 ? 234.246 200.075 178.856 1.00 39.36  ? 2872 LEU A CD1   1 
ATOM   10563 C  CD2   . LEU A 1 2872 ? 234.622 199.929 181.312 1.00 38.06  ? 2872 LEU A CD2   1 
ATOM   10564 N  N     . TYR A 1 2873 ? 233.642 195.226 181.900 1.00 31.83  ? 2873 TYR A N     1 
ATOM   10565 C  CA    . TYR A 1 2873 ? 232.944 193.950 181.904 1.00 33.43  ? 2873 TYR A CA    1 
ATOM   10566 C  C     . TYR A 1 2873 ? 231.447 194.210 181.949 1.00 39.19  ? 2873 TYR A C     1 
ATOM   10567 O  O     . TYR A 1 2873 ? 230.987 195.096 182.675 1.00 46.08  ? 2873 TYR A O     1 
ATOM   10568 C  CB    . TYR A 1 2873 ? 233.350 193.090 183.104 1.00 38.47  ? 2873 TYR A CB    1 
ATOM   10569 C  CG    . TYR A 1 2873 ? 234.652 192.343 182.941 1.00 33.47  ? 2873 TYR A CG    1 
ATOM   10570 C  CD1   . TYR A 1 2873 ? 235.859 193.019 182.862 1.00 34.97  ? 2873 TYR A CD1   1 
ATOM   10571 C  CD2   . TYR A 1 2873 ? 234.672 190.960 182.874 1.00 29.41  ? 2873 TYR A CD2   1 
ATOM   10572 C  CE1   . TYR A 1 2873 ? 237.048 192.339 182.718 1.00 28.18  ? 2873 TYR A CE1   1 
ATOM   10573 C  CE2   . TYR A 1 2873 ? 235.854 190.274 182.731 1.00 40.04  ? 2873 TYR A CE2   1 
ATOM   10574 C  CZ    . TYR A 1 2873 ? 237.038 190.966 182.652 1.00 40.23  ? 2873 TYR A CZ    1 
ATOM   10575 O  OH    . TYR A 1 2873 ? 238.219 190.279 182.505 1.00 44.30  ? 2873 TYR A OH    1 
ATOM   10576 N  N     . SER A 1 2874 ? 230.687 193.435 181.179 1.00 41.40  ? 2874 SER A N     1 
ATOM   10577 C  CA    . SER A 1 2874 ? 229.247 193.633 181.130 1.00 41.83  ? 2874 SER A CA    1 
ATOM   10578 C  C     . SER A 1 2874 ? 228.574 192.376 180.605 1.00 41.44  ? 2874 SER A C     1 
ATOM   10579 O  O     . SER A 1 2874 ? 229.101 191.707 179.715 1.00 48.22  ? 2874 SER A O     1 
ATOM   10580 C  CB    . SER A 1 2874 ? 228.884 194.831 180.247 1.00 45.90  ? 2874 SER A CB    1 
ATOM   10581 O  OG    . SER A 1 2874 ? 227.489 195.070 180.266 1.00 48.34  ? 2874 SER A OG    1 
ATOM   10582 N  N     . ASN A 1 2875 ? 227.405 192.066 181.165 1.00 45.08  ? 2875 ASN A N     1 
ATOM   10583 C  CA    . ASN A 1 2875 ? 226.562 190.977 180.690 1.00 47.48  ? 2875 ASN A CA    1 
ATOM   10584 C  C     . ASN A 1 2875 ? 225.403 191.484 179.842 1.00 53.53  ? 2875 ASN A C     1 
ATOM   10585 O  O     . ASN A 1 2875 ? 224.367 190.819 179.741 1.00 54.69  ? 2875 ASN A O     1 
ATOM   10586 C  CB    . ASN A 1 2875 ? 226.038 190.152 181.865 1.00 44.67  ? 2875 ASN A CB    1 
ATOM   10587 C  CG    . ASN A 1 2875 ? 225.169 190.961 182.804 1.00 51.26  ? 2875 ASN A CG    1 
ATOM   10588 O  OD1   . ASN A 1 2875 ? 225.105 192.185 182.713 1.00 53.05  ? 2875 ASN A OD1   1 
ATOM   10589 N  ND2   . ASN A 1 2875 ? 224.487 190.275 183.712 1.00 55.39  ? 2875 ASN A ND2   1 
ATOM   10590 N  N     . TRP A 1 2876 ? 225.555 192.664 179.245 1.00 53.08  ? 2876 TRP A N     1 
ATOM   10591 C  CA    . TRP A 1 2876 ? 224.494 193.273 178.454 1.00 44.87  ? 2876 TRP A CA    1 
ATOM   10592 C  C     . TRP A 1 2876 ? 224.521 192.802 177.008 1.00 50.36  ? 2876 TRP A C     1 
ATOM   10593 O  O     . TRP A 1 2876 ? 223.470 192.498 176.434 1.00 59.24  ? 2876 TRP A O     1 
ATOM   10594 C  CB    . TRP A 1 2876 ? 224.618 194.796 178.503 1.00 46.14  ? 2876 TRP A CB    1 
ATOM   10595 C  CG    . TRP A 1 2876 ? 224.056 195.399 179.745 1.00 50.88  ? 2876 TRP A CG    1 
ATOM   10596 C  CD1   . TRP A 1 2876 ? 223.205 194.809 180.629 1.00 47.37  ? 2876 TRP A CD1   1 
ATOM   10597 C  CD2   . TRP A 1 2876 ? 224.310 196.714 180.250 1.00 47.94  ? 2876 TRP A CD2   1 
ATOM   10598 N  NE1   . TRP A 1 2876 ? 222.912 195.673 181.654 1.00 44.91  ? 2876 TRP A NE1   1 
ATOM   10599 C  CE2   . TRP A 1 2876 ? 223.578 196.851 181.443 1.00 43.55  ? 2876 TRP A CE2   1 
ATOM   10600 C  CE3   . TRP A 1 2876 ? 225.085 197.789 179.807 1.00 48.20  ? 2876 TRP A CE3   1 
ATOM   10601 C  CZ2   . TRP A 1 2876 ? 223.602 198.017 182.202 1.00 42.68  ? 2876 TRP A CZ2   1 
ATOM   10602 C  CZ3   . TRP A 1 2876 ? 225.102 198.946 180.558 1.00 50.13  ? 2876 TRP A CZ3   1 
ATOM   10603 C  CH2   . TRP A 1 2876 ? 224.364 199.053 181.740 1.00 43.91  ? 2876 TRP A CH2   1 
ATOM   10604 N  N     . LEU A 1 2877 ? 225.709 192.739 176.409 1.00 57.02  ? 2877 LEU A N     1 
ATOM   10605 C  CA    . LEU A 1 2877 ? 225.828 192.300 175.024 1.00 59.40  ? 2877 LEU A CA    1 
ATOM   10606 C  C     . LEU A 1 2877 ? 225.697 190.787 174.901 1.00 59.91  ? 2877 LEU A C     1 
ATOM   10607 O  O     . LEU A 1 2877 ? 225.125 190.289 173.925 1.00 63.14  ? 2877 LEU A O     1 
ATOM   10608 C  CB    . LEU A 1 2877 ? 227.159 192.772 174.441 1.00 53.44  ? 2877 LEU A CB    1 
ATOM   10609 C  CG    . LEU A 1 2877 ? 227.177 194.144 173.763 1.00 55.62  ? 2877 LEU A CG    1 
ATOM   10610 C  CD1   . LEU A 1 2877 ? 226.835 195.250 174.745 1.00 55.07  ? 2877 LEU A CD1   1 
ATOM   10611 C  CD2   . LEU A 1 2877 ? 228.533 194.399 173.135 1.00 58.97  ? 2877 LEU A CD2   1 
ATOM   10612 N  N     . SER A 1 2878 ? 226.213 190.045 175.873 1.00 59.80  ? 2878 SER A N     1 
ATOM   10613 C  CA    . SER A 1 2878 ? 226.198 188.589 175.859 1.00 60.90  ? 2878 SER A CA    1 
ATOM   10614 C  C     . SER A 1 2878 ? 225.457 188.067 177.085 1.00 63.10  ? 2878 SER A C     1 
ATOM   10615 O  O     . SER A 1 2878 ? 224.971 188.830 177.921 1.00 65.48  ? 2878 SER A O     1 
ATOM   10616 C  CB    . SER A 1 2878 ? 227.621 188.031 175.813 1.00 63.64  ? 2878 SER A CB    1 
ATOM   10617 O  OG    . SER A 1 2878 ? 228.264 188.211 177.060 1.00 64.81  ? 2878 SER A OG    1 
ATOM   10618 N  N     . LYS A 1 2879 ? 225.369 186.739 177.178 1.00 66.72  ? 2879 LYS A N     1 
ATOM   10619 C  CA    . LYS A 1 2879 ? 224.721 186.112 178.325 1.00 67.09  ? 2879 LYS A CA    1 
ATOM   10620 C  C     . LYS A 1 2879 ? 225.622 186.113 179.555 1.00 65.32  ? 2879 LYS A C     1 
ATOM   10621 O  O     . LYS A 1 2879 ? 225.128 186.171 180.687 1.00 60.85  ? 2879 LYS A O     1 
ATOM   10622 C  CB    . LYS A 1 2879 ? 224.299 184.685 177.969 1.00 63.82  ? 2879 LYS A CB    1 
ATOM   10623 C  CG    . LYS A 1 2879 ? 225.458 183.729 177.737 1.00 64.07  ? 2879 LYS A CG    1 
ATOM   10624 C  CD    . LYS A 1 2879 ? 224.971 182.339 177.367 1.00 69.51  ? 2879 LYS A CD    1 
ATOM   10625 C  CE    . LYS A 1 2879 ? 226.138 181.403 177.096 1.00 68.51  ? 2879 LYS A CE    1 
ATOM   10626 N  NZ    . LYS A 1 2879 ? 226.931 181.136 178.327 1.00 67.19  ? 2879 LYS A NZ    1 
ATOM   10627 N  N     . ASP A 1 2880 ? 226.935 186.053 179.358 1.00 62.03  ? 2880 ASP A N     1 
ATOM   10628 C  CA    . ASP A 1 2880 ? 227.881 185.940 180.456 1.00 59.75  ? 2880 ASP A CA    1 
ATOM   10629 C  C     . ASP A 1 2880 ? 228.460 187.304 180.818 1.00 61.76  ? 2880 ASP A C     1 
ATOM   10630 O  O     . ASP A 1 2880 ? 228.251 188.305 180.132 1.00 64.88  ? 2880 ASP A O     1 
ATOM   10631 C  CB    . ASP A 1 2880 ? 229.003 184.968 180.093 1.00 60.08  ? 2880 ASP A CB    1 
ATOM   10632 C  CG    . ASP A 1 2880 ? 228.542 183.527 180.076 1.00 65.83  ? 2880 ASP A CG    1 
ATOM   10633 O  OD1   . ASP A 1 2880 ? 227.447 183.245 180.605 1.00 68.04  ? 2880 ASP A OD1   1 
ATOM   10634 O  OD2   . ASP A 1 2880 ? 229.272 182.675 179.529 1.00 62.21  ? 2880 ASP A OD2   1 
ATOM   10635 N  N     . TYR A 1 2881 ? 229.210 187.328 181.918 1.00 50.76  ? 2881 TYR A N     1 
ATOM   10636 C  CA    . TYR A 1 2881 ? 229.884 188.541 182.381 1.00 42.74  ? 2881 TYR A CA    1 
ATOM   10637 C  C     . TYR A 1 2881 ? 231.290 188.624 181.785 1.00 44.18  ? 2881 TYR A C     1 
ATOM   10638 O  O     . TYR A 1 2881 ? 232.300 188.680 182.484 1.00 51.69  ? 2881 TYR A O     1 
ATOM   10639 C  CB    . TYR A 1 2881 ? 229.924 188.568 183.903 1.00 41.45  ? 2881 TYR A CB    1 
ATOM   10640 C  CG    . TYR A 1 2881 ? 230.264 189.913 184.492 1.00 42.06  ? 2881 TYR A CG    1 
ATOM   10641 C  CD1   . TYR A 1 2881 ? 229.397 190.986 184.365 1.00 44.44  ? 2881 TYR A CD1   1 
ATOM   10642 C  CD2   . TYR A 1 2881 ? 231.448 190.108 185.185 1.00 41.79  ? 2881 TYR A CD2   1 
ATOM   10643 C  CE1   . TYR A 1 2881 ? 229.702 192.215 184.907 1.00 41.54  ? 2881 TYR A CE1   1 
ATOM   10644 C  CE2   . TYR A 1 2881 ? 231.761 191.333 185.729 1.00 43.16  ? 2881 TYR A CE2   1 
ATOM   10645 C  CZ    . TYR A 1 2881 ? 230.886 192.383 185.586 1.00 44.68  ? 2881 TYR A CZ    1 
ATOM   10646 O  OH    . TYR A 1 2881 ? 231.197 193.606 186.128 1.00 49.24  ? 2881 TYR A OH    1 
ATOM   10647 N  N     . ILE A 1 2882 ? 231.334 188.619 180.458 1.00 39.78  ? 2882 ILE A N     1 
ATOM   10648 C  CA    . ILE A 1 2882 ? 232.590 188.672 179.716 1.00 42.40  ? 2882 ILE A CA    1 
ATOM   10649 C  C     . ILE A 1 2882 ? 233.003 190.131 179.572 1.00 40.77  ? 2882 ILE A C     1 
ATOM   10650 O  O     . ILE A 1 2882 ? 232.159 191.025 179.729 1.00 37.71  ? 2882 ILE A O     1 
ATOM   10651 C  CB    . ILE A 1 2882 ? 232.452 187.991 178.347 1.00 47.17  ? 2882 ILE A CB    1 
ATOM   10652 C  CG1   . ILE A 1 2882 ? 231.333 188.646 177.541 1.00 45.07  ? 2882 ILE A CG1   1 
ATOM   10653 C  CG2   . ILE A 1 2882 ? 232.176 186.509 178.522 1.00 48.89  ? 2882 ILE A CG2   1 
ATOM   10654 C  CD1   . ILE A 1 2882 ? 231.579 188.654 176.052 1.00 44.52  ? 2882 ILE A CD1   1 
ATOM   10655 N  N     . PRO A 1 2883 ? 234.274 190.427 179.300 1.00 42.31  ? 2883 PRO A N     1 
ATOM   10656 C  CA    . PRO A 1 2883 ? 234.661 191.820 179.058 1.00 41.11  ? 2883 PRO A CA    1 
ATOM   10657 C  C     . PRO A 1 2883 ? 233.961 192.386 177.833 1.00 46.55  ? 2883 PRO A C     1 
ATOM   10658 O  O     . PRO A 1 2883 ? 233.705 191.685 176.853 1.00 54.15  ? 2883 PRO A O     1 
ATOM   10659 C  CB    . PRO A 1 2883 ? 236.178 191.739 178.849 1.00 32.63  ? 2883 PRO A CB    1 
ATOM   10660 C  CG    . PRO A 1 2883 ? 236.447 190.320 178.508 1.00 34.94  ? 2883 PRO A CG    1 
ATOM   10661 C  CD    . PRO A 1 2883 ? 235.438 189.527 179.269 1.00 37.91  ? 2883 PRO A CD    1 
ATOM   10662 N  N     . VAL A 1 2884 ? 233.650 193.676 177.902 1.00 50.82  ? 2884 VAL A N     1 
ATOM   10663 C  CA    . VAL A 1 2884 ? 232.974 194.389 176.826 1.00 45.43  ? 2884 VAL A CA    1 
ATOM   10664 C  C     . VAL A 1 2884 ? 233.887 195.509 176.349 1.00 45.12  ? 2884 VAL A C     1 
ATOM   10665 O  O     . VAL A 1 2884 ? 234.685 196.046 177.124 1.00 50.26  ? 2884 VAL A O     1 
ATOM   10666 C  CB    . VAL A 1 2884 ? 231.603 194.938 177.279 1.00 43.58  ? 2884 VAL A CB    1 
ATOM   10667 C  CG1   . VAL A 1 2884 ? 231.769 196.112 178.229 1.00 37.61  ? 2884 VAL A CG1   1 
ATOM   10668 C  CG2   . VAL A 1 2884 ? 230.754 195.327 176.080 1.00 49.11  ? 2884 VAL A CG2   1 
ATOM   10669 N  N     . ASP A 1 2885 ? 233.796 195.833 175.064 1.00 51.40  ? 2885 ASP A N     1 
ATOM   10670 C  CA    . ASP A 1 2885 ? 234.568 196.937 174.519 1.00 55.22  ? 2885 ASP A CA    1 
ATOM   10671 C  C     . ASP A 1 2885 ? 233.772 198.233 174.611 1.00 56.86  ? 2885 ASP A C     1 
ATOM   10672 O  O     . ASP A 1 2885 ? 232.546 198.226 174.744 1.00 56.10  ? 2885 ASP A O     1 
ATOM   10673 C  CB    . ASP A 1 2885 ? 234.964 196.655 173.071 1.00 53.87  ? 2885 ASP A CB    1 
ATOM   10674 C  CG    . ASP A 1 2885 ? 236.084 197.551 172.590 1.00 62.56  ? 2885 ASP A CG    1 
ATOM   10675 O  OD1   . ASP A 1 2885 ? 236.816 198.096 173.443 1.00 63.69  ? 2885 ASP A OD1   1 
ATOM   10676 O  OD2   . ASP A 1 2885 ? 236.231 197.714 171.361 1.00 58.32  ? 2885 ASP A OD2   1 
ATOM   10677 N  N     . GLN A 1 2886 ? 234.488 199.356 174.541 1.00 54.85  ? 2886 GLN A N     1 
ATOM   10678 C  CA    . GLN A 1 2886 ? 233.866 200.646 174.821 1.00 50.54  ? 2886 GLN A CA    1 
ATOM   10679 C  C     . GLN A 1 2886 ? 232.898 201.064 173.722 1.00 60.42  ? 2886 GLN A C     1 
ATOM   10680 O  O     . GLN A 1 2886 ? 231.819 201.591 174.012 1.00 64.13  ? 2886 GLN A O     1 
ATOM   10681 C  CB    . GLN A 1 2886 ? 234.943 201.709 175.020 1.00 52.20  ? 2886 GLN A CB    1 
ATOM   10682 C  CG    . GLN A 1 2886 ? 234.433 202.983 175.658 1.00 54.34  ? 2886 GLN A CG    1 
ATOM   10683 C  CD    . GLN A 1 2886 ? 235.529 203.756 176.351 1.00 55.43  ? 2886 GLN A CD    1 
ATOM   10684 O  OE1   . GLN A 1 2886 ? 236.523 204.132 175.735 1.00 59.75  ? 2886 GLN A OE1   1 
ATOM   10685 N  NE2   . GLN A 1 2886 ? 235.357 203.994 177.645 1.00 54.51  ? 2886 GLN A NE2   1 
ATOM   10686 N  N     . GLU A 1 2887 ? 233.259 200.845 172.456 1.00 65.30  ? 2887 GLU A N     1 
ATOM   10687 C  CA    . GLU A 1 2887 ? 232.433 201.345 171.359 1.00 58.49  ? 2887 GLU A CA    1 
ATOM   10688 C  C     . GLU A 1 2887 ? 231.134 200.556 171.226 1.00 61.26  ? 2887 GLU A C     1 
ATOM   10689 O  O     . GLU A 1 2887 ? 230.057 201.141 171.057 1.00 64.53  ? 2887 GLU A O     1 
ATOM   10690 C  CB    . GLU A 1 2887 ? 233.224 201.313 170.053 1.00 61.37  ? 2887 GLU A CB    1 
ATOM   10691 C  CG    . GLU A 1 2887 ? 234.440 202.227 170.047 1.00 65.79  ? 2887 GLU A CG    1 
ATOM   10692 C  CD    . GLU A 1 2887 ? 234.112 203.643 170.483 1.00 69.92  ? 2887 GLU A CD    1 
ATOM   10693 O  OE1   . GLU A 1 2887 ? 233.102 204.199 170.002 1.00 70.80  ? 2887 GLU A OE1   1 
ATOM   10694 O  OE2   . GLU A 1 2887 ? 234.867 204.205 171.305 1.00 64.38  ? 2887 GLU A OE2   1 
ATOM   10695 N  N     . GLU A 1 2888 ? 231.213 199.225 171.282 1.00 59.28  ? 2888 GLU A N     1 
ATOM   10696 C  CA    . GLU A 1 2888 ? 229.999 198.415 171.218 1.00 59.07  ? 2888 GLU A CA    1 
ATOM   10697 C  C     . GLU A 1 2888 ? 229.102 198.668 172.421 1.00 63.32  ? 2888 GLU A C     1 
ATOM   10698 O  O     . GLU A 1 2888 ? 227.872 198.717 172.290 1.00 69.48  ? 2888 GLU A O     1 
ATOM   10699 C  CB    . GLU A 1 2888 ? 230.355 196.933 171.104 1.00 58.74  ? 2888 GLU A CB    1 
ATOM   10700 C  CG    . GLU A 1 2888 ? 231.023 196.552 169.789 1.00 64.44  ? 2888 GLU A CG    1 
ATOM   10701 C  CD    . GLU A 1 2888 ? 232.509 196.834 169.775 1.00 71.43  ? 2888 GLU A CD    1 
ATOM   10702 O  OE1   . GLU A 1 2888 ? 233.037 197.274 170.813 1.00 68.57  ? 2888 GLU A OE1   1 
ATOM   10703 O  OE2   . GLU A 1 2888 ? 233.151 196.614 168.726 1.00 71.13  ? 2888 GLU A OE2   1 
ATOM   10704 N  N     . LEU A 1 2889 ? 229.697 198.834 173.603 1.00 52.16  ? 2889 LEU A N     1 
ATOM   10705 C  CA    . LEU A 1 2889 ? 228.906 199.186 174.776 1.00 49.05  ? 2889 LEU A CA    1 
ATOM   10706 C  C     . LEU A 1 2889 ? 228.230 200.537 174.589 1.00 54.27  ? 2889 LEU A C     1 
ATOM   10707 O  O     . LEU A 1 2889 ? 227.066 200.711 174.961 1.00 60.45  ? 2889 LEU A O     1 
ATOM   10708 C  CB    . LEU A 1 2889 ? 229.784 199.189 176.026 1.00 50.75  ? 2889 LEU A CB    1 
ATOM   10709 C  CG    . LEU A 1 2889 ? 229.195 199.861 177.266 1.00 51.40  ? 2889 LEU A CG    1 
ATOM   10710 C  CD1   . LEU A 1 2889 ? 228.085 199.013 177.859 1.00 52.36  ? 2889 LEU A CD1   1 
ATOM   10711 C  CD2   . LEU A 1 2889 ? 230.279 200.130 178.294 1.00 46.94  ? 2889 LEU A CD2   1 
ATOM   10712 N  N     . ARG A 1 2890 ? 228.941 201.504 174.005 1.00 50.41  ? 2890 ARG A N     1 
ATOM   10713 C  CA    . ARG A 1 2890 ? 228.348 202.814 173.759 1.00 49.00  ? 2890 ARG A CA    1 
ATOM   10714 C  C     . ARG A 1 2890 ? 227.176 202.720 172.792 1.00 52.83  ? 2890 ARG A C     1 
ATOM   10715 O  O     . ARG A 1 2890 ? 226.141 203.360 172.999 1.00 58.45  ? 2890 ARG A O     1 
ATOM   10716 C  CB    . ARG A 1 2890 ? 229.406 203.777 173.224 1.00 52.93  ? 2890 ARG A CB    1 
ATOM   10717 C  CG    . ARG A 1 2890 ? 228.998 205.237 173.283 1.00 53.76  ? 2890 ARG A CG    1 
ATOM   10718 C  CD    . ARG A 1 2890 ? 229.889 206.091 172.400 1.00 52.94  ? 2890 ARG A CD    1 
ATOM   10719 N  NE    . ARG A 1 2890 ? 231.303 205.812 172.613 1.00 54.17  ? 2890 ARG A NE    1 
ATOM   10720 C  CZ    . ARG A 1 2890 ? 232.029 206.330 173.594 1.00 57.19  ? 2890 ARG A CZ    1 
ATOM   10721 N  NH1   . ARG A 1 2890 ? 231.504 207.162 174.477 1.00 56.79  ? 2890 ARG A NH1   1 
ATOM   10722 N  NH2   . ARG A 1 2890 ? 233.315 206.005 173.690 1.00 52.24  ? 2890 ARG A NH2   1 
ATOM   10723 N  N     . ASP A 1 2891 ? 227.320 201.932 171.725 1.00 51.92  ? 2891 ASP A N     1 
ATOM   10724 C  CA    . ASP A 1 2891 ? 226.219 201.766 170.778 1.00 52.05  ? 2891 ASP A CA    1 
ATOM   10725 C  C     . ASP A 1 2891 ? 225.018 201.096 171.436 1.00 56.05  ? 2891 ASP A C     1 
ATOM   10726 O  O     . ASP A 1 2891 ? 223.866 201.507 171.221 1.00 60.42  ? 2891 ASP A O     1 
ATOM   10727 C  CB    . ASP A 1 2891 ? 226.683 200.960 169.566 1.00 56.39  ? 2891 ASP A CB    1 
ATOM   10728 C  CG    . ASP A 1 2891 ? 227.950 201.513 168.947 1.00 62.51  ? 2891 ASP A CG    1 
ATOM   10729 O  OD1   . ASP A 1 2891 ? 228.160 202.742 169.011 1.00 60.34  ? 2891 ASP A OD1   1 
ATOM   10730 O  OD2   . ASP A 1 2891 ? 228.736 200.718 168.393 1.00 63.67  ? 2891 ASP A OD2   1 
ATOM   10731 N  N     . TYR A 1 2892 ? 225.265 200.057 172.238 1.00 50.96  ? 2892 TYR A N     1 
ATOM   10732 C  CA    . TYR A 1 2892 ? 224.172 199.389 172.934 1.00 48.60  ? 2892 TYR A CA    1 
ATOM   10733 C  C     . TYR A 1 2892 ? 223.466 200.341 173.888 1.00 49.36  ? 2892 TYR A C     1 
ATOM   10734 O  O     . TYR A 1 2892 ? 222.232 200.359 173.961 1.00 51.64  ? 2892 TYR A O     1 
ATOM   10735 C  CB    . TYR A 1 2892 ? 224.696 198.167 173.687 1.00 48.49  ? 2892 TYR A CB    1 
ATOM   10736 C  CG    . TYR A 1 2892 ? 223.643 197.459 174.509 1.00 53.85  ? 2892 TYR A CG    1 
ATOM   10737 C  CD1   . TYR A 1 2892 ? 222.746 196.586 173.915 1.00 53.89  ? 2892 TYR A CD1   1 
ATOM   10738 C  CD2   . TYR A 1 2892 ? 223.545 197.667 175.877 1.00 50.26  ? 2892 TYR A CD2   1 
ATOM   10739 C  CE1   . TYR A 1 2892 ? 221.783 195.939 174.658 1.00 52.45  ? 2892 TYR A CE1   1 
ATOM   10740 C  CE2   . TYR A 1 2892 ? 222.584 197.025 176.628 1.00 49.44  ? 2892 TYR A CE2   1 
ATOM   10741 C  CZ    . TYR A 1 2892 ? 221.707 196.162 176.014 1.00 52.99  ? 2892 TYR A CZ    1 
ATOM   10742 O  OH    . TYR A 1 2892 ? 220.747 195.519 176.759 1.00 53.80  ? 2892 TYR A OH    1 
ATOM   10743 N  N     . VAL A 1 2893 ? 224.234 201.145 174.626 1.00 45.33  ? 2893 VAL A N     1 
ATOM   10744 C  CA    . VAL A 1 2893 ? 223.640 202.095 175.559 1.00 47.54  ? 2893 VAL A CA    1 
ATOM   10745 C  C     . VAL A 1 2893 ? 222.868 203.171 174.808 1.00 56.82  ? 2893 VAL A C     1 
ATOM   10746 O  O     . VAL A 1 2893 ? 221.833 203.644 175.278 1.00 58.60  ? 2893 VAL A O     1 
ATOM   10747 C  CB    . VAL A 1 2893 ? 224.720 202.694 176.479 1.00 50.60  ? 2893 VAL A CB    1 
ATOM   10748 C  CG1   . VAL A 1 2893 ? 224.134 203.792 177.348 1.00 47.01  ? 2893 VAL A CG1   1 
ATOM   10749 C  CG2   . VAL A 1 2893 ? 225.320 201.615 177.357 1.00 53.62  ? 2893 VAL A CG2   1 
ATOM   10750 N  N     . LYS A 1 2894 ? 223.349 203.572 173.628 1.00 54.61  ? 2894 LYS A N     1 
ATOM   10751 C  CA    . LYS A 1 2894 ? 222.611 204.543 172.823 1.00 43.19  ? 2894 LYS A CA    1 
ATOM   10752 C  C     . LYS A 1 2894 ? 221.256 203.992 172.393 1.00 47.26  ? 2894 LYS A C     1 
ATOM   10753 O  O     . LYS A 1 2894 ? 220.232 204.681 172.499 1.00 55.77  ? 2894 LYS A O     1 
ATOM   10754 C  CB    . LYS A 1 2894 ? 223.434 204.939 171.598 1.00 46.55  ? 2894 LYS A CB    1 
ATOM   10755 C  CG    . LYS A 1 2894 ? 224.358 206.119 171.821 1.00 50.47  ? 2894 LYS A CG    1 
ATOM   10756 C  CD    . LYS A 1 2894 ? 225.366 206.242 170.692 1.00 56.76  ? 2894 LYS A CD    1 
ATOM   10757 C  CE    . LYS A 1 2894 ? 226.329 207.391 170.933 1.00 59.04  ? 2894 LYS A CE    1 
ATOM   10758 N  NZ    . LYS A 1 2894 ? 227.487 207.348 169.999 1.00 55.27  ? 2894 LYS A NZ    1 
ATOM   10759 N  N     . ALA A 1 2895 ? 221.231 202.752 171.898 1.00 42.83  ? 2895 ALA A N     1 
ATOM   10760 C  CA    . ALA A 1 2895 ? 219.957 202.152 171.507 1.00 43.41  ? 2895 ALA A CA    1 
ATOM   10761 C  C     . ALA A 1 2895 ? 219.025 202.004 172.705 1.00 47.08  ? 2895 ALA A C     1 
ATOM   10762 O  O     . ALA A 1 2895 ? 217.828 202.332 172.627 1.00 52.84  ? 2895 ALA A O     1 
ATOM   10763 C  CB    . ALA A 1 2895 ? 220.197 200.798 170.842 1.00 45.33  ? 2895 ALA A CB    1 
ATOM   10764 N  N     . ARG A 1 2896 ? 219.558 201.522 173.830 1.00 44.48  ? 2896 ARG A N     1 
ATOM   10765 C  CA    . ARG A 1 2896 ? 218.736 201.371 175.021 1.00 41.20  ? 2896 ARG A CA    1 
ATOM   10766 C  C     . ARG A 1 2896 ? 218.257 202.718 175.539 1.00 48.78  ? 2896 ARG A C     1 
ATOM   10767 O  O     . ARG A 1 2896 ? 217.171 202.803 176.110 1.00 55.53  ? 2896 ARG A O     1 
ATOM   10768 C  CB    . ARG A 1 2896 ? 219.504 200.626 176.110 1.00 48.16  ? 2896 ARG A CB    1 
ATOM   10769 C  CG    . ARG A 1 2896 ? 219.889 199.202 175.748 1.00 53.71  ? 2896 ARG A CG    1 
ATOM   10770 C  CD    . ARG A 1 2896 ? 218.808 198.503 174.942 1.00 51.44  ? 2896 ARG A CD    1 
ATOM   10771 N  NE    . ARG A 1 2896 ? 217.637 198.174 175.743 1.00 51.57  ? 2896 ARG A NE    1 
ATOM   10772 C  CZ    . ARG A 1 2896 ? 216.440 197.915 175.237 1.00 53.10  ? 2896 ARG A CZ    1 
ATOM   10773 N  NH1   . ARG A 1 2896 ? 216.226 197.921 173.931 1.00 47.95  ? 2896 ARG A NH1   1 
ATOM   10774 N  NH2   . ARG A 1 2896 ? 215.432 197.644 176.060 1.00 53.44  ? 2896 ARG A NH2   1 
ATOM   10775 N  N     . LEU A 1 2897 ? 219.034 203.781 175.332 1.00 50.26  ? 2897 LEU A N     1 
ATOM   10776 C  CA    . LEU A 1 2897 ? 218.613 205.111 175.754 1.00 39.62  ? 2897 LEU A CA    1 
ATOM   10777 C  C     . LEU A 1 2897 ? 217.502 205.641 174.863 1.00 44.43  ? 2897 LEU A C     1 
ATOM   10778 O  O     . LEU A 1 2897 ? 216.604 206.340 175.337 1.00 56.25  ? 2897 LEU A O     1 
ATOM   10779 C  CB    . LEU A 1 2897 ? 219.804 206.066 175.744 1.00 44.68  ? 2897 LEU A CB    1 
ATOM   10780 C  CG    . LEU A 1 2897 ? 220.500 206.343 177.074 1.00 45.64  ? 2897 LEU A CG    1 
ATOM   10781 C  CD1   . LEU A 1 2897 ? 221.748 207.163 176.837 1.00 43.93  ? 2897 LEU A CD1   1 
ATOM   10782 C  CD2   . LEU A 1 2897 ? 219.571 207.056 178.034 1.00 43.92  ? 2897 LEU A CD2   1 
ATOM   10783 N  N     . LYS A 1 2898 ? 217.555 205.339 173.565 1.00 45.75  ? 2898 LYS A N     1 
ATOM   10784 C  CA    . LYS A 1 2898 ? 216.433 205.692 172.700 1.00 48.20  ? 2898 LYS A CA    1 
ATOM   10785 C  C     . LYS A 1 2898 ? 215.156 205.001 173.164 1.00 50.51  ? 2898 LYS A C     1 
ATOM   10786 O  O     . LYS A 1 2898 ? 214.099 205.638 173.295 1.00 55.06  ? 2898 LYS A O     1 
ATOM   10787 C  CB    . LYS A 1 2898 ? 216.747 205.326 171.251 1.00 48.00  ? 2898 LYS A CB    1 
ATOM   10788 C  CG    . LYS A 1 2898 ? 217.909 206.101 170.655 1.00 54.68  ? 2898 LYS A CG    1 
ATOM   10789 C  CD    . LYS A 1 2898 ? 218.045 205.835 169.165 1.00 52.98  ? 2898 LYS A CD    1 
ATOM   10790 C  CE    . LYS A 1 2898 ? 219.493 205.937 168.717 1.00 54.31  ? 2898 LYS A CE    1 
ATOM   10791 N  NZ    . LYS A 1 2898 ? 219.930 204.727 167.966 1.00 51.95  ? 2898 LYS A NZ    1 
ATOM   10792 N  N     . VAL A 1 2899 ? 215.247 203.702 173.454 1.00 53.12  ? 2899 VAL A N     1 
ATOM   10793 C  CA    . VAL A 1 2899 ? 214.072 202.995 173.960 1.00 46.88  ? 2899 VAL A CA    1 
ATOM   10794 C  C     . VAL A 1 2899 ? 213.645 203.551 175.318 1.00 49.42  ? 2899 VAL A C     1 
ATOM   10795 O  O     . VAL A 1 2899 ? 212.449 203.616 175.624 1.00 51.30  ? 2899 VAL A O     1 
ATOM   10796 C  CB    . VAL A 1 2899 ? 214.348 201.483 174.022 1.00 49.65  ? 2899 VAL A CB    1 
ATOM   10797 C  CG1   . VAL A 1 2899 ? 213.081 200.733 174.361 1.00 51.56  ? 2899 VAL A CG1   1 
ATOM   10798 C  CG2   . VAL A 1 2899 ? 214.906 201.000 172.698 1.00 52.72  ? 2899 VAL A CG2   1 
ATOM   10799 N  N     . PHE A 1 2900 ? 214.610 203.960 176.144 1.00 53.55  ? 2900 PHE A N     1 
ATOM   10800 C  CA    . PHE A 1 2900 ? 214.320 204.560 177.442 1.00 44.83  ? 2900 PHE A CA    1 
ATOM   10801 C  C     . PHE A 1 2900 ? 213.549 205.862 177.285 1.00 48.93  ? 2900 PHE A C     1 
ATOM   10802 O  O     . PHE A 1 2900 ? 212.601 206.126 178.031 1.00 51.98  ? 2900 PHE A O     1 
ATOM   10803 C  CB    . PHE A 1 2900 ? 215.640 204.792 178.181 1.00 45.55  ? 2900 PHE A CB    1 
ATOM   10804 C  CG    . PHE A 1 2900 ? 215.493 205.393 179.547 1.00 42.28  ? 2900 PHE A CG    1 
ATOM   10805 C  CD1   . PHE A 1 2900 ? 214.820 204.721 180.548 1.00 44.28  ? 2900 PHE A CD1   1 
ATOM   10806 C  CD2   . PHE A 1 2900 ? 216.063 206.619 179.838 1.00 46.43  ? 2900 PHE A CD2   1 
ATOM   10807 C  CE1   . PHE A 1 2900 ? 214.704 205.268 181.808 1.00 42.77  ? 2900 PHE A CE1   1 
ATOM   10808 C  CE2   . PHE A 1 2900 ? 215.945 207.171 181.095 1.00 44.15  ? 2900 PHE A CE2   1 
ATOM   10809 C  CZ    . PHE A 1 2900 ? 215.263 206.495 182.079 1.00 39.53  ? 2900 PHE A CZ    1 
ATOM   10810 N  N     . TYR A 1 2901 ? 213.947 206.690 176.319 1.00 56.64  ? 2901 TYR A N     1 
ATOM   10811 C  CA    . TYR A 1 2901 ? 213.211 207.917 176.035 1.00 55.10  ? 2901 TYR A CA    1 
ATOM   10812 C  C     . TYR A 1 2901 ? 211.795 207.605 175.576 1.00 56.68  ? 2901 TYR A C     1 
ATOM   10813 O  O     . TYR A 1 2901 ? 210.848 208.307 175.947 1.00 47.62  ? 2901 TYR A O     1 
ATOM   10814 C  CB    . TYR A 1 2901 ? 213.933 208.742 174.971 1.00 50.65  ? 2901 TYR A CB    1 
ATOM   10815 C  CG    . TYR A 1 2901 ? 215.364 209.096 175.294 1.00 49.99  ? 2901 TYR A CG    1 
ATOM   10816 C  CD1   . TYR A 1 2901 ? 215.801 209.197 176.606 1.00 52.70  ? 2901 TYR A CD1   1 
ATOM   10817 C  CD2   . TYR A 1 2901 ? 216.279 209.337 174.280 1.00 53.91  ? 2901 TYR A CD2   1 
ATOM   10818 C  CE1   . TYR A 1 2901 ? 217.109 209.518 176.895 1.00 52.50  ? 2901 TYR A CE1   1 
ATOM   10819 C  CE2   . TYR A 1 2901 ? 217.585 209.659 174.560 1.00 49.32  ? 2901 TYR A CE2   1 
ATOM   10820 C  CZ    . TYR A 1 2901 ? 217.996 209.750 175.868 1.00 49.08  ? 2901 TYR A CZ    1 
ATOM   10821 O  OH    . TYR A 1 2901 ? 219.302 210.075 176.144 1.00 55.34  ? 2901 TYR A OH    1 
ATOM   10822 N  N     . GLU A 1 2902 ? 211.635 206.561 174.756 1.00 61.23  ? 2902 GLU A N     1 
ATOM   10823 C  CA    . GLU A 1 2902 ? 210.302 206.230 174.255 1.00 58.39  ? 2902 GLU A CA    1 
ATOM   10824 C  C     . GLU A 1 2902 ? 209.337 205.880 175.386 1.00 59.09  ? 2902 GLU A C     1 
ATOM   10825 O  O     . GLU A 1 2902 ? 208.190 206.340 175.389 1.00 60.42  ? 2902 GLU A O     1 
ATOM   10826 C  CB    . GLU A 1 2902 ? 210.379 205.085 173.245 1.00 56.97  ? 2902 GLU A CB    1 
ATOM   10827 C  CG    . GLU A 1 2902 ? 211.235 205.381 172.028 1.00 59.39  ? 2902 GLU A CG    1 
ATOM   10828 C  CD    . GLU A 1 2902 ? 211.365 204.188 171.101 1.00 65.13  ? 2902 GLU A CD    1 
ATOM   10829 O  OE1   . GLU A 1 2902 ? 210.953 203.077 171.495 1.00 62.31  ? 2902 GLU A OE1   1 
ATOM   10830 O  OE2   . GLU A 1 2902 ? 211.877 204.361 169.975 1.00 59.89  ? 2902 GLU A OE2   1 
ATOM   10831 N  N     . GLU A 1 2903 ? 209.774 205.074 176.356 1.00 61.76  ? 2903 GLU A N     1 
ATOM   10832 C  CA    . GLU A 1 2903 ? 208.879 204.604 177.409 1.00 62.76  ? 2903 GLU A CA    1 
ATOM   10833 C  C     . GLU A 1 2903 ? 209.027 205.349 178.729 1.00 65.54  ? 2903 GLU A C     1 
ATOM   10834 O  O     . GLU A 1 2903 ? 208.073 205.376 179.514 1.00 67.13  ? 2903 GLU A O     1 
ATOM   10835 C  CB    . GLU A 1 2903 ? 209.089 203.108 177.668 1.00 63.43  ? 2903 GLU A CB    1 
ATOM   10836 C  CG    . GLU A 1 2903 ? 209.360 202.278 176.428 1.00 65.37  ? 2903 GLU A CG    1 
ATOM   10837 C  CD    . GLU A 1 2903 ? 209.722 200.844 176.764 1.00 69.92  ? 2903 GLU A CD    1 
ATOM   10838 O  OE1   . GLU A 1 2903 ? 209.262 200.345 177.811 1.00 71.92  ? 2903 GLU A OE1   1 
ATOM   10839 O  OE2   . GLU A 1 2903 ? 210.457 200.212 175.979 1.00 65.54  ? 2903 GLU A OE2   1 
ATOM   10840 N  N     . GLU A 1 2904 ? 210.187 205.943 178.993 1.00 66.87  ? 2904 GLU A N     1 
ATOM   10841 C  CA    . GLU A 1 2904 ? 210.451 206.628 180.253 1.00 60.76  ? 2904 GLU A CA    1 
ATOM   10842 C  C     . GLU A 1 2904 ? 210.928 208.046 179.971 1.00 65.38  ? 2904 GLU A C     1 
ATOM   10843 O  O     . GLU A 1 2904 ? 210.726 208.551 178.862 1.00 71.87  ? 2904 GLU A O     1 
ATOM   10844 C  CB    . GLU A 1 2904 ? 211.480 205.862 181.082 1.00 58.49  ? 2904 GLU A CB    1 
ATOM   10845 C  CG    . GLU A 1 2904 ? 211.104 204.422 181.383 1.00 59.41  ? 2904 GLU A CG    1 
ATOM   10846 C  CD    . GLU A 1 2904 ? 210.280 204.284 182.645 1.00 66.33  ? 2904 GLU A CD    1 
ATOM   10847 O  OE1   . GLU A 1 2904 ? 210.671 204.868 183.676 1.00 66.03  ? 2904 GLU A OE1   1 
ATOM   10848 O  OE2   . GLU A 1 2904 ? 209.246 203.585 182.611 1.00 70.96  ? 2904 GLU A OE2   1 
ATOM   10849 N  N     . LEU A 1 2905 ? 211.519 208.696 180.977 1.00 62.85  ? 2905 LEU A N     1 
ATOM   10850 C  CA    . LEU A 1 2905 ? 212.006 210.071 180.879 1.00 60.64  ? 2905 LEU A CA    1 
ATOM   10851 C  C     . LEU A 1 2905 ? 212.601 210.372 179.511 1.00 58.97  ? 2905 LEU A C     1 
ATOM   10852 O  O     . LEU A 1 2905 ? 213.459 209.639 179.016 1.00 58.60  ? 2905 LEU A O     1 
ATOM   10853 C  CB    . LEU A 1 2905 ? 213.066 210.328 181.954 1.00 58.64  ? 2905 LEU A CB    1 
ATOM   10854 C  CG    . LEU A 1 2905 ? 212.708 210.673 183.400 1.00 62.96  ? 2905 LEU A CG    1 
ATOM   10855 C  CD1   . LEU A 1 2905 ? 211.697 209.714 184.006 1.00 65.33  ? 2905 LEU A CD1   1 
ATOM   10856 C  CD2   . LEU A 1 2905 ? 213.984 210.695 184.217 1.00 63.48  ? 2905 LEU A CD2   1 
ATOM   10857 N  N     . ASP A 1 2906 ? 212.137 211.465 178.905 1.00 56.57  ? 2906 ASP A N     1 
ATOM   10858 C  CA    . ASP A 1 2906 ? 212.556 211.859 177.569 1.00 62.19  ? 2906 ASP A CA    1 
ATOM   10859 C  C     . ASP A 1 2906 ? 213.665 212.903 177.588 1.00 66.23  ? 2906 ASP A C     1 
ATOM   10860 O  O     . ASP A 1 2906 ? 213.822 213.647 176.616 1.00 67.31  ? 2906 ASP A O     1 
ATOM   10861 C  CB    . ASP A 1 2906 ? 211.359 212.378 176.772 1.00 64.19  ? 2906 ASP A CB    1 
ATOM   10862 C  CG    . ASP A 1 2906 ? 211.466 212.069 175.291 1.00 70.80  ? 2906 ASP A CG    1 
ATOM   10863 O  OD1   . ASP A 1 2906 ? 212.598 212.034 174.765 1.00 66.94  ? 2906 ASP A OD1   1 
ATOM   10864 O  OD2   . ASP A 1 2906 ? 210.417 211.855 174.650 1.00 72.26  ? 2906 ASP A OD2   1 
ATOM   10865 N  N     . VAL A 1 2907 ? 214.432 212.979 178.670 1.00 63.74  ? 2907 VAL A N     1 
ATOM   10866 C  CA    . VAL A 1 2907 ? 215.541 213.925 178.744 1.00 58.69  ? 2907 VAL A CA    1 
ATOM   10867 C  C     . VAL A 1 2907 ? 216.727 213.349 177.976 1.00 59.99  ? 2907 VAL A C     1 
ATOM   10868 O  O     . VAL A 1 2907 ? 217.212 212.256 178.302 1.00 64.96  ? 2907 VAL A O     1 
ATOM   10869 C  CB    . VAL A 1 2907 ? 215.892 214.260 180.205 1.00 62.44  ? 2907 VAL A CB    1 
ATOM   10870 C  CG1   . VAL A 1 2907 ? 214.723 214.967 180.868 1.00 57.23  ? 2907 VAL A CG1   1 
ATOM   10871 C  CG2   . VAL A 1 2907 ? 216.234 213.005 180.995 1.00 62.72  ? 2907 VAL A CG2   1 
ATOM   10872 N  N     . PRO A 1 2908 ? 217.201 214.022 176.931 1.00 51.82  ? 2908 PRO A N     1 
ATOM   10873 C  CA    . PRO A 1 2908 ? 218.358 213.506 176.193 1.00 51.63  ? 2908 PRO A CA    1 
ATOM   10874 C  C     . PRO A 1 2908 ? 219.626 213.573 177.026 1.00 51.86  ? 2908 PRO A C     1 
ATOM   10875 O  O     . PRO A 1 2908 ? 219.831 214.494 177.820 1.00 57.40  ? 2908 PRO A O     1 
ATOM   10876 C  CB    . PRO A 1 2908 ? 218.444 214.429 174.971 1.00 51.82  ? 2908 PRO A CB    1 
ATOM   10877 C  CG    . PRO A 1 2908 ? 217.110 215.102 174.890 1.00 51.16  ? 2908 PRO A CG    1 
ATOM   10878 C  CD    . PRO A 1 2908 ? 216.633 215.221 176.298 1.00 52.16  ? 2908 PRO A CD    1 
ATOM   10879 N  N     . LEU A 1 2909 ? 220.490 212.581 176.827 1.00 47.40  ? 2909 LEU A N     1 
ATOM   10880 C  CA    . LEU A 1 2909 ? 221.745 212.480 177.555 1.00 48.62  ? 2909 LEU A CA    1 
ATOM   10881 C  C     . LEU A 1 2909 ? 222.903 212.388 176.576 1.00 53.39  ? 2909 LEU A C     1 
ATOM   10882 O  O     . LEU A 1 2909 ? 222.784 211.770 175.514 1.00 55.42  ? 2909 LEU A O     1 
ATOM   10883 C  CB    . LEU A 1 2909 ? 221.763 211.260 178.483 1.00 46.39  ? 2909 LEU A CB    1 
ATOM   10884 C  CG    . LEU A 1 2909 ? 220.635 211.110 179.503 1.00 48.73  ? 2909 LEU A CG    1 
ATOM   10885 C  CD1   . LEU A 1 2909 ? 220.948 209.975 180.459 1.00 49.00  ? 2909 LEU A CD1   1 
ATOM   10886 C  CD2   . LEU A 1 2909 ? 220.411 212.403 180.264 1.00 50.23  ? 2909 LEU A CD2   1 
ATOM   10887 N  N     . VAL A 1 2910 ? 224.023 213.004 176.940 1.00 51.59  ? 2910 VAL A N     1 
ATOM   10888 C  CA    . VAL A 1 2910 ? 225.261 212.908 176.179 1.00 49.67  ? 2910 VAL A CA    1 
ATOM   10889 C  C     . VAL A 1 2910 ? 226.098 211.794 176.787 1.00 51.78  ? 2910 VAL A C     1 
ATOM   10890 O  O     . VAL A 1 2910 ? 226.314 211.765 178.004 1.00 55.32  ? 2910 VAL A O     1 
ATOM   10891 C  CB    . VAL A 1 2910 ? 226.028 214.241 176.185 1.00 46.39  ? 2910 VAL A CB    1 
ATOM   10892 C  CG1   . VAL A 1 2910 ? 227.179 214.189 175.199 1.00 47.18  ? 2910 VAL A CG1   1 
ATOM   10893 C  CG2   . VAL A 1 2910 ? 225.095 215.391 175.863 1.00 45.58  ? 2910 VAL A CG2   1 
ATOM   10894 N  N     . LEU A 1 2911 ? 226.562 210.875 175.947 1.00 48.42  ? 2911 LEU A N     1 
ATOM   10895 C  CA    . LEU A 1 2911 ? 227.297 209.709 176.414 1.00 48.67  ? 2911 LEU A CA    1 
ATOM   10896 C  C     . LEU A 1 2911 ? 228.794 209.967 176.314 1.00 53.91  ? 2911 LEU A C     1 
ATOM   10897 O  O     . LEU A 1 2911 ? 229.320 210.197 175.221 1.00 63.47  ? 2911 LEU A O     1 
ATOM   10898 C  CB    . LEU A 1 2911 ? 226.919 208.469 175.607 1.00 47.98  ? 2911 LEU A CB    1 
ATOM   10899 C  CG    . LEU A 1 2911 ? 225.532 207.884 175.862 1.00 50.43  ? 2911 LEU A CG    1 
ATOM   10900 C  CD1   . LEU A 1 2911 ? 225.430 206.503 175.249 1.00 46.83  ? 2911 LEU A CD1   1 
ATOM   10901 C  CD2   . LEU A 1 2911 ? 225.245 207.834 177.346 1.00 50.43  ? 2911 LEU A CD2   1 
ATOM   10902 N  N     . PHE A 1 2912 ? 229.472 209.928 177.455 1.00 42.00  ? 2912 PHE A N     1 
ATOM   10903 C  CA    . PHE A 1 2912 ? 230.922 209.946 177.516 1.00 39.99  ? 2912 PHE A CA    1 
ATOM   10904 C  C     . PHE A 1 2912 ? 231.378 208.765 178.360 1.00 49.99  ? 2912 PHE A C     1 
ATOM   10905 O  O     . PHE A 1 2912 ? 230.582 208.136 179.061 1.00 56.65  ? 2912 PHE A O     1 
ATOM   10906 C  CB    . PHE A 1 2912 ? 231.453 211.284 178.058 1.00 35.06  ? 2912 PHE A CB    1 
ATOM   10907 C  CG    . PHE A 1 2912 ? 230.762 211.767 179.303 1.00 41.66  ? 2912 PHE A CG    1 
ATOM   10908 C  CD1   . PHE A 1 2912 ? 229.590 212.498 179.219 1.00 40.81  ? 2912 PHE A CD1   1 
ATOM   10909 C  CD2   . PHE A 1 2912 ? 231.302 211.527 180.552 1.00 49.67  ? 2912 PHE A CD2   1 
ATOM   10910 C  CE1   . PHE A 1 2912 ? 228.957 212.952 180.357 1.00 45.36  ? 2912 PHE A CE1   1 
ATOM   10911 C  CE2   . PHE A 1 2912 ? 230.671 211.982 181.694 1.00 41.32  ? 2912 PHE A CE2   1 
ATOM   10912 C  CZ    . PHE A 1 2912 ? 229.501 212.698 181.595 1.00 37.84  ? 2912 PHE A CZ    1 
ATOM   10913 N  N     . ASN A 1 2913 ? 232.674 208.455 178.271 1.00 45.45  ? 2913 ASN A N     1 
ATOM   10914 C  CA    . ASN A 1 2913 ? 233.197 207.224 178.856 1.00 46.81  ? 2913 ASN A CA    1 
ATOM   10915 C  C     . ASN A 1 2913 ? 232.863 207.102 180.338 1.00 48.19  ? 2913 ASN A C     1 
ATOM   10916 O  O     . ASN A 1 2913 ? 232.624 205.992 180.832 1.00 51.67  ? 2913 ASN A O     1 
ATOM   10917 C  CB    . ASN A 1 2913 ? 234.707 207.157 178.642 1.00 52.33  ? 2913 ASN A CB    1 
ATOM   10918 C  CG    . ASN A 1 2913 ? 235.095 207.358 177.193 1.00 50.55  ? 2913 ASN A CG    1 
ATOM   10919 O  OD1   . ASN A 1 2913 ? 234.255 207.278 176.298 1.00 46.52  ? 2913 ASN A OD1   1 
ATOM   10920 N  ND2   . ASN A 1 2913 ? 236.371 207.630 176.955 1.00 48.59  ? 2913 ASN A ND2   1 
ATOM   10921 N  N     . GLU A 1 2914 ? 232.835 208.224 181.058 1.00 44.86  ? 2914 GLU A N     1 
ATOM   10922 C  CA    . GLU A 1 2914 ? 232.491 208.180 182.474 1.00 40.87  ? 2914 GLU A CA    1 
ATOM   10923 C  C     . GLU A 1 2914 ? 231.053 207.719 182.678 1.00 47.60  ? 2914 GLU A C     1 
ATOM   10924 O  O     . GLU A 1 2914 ? 230.756 207.017 183.649 1.00 57.32  ? 2914 GLU A O     1 
ATOM   10925 C  CB    . GLU A 1 2914 ? 232.719 209.549 183.111 1.00 43.42  ? 2914 GLU A CB    1 
ATOM   10926 C  CG    . GLU A 1 2914 ? 234.150 209.791 183.568 1.00 53.23  ? 2914 GLU A CG    1 
ATOM   10927 C  CD    . GLU A 1 2914 ? 235.051 210.289 182.451 1.00 60.28  ? 2914 GLU A CD    1 
ATOM   10928 O  OE1   . GLU A 1 2914 ? 234.555 210.495 181.324 1.00 59.73  ? 2914 GLU A OE1   1 
ATOM   10929 O  OE2   . GLU A 1 2914 ? 236.259 210.479 182.703 1.00 58.38  ? 2914 GLU A OE2   1 
ATOM   10930 N  N     . VAL A 1 2915 ? 230.148 208.095 181.772 1.00 37.27  ? 2915 VAL A N     1 
ATOM   10931 C  CA    . VAL A 1 2915 ? 228.765 207.638 181.876 1.00 31.98  ? 2915 VAL A CA    1 
ATOM   10932 C  C     . VAL A 1 2915 ? 228.683 206.127 181.701 1.00 42.89  ? 2915 VAL A C     1 
ATOM   10933 O  O     . VAL A 1 2915 ? 227.946 205.446 182.423 1.00 52.05  ? 2915 VAL A O     1 
ATOM   10934 C  CB    . VAL A 1 2915 ? 227.875 208.375 180.860 1.00 39.27  ? 2915 VAL A CB    1 
ATOM   10935 C  CG1   . VAL A 1 2915 ? 226.556 207.649 180.686 1.00 44.92  ? 2915 VAL A CG1   1 
ATOM   10936 C  CG2   . VAL A 1 2915 ? 227.621 209.790 181.323 1.00 44.37  ? 2915 VAL A CG2   1 
ATOM   10937 N  N     . LEU A 1 2916 ? 229.424 205.579 180.736 1.00 42.54  ? 2916 LEU A N     1 
ATOM   10938 C  CA    . LEU A 1 2916 ? 229.439 204.131 180.549 1.00 38.93  ? 2916 LEU A CA    1 
ATOM   10939 C  C     . LEU A 1 2916 ? 230.003 203.425 181.775 1.00 36.94  ? 2916 LEU A C     1 
ATOM   10940 O  O     . LEU A 1 2916 ? 229.446 202.418 182.238 1.00 49.95  ? 2916 LEU A O     1 
ATOM   10941 C  CB    . LEU A 1 2916 ? 230.246 203.777 179.301 1.00 47.95  ? 2916 LEU A CB    1 
ATOM   10942 C  CG    . LEU A 1 2916 ? 229.843 204.500 178.015 1.00 39.34  ? 2916 LEU A CG    1 
ATOM   10943 C  CD1   . LEU A 1 2916 ? 230.683 204.015 176.852 1.00 40.45  ? 2916 LEU A CD1   1 
ATOM   10944 C  CD2   . LEU A 1 2916 ? 228.368 204.301 177.730 1.00 40.33  ? 2916 LEU A CD2   1 
ATOM   10945 N  N     . ASP A 1 2917 ? 231.104 203.946 182.324 1.00 28.61  ? 2917 ASP A N     1 
ATOM   10946 C  CA    . ASP A 1 2917 ? 231.650 203.380 183.553 1.00 39.39  ? 2917 ASP A CA    1 
ATOM   10947 C  C     . ASP A 1 2917 ? 230.617 203.395 184.671 1.00 37.50  ? 2917 ASP A C     1 
ATOM   10948 O  O     . ASP A 1 2917 ? 230.429 202.392 185.369 1.00 48.69  ? 2917 ASP A O     1 
ATOM   10949 C  CB    . ASP A 1 2917 ? 232.898 204.151 183.983 1.00 47.90  ? 2917 ASP A CB    1 
ATOM   10950 C  CG    . ASP A 1 2917 ? 234.073 203.930 183.056 1.00 55.79  ? 2917 ASP A CG    1 
ATOM   10951 O  OD1   . ASP A 1 2917 ? 234.148 202.849 182.441 1.00 60.60  ? 2917 ASP A OD1   1 
ATOM   10952 O  OD2   . ASP A 1 2917 ? 234.925 204.835 182.946 1.00 55.69  ? 2917 ASP A OD2   1 
ATOM   10953 N  N     . HIS A 1 2918 ? 229.931 204.524 184.849 1.00 33.16  ? 2918 HIS A N     1 
ATOM   10954 C  CA    . HIS A 1 2918 ? 228.993 204.660 185.955 1.00 30.24  ? 2918 HIS A CA    1 
ATOM   10955 C  C     . HIS A 1 2918 ? 227.787 203.746 185.785 1.00 38.55  ? 2918 HIS A C     1 
ATOM   10956 O  O     . HIS A 1 2918 ? 227.307 203.162 186.763 1.00 57.57  ? 2918 HIS A O     1 
ATOM   10957 C  CB    . HIS A 1 2918 ? 228.561 206.118 186.085 1.00 34.12  ? 2918 HIS A CB    1 
ATOM   10958 C  CG    . HIS A 1 2918 ? 229.650 207.023 186.570 1.00 41.31  ? 2918 HIS A CG    1 
ATOM   10959 N  ND1   . HIS A 1 2918 ? 229.706 208.361 186.247 1.00 46.29  ? 2918 HIS A ND1   1 
ATOM   10960 C  CD2   . HIS A 1 2918 ? 230.726 206.780 187.354 1.00 41.02  ? 2918 HIS A CD2   1 
ATOM   10961 C  CE1   . HIS A 1 2918 ? 230.770 208.904 186.811 1.00 47.85  ? 2918 HIS A CE1   1 
ATOM   10962 N  NE2   . HIS A 1 2918 ? 231.406 207.966 187.488 1.00 42.86  ? 2918 HIS A NE2   1 
ATOM   10963 N  N     . VAL A 1 2919 ? 227.276 203.605 184.559 1.00 34.83  ? 2919 VAL A N     1 
ATOM   10964 C  CA    . VAL A 1 2919 ? 226.131 202.721 184.370 1.00 36.68  ? 2919 VAL A CA    1 
ATOM   10965 C  C     . VAL A 1 2919 ? 226.536 201.270 184.586 1.00 35.51  ? 2919 VAL A C     1 
ATOM   10966 O  O     . VAL A 1 2919 ? 225.764 200.488 185.153 1.00 41.51  ? 2919 VAL A O     1 
ATOM   10967 C  CB    . VAL A 1 2919 ? 225.464 202.930 182.994 1.00 36.71  ? 2919 VAL A CB    1 
ATOM   10968 C  CG1   . VAL A 1 2919 ? 224.954 204.351 182.861 1.00 35.40  ? 2919 VAL A CG1   1 
ATOM   10969 C  CG2   . VAL A 1 2919 ? 226.397 202.581 181.855 1.00 37.74  ? 2919 VAL A CG2   1 
ATOM   10970 N  N     . LEU A 1 2920 ? 227.745 200.880 184.168 1.00 37.22  ? 2920 LEU A N     1 
ATOM   10971 C  CA    . LEU A 1 2920 ? 228.205 199.526 184.466 1.00 36.04  ? 2920 LEU A CA    1 
ATOM   10972 C  C     . LEU A 1 2920 ? 228.346 199.306 185.970 1.00 40.41  ? 2920 LEU A C     1 
ATOM   10973 O  O     . LEU A 1 2920 ? 227.968 198.247 186.489 1.00 45.78  ? 2920 LEU A O     1 
ATOM   10974 C  CB    . LEU A 1 2920 ? 229.526 199.252 183.750 1.00 34.99  ? 2920 LEU A CB    1 
ATOM   10975 C  CG    . LEU A 1 2920 ? 229.441 199.061 182.236 1.00 32.56  ? 2920 LEU A CG    1 
ATOM   10976 C  CD1   . LEU A 1 2920 ? 230.776 198.608 181.686 1.00 39.24  ? 2920 LEU A CD1   1 
ATOM   10977 C  CD2   . LEU A 1 2920 ? 228.352 198.070 181.877 1.00 29.12  ? 2920 LEU A CD2   1 
ATOM   10978 N  N     . ARG A 1 2921 ? 228.874 200.302 186.686 1.00 37.09  ? 2921 ARG A N     1 
ATOM   10979 C  CA    . ARG A 1 2921 ? 229.012 200.188 188.135 1.00 30.93  ? 2921 ARG A CA    1 
ATOM   10980 C  C     . ARG A 1 2921 ? 227.658 200.041 188.816 1.00 36.05  ? 2921 ARG A C     1 
ATOM   10981 O  O     . ARG A 1 2921 ? 227.503 199.233 189.738 1.00 48.76  ? 2921 ARG A O     1 
ATOM   10982 C  CB    . ARG A 1 2921 ? 229.745 201.406 188.691 1.00 26.34  ? 2921 ARG A CB    1 
ATOM   10983 C  CG    . ARG A 1 2921 ? 231.195 201.508 188.291 1.00 35.38  ? 2921 ARG A CG    1 
ATOM   10984 C  CD    . ARG A 1 2921 ? 231.801 202.777 188.846 1.00 39.96  ? 2921 ARG A CD    1 
ATOM   10985 N  NE    . ARG A 1 2921 ? 232.972 203.202 188.092 1.00 43.36  ? 2921 ARG A NE    1 
ATOM   10986 C  CZ    . ARG A 1 2921 ? 233.702 204.267 188.389 1.00 46.20  ? 2921 ARG A CZ    1 
ATOM   10987 N  NH1   . ARG A 1 2921 ? 233.408 205.040 189.422 1.00 43.17  ? 2921 ARG A NH1   1 
ATOM   10988 N  NH2   . ARG A 1 2921 ? 234.753 204.564 187.632 1.00 47.17  ? 2921 ARG A NH2   1 
ATOM   10989 N  N     . ILE A 1 2922 ? 226.670 200.826 188.386 1.00 34.01  ? 2922 ILE A N     1 
ATOM   10990 C  CA    . ILE A 1 2922 ? 225.338 200.741 188.978 1.00 33.84  ? 2922 ILE A CA    1 
ATOM   10991 C  C     . ILE A 1 2922 ? 224.694 199.396 188.658 1.00 33.74  ? 2922 ILE A C     1 
ATOM   10992 O  O     . ILE A 1 2922 ? 224.049 198.778 189.516 1.00 39.36  ? 2922 ILE A O     1 
ATOM   10993 C  CB    . ILE A 1 2922 ? 224.473 201.921 188.500 1.00 34.22  ? 2922 ILE A CB    1 
ATOM   10994 C  CG1   . ILE A 1 2922 ? 225.082 203.245 188.958 1.00 35.83  ? 2922 ILE A CG1   1 
ATOM   10995 C  CG2   . ILE A 1 2922 ? 223.060 201.795 189.017 1.00 27.92  ? 2922 ILE A CG2   1 
ATOM   10996 C  CD1   . ILE A 1 2922 ? 224.485 204.453 188.287 1.00 33.91  ? 2922 ILE A CD1   1 
ATOM   10997 N  N     . ASP A 1 2923 ? 224.863 198.920 187.421 1.00 38.09  ? 2923 ASP A N     1 
ATOM   10998 C  CA    . ASP A 1 2923 ? 224.309 197.628 187.036 1.00 29.66  ? 2923 ASP A CA    1 
ATOM   10999 C  C     . ASP A 1 2923 ? 224.922 196.494 187.843 1.00 37.34  ? 2923 ASP A C     1 
ATOM   11000 O  O     . ASP A 1 2923 ? 224.241 195.505 188.134 1.00 41.80  ? 2923 ASP A O     1 
ATOM   11001 C  CB    . ASP A 1 2923 ? 224.523 197.398 185.541 1.00 33.46  ? 2923 ASP A CB    1 
ATOM   11002 C  CG    . ASP A 1 2923 ? 224.179 195.989 185.112 1.00 53.34  ? 2923 ASP A CG    1 
ATOM   11003 O  OD1   . ASP A 1 2923 ? 223.039 195.550 185.369 1.00 53.84  ? 2923 ASP A OD1   1 
ATOM   11004 O  OD2   . ASP A 1 2923 ? 225.047 195.320 184.514 1.00 59.63  ? 2923 ASP A OD2   1 
ATOM   11005 N  N     . ARG A 1 2924 ? 226.200 196.614 188.208 1.00 43.24  ? 2924 ARG A N     1 
ATOM   11006 C  CA    . ARG A 1 2924 ? 226.814 195.597 189.057 1.00 29.15  ? 2924 ARG A CA    1 
ATOM   11007 C  C     . ARG A 1 2924 ? 226.096 195.487 190.395 1.00 34.68  ? 2924 ARG A C     1 
ATOM   11008 O  O     . ARG A 1 2924 ? 225.819 194.380 190.870 1.00 43.10  ? 2924 ARG A O     1 
ATOM   11009 C  CB    . ARG A 1 2924 ? 228.291 195.915 189.280 1.00 33.68  ? 2924 ARG A CB    1 
ATOM   11010 C  CG    . ARG A 1 2924 ? 229.223 195.306 188.259 1.00 43.45  ? 2924 ARG A CG    1 
ATOM   11011 C  CD    . ARG A 1 2924 ? 230.662 195.664 188.565 1.00 42.96  ? 2924 ARG A CD    1 
ATOM   11012 N  NE    . ARG A 1 2924 ? 230.925 195.666 189.998 1.00 47.08  ? 2924 ARG A NE    1 
ATOM   11013 C  CZ    . ARG A 1 2924 ? 231.728 194.809 190.612 1.00 45.85  ? 2924 ARG A CZ    1 
ATOM   11014 N  NH1   . ARG A 1 2924 ? 232.366 193.861 189.947 1.00 34.49  ? 2924 ARG A NH1   1 
ATOM   11015 N  NH2   . ARG A 1 2924 ? 231.897 194.908 191.927 1.00 45.28  ? 2924 ARG A NH2   1 
ATOM   11016 N  N     . ILE A 1 2925 ? 225.789 196.625 191.019 1.00 46.00  ? 2925 ILE A N     1 
ATOM   11017 C  CA    . ILE A 1 2925 ? 225.155 196.606 192.334 1.00 38.37  ? 2925 ILE A CA    1 
ATOM   11018 C  C     . ILE A 1 2925 ? 223.706 196.150 192.230 1.00 37.83  ? 2925 ILE A C     1 
ATOM   11019 O  O     . ILE A 1 2925 ? 223.211 195.420 193.096 1.00 44.45  ? 2925 ILE A O     1 
ATOM   11020 C  CB    . ILE A 1 2925 ? 225.272 197.985 193.004 1.00 35.21  ? 2925 ILE A CB    1 
ATOM   11021 C  CG1   . ILE A 1 2925 ? 226.742 198.376 193.154 1.00 40.79  ? 2925 ILE A CG1   1 
ATOM   11022 C  CG2   . ILE A 1 2925 ? 224.592 197.978 194.358 1.00 38.79  ? 2925 ILE A CG2   1 
ATOM   11023 C  CD1   . ILE A 1 2925 ? 227.617 197.266 193.688 1.00 41.50  ? 2925 ILE A CD1   1 
ATOM   11024 N  N     . PHE A 1 2926 ? 223.000 196.565 191.176 1.00 41.85  ? 2926 PHE A N     1 
ATOM   11025 C  CA    . PHE A 1 2926 ? 221.601 196.171 191.037 1.00 38.08  ? 2926 PHE A CA    1 
ATOM   11026 C  C     . PHE A 1 2926 ? 221.421 194.672 190.829 1.00 41.75  ? 2926 PHE A C     1 
ATOM   11027 O  O     . PHE A 1 2926 ? 220.297 194.176 190.955 1.00 50.53  ? 2926 PHE A O     1 
ATOM   11028 C  CB    . PHE A 1 2926 ? 220.942 196.933 189.888 1.00 33.36  ? 2926 PHE A CB    1 
ATOM   11029 C  CG    . PHE A 1 2926 ? 220.570 198.343 190.233 1.00 31.48  ? 2926 PHE A CG    1 
ATOM   11030 C  CD1   . PHE A 1 2926 ? 220.512 198.753 191.552 1.00 41.44  ? 2926 PHE A CD1   1 
ATOM   11031 C  CD2   . PHE A 1 2926 ? 220.250 199.252 189.242 1.00 34.04  ? 2926 PHE A CD2   1 
ATOM   11032 C  CE1   . PHE A 1 2926 ? 220.159 200.044 191.874 1.00 44.36  ? 2926 PHE A CE1   1 
ATOM   11033 C  CE2   . PHE A 1 2926 ? 219.893 200.544 189.562 1.00 38.04  ? 2926 PHE A CE2   1 
ATOM   11034 C  CZ    . PHE A 1 2926 ? 219.851 200.941 190.878 1.00 39.03  ? 2926 PHE A CZ    1 
ATOM   11035 N  N     . ARG A 1 2927 ? 222.490 193.940 190.520 1.00 42.85  ? 2927 ARG A N     1 
ATOM   11036 C  CA    . ARG A 1 2927 ? 222.424 192.501 190.304 1.00 41.04  ? 2927 ARG A CA    1 
ATOM   11037 C  C     . ARG A 1 2927 ? 222.909 191.703 191.509 1.00 45.60  ? 2927 ARG A C     1 
ATOM   11038 O  O     . ARG A 1 2927 ? 223.365 190.567 191.347 1.00 49.67  ? 2927 ARG A O     1 
ATOM   11039 C  CB    . ARG A 1 2927 ? 223.231 192.118 189.064 1.00 42.08  ? 2927 ARG A CB    1 
ATOM   11040 C  CG    . ARG A 1 2927 ? 222.618 192.582 187.756 1.00 41.18  ? 2927 ARG A CG    1 
ATOM   11041 C  CD    . ARG A 1 2927 ? 223.431 192.100 186.567 1.00 46.28  ? 2927 ARG A CD    1 
ATOM   11042 N  NE    . ARG A 1 2927 ? 224.766 192.685 186.539 1.00 50.05  ? 2927 ARG A NE    1 
ATOM   11043 C  CZ    . ARG A 1 2927 ? 225.879 192.027 186.835 1.00 50.08  ? 2927 ARG A CZ    1 
ATOM   11044 N  NH1   . ARG A 1 2927 ? 225.853 190.759 187.209 1.00 49.01  ? 2927 ARG A NH1   1 
ATOM   11045 N  NH2   . ARG A 1 2927 ? 227.046 192.658 186.756 1.00 44.19  ? 2927 ARG A NH2   1 
ATOM   11046 N  N     . GLN A 1 2928 ? 222.820 192.268 192.708 1.00 46.74  ? 2928 GLN A N     1 
ATOM   11047 C  CA    . GLN A 1 2928 ? 223.291 191.608 193.914 1.00 44.65  ? 2928 GLN A CA    1 
ATOM   11048 C  C     . GLN A 1 2928 ? 222.200 191.610 194.973 1.00 48.02  ? 2928 GLN A C     1 
ATOM   11049 O  O     . GLN A 1 2928 ? 221.365 192.519 195.009 1.00 43.79  ? 2928 GLN A O     1 
ATOM   11050 C  CB    . GLN A 1 2928 ? 224.542 192.301 194.472 1.00 31.41  ? 2928 GLN A CB    1 
ATOM   11051 C  CG    . GLN A 1 2928 ? 225.794 192.090 193.645 1.00 41.65  ? 2928 GLN A CG    1 
ATOM   11052 C  CD    . GLN A 1 2928 ? 226.957 192.925 194.137 1.00 56.21  ? 2928 GLN A CD    1 
ATOM   11053 O  OE1   . GLN A 1 2928 ? 226.921 193.468 195.241 1.00 51.92  ? 2928 GLN A OE1   1 
ATOM   11054 N  NE2   . GLN A 1 2928 ? 227.995 193.038 193.317 1.00 48.85  ? 2928 GLN A NE2   1 
ATOM   11055 N  N     . PRO A 1 2929 ? 222.178 190.603 195.844 1.00 46.33  ? 2929 PRO A N     1 
ATOM   11056 C  CA    . PRO A 1 2929 ? 221.208 190.609 196.943 1.00 43.89  ? 2929 PRO A CA    1 
ATOM   11057 C  C     . PRO A 1 2929 ? 221.589 191.632 197.999 1.00 48.53  ? 2929 PRO A C     1 
ATOM   11058 O  O     . PRO A 1 2929 ? 222.754 191.743 198.387 1.00 46.57  ? 2929 PRO A O     1 
ATOM   11059 C  CB    . PRO A 1 2929 ? 221.285 189.181 197.492 1.00 42.61  ? 2929 PRO A CB    1 
ATOM   11060 C  CG    . PRO A 1 2929 ? 222.663 188.735 197.153 1.00 43.22  ? 2929 PRO A CG    1 
ATOM   11061 C  CD    . PRO A 1 2929 ? 222.997 189.379 195.837 1.00 44.65  ? 2929 PRO A CD    1 
ATOM   11062 N  N     . GLN A 1 2930 ? 220.586 192.375 198.467 1.00 52.07  ? 2930 GLN A N     1 
ATOM   11063 C  CA    . GLN A 1 2930 ? 220.794 193.466 199.419 1.00 41.86  ? 2930 GLN A CA    1 
ATOM   11064 C  C     . GLN A 1 2930 ? 221.843 194.445 198.902 1.00 44.78  ? 2930 GLN A C     1 
ATOM   11065 O  O     . GLN A 1 2930 ? 222.720 194.901 199.638 1.00 45.23  ? 2930 GLN A O     1 
ATOM   11066 C  CB    . GLN A 1 2930 ? 221.175 192.932 200.800 1.00 41.40  ? 2930 GLN A CB    1 
ATOM   11067 C  CG    . GLN A 1 2930 ? 220.579 193.719 201.953 1.00 42.86  ? 2930 GLN A CG    1 
ATOM   11068 C  CD    . GLN A 1 2930 ? 221.024 193.199 203.303 1.00 47.91  ? 2930 GLN A CD    1 
ATOM   11069 O  OE1   . GLN A 1 2930 ? 221.651 192.146 203.400 1.00 46.80  ? 2930 GLN A OE1   1 
ATOM   11070 N  NE2   . GLN A 1 2930 ? 220.704 193.940 204.355 1.00 44.27  ? 2930 GLN A NE2   1 
ATOM   11071 N  N     . GLY A 1 2931 ? 221.754 194.766 197.614 1.00 39.65  ? 2931 GLY A N     1 
ATOM   11072 C  CA    . GLY A 1 2931 ? 222.696 195.670 196.988 1.00 34.09  ? 2931 GLY A CA    1 
ATOM   11073 C  C     . GLY A 1 2931 ? 222.235 197.111 197.016 1.00 39.68  ? 2931 GLY A C     1 
ATOM   11074 O  O     . GLY A 1 2931 ? 221.311 197.491 196.293 1.00 39.91  ? 2931 GLY A O     1 
ATOM   11075 N  N     . HIS A 1 2932 ? 222.873 197.922 197.852 1.00 43.37  ? 2932 HIS A N     1 
ATOM   11076 C  CA    . HIS A 1 2932 ? 222.535 199.326 198.003 1.00 29.32  ? 2932 HIS A CA    1 
ATOM   11077 C  C     . HIS A 1 2932 ? 223.688 200.193 197.517 1.00 34.03  ? 2932 HIS A C     1 
ATOM   11078 O  O     . HIS A 1 2932 ? 224.860 199.847 197.684 1.00 43.40  ? 2932 HIS A O     1 
ATOM   11079 C  CB    . HIS A 1 2932 ? 222.209 199.661 199.460 1.00 34.94  ? 2932 HIS A CB    1 
ATOM   11080 C  CG    . HIS A 1 2932 ? 221.174 198.769 200.069 1.00 31.73  ? 2932 HIS A CG    1 
ATOM   11081 N  ND1   . HIS A 1 2932 ? 219.959 198.523 199.469 1.00 34.94  ? 2932 HIS A ND1   1 
ATOM   11082 C  CD2   . HIS A 1 2932 ? 221.171 198.066 201.226 1.00 37.13  ? 2932 HIS A CD2   1 
ATOM   11083 C  CE1   . HIS A 1 2932 ? 219.252 197.707 200.229 1.00 35.85  ? 2932 HIS A CE1   1 
ATOM   11084 N  NE2   . HIS A 1 2932 ? 219.965 197.415 201.301 1.00 39.22  ? 2932 HIS A NE2   1 
ATOM   11085 N  N     . LEU A 1 2933 ? 223.343 201.325 196.914 1.00 38.34  ? 2933 LEU A N     1 
ATOM   11086 C  CA    . LEU A 1 2933 ? 224.315 202.240 196.338 1.00 32.52  ? 2933 LEU A CA    1 
ATOM   11087 C  C     . LEU A 1 2933 ? 224.335 203.544 197.119 1.00 36.05  ? 2933 LEU A C     1 
ATOM   11088 O  O     . LEU A 1 2933 ? 223.327 203.956 197.700 1.00 43.98  ? 2933 LEU A O     1 
ATOM   11089 C  CB    . LEU A 1 2933 ? 223.999 202.533 194.870 1.00 32.14  ? 2933 LEU A CB    1 
ATOM   11090 C  CG    . LEU A 1 2933 ? 224.762 201.739 193.814 1.00 36.18  ? 2933 LEU A CG    1 
ATOM   11091 C  CD1   . LEU A 1 2933 ? 224.192 202.036 192.447 1.00 40.37  ? 2933 LEU A CD1   1 
ATOM   11092 C  CD2   . LEU A 1 2933 ? 226.243 202.067 193.861 1.00 40.53  ? 2933 LEU A CD2   1 
ATOM   11093 N  N     . LEU A 1 2934 ? 225.500 204.189 197.131 1.00 28.87  ? 2934 LEU A N     1 
ATOM   11094 C  CA    . LEU A 1 2934 ? 225.676 205.517 197.715 1.00 27.85  ? 2934 LEU A CA    1 
ATOM   11095 C  C     . LEU A 1 2934 ? 226.455 206.333 196.689 1.00 37.45  ? 2934 LEU A C     1 
ATOM   11096 O  O     . LEU A 1 2934 ? 227.684 206.263 196.632 1.00 43.95  ? 2934 LEU A O     1 
ATOM   11097 C  CB    . LEU A 1 2934 ? 226.391 205.451 199.061 1.00 32.96  ? 2934 LEU A CB    1 
ATOM   11098 C  CG    . LEU A 1 2934 ? 226.834 206.779 199.678 1.00 31.50  ? 2934 LEU A CG    1 
ATOM   11099 C  CD1   . LEU A 1 2934 ? 225.657 207.725 199.819 1.00 36.85  ? 2934 LEU A CD1   1 
ATOM   11100 C  CD2   . LEU A 1 2934 ? 227.499 206.554 201.020 1.00 37.48  ? 2934 LEU A CD2   1 
ATOM   11101 N  N     . LEU A 1 2935 ? 225.735 207.094 195.870 1.00 41.08  ? 2935 LEU A N     1 
ATOM   11102 C  CA    . LEU A 1 2935 ? 226.347 207.901 194.824 1.00 35.34  ? 2935 LEU A CA    1 
ATOM   11103 C  C     . LEU A 1 2935 ? 226.624 209.296 195.367 1.00 39.82  ? 2935 LEU A C     1 
ATOM   11104 O  O     . LEU A 1 2935 ? 225.699 209.997 195.787 1.00 42.94  ? 2935 LEU A O     1 
ATOM   11105 C  CB    . LEU A 1 2935 ? 225.442 207.976 193.597 1.00 34.98  ? 2935 LEU A CB    1 
ATOM   11106 C  CG    . LEU A 1 2935 ? 224.865 206.659 193.085 1.00 35.23  ? 2935 LEU A CG    1 
ATOM   11107 C  CD1   . LEU A 1 2935 ? 223.978 206.915 191.888 1.00 32.89  ? 2935 LEU A CD1   1 
ATOM   11108 C  CD2   . LEU A 1 2935 ? 225.979 205.695 192.728 1.00 40.16  ? 2935 LEU A CD2   1 
ATOM   11109 N  N     . ILE A 1 2936 ? 227.890 209.696 195.354 1.00 36.94  ? 2936 ILE A N     1 
ATOM   11110 C  CA    . ILE A 1 2936 ? 228.313 210.988 195.877 1.00 38.27  ? 2936 ILE A CA    1 
ATOM   11111 C  C     . ILE A 1 2936 ? 228.905 211.792 194.730 1.00 36.70  ? 2936 ILE A C     1 
ATOM   11112 O  O     . ILE A 1 2936 ? 229.849 211.343 194.071 1.00 39.29  ? 2936 ILE A O     1 
ATOM   11113 C  CB    . ILE A 1 2936 ? 229.323 210.838 197.023 1.00 39.71  ? 2936 ILE A CB    1 
ATOM   11114 C  CG1   . ILE A 1 2936 ? 228.796 209.855 198.066 1.00 39.24  ? 2936 ILE A CG1   1 
ATOM   11115 C  CG2   . ILE A 1 2936 ? 229.589 212.179 197.666 1.00 39.92  ? 2936 ILE A CG2   1 
ATOM   11116 C  CD1   . ILE A 1 2936 ? 229.771 209.567 199.170 1.00 41.71  ? 2936 ILE A CD1   1 
ATOM   11117 N  N     . GLY A 1 2937 ? 228.350 212.972 194.496 1.00 39.89  ? 2937 GLY A N     1 
ATOM   11118 C  CA    . GLY A 1 2937 ? 228.831 213.835 193.435 1.00 33.91  ? 2937 GLY A CA    1 
ATOM   11119 C  C     . GLY A 1 2937 ? 228.027 215.114 193.425 1.00 42.07  ? 2937 GLY A C     1 
ATOM   11120 O  O     . GLY A 1 2937 ? 227.037 215.260 194.150 1.00 44.45  ? 2937 GLY A O     1 
ATOM   11121 N  N     . VAL A 1 2938 ? 228.474 216.049 192.589 1.00 39.44  ? 2938 VAL A N     1 
ATOM   11122 C  CA    . VAL A 1 2938 ? 227.796 217.332 192.484 1.00 41.55  ? 2938 VAL A CA    1 
ATOM   11123 C  C     . VAL A 1 2938 ? 226.415 217.131 191.871 1.00 46.51  ? 2938 VAL A C     1 
ATOM   11124 O  O     . VAL A 1 2938 ? 226.177 216.186 191.106 1.00 51.59  ? 2938 VAL A O     1 
ATOM   11125 C  CB    . VAL A 1 2938 ? 228.643 218.321 191.662 1.00 37.10  ? 2938 VAL A CB    1 
ATOM   11126 C  CG1   . VAL A 1 2938 ? 228.664 217.914 190.207 1.00 37.41  ? 2938 VAL A CG1   1 
ATOM   11127 C  CG2   . VAL A 1 2938 ? 228.129 219.741 191.825 1.00 43.85  ? 2938 VAL A CG2   1 
ATOM   11128 N  N     . SER A 1 2939 ? 225.484 218.010 192.231 1.00 33.30  ? 2939 SER A N     1 
ATOM   11129 C  CA    . SER A 1 2939 ? 224.133 217.933 191.699 1.00 33.55  ? 2939 SER A CA    1 
ATOM   11130 C  C     . SER A 1 2939 ? 224.127 218.228 190.204 1.00 41.09  ? 2939 SER A C     1 
ATOM   11131 O  O     . SER A 1 2939 ? 224.938 219.005 189.697 1.00 44.90  ? 2939 SER A O     1 
ATOM   11132 C  CB    . SER A 1 2939 ? 223.218 218.911 192.429 1.00 38.16  ? 2939 SER A CB    1 
ATOM   11133 O  OG    . SER A 1 2939 ? 223.133 218.591 193.804 1.00 47.26  ? 2939 SER A OG    1 
ATOM   11134 N  N     . GLY A 1 2940 ? 223.199 217.594 189.496 1.00 37.38  ? 2940 GLY A N     1 
ATOM   11135 C  CA    . GLY A 1 2940 ? 223.133 217.738 188.059 1.00 27.62  ? 2940 GLY A CA    1 
ATOM   11136 C  C     . GLY A 1 2940 ? 224.158 216.939 187.292 1.00 39.14  ? 2940 GLY A C     1 
ATOM   11137 O  O     . GLY A 1 2940 ? 224.328 217.171 186.090 1.00 46.94  ? 2940 GLY A O     1 
ATOM   11138 N  N     . ALA A 1 2941 ? 224.848 216.007 187.943 1.00 35.55  ? 2941 ALA A N     1 
ATOM   11139 C  CA    . ALA A 1 2941 ? 225.852 215.181 187.289 1.00 38.30  ? 2941 ALA A CA    1 
ATOM   11140 C  C     . ALA A 1 2941 ? 225.262 213.939 186.638 1.00 37.80  ? 2941 ALA A C     1 
ATOM   11141 O  O     . ALA A 1 2941 ? 225.994 213.202 185.971 1.00 42.35  ? 2941 ALA A O     1 
ATOM   11142 C  CB    . ALA A 1 2941 ? 226.933 214.770 188.292 1.00 41.66  ? 2941 ALA A CB    1 
ATOM   11143 N  N     . GLY A 1 2942 ? 223.969 213.692 186.810 1.00 40.87  ? 2942 GLY A N     1 
ATOM   11144 C  CA    . GLY A 1 2942 ? 223.318 212.551 186.207 1.00 36.96  ? 2942 GLY A CA    1 
ATOM   11145 C  C     . GLY A 1 2942 ? 223.130 211.347 187.101 1.00 33.81  ? 2942 GLY A C     1 
ATOM   11146 O  O     . GLY A 1 2942 ? 222.788 210.277 186.591 1.00 41.19  ? 2942 GLY A O     1 
ATOM   11147 N  N     . LYS A 1 2943 ? 223.334 211.484 188.413 1.00 37.81  ? 2943 LYS A N     1 
ATOM   11148 C  CA    . LYS A 1 2943 ? 223.251 210.329 189.301 1.00 32.31  ? 2943 LYS A CA    1 
ATOM   11149 C  C     . LYS A 1 2943 ? 221.854 209.719 189.304 1.00 40.66  ? 2943 LYS A C     1 
ATOM   11150 O  O     . LYS A 1 2943 ? 221.698 208.508 189.110 1.00 49.28  ? 2943 LYS A O     1 
ATOM   11151 C  CB    . LYS A 1 2943 ? 223.664 210.732 190.716 1.00 33.70  ? 2943 LYS A CB    1 
ATOM   11152 C  CG    . LYS A 1 2943 ? 224.909 211.598 190.765 1.00 37.34  ? 2943 LYS A CG    1 
ATOM   11153 C  CD    . LYS A 1 2943 ? 225.483 211.674 192.164 1.00 33.03  ? 2943 LYS A CD    1 
ATOM   11154 C  CE    . LYS A 1 2943 ? 224.523 212.358 193.116 1.00 40.93  ? 2943 LYS A CE    1 
ATOM   11155 N  NZ    . LYS A 1 2943 ? 224.522 213.834 192.946 1.00 36.65  ? 2943 LYS A NZ    1 
ATOM   11156 N  N     . THR A 1 2944 ? 220.824 210.541 189.517 1.00 34.39  ? 2944 THR A N     1 
ATOM   11157 C  CA    . THR A 1 2944 ? 219.460 210.021 189.560 1.00 27.78  ? 2944 THR A CA    1 
ATOM   11158 C  C     . THR A 1 2944 ? 219.022 209.487 188.202 1.00 34.12  ? 2944 THR A C     1 
ATOM   11159 O  O     . THR A 1 2944 ? 218.379 208.435 188.123 1.00 48.21  ? 2944 THR A O     1 
ATOM   11160 C  CB    . THR A 1 2944 ? 218.498 211.105 190.040 1.00 35.60  ? 2944 THR A CB    1 
ATOM   11161 O  OG1   . THR A 1 2944 ? 218.948 211.623 191.298 1.00 41.13  ? 2944 THR A OG1   1 
ATOM   11162 C  CG2   . THR A 1 2944 ? 217.098 210.542 190.205 1.00 38.98  ? 2944 THR A CG2   1 
ATOM   11163 N  N     . THR A 1 2945 ? 219.352 210.201 187.124 1.00 38.21  ? 2945 THR A N     1 
ATOM   11164 C  CA    . THR A 1 2945 ? 218.964 209.746 185.793 1.00 35.60  ? 2945 THR A CA    1 
ATOM   11165 C  C     . THR A 1 2945 ? 219.648 208.434 185.433 1.00 33.37  ? 2945 THR A C     1 
ATOM   11166 O  O     . THR A 1 2945 ? 219.012 207.527 184.887 1.00 42.56  ? 2945 THR A O     1 
ATOM   11167 C  CB    . THR A 1 2945 ? 219.286 210.819 184.754 1.00 37.41  ? 2945 THR A CB    1 
ATOM   11168 O  OG1   . THR A 1 2945 ? 218.693 212.060 185.151 1.00 45.68  ? 2945 THR A OG1   1 
ATOM   11169 C  CG2   . THR A 1 2945 ? 218.737 210.421 183.398 1.00 41.83  ? 2945 THR A CG2   1 
ATOM   11170 N  N     . LEU A 1 2946 ? 220.943 208.313 185.733 1.00 31.16  ? 2946 LEU A N     1 
ATOM   11171 C  CA    . LEU A 1 2946 ? 221.644 207.062 185.465 1.00 32.74  ? 2946 LEU A CA    1 
ATOM   11172 C  C     . LEU A 1 2946 ? 221.089 205.926 186.314 1.00 33.44  ? 2946 LEU A C     1 
ATOM   11173 O  O     . LEU A 1 2946 ? 220.953 204.796 185.831 1.00 44.90  ? 2946 LEU A O     1 
ATOM   11174 C  CB    . LEU A 1 2946 ? 223.143 207.227 185.708 1.00 33.82  ? 2946 LEU A CB    1 
ATOM   11175 C  CG    . LEU A 1 2946 ? 223.930 208.032 184.674 1.00 33.40  ? 2946 LEU A CG    1 
ATOM   11176 C  CD1   . LEU A 1 2946 ? 225.419 207.815 184.861 1.00 38.71  ? 2946 LEU A CD1   1 
ATOM   11177 C  CD2   . LEU A 1 2946 ? 223.504 207.675 183.263 1.00 32.00  ? 2946 LEU A CD2   1 
ATOM   11178 N  N     . SER A 1 2947 ? 220.771 206.201 187.581 1.00 27.34  ? 2947 SER A N     1 
ATOM   11179 C  CA    . SER A 1 2947 ? 220.179 205.170 188.426 1.00 27.15  ? 2947 SER A CA    1 
ATOM   11180 C  C     . SER A 1 2947 ? 218.846 204.698 187.864 1.00 35.50  ? 2947 SER A C     1 
ATOM   11181 O  O     . SER A 1 2947 ? 218.593 203.492 187.781 1.00 45.16  ? 2947 SER A O     1 
ATOM   11182 C  CB    . SER A 1 2947 ? 220.001 205.694 189.848 1.00 31.10  ? 2947 SER A CB    1 
ATOM   11183 O  OG    . SER A 1 2947 ? 221.223 206.185 190.363 1.00 44.82  ? 2947 SER A OG    1 
ATOM   11184 N  N     . ARG A 1 2948 ? 217.989 205.637 187.458 1.00 45.01  ? 2948 ARG A N     1 
ATOM   11185 C  CA    . ARG A 1 2948 ? 216.697 205.270 186.886 1.00 40.06  ? 2948 ARG A CA    1 
ATOM   11186 C  C     . ARG A 1 2948 ? 216.868 204.483 185.595 1.00 37.64  ? 2948 ARG A C     1 
ATOM   11187 O  O     . ARG A 1 2948 ? 216.152 203.507 185.355 1.00 50.97  ? 2948 ARG A O     1 
ATOM   11188 C  CB    . ARG A 1 2948 ? 215.857 206.521 186.643 1.00 36.94  ? 2948 ARG A CB    1 
ATOM   11189 C  CG    . ARG A 1 2948 ? 215.084 206.977 187.858 1.00 41.09  ? 2948 ARG A CG    1 
ATOM   11190 C  CD    . ARG A 1 2948 ? 214.064 208.039 187.510 1.00 41.23  ? 2948 ARG A CD    1 
ATOM   11191 N  NE    . ARG A 1 2948 ? 214.639 209.375 187.581 1.00 52.50  ? 2948 ARG A NE    1 
ATOM   11192 C  CZ    . ARG A 1 2948 ? 213.931 210.495 187.592 1.00 56.73  ? 2948 ARG A CZ    1 
ATOM   11193 N  NH1   . ARG A 1 2948 ? 212.611 210.478 187.524 1.00 53.42  ? 2948 ARG A NH1   1 
ATOM   11194 N  NH2   . ARG A 1 2948 ? 214.565 211.661 187.673 1.00 46.03  ? 2948 ARG A NH2   1 
ATOM   11195 N  N     . PHE A 1 2949 ? 217.818 204.887 184.757 1.00 30.39  ? 2949 PHE A N     1 
ATOM   11196 C  CA    . PHE A 1 2949 ? 218.026 204.214 183.481 1.00 30.85  ? 2949 PHE A CA    1 
ATOM   11197 C  C     . PHE A 1 2949 ? 218.519 202.785 183.687 1.00 38.67  ? 2949 PHE A C     1 
ATOM   11198 O  O     . PHE A 1 2949 ? 218.015 201.839 183.064 1.00 51.40  ? 2949 PHE A O     1 
ATOM   11199 C  CB    . PHE A 1 2949 ? 219.010 205.034 182.652 1.00 34.84  ? 2949 PHE A CB    1 
ATOM   11200 C  CG    . PHE A 1 2949 ? 219.397 204.406 181.359 1.00 37.16  ? 2949 PHE A CG    1 
ATOM   11201 C  CD1   . PHE A 1 2949 ? 218.430 204.011 180.458 1.00 44.18  ? 2949 PHE A CD1   1 
ATOM   11202 C  CD2   . PHE A 1 2949 ? 220.725 204.264 181.017 1.00 39.13  ? 2949 PHE A CD2   1 
ATOM   11203 C  CE1   . PHE A 1 2949 ? 218.778 203.452 179.257 1.00 42.99  ? 2949 PHE A CE1   1 
ATOM   11204 C  CE2   . PHE A 1 2949 ? 221.079 203.709 179.814 1.00 43.55  ? 2949 PHE A CE2   1 
ATOM   11205 C  CZ    . PHE A 1 2949 ? 220.100 203.310 178.930 1.00 46.32  ? 2949 PHE A CZ    1 
ATOM   11206 N  N     . VAL A 1 2950 ? 219.494 202.606 184.579 1.00 38.17  ? 2950 VAL A N     1 
ATOM   11207 C  CA    . VAL A 1 2950 ? 220.020 201.272 184.846 1.00 31.99  ? 2950 VAL A CA    1 
ATOM   11208 C  C     . VAL A 1 2950 ? 218.960 200.399 185.503 1.00 41.56  ? 2950 VAL A C     1 
ATOM   11209 O  O     . VAL A 1 2950 ? 218.847 199.206 185.200 1.00 48.24  ? 2950 VAL A O     1 
ATOM   11210 C  CB    . VAL A 1 2950 ? 221.296 201.364 185.700 1.00 32.87  ? 2950 VAL A CB    1 
ATOM   11211 C  CG1   . VAL A 1 2950 ? 221.779 199.982 186.068 1.00 44.17  ? 2950 VAL A CG1   1 
ATOM   11212 C  CG2   . VAL A 1 2950 ? 222.375 202.112 184.949 1.00 28.44  ? 2950 VAL A CG2   1 
ATOM   11213 N  N     . ALA A 1 2951 ? 218.161 200.974 186.407 1.00 40.12  ? 2951 ALA A N     1 
ATOM   11214 C  CA    . ALA A 1 2951 ? 217.054 200.229 186.992 1.00 25.06  ? 2951 ALA A CA    1 
ATOM   11215 C  C     . ALA A 1 2951 ? 216.043 199.826 185.929 1.00 37.15  ? 2951 ALA A C     1 
ATOM   11216 O  O     . ALA A 1 2951 ? 215.435 198.754 186.012 1.00 50.34  ? 2951 ALA A O     1 
ATOM   11217 C  CB    . ALA A 1 2951 ? 216.382 201.061 188.083 1.00 27.81  ? 2951 ALA A CB    1 
ATOM   11218 N  N     . TRP A 1 2952 ? 215.840 200.681 184.926 1.00 45.79  ? 2952 TRP A N     1 
ATOM   11219 C  CA    . TRP A 1 2952 ? 214.951 200.337 183.825 1.00 41.63  ? 2952 TRP A CA    1 
ATOM   11220 C  C     . TRP A 1 2952 ? 215.492 199.153 183.034 1.00 43.52  ? 2952 TRP A C     1 
ATOM   11221 O  O     . TRP A 1 2952 ? 214.735 198.256 182.649 1.00 46.75  ? 2952 TRP A O     1 
ATOM   11222 C  CB    . TRP A 1 2952 ? 214.745 201.550 182.919 1.00 43.67  ? 2952 TRP A CB    1 
ATOM   11223 C  CG    . TRP A 1 2952 ? 214.035 201.234 181.641 1.00 48.22  ? 2952 TRP A CG    1 
ATOM   11224 C  CD1   . TRP A 1 2952 ? 212.699 201.022 181.477 1.00 43.47  ? 2952 TRP A CD1   1 
ATOM   11225 C  CD2   . TRP A 1 2952 ? 214.626 201.094 180.346 1.00 45.73  ? 2952 TRP A CD2   1 
ATOM   11226 N  NE1   . TRP A 1 2952 ? 212.420 200.759 180.159 1.00 40.18  ? 2952 TRP A NE1   1 
ATOM   11227 C  CE2   . TRP A 1 2952 ? 213.587 200.796 179.444 1.00 40.96  ? 2952 TRP A CE2   1 
ATOM   11228 C  CE3   . TRP A 1 2952 ? 215.933 201.189 179.861 1.00 45.14  ? 2952 TRP A CE3   1 
ATOM   11229 C  CZ2   . TRP A 1 2952 ? 213.815 200.594 178.088 1.00 48.06  ? 2952 TRP A CZ2   1 
ATOM   11230 C  CZ3   . TRP A 1 2952 ? 216.156 200.989 178.516 1.00 46.84  ? 2952 TRP A CZ3   1 
ATOM   11231 C  CH2   . TRP A 1 2952 ? 215.104 200.695 177.644 1.00 45.97  ? 2952 TRP A CH2   1 
ATOM   11232 N  N     . MET A 1 2953 ? 216.805 199.130 182.774 1.00 40.34  ? 2953 MET A N     1 
ATOM   11233 C  CA    . MET A 1 2953 ? 217.365 197.946 182.123 1.00 47.44  ? 2953 MET A CA    1 
ATOM   11234 C  C     . MET A 1 2953 ? 217.210 196.688 182.968 1.00 48.98  ? 2953 MET A C     1 
ATOM   11235 O  O     . MET A 1 2953 ? 216.833 195.637 182.439 1.00 48.79  ? 2953 MET A O     1 
ATOM   11236 C  CB    . MET A 1 2953 ? 218.840 198.117 181.773 1.00 40.63  ? 2953 MET A CB    1 
ATOM   11237 C  CG    . MET A 1 2953 ? 219.179 199.119 180.702 1.00 40.07  ? 2953 MET A CG    1 
ATOM   11238 S  SD    . MET A 1 2953 ? 220.967 199.062 180.541 1.00 80.16  ? 2953 MET A SD    1 
ATOM   11239 C  CE    . MET A 1 2953 ? 221.293 200.317 179.328 1.00 49.76  ? 2953 MET A CE    1 
ATOM   11240 N  N     . ASN A 1 2954 ? 217.495 196.764 184.263 1.00 40.74  ? 2954 ASN A N     1 
ATOM   11241 C  CA    . ASN A 1 2954 ? 217.475 195.590 185.123 1.00 38.75  ? 2954 ASN A CA    1 
ATOM   11242 C  C     . ASN A 1 2954 ? 216.069 195.194 185.551 1.00 45.33  ? 2954 ASN A C     1 
ATOM   11243 O  O     . ASN A 1 2954 ? 215.920 194.313 186.401 1.00 52.77  ? 2954 ASN A O     1 
ATOM   11244 C  CB    . ASN A 1 2954 ? 218.346 195.829 186.357 1.00 38.59  ? 2954 ASN A CB    1 
ATOM   11245 C  CG    . ASN A 1 2954 ? 219.819 195.893 186.023 1.00 43.58  ? 2954 ASN A CG    1 
ATOM   11246 O  OD1   . ASN A 1 2954 ? 220.496 196.868 186.341 1.00 50.28  ? 2954 ASN A OD1   1 
ATOM   11247 N  ND2   . ASN A 1 2954 ? 220.323 194.853 185.374 1.00 45.79  ? 2954 ASN A ND2   1 
ATOM   11248 N  N     . GLY A 1 2955 ? 215.043 195.814 184.980 1.00 44.22  ? 2955 GLY A N     1 
ATOM   11249 C  CA    . GLY A 1 2955 ? 213.680 195.494 185.366 1.00 37.22  ? 2955 GLY A CA    1 
ATOM   11250 C  C     . GLY A 1 2955 ? 213.363 195.851 186.800 1.00 45.64  ? 2955 GLY A C     1 
ATOM   11251 O  O     . GLY A 1 2955 ? 212.563 195.165 187.447 1.00 58.18  ? 2955 GLY A O     1 
ATOM   11252 N  N     . LEU A 1 2956 ? 213.973 196.913 187.313 1.00 42.85  ? 2956 LEU A N     1 
ATOM   11253 C  CA    . LEU A 1 2956 ? 213.715 197.389 188.663 1.00 42.45  ? 2956 LEU A CA    1 
ATOM   11254 C  C     . LEU A 1 2956 ? 212.704 198.523 188.607 1.00 39.40  ? 2956 LEU A C     1 
ATOM   11255 O  O     . LEU A 1 2956 ? 212.852 199.453 187.808 1.00 52.56  ? 2956 LEU A O     1 
ATOM   11256 C  CB    . LEU A 1 2956 ? 214.999 197.880 189.333 1.00 39.67  ? 2956 LEU A CB    1 
ATOM   11257 C  CG    . LEU A 1 2956 ? 216.132 196.906 189.650 1.00 33.59  ? 2956 LEU A CG    1 
ATOM   11258 C  CD1   . LEU A 1 2956 ? 217.299 197.683 190.184 1.00 39.69  ? 2956 LEU A CD1   1 
ATOM   11259 C  CD2   . LEU A 1 2956 ? 215.709 195.881 190.658 1.00 46.51  ? 2956 LEU A CD2   1 
ATOM   11260 N  N     . SER A 1 2957 ? 211.677 198.443 189.446 1.00 36.06  ? 2957 SER A N     1 
ATOM   11261 C  CA    . SER A 1 2957 ? 210.750 199.555 189.585 1.00 40.30  ? 2957 SER A CA    1 
ATOM   11262 C  C     . SER A 1 2957 ? 211.423 200.681 190.355 1.00 45.24  ? 2957 SER A C     1 
ATOM   11263 O  O     . SER A 1 2957 ? 212.075 200.444 191.375 1.00 56.13  ? 2957 SER A O     1 
ATOM   11264 C  CB    . SER A 1 2957 ? 209.480 199.104 190.301 1.00 42.25  ? 2957 SER A CB    1 
ATOM   11265 O  OG    . SER A 1 2957 ? 208.958 197.925 189.716 1.00 52.31  ? 2957 SER A OG    1 
ATOM   11266 N  N     . VAL A 1 2958 ? 211.277 201.906 189.867 1.00 43.79  ? 2958 VAL A N     1 
ATOM   11267 C  CA    . VAL A 1 2958 ? 211.879 203.064 190.516 1.00 42.16  ? 2958 VAL A CA    1 
ATOM   11268 C  C     . VAL A 1 2958 ? 210.848 203.687 191.445 1.00 40.58  ? 2958 VAL A C     1 
ATOM   11269 O  O     . VAL A 1 2958 ? 209.754 204.063 191.012 1.00 51.36  ? 2958 VAL A O     1 
ATOM   11270 C  CB    . VAL A 1 2958 ? 212.382 204.084 189.487 1.00 44.73  ? 2958 VAL A CB    1 
ATOM   11271 C  CG1   . VAL A 1 2958 ? 212.830 205.351 190.188 1.00 40.17  ? 2958 VAL A CG1   1 
ATOM   11272 C  CG2   . VAL A 1 2958 ? 213.520 203.495 188.672 1.00 41.27  ? 2958 VAL A CG2   1 
ATOM   11273 N  N     . TYR A 1 2959 ? 211.194 203.789 192.724 1.00 37.87  ? 2959 TYR A N     1 
ATOM   11274 C  CA    . TYR A 1 2959 ? 210.357 204.441 193.718 1.00 45.36  ? 2959 TYR A CA    1 
ATOM   11275 C  C     . TYR A 1 2959 ? 211.127 205.602 194.325 1.00 50.95  ? 2959 TYR A C     1 
ATOM   11276 O  O     . TYR A 1 2959 ? 212.242 205.419 194.823 1.00 55.72  ? 2959 TYR A O     1 
ATOM   11277 C  CB    . TYR A 1 2959 ? 209.923 203.463 194.813 1.00 47.28  ? 2959 TYR A CB    1 
ATOM   11278 C  CG    . TYR A 1 2959 ? 208.876 204.019 195.754 1.00 46.80  ? 2959 TYR A CG    1 
ATOM   11279 C  CD1   . TYR A 1 2959 ? 209.229 204.853 196.805 1.00 47.43  ? 2959 TYR A CD1   1 
ATOM   11280 C  CD2   . TYR A 1 2959 ? 207.535 203.710 195.590 1.00 51.07  ? 2959 TYR A CD2   1 
ATOM   11281 C  CE1   . TYR A 1 2959 ? 208.280 205.364 197.663 1.00 48.24  ? 2959 TYR A CE1   1 
ATOM   11282 C  CE2   . TYR A 1 2959 ? 206.577 204.216 196.445 1.00 53.66  ? 2959 TYR A CE2   1 
ATOM   11283 C  CZ    . TYR A 1 2959 ? 206.955 205.041 197.480 1.00 52.62  ? 2959 TYR A CZ    1 
ATOM   11284 O  OH    . TYR A 1 2959 ? 206.005 205.549 198.335 1.00 48.52  ? 2959 TYR A OH    1 
ATOM   11285 N  N     . GLN A 1 2960 ? 210.533 206.789 194.277 1.00 51.44  ? 2960 GLN A N     1 
ATOM   11286 C  CA    . GLN A 1 2960 ? 211.082 207.973 194.917 1.00 52.02  ? 2960 GLN A CA    1 
ATOM   11287 C  C     . GLN A 1 2960 ? 210.011 208.578 195.809 1.00 53.89  ? 2960 GLN A C     1 
ATOM   11288 O  O     . GLN A 1 2960 ? 208.842 208.654 195.422 1.00 55.25  ? 2960 GLN A O     1 
ATOM   11289 C  CB    . GLN A 1 2960 ? 211.557 209.005 193.887 1.00 50.92  ? 2960 GLN A CB    1 
ATOM   11290 C  CG    . GLN A 1 2960 ? 212.439 208.433 192.792 1.00 52.51  ? 2960 GLN A CG    1 
ATOM   11291 C  CD    . GLN A 1 2960 ? 212.905 209.488 191.810 1.00 50.95  ? 2960 GLN A CD    1 
ATOM   11292 O  OE1   . GLN A 1 2960 ? 212.574 209.438 190.626 1.00 49.05  ? 2960 GLN A OE1   1 
ATOM   11293 N  NE2   . GLN A 1 2960 ? 213.680 210.448 192.296 1.00 48.10  ? 2960 GLN A NE2   1 
ATOM   11294 N  N     . ILE A 1 2961 ? 210.410 209.000 197.002 1.00 61.58  ? 2961 ILE A N     1 
ATOM   11295 C  CA    . ILE A 1 2961 ? 209.471 209.595 197.945 1.00 63.60  ? 2961 ILE A CA    1 
ATOM   11296 C  C     . ILE A 1 2961 ? 209.216 211.045 197.553 1.00 66.60  ? 2961 ILE A C     1 
ATOM   11297 O  O     . ILE A 1 2961 ? 210.150 211.799 197.253 1.00 67.69  ? 2961 ILE A O     1 
ATOM   11298 C  CB    . ILE A 1 2961 ? 209.990 209.469 199.388 1.00 61.31  ? 2961 ILE A CB    1 
ATOM   11299 C  CG1   . ILE A 1 2961 ? 211.313 210.213 199.573 1.00 61.42  ? 2961 ILE A CG1   1 
ATOM   11300 C  CG2   . ILE A 1 2961 ? 210.141 208.007 199.772 1.00 63.26  ? 2961 ILE A CG2   1 
ATOM   11301 C  CD1   . ILE A 1 2961 ? 211.752 210.319 201.014 1.00 66.03  ? 2961 ILE A CD1   1 
ATOM   11302 N  N     . LYS A 1 2962 ? 207.942 211.427 197.518 1.00 76.86  ? 2962 LYS A N     1 
ATOM   11303 C  CA    . LYS A 1 2962 ? 207.537 212.776 197.129 1.00 74.83  ? 2962 LYS A CA    1 
ATOM   11304 C  C     . LYS A 1 2962 ? 207.530 213.647 198.379 1.00 73.48  ? 2962 LYS A C     1 
ATOM   11305 O  O     . LYS A 1 2962 ? 206.548 213.681 199.123 1.00 75.52  ? 2962 LYS A O     1 
ATOM   11306 C  CB    . LYS A 1 2962 ? 206.173 212.750 196.450 1.00 74.30  ? 2962 LYS A CB    1 
ATOM   11307 C  CG    . LYS A 1 2962 ? 206.153 211.977 195.141 1.00 74.69  ? 2962 LYS A CG    1 
ATOM   11308 C  CD    . LYS A 1 2962 ? 207.368 212.300 194.290 1.00 72.77  ? 2962 LYS A CD    1 
ATOM   11309 C  CE    . LYS A 1 2962 ? 207.199 211.787 192.871 1.00 75.94  ? 2962 LYS A CE    1 
ATOM   11310 N  NZ    . LYS A 1 2962 ? 207.052 210.308 192.827 1.00 76.34  ? 2962 LYS A NZ    1 
ATOM   11311 N  N     . VAL A 1 2963 ? 208.629 214.355 198.606 1.00 70.35  ? 2963 VAL A N     1 
ATOM   11312 C  CA    . VAL A 1 2963 ? 208.809 215.159 199.808 1.00 73.38  ? 2963 VAL A CA    1 
ATOM   11313 C  C     . VAL A 1 2963 ? 208.296 216.567 199.545 1.00 76.66  ? 2963 VAL A C     1 
ATOM   11314 O  O     . VAL A 1 2963 ? 208.521 217.130 198.468 1.00 84.05  ? 2963 VAL A O     1 
ATOM   11315 C  CB    . VAL A 1 2963 ? 210.287 215.177 200.234 1.00 75.95  ? 2963 VAL A CB    1 
ATOM   11316 C  CG1   . VAL A 1 2963 ? 210.546 216.275 201.247 1.00 72.80  ? 2963 VAL A CG1   1 
ATOM   11317 C  CG2   . VAL A 1 2963 ? 210.682 213.828 200.803 1.00 75.53  ? 2963 VAL A CG2   1 
ATOM   11318 N  N     . HIS A 1 2964 ? 207.592 217.131 200.526 1.00 78.87  ? 2964 HIS A N     1 
ATOM   11319 C  CA    . HIS A 1 2964 ? 207.116 218.505 200.434 1.00 76.64  ? 2964 HIS A CA    1 
ATOM   11320 C  C     . HIS A 1 2964 ? 207.247 219.209 201.778 1.00 80.77  ? 2964 HIS A C     1 
ATOM   11321 O  O     . HIS A 1 2964 ? 207.921 218.708 202.684 1.00 83.29  ? 2964 HIS A O     1 
ATOM   11322 C  CB    . HIS A 1 2964 ? 205.669 218.539 199.945 1.00 78.34  ? 2964 HIS A CB    1 
ATOM   11323 C  CG    . HIS A 1 2964 ? 204.792 217.504 200.575 1.00 80.93  ? 2964 HIS A CG    1 
ATOM   11324 N  ND1   . HIS A 1 2964 ? 204.306 217.621 201.859 1.00 79.06  ? 2964 HIS A ND1   1 
ATOM   11325 C  CD2   . HIS A 1 2964 ? 204.311 216.333 200.096 1.00 79.36  ? 2964 HIS A CD2   1 
ATOM   11326 C  CE1   . HIS A 1 2964 ? 203.564 216.566 202.144 1.00 82.29  ? 2964 HIS A CE1   1 
ATOM   11327 N  NE2   . HIS A 1 2964 ? 203.552 215.769 201.092 1.00 82.88  ? 2964 HIS A NE2   1 
ATOM   11328 N  N     . ARG A 1 2965 ? 206.617 220.378 201.914 1.00 85.13  ? 2965 ARG A N     1 
ATOM   11329 C  CA    . ARG A 1 2965 ? 206.737 221.144 203.151 1.00 85.15  ? 2965 ARG A CA    1 
ATOM   11330 C  C     . ARG A 1 2965 ? 206.030 220.454 204.311 1.00 85.61  ? 2965 ARG A C     1 
ATOM   11331 O  O     . ARG A 1 2965 ? 206.538 220.446 205.438 1.00 84.52  ? 2965 ARG A O     1 
ATOM   11332 C  CB    . ARG A 1 2965 ? 206.182 222.553 202.948 1.00 86.13  ? 2965 ARG A CB    1 
ATOM   11333 C  CG    . ARG A 1 2965 ? 206.239 223.430 204.187 1.00 87.61  ? 2965 ARG A CG    1 
ATOM   11334 C  CD    . ARG A 1 2965 ? 205.739 224.823 203.869 1.00 85.02  ? 2965 ARG A CD    1 
ATOM   11335 N  NE    . ARG A 1 2965 ? 206.447 225.386 202.727 1.00 87.40  ? 2965 ARG A NE    1 
ATOM   11336 C  CZ    . ARG A 1 2965 ? 205.858 226.010 201.717 1.00 89.52  ? 2965 ARG A CZ    1 
ATOM   11337 N  NH1   . ARG A 1 2965 ? 204.545 226.170 201.676 1.00 87.51  ? 2965 ARG A NH1   1 
ATOM   11338 N  NH2   . ARG A 1 2965 ? 206.602 226.479 200.721 1.00 89.97  ? 2965 ARG A NH2   1 
ATOM   11339 N  N     . LYS A 1 2966 ? 204.863 219.869 204.059 1.00 88.96  ? 2966 LYS A N     1 
ATOM   11340 C  CA    . LYS A 1 2966 ? 204.087 219.209 205.101 1.00 89.64  ? 2966 LYS A CA    1 
ATOM   11341 C  C     . LYS A 1 2966 ? 204.510 217.765 205.332 1.00 88.04  ? 2966 LYS A C     1 
ATOM   11342 O  O     . LYS A 1 2966 ? 203.909 217.086 206.170 1.00 87.10  ? 2966 LYS A O     1 
ATOM   11343 C  CB    . LYS A 1 2966 ? 202.594 219.264 204.761 1.00 90.72  ? 2966 LYS A CB    1 
ATOM   11344 C  CG    . LYS A 1 2966 ? 201.995 220.660 204.843 1.00 89.31  ? 2966 LYS A CG    1 
ATOM   11345 C  CD    . LYS A 1 2966 ? 202.491 221.405 206.073 1.00 88.35  ? 2966 LYS A CD    1 
ATOM   11346 C  CE    . LYS A 1 2966 ? 201.418 222.323 206.638 1.00 87.74  ? 2966 LYS A CE    1 
ATOM   11347 N  NZ    . LYS A 1 2966 ? 201.332 223.607 205.890 1.00 87.63  ? 2966 LYS A NZ    1 
ATOM   11348 N  N     . TYR A 1 2967 ? 205.516 217.283 204.605 1.00 78.06  ? 2967 TYR A N     1 
ATOM   11349 C  CA    . TYR A 1 2967 ? 206.019 215.932 204.807 1.00 77.82  ? 2967 TYR A CA    1 
ATOM   11350 C  C     . TYR A 1 2967 ? 206.590 215.781 206.211 1.00 81.79  ? 2967 TYR A C     1 
ATOM   11351 O  O     . TYR A 1 2967 ? 207.318 216.653 206.694 1.00 83.83  ? 2967 TYR A O     1 
ATOM   11352 C  CB    . TYR A 1 2967 ? 207.090 215.618 203.765 1.00 76.32  ? 2967 TYR A CB    1 
ATOM   11353 C  CG    . TYR A 1 2967 ? 207.232 214.154 203.431 1.00 74.31  ? 2967 TYR A CG    1 
ATOM   11354 C  CD1   . TYR A 1 2967 ? 206.361 213.535 202.547 1.00 74.29  ? 2967 TYR A CD1   1 
ATOM   11355 C  CD2   . TYR A 1 2967 ? 208.244 213.392 203.994 1.00 74.85  ? 2967 TYR A CD2   1 
ATOM   11356 C  CE1   . TYR A 1 2967 ? 206.493 212.199 202.236 1.00 75.21  ? 2967 TYR A CE1   1 
ATOM   11357 C  CE2   . TYR A 1 2967 ? 208.383 212.058 203.691 1.00 75.26  ? 2967 TYR A CE2   1 
ATOM   11358 C  CZ    . TYR A 1 2967 ? 207.506 211.466 202.812 1.00 76.18  ? 2967 TYR A CZ    1 
ATOM   11359 O  OH    . TYR A 1 2967 ? 207.648 210.133 202.512 1.00 76.07  ? 2967 TYR A OH    1 
ATOM   11360 N  N     . THR A 1 2968 ? 206.259 214.670 206.866 1.00 78.72  ? 2968 THR A N     1 
ATOM   11361 C  CA    . THR A 1 2968 ? 206.752 214.414 208.213 1.00 77.45  ? 2968 THR A CA    1 
ATOM   11362 C  C     . THR A 1 2968 ? 207.109 212.945 208.397 1.00 77.61  ? 2968 THR A C     1 
ATOM   11363 O  O     . THR A 1 2968 ? 207.170 212.187 207.424 1.00 76.77  ? 2968 THR A O     1 
ATOM   11364 C  CB    . THR A 1 2968 ? 205.719 214.849 209.256 1.00 76.28  ? 2968 THR A CB    1 
ATOM   11365 O  OG1   . THR A 1 2968 ? 206.227 214.596 210.571 1.00 77.46  ? 2968 THR A OG1   1 
ATOM   11366 C  CG2   . THR A 1 2968 ? 204.418 214.095 209.067 1.00 74.48  ? 2968 THR A CG2   1 
ATOM   11367 N  N     . GLY A 1 2969 ? 207.350 212.537 209.645 1.00 76.53  ? 2969 GLY A N     1 
ATOM   11368 C  CA    . GLY A 1 2969 ? 207.796 211.178 209.903 1.00 72.94  ? 2969 GLY A CA    1 
ATOM   11369 C  C     . GLY A 1 2969 ? 206.783 210.119 209.519 1.00 74.24  ? 2969 GLY A C     1 
ATOM   11370 O  O     . GLY A 1 2969 ? 207.153 209.067 208.991 1.00 78.80  ? 2969 GLY A O     1 
ATOM   11371 N  N     . GLU A 1 2970 ? 205.499 210.370 209.783 1.00 76.74  ? 2970 GLU A N     1 
ATOM   11372 C  CA    . GLU A 1 2970 ? 204.479 209.373 209.474 1.00 74.86  ? 2970 GLU A CA    1 
ATOM   11373 C  C     . GLU A 1 2970 ? 204.362 209.149 207.971 1.00 78.15  ? 2970 GLU A C     1 
ATOM   11374 O  O     . GLU A 1 2970 ? 204.109 208.025 207.523 1.00 80.52  ? 2970 GLU A O     1 
ATOM   11375 C  CB    . GLU A 1 2970 ? 203.133 209.787 210.071 1.00 78.66  ? 2970 GLU A CB    1 
ATOM   11376 C  CG    . GLU A 1 2970 ? 202.532 211.049 209.477 1.00 81.96  ? 2970 GLU A CG    1 
ATOM   11377 C  CD    . GLU A 1 2970 ? 201.233 211.447 210.148 1.00 85.25  ? 2970 GLU A CD    1 
ATOM   11378 O  OE1   . GLU A 1 2970 ? 200.813 210.749 211.095 1.00 83.04  ? 2970 GLU A OE1   1 
ATOM   11379 O  OE2   . GLU A 1 2970 ? 200.632 212.457 209.727 1.00 83.13  ? 2970 GLU A OE2   1 
ATOM   11380 N  N     . ASP A 1 2971 ? 204.546 210.204 207.174 1.00 73.51  ? 2971 ASP A N     1 
ATOM   11381 C  CA    . ASP A 1 2971 ? 204.520 210.040 205.724 1.00 70.47  ? 2971 ASP A CA    1 
ATOM   11382 C  C     . ASP A 1 2971 ? 205.672 209.165 205.249 1.00 73.86  ? 2971 ASP A C     1 
ATOM   11383 O  O     . ASP A 1 2971 ? 205.493 208.310 204.372 1.00 76.11  ? 2971 ASP A O     1 
ATOM   11384 C  CB    . ASP A 1 2971 ? 204.568 211.404 205.038 1.00 75.09  ? 2971 ASP A CB    1 
ATOM   11385 C  CG    . ASP A 1 2971 ? 203.393 212.280 205.401 1.00 78.77  ? 2971 ASP A CG    1 
ATOM   11386 O  OD1   . ASP A 1 2971 ? 202.257 211.942 205.009 1.00 78.52  ? 2971 ASP A OD1   1 
ATOM   11387 O  OD2   . ASP A 1 2971 ? 203.606 213.311 206.069 1.00 79.57  ? 2971 ASP A OD2   1 
ATOM   11388 N  N     . PHE A 1 2972 ? 206.865 209.366 205.814 1.00 70.06  ? 2972 PHE A N     1 
ATOM   11389 C  CA    . PHE A 1 2972 ? 207.994 208.518 205.450 1.00 66.14  ? 2972 PHE A CA    1 
ATOM   11390 C  C     . PHE A 1 2972 ? 207.763 207.081 205.887 1.00 68.06  ? 2972 PHE A C     1 
ATOM   11391 O  O     . PHE A 1 2972 ? 208.132 206.143 205.173 1.00 72.92  ? 2972 PHE A O     1 
ATOM   11392 C  CB    . PHE A 1 2972 ? 209.287 209.053 206.056 1.00 63.47  ? 2972 PHE A CB    1 
ATOM   11393 C  CG    . PHE A 1 2972 ? 210.515 208.346 205.565 1.00 68.87  ? 2972 PHE A CG    1 
ATOM   11394 C  CD1   . PHE A 1 2972 ? 210.779 208.258 204.210 1.00 70.70  ? 2972 PHE A CD1   1 
ATOM   11395 C  CD2   . PHE A 1 2972 ? 211.396 207.755 206.452 1.00 70.72  ? 2972 PHE A CD2   1 
ATOM   11396 C  CE1   . PHE A 1 2972 ? 211.902 207.605 203.750 1.00 64.31  ? 2972 PHE A CE1   1 
ATOM   11397 C  CE2   . PHE A 1 2972 ? 212.521 207.101 205.997 1.00 70.99  ? 2972 PHE A CE2   1 
ATOM   11398 C  CZ    . PHE A 1 2972 ? 212.774 207.026 204.645 1.00 66.26  ? 2972 PHE A CZ    1 
ATOM   11399 N  N     . ASP A 1 2973 ? 207.161 206.885 207.062 1.00 65.67  ? 2973 ASP A N     1 
ATOM   11400 C  CA    . ASP A 1 2973 ? 206.838 205.533 207.503 1.00 62.26  ? 2973 ASP A CA    1 
ATOM   11401 C  C     . ASP A 1 2973 ? 205.847 204.868 206.559 1.00 61.93  ? 2973 ASP A C     1 
ATOM   11402 O  O     . ASP A 1 2973 ? 205.975 203.679 206.250 1.00 64.63  ? 2973 ASP A O     1 
ATOM   11403 C  CB    . ASP A 1 2973 ? 206.286 205.559 208.926 1.00 65.23  ? 2973 ASP A CB    1 
ATOM   11404 C  CG    . ASP A 1 2973 ? 207.298 206.053 209.932 1.00 69.61  ? 2973 ASP A CG    1 
ATOM   11405 O  OD1   . ASP A 1 2973 ? 208.358 206.556 209.506 1.00 72.82  ? 2973 ASP A OD1   1 
ATOM   11406 O  OD2   . ASP A 1 2973 ? 207.039 205.937 211.147 1.00 68.89  ? 2973 ASP A OD2   1 
ATOM   11407 N  N     . GLU A 1 2974 ? 204.847 205.618 206.092 1.00 62.67  ? 2974 GLU A N     1 
ATOM   11408 C  CA    . GLU A 1 2974 ? 203.879 205.056 205.156 1.00 60.57  ? 2974 GLU A CA    1 
ATOM   11409 C  C     . GLU A 1 2974 ? 204.527 204.715 203.820 1.00 64.38  ? 2974 GLU A C     1 
ATOM   11410 O  O     . GLU A 1 2974 ? 204.221 203.676 203.224 1.00 67.16  ? 2974 GLU A O     1 
ATOM   11411 C  CB    . GLU A 1 2974 ? 202.713 206.023 204.961 1.00 61.76  ? 2974 GLU A CB    1 
ATOM   11412 C  CG    . GLU A 1 2974 ? 201.634 205.499 204.031 1.00 68.23  ? 2974 GLU A CG    1 
ATOM   11413 C  CD    . GLU A 1 2974 ? 200.929 204.276 204.584 1.00 72.79  ? 2974 GLU A CD    1 
ATOM   11414 O  OE1   . GLU A 1 2974 ? 200.896 204.109 205.822 1.00 71.70  ? 2974 GLU A OE1   1 
ATOM   11415 O  OE2   . GLU A 1 2974 ? 200.411 203.476 203.778 1.00 70.36  ? 2974 GLU A OE2   1 
ATOM   11416 N  N     . ASP A 1 2975 ? 205.418 205.578 203.327 1.00 64.21  ? 2975 ASP A N     1 
ATOM   11417 C  CA    . ASP A 1 2975 ? 206.126 205.268 202.087 1.00 61.60  ? 2975 ASP A CA    1 
ATOM   11418 C  C     . ASP A 1 2975 ? 207.019 204.045 202.254 1.00 62.62  ? 2975 ASP A C     1 
ATOM   11419 O  O     . ASP A 1 2975 ? 207.111 203.203 201.352 1.00 65.02  ? 2975 ASP A O     1 
ATOM   11420 C  CB    . ASP A 1 2975 ? 206.942 206.476 201.630 1.00 64.15  ? 2975 ASP A CB    1 
ATOM   11421 C  CG    . ASP A 1 2975 ? 206.070 207.623 201.166 1.00 70.47  ? 2975 ASP A CG    1 
ATOM   11422 O  OD1   . ASP A 1 2975 ? 204.953 207.360 200.675 1.00 72.68  ? 2975 ASP A OD1   1 
ATOM   11423 O  OD2   . ASP A 1 2975 ? 206.499 208.788 201.289 1.00 71.07  ? 2975 ASP A OD2   1 
ATOM   11424 N  N     . LEU A 1 2976 ? 207.683 203.930 203.406 1.00 55.92  ? 2976 LEU A N     1 
ATOM   11425 C  CA    . LEU A 1 2976 ? 208.486 202.748 203.691 1.00 51.76  ? 2976 LEU A CA    1 
ATOM   11426 C  C     . LEU A 1 2976 ? 207.623 201.495 203.728 1.00 58.02  ? 2976 LEU A C     1 
ATOM   11427 O  O     . LEU A 1 2976 ? 208.022 200.447 203.215 1.00 65.53  ? 2976 LEU A O     1 
ATOM   11428 C  CB    . LEU A 1 2976 ? 209.222 202.923 205.017 1.00 55.09  ? 2976 LEU A CB    1 
ATOM   11429 C  CG    . LEU A 1 2976 ? 210.637 203.491 204.957 1.00 59.69  ? 2976 LEU A CG    1 
ATOM   11430 C  CD1   . LEU A 1 2976 ? 211.178 203.691 206.359 1.00 54.13  ? 2976 LEU A CD1   1 
ATOM   11431 C  CD2   . LEU A 1 2976 ? 211.540 202.571 204.159 1.00 59.55  ? 2976 LEU A CD2   1 
ATOM   11432 N  N     . ARG A 1 2977 ? 206.442 201.583 204.342 1.00 58.24  ? 2977 ARG A N     1 
ATOM   11433 C  CA    . ARG A 1 2977 ? 205.539 200.439 204.381 1.00 54.58  ? 2977 ARG A CA    1 
ATOM   11434 C  C     . ARG A 1 2977 ? 205.083 200.051 202.982 1.00 54.16  ? 2977 ARG A C     1 
ATOM   11435 O  O     . ARG A 1 2977 ? 204.997 198.863 202.659 1.00 63.26  ? 2977 ARG A O     1 
ATOM   11436 C  CB    . ARG A 1 2977 ? 204.335 200.745 205.269 1.00 59.73  ? 2977 ARG A CB    1 
ATOM   11437 C  CG    . ARG A 1 2977 ? 204.627 200.670 206.755 1.00 57.07  ? 2977 ARG A CG    1 
ATOM   11438 C  CD    . ARG A 1 2977 ? 203.390 200.977 207.572 1.00 52.75  ? 2977 ARG A CD    1 
ATOM   11439 N  NE    . ARG A 1 2977 ? 203.691 201.858 208.691 1.00 58.94  ? 2977 ARG A NE    1 
ATOM   11440 C  CZ    . ARG A 1 2977 ? 203.145 203.053 208.870 1.00 62.78  ? 2977 ARG A CZ    1 
ATOM   11441 N  NH1   . ARG A 1 2977 ? 202.254 203.540 208.023 1.00 62.31  ? 2977 ARG A NH1   1 
ATOM   11442 N  NH2   . ARG A 1 2977 ? 203.504 203.779 209.925 1.00 60.64  ? 2977 ARG A NH2   1 
ATOM   11443 N  N     . THR A 1 2978 ? 204.784 201.041 202.139 1.00 50.37  ? 2978 THR A N     1 
ATOM   11444 C  CA    . THR A 1 2978 ? 204.400 200.747 200.762 1.00 55.97  ? 2978 THR A CA    1 
ATOM   11445 C  C     . THR A 1 2978 ? 205.524 200.039 200.017 1.00 56.82  ? 2978 THR A C     1 
ATOM   11446 O  O     . THR A 1 2978 ? 205.294 199.026 199.342 1.00 62.61  ? 2978 THR A O     1 
ATOM   11447 C  CB    . THR A 1 2978 ? 204.014 202.036 200.038 1.00 57.24  ? 2978 THR A CB    1 
ATOM   11448 O  OG1   . THR A 1 2978 ? 202.993 202.716 200.778 1.00 58.20  ? 2978 THR A OG1   1 
ATOM   11449 C  CG2   . THR A 1 2978 ? 203.504 201.729 198.642 1.00 57.62  ? 2978 THR A CG2   1 
ATOM   11450 N  N     . VAL A 1 2979 ? 206.750 200.550 200.143 1.00 50.84  ? 2979 VAL A N     1 
ATOM   11451 C  CA    . VAL A 1 2979 ? 207.887 199.942 199.458 1.00 46.56  ? 2979 VAL A CA    1 
ATOM   11452 C  C     . VAL A 1 2979 ? 208.126 198.526 199.965 1.00 56.02  ? 2979 VAL A C     1 
ATOM   11453 O  O     . VAL A 1 2979 ? 208.370 197.605 199.177 1.00 61.03  ? 2979 VAL A O     1 
ATOM   11454 C  CB    . VAL A 1 2979 ? 209.139 200.820 199.627 1.00 48.91  ? 2979 VAL A CB    1 
ATOM   11455 C  CG1   . VAL A 1 2979 ? 210.357 200.113 199.079 1.00 56.21  ? 2979 VAL A CG1   1 
ATOM   11456 C  CG2   . VAL A 1 2979 ? 208.946 202.143 198.934 1.00 52.38  ? 2979 VAL A CG2   1 
ATOM   11457 N  N     . LEU A 1 2980 ? 208.067 198.330 201.284 1.00 52.18  ? 2980 LEU A N     1 
ATOM   11458 C  CA    . LEU A 1 2980 ? 208.320 197.012 201.853 1.00 45.01  ? 2980 LEU A CA    1 
ATOM   11459 C  C     . LEU A 1 2980 ? 207.238 196.021 201.453 1.00 54.98  ? 2980 LEU A C     1 
ATOM   11460 O  O     . LEU A 1 2980 ? 207.531 194.855 201.176 1.00 61.52  ? 2980 LEU A O     1 
ATOM   11461 C  CB    . LEU A 1 2980 ? 208.426 197.107 203.374 1.00 49.81  ? 2980 LEU A CB    1 
ATOM   11462 C  CG    . LEU A 1 2980 ? 209.650 197.837 203.931 1.00 51.62  ? 2980 LEU A CG    1 
ATOM   11463 C  CD1   . LEU A 1 2980 ? 209.906 197.438 205.372 1.00 54.51  ? 2980 LEU A CD1   1 
ATOM   11464 C  CD2   . LEU A 1 2980 ? 210.872 197.571 203.076 1.00 54.88  ? 2980 LEU A CD2   1 
ATOM   11465 N  N     . ARG A 1 2981 ? 205.978 196.460 201.424 1.00 59.38  ? 2981 ARG A N     1 
ATOM   11466 C  CA    . ARG A 1 2981 ? 204.906 195.577 200.986 1.00 60.44  ? 2981 ARG A CA    1 
ATOM   11467 C  C     . ARG A 1 2981 ? 205.058 195.198 199.522 1.00 62.06  ? 2981 ARG A C     1 
ATOM   11468 O  O     . ARG A 1 2981 ? 204.837 194.038 199.160 1.00 67.07  ? 2981 ARG A O     1 
ATOM   11469 C  CB    . ARG A 1 2981 ? 203.550 196.235 201.225 1.00 59.71  ? 2981 ARG A CB    1 
ATOM   11470 C  CG    . ARG A 1 2981 ? 203.083 196.155 202.661 1.00 64.97  ? 2981 ARG A CG    1 
ATOM   11471 C  CD    . ARG A 1 2981 ? 201.726 196.800 202.838 1.00 60.60  ? 2981 ARG A CD    1 
ATOM   11472 N  NE    . ARG A 1 2981 ? 201.161 196.501 204.147 1.00 62.19  ? 2981 ARG A NE    1 
ATOM   11473 C  CZ    . ARG A 1 2981 ? 200.935 197.407 205.087 1.00 68.62  ? 2981 ARG A CZ    1 
ATOM   11474 N  NH1   . ARG A 1 2981 ? 201.221 198.685 204.896 1.00 67.17  ? 2981 ARG A NH1   1 
ATOM   11475 N  NH2   . ARG A 1 2981 ? 200.410 197.023 206.247 1.00 68.07  ? 2981 ARG A NH2   1 
ATOM   11476 N  N     . ARG A 1 2982 ? 205.430 196.151 198.667 1.00 54.36  ? 2982 ARG A N     1 
ATOM   11477 C  CA    . ARG A 1 2982 ? 205.606 195.826 197.256 1.00 50.35  ? 2982 ARG A CA    1 
ATOM   11478 C  C     . ARG A 1 2982 ? 206.783 194.880 197.048 1.00 52.75  ? 2982 ARG A C     1 
ATOM   11479 O  O     . ARG A 1 2982 ? 206.685 193.913 196.286 1.00 58.24  ? 2982 ARG A O     1 
ATOM   11480 C  CB    . ARG A 1 2982 ? 205.786 197.104 196.439 1.00 54.02  ? 2982 ARG A CB    1 
ATOM   11481 C  CG    . ARG A 1 2982 ? 204.541 197.966 196.353 1.00 54.56  ? 2982 ARG A CG    1 
ATOM   11482 C  CD    . ARG A 1 2982 ? 204.846 199.304 195.708 1.00 58.25  ? 2982 ARG A CD    1 
ATOM   11483 N  NE    . ARG A 1 2982 ? 205.597 199.148 194.469 1.00 60.09  ? 2982 ARG A NE    1 
ATOM   11484 C  CZ    . ARG A 1 2982 ? 206.037 200.156 193.729 1.00 58.79  ? 2982 ARG A CZ    1 
ATOM   11485 N  NH1   . ARG A 1 2982 ? 205.827 201.413 194.080 1.00 51.69  ? 2982 ARG A NH1   1 
ATOM   11486 N  NH2   . ARG A 1 2982 ? 206.706 199.896 192.609 1.00 58.06  ? 2982 ARG A NH2   1 
ATOM   11487 N  N     . SER A 1 2983 ? 207.905 195.135 197.725 1.00 54.93  ? 2983 SER A N     1 
ATOM   11488 C  CA    . SER A 1 2983 ? 209.110 194.353 197.468 1.00 53.09  ? 2983 SER A CA    1 
ATOM   11489 C  C     . SER A 1 2983 ? 209.044 192.975 198.118 1.00 55.06  ? 2983 SER A C     1 
ATOM   11490 O  O     . SER A 1 2983 ? 209.484 191.984 197.525 1.00 55.50  ? 2983 SER A O     1 
ATOM   11491 C  CB    . SER A 1 2983 ? 210.344 195.115 197.948 1.00 49.10  ? 2983 SER A CB    1 
ATOM   11492 O  OG    . SER A 1 2983 ? 210.241 195.441 199.321 1.00 57.07  ? 2983 SER A OG    1 
ATOM   11493 N  N     . GLY A 1 2984 ? 208.509 192.890 199.332 1.00 60.80  ? 2984 GLY A N     1 
ATOM   11494 C  CA    . GLY A 1 2984 ? 208.469 191.635 200.053 1.00 58.92  ? 2984 GLY A CA    1 
ATOM   11495 C  C     . GLY A 1 2984 ? 207.242 190.793 199.778 1.00 64.67  ? 2984 GLY A C     1 
ATOM   11496 O  O     . GLY A 1 2984 ? 207.356 189.641 199.349 1.00 66.08  ? 2984 GLY A O     1 
ATOM   11497 N  N     . CYS A 1 2985 ? 206.059 191.358 200.023 1.00 65.10  ? 2985 CYS A N     1 
ATOM   11498 C  CA    . CYS A 1 2985 ? 204.827 190.593 199.861 1.00 64.12  ? 2985 CYS A CA    1 
ATOM   11499 C  C     . CYS A 1 2985 ? 204.554 190.271 198.397 1.00 68.57  ? 2985 CYS A C     1 
ATOM   11500 O  O     . CYS A 1 2985 ? 204.163 189.145 198.068 1.00 75.01  ? 2985 CYS A O     1 
ATOM   11501 C  CB    . CYS A 1 2985 ? 203.651 191.356 200.467 1.00 66.82  ? 2985 CYS A CB    1 
ATOM   11502 S  SG    . CYS A 1 2985 ? 203.861 191.805 202.202 1.00 79.51  ? 2985 CYS A SG    1 
ATOM   11503 N  N     . LYS A 1 2986 ? 204.749 191.240 197.504 1.00 61.22  ? 2986 LYS A N     1 
ATOM   11504 C  CA    . LYS A 1 2986 ? 204.389 191.087 196.101 1.00 59.55  ? 2986 LYS A CA    1 
ATOM   11505 C  C     . LYS A 1 2986 ? 205.561 190.673 195.220 1.00 60.45  ? 2986 LYS A C     1 
ATOM   11506 O  O     . LYS A 1 2986 ? 205.382 190.531 194.007 1.00 63.86  ? 2986 LYS A O     1 
ATOM   11507 C  CB    . LYS A 1 2986 ? 203.773 192.382 195.572 1.00 57.35  ? 2986 LYS A CB    1 
ATOM   11508 C  CG    . LYS A 1 2986 ? 202.528 192.821 196.318 1.00 60.19  ? 2986 LYS A CG    1 
ATOM   11509 C  CD    . LYS A 1 2986 ? 201.916 194.061 195.691 1.00 64.22  ? 2986 LYS A CD    1 
ATOM   11510 C  CE    . LYS A 1 2986 ? 201.493 195.069 196.748 1.00 65.78  ? 2986 LYS A CE    1 
ATOM   11511 N  NZ    . LYS A 1 2986 ? 201.469 196.458 196.211 1.00 61.06  ? 2986 LYS A NZ    1 
ATOM   11512 N  N     . ASN A 1 2987 ? 206.743 190.475 195.796 1.00 53.23  ? 2987 ASN A N     1 
ATOM   11513 C  CA    . ASN A 1 2987 ? 207.925 190.015 195.067 1.00 54.34  ? 2987 ASN A CA    1 
ATOM   11514 C  C     . ASN A 1 2987 ? 208.241 190.935 193.889 1.00 57.04  ? 2987 ASN A C     1 
ATOM   11515 O  O     . ASN A 1 2987 ? 208.383 190.506 192.744 1.00 61.80  ? 2987 ASN A O     1 
ATOM   11516 C  CB    . ASN A 1 2987 ? 207.744 188.573 194.597 1.00 54.49  ? 2987 ASN A CB    1 
ATOM   11517 C  CG    . ASN A 1 2987 ? 209.060 187.882 194.313 1.00 56.19  ? 2987 ASN A CG    1 
ATOM   11518 O  OD1   . ASN A 1 2987 ? 209.770 187.474 195.229 1.00 58.49  ? 2987 ASN A OD1   1 
ATOM   11519 N  ND2   . ASN A 1 2987 ? 209.389 187.741 193.036 1.00 51.27  ? 2987 ASN A ND2   1 
ATOM   11520 N  N     . GLU A 1 2988 ? 208.357 192.224 194.193 1.00 53.08  ? 2988 GLU A N     1 
ATOM   11521 C  CA    . GLU A 1 2988 ? 208.625 193.246 193.190 1.00 50.89  ? 2988 GLU A CA    1 
ATOM   11522 C  C     . GLU A 1 2988 ? 210.019 193.814 193.412 1.00 53.33  ? 2988 GLU A C     1 
ATOM   11523 O  O     . GLU A 1 2988 ? 210.352 194.237 194.523 1.00 56.32  ? 2988 GLU A O     1 
ATOM   11524 C  CB    . GLU A 1 2988 ? 207.579 194.359 193.246 1.00 46.40  ? 2988 GLU A CB    1 
ATOM   11525 C  CG    . GLU A 1 2988 ? 207.801 195.463 192.229 1.00 48.30  ? 2988 GLU A CG    1 
ATOM   11526 C  CD    . GLU A 1 2988 ? 206.777 196.574 192.341 1.00 61.88  ? 2988 GLU A CD    1 
ATOM   11527 O  OE1   . GLU A 1 2988 ? 205.896 196.488 193.221 1.00 57.63  ? 2988 GLU A OE1   1 
ATOM   11528 O  OE2   . GLU A 1 2988 ? 206.853 197.535 191.547 1.00 63.68  ? 2988 GLU A OE2   1 
ATOM   11529 N  N     . LYS A 1 2989 ? 210.828 193.823 192.357 1.00 48.53  ? 2989 LYS A N     1 
ATOM   11530 C  CA    . LYS A 1 2989 ? 212.163 194.400 192.436 1.00 42.54  ? 2989 LYS A CA    1 
ATOM   11531 C  C     . LYS A 1 2989 ? 212.072 195.916 192.315 1.00 45.63  ? 2989 LYS A C     1 
ATOM   11532 O  O     . LYS A 1 2989 ? 211.636 196.437 191.284 1.00 54.81  ? 2989 LYS A O     1 
ATOM   11533 C  CB    . LYS A 1 2989 ? 213.050 193.820 191.341 1.00 39.81  ? 2989 LYS A CB    1 
ATOM   11534 C  CG    . LYS A 1 2989 ? 213.169 192.310 191.368 1.00 48.85  ? 2989 LYS A CG    1 
ATOM   11535 C  CD    . LYS A 1 2989 ? 214.163 191.816 190.331 1.00 48.94  ? 2989 LYS A CD    1 
ATOM   11536 C  CE    . LYS A 1 2989 ? 213.850 192.364 188.950 1.00 51.15  ? 2989 LYS A CE    1 
ATOM   11537 N  NZ    . LYS A 1 2989 ? 212.464 192.044 188.516 1.00 50.17  ? 2989 LYS A NZ    1 
ATOM   11538 N  N     . ILE A 1 2990 ? 212.488 196.624 193.362 1.00 37.58  ? 2990 ILE A N     1 
ATOM   11539 C  CA    . ILE A 1 2990 ? 212.317 198.068 193.458 1.00 42.27  ? 2990 ILE A CA    1 
ATOM   11540 C  C     . ILE A 1 2990 ? 213.677 198.720 193.654 1.00 41.46  ? 2990 ILE A C     1 
ATOM   11541 O  O     . ILE A 1 2990 ? 214.477 198.263 194.478 1.00 45.95  ? 2990 ILE A O     1 
ATOM   11542 C  CB    . ILE A 1 2990 ? 211.369 198.456 194.609 1.00 41.22  ? 2990 ILE A CB    1 
ATOM   11543 C  CG1   . ILE A 1 2990 ? 209.979 197.873 194.377 1.00 38.97  ? 2990 ILE A CG1   1 
ATOM   11544 C  CG2   . ILE A 1 2990 ? 211.283 199.964 194.754 1.00 44.27  ? 2990 ILE A CG2   1 
ATOM   11545 C  CD1   . ILE A 1 2990 ? 209.017 198.188 195.483 1.00 47.43  ? 2990 ILE A CD1   1 
ATOM   11546 N  N     . ALA A 1 2991 ? 213.939 199.781 192.892 1.00 40.38  ? 2991 ALA A N     1 
ATOM   11547 C  CA    . ALA A 1 2991 ? 215.114 200.628 193.093 1.00 38.29  ? 2991 ALA A CA    1 
ATOM   11548 C  C     . ALA A 1 2991 ? 214.660 201.860 193.863 1.00 40.77  ? 2991 ALA A C     1 
ATOM   11549 O  O     . ALA A 1 2991 ? 214.129 202.815 193.296 1.00 53.13  ? 2991 ALA A O     1 
ATOM   11550 C  CB    . ALA A 1 2991 ? 215.756 200.996 191.763 1.00 36.02  ? 2991 ALA A CB    1 
ATOM   11551 N  N     . PHE A 1 2992 ? 214.866 201.835 195.175 1.00 43.40  ? 2992 PHE A N     1 
ATOM   11552 C  CA    . PHE A 1 2992 ? 214.431 202.918 196.053 1.00 35.94  ? 2992 PHE A CA    1 
ATOM   11553 C  C     . PHE A 1 2992 ? 215.472 204.027 195.996 1.00 38.61  ? 2992 PHE A C     1 
ATOM   11554 O  O     . PHE A 1 2992 ? 216.471 203.997 196.715 1.00 53.25  ? 2992 PHE A O     1 
ATOM   11555 C  CB    . PHE A 1 2992 ? 214.238 202.399 197.474 1.00 37.26  ? 2992 PHE A CB    1 
ATOM   11556 C  CG    . PHE A 1 2992 ? 213.604 203.390 198.409 1.00 43.52  ? 2992 PHE A CG    1 
ATOM   11557 C  CD1   . PHE A 1 2992 ? 212.952 204.510 197.927 1.00 47.60  ? 2992 PHE A CD1   1 
ATOM   11558 C  CD2   . PHE A 1 2992 ? 213.661 203.194 199.776 1.00 44.10  ? 2992 PHE A CD2   1 
ATOM   11559 C  CE1   . PHE A 1 2992 ? 212.375 205.414 198.791 1.00 48.00  ? 2992 PHE A CE1   1 
ATOM   11560 C  CE2   . PHE A 1 2992 ? 213.084 204.095 200.643 1.00 47.91  ? 2992 PHE A CE2   1 
ATOM   11561 C  CZ    . PHE A 1 2992 ? 212.441 205.206 200.150 1.00 48.64  ? 2992 PHE A CZ    1 
ATOM   11562 N  N     . ILE A 1 2993 ? 215.238 205.017 195.140 1.00 37.47  ? 2993 ILE A N     1 
ATOM   11563 C  CA    . ILE A 1 2993 ? 216.151 206.142 194.979 1.00 43.76  ? 2993 ILE A CA    1 
ATOM   11564 C  C     . ILE A 1 2993 ? 215.767 207.221 195.981 1.00 45.74  ? 2993 ILE A C     1 
ATOM   11565 O  O     . ILE A 1 2993 ? 214.626 207.693 195.991 1.00 49.78  ? 2993 ILE A O     1 
ATOM   11566 C  CB    . ILE A 1 2993 ? 216.118 206.684 193.544 1.00 41.87  ? 2993 ILE A CB    1 
ATOM   11567 C  CG1   . ILE A 1 2993 ? 216.422 205.564 192.549 1.00 43.34  ? 2993 ILE A CG1   1 
ATOM   11568 C  CG2   . ILE A 1 2993 ? 217.112 207.819 193.385 1.00 41.09  ? 2993 ILE A CG2   1 
ATOM   11569 C  CD1   . ILE A 1 2993 ? 216.461 206.016 191.117 1.00 37.16  ? 2993 ILE A CD1   1 
ATOM   11570 N  N     . MET A 1 2994 ? 216.718 207.612 196.825 1.00 45.36  ? 2994 MET A N     1 
ATOM   11571 C  CA    . MET A 1 2994 ? 216.475 208.583 197.882 1.00 50.60  ? 2994 MET A CA    1 
ATOM   11572 C  C     . MET A 1 2994 ? 217.592 209.613 197.878 1.00 54.96  ? 2994 MET A C     1 
ATOM   11573 O  O     . MET A 1 2994 ? 218.770 209.255 197.782 1.00 57.92  ? 2994 MET A O     1 
ATOM   11574 C  CB    . MET A 1 2994 ? 216.381 207.890 199.244 1.00 53.32  ? 2994 MET A CB    1 
ATOM   11575 C  CG    . MET A 1 2994 ? 216.046 208.809 200.400 1.00 57.26  ? 2994 MET A CG    1 
ATOM   11576 S  SD    . MET A 1 2994 ? 215.863 207.894 201.940 1.00 74.10  ? 2994 MET A SD    1 
ATOM   11577 C  CE    . MET A 1 2994 ? 215.584 209.226 203.101 1.00 57.75  ? 2994 MET A CE    1 
ATOM   11578 N  N     . ASP A 1 2995 ? 217.224 210.885 197.980 1.00 66.56  ? 2995 ASP A N     1 
ATOM   11579 C  CA    . ASP A 1 2995 ? 218.171 211.988 197.947 1.00 61.66  ? 2995 ASP A CA    1 
ATOM   11580 C  C     . ASP A 1 2995 ? 218.356 212.555 199.349 1.00 66.65  ? 2995 ASP A C     1 
ATOM   11581 O  O     . ASP A 1 2995 ? 217.462 212.465 200.194 1.00 71.93  ? 2995 ASP A O     1 
ATOM   11582 C  CB    . ASP A 1 2995 ? 217.694 213.085 196.990 1.00 64.07  ? 2995 ASP A CB    1 
ATOM   11583 C  CG    . ASP A 1 2995 ? 218.695 214.212 196.845 1.00 69.72  ? 2995 ASP A CG    1 
ATOM   11584 O  OD1   . ASP A 1 2995 ? 219.888 213.925 196.616 1.00 71.99  ? 2995 ASP A OD1   1 
ATOM   11585 O  OD2   . ASP A 1 2995 ? 218.289 215.387 196.952 1.00 70.65  ? 2995 ASP A OD2   1 
ATOM   11586 N  N     . GLU A 1 2996 ? 219.534 213.135 199.592 1.00 70.14  ? 2996 GLU A N     1 
ATOM   11587 C  CA    . GLU A 1 2996 ? 219.816 213.706 200.906 1.00 71.46  ? 2996 GLU A CA    1 
ATOM   11588 C  C     . GLU A 1 2996 ? 218.887 214.869 201.226 1.00 70.43  ? 2996 GLU A C     1 
ATOM   11589 O  O     . GLU A 1 2996 ? 218.628 215.148 202.402 1.00 70.58  ? 2996 GLU A O     1 
ATOM   11590 C  CB    . GLU A 1 2996 ? 221.276 214.152 200.986 1.00 69.52  ? 2996 GLU A CB    1 
ATOM   11591 C  CG    . GLU A 1 2996 ? 221.671 215.186 199.947 1.00 71.14  ? 2996 GLU A CG    1 
ATOM   11592 C  CD    . GLU A 1 2996 ? 222.908 215.966 200.346 1.00 75.64  ? 2996 GLU A CD    1 
ATOM   11593 O  OE1   . GLU A 1 2996 ? 223.428 215.729 201.456 1.00 74.80  ? 2996 GLU A OE1   1 
ATOM   11594 O  OE2   . GLU A 1 2996 ? 223.363 216.811 199.548 1.00 72.73  ? 2996 GLU A OE2   1 
ATOM   11595 N  N     . SER A 1 2997 ? 218.381 215.561 200.203 1.00 71.36  ? 2997 SER A N     1 
ATOM   11596 C  CA    . SER A 1 2997 ? 217.421 216.633 200.438 1.00 73.62  ? 2997 SER A CA    1 
ATOM   11597 C  C     . SER A 1 2997 ? 216.080 216.108 200.929 1.00 77.26  ? 2997 SER A C     1 
ATOM   11598 O  O     . SER A 1 2997 ? 215.305 216.874 201.511 1.00 76.30  ? 2997 SER A O     1 
ATOM   11599 C  CB    . SER A 1 2997 ? 217.223 217.454 199.164 1.00 74.09  ? 2997 SER A CB    1 
ATOM   11600 O  OG    . SER A 1 2997 ? 216.724 216.649 198.112 1.00 76.20  ? 2997 SER A OG    1 
ATOM   11601 N  N     . ASN A 1 2998 ? 215.788 214.826 200.705 1.00 74.58  ? 2998 ASN A N     1 
ATOM   11602 C  CA    . ASN A 1 2998 ? 214.570 214.220 201.226 1.00 68.62  ? 2998 ASN A CA    1 
ATOM   11603 C  C     . ASN A 1 2998 ? 214.646 213.952 202.720 1.00 70.49  ? 2998 ASN A C     1 
ATOM   11604 O  O     . ASN A 1 2998 ? 213.607 213.701 203.340 1.00 75.94  ? 2998 ASN A O     1 
ATOM   11605 C  CB    . ASN A 1 2998 ? 214.278 212.914 200.488 1.00 67.88  ? 2998 ASN A CB    1 
ATOM   11606 C  CG    . ASN A 1 2998 ? 214.106 213.113 198.998 1.00 72.57  ? 2998 ASN A CG    1 
ATOM   11607 O  OD1   . ASN A 1 2998 ? 214.031 214.242 198.515 1.00 73.55  ? 2998 ASN A OD1   1 
ATOM   11608 N  ND2   . ASN A 1 2998 ? 214.050 212.012 198.258 1.00 68.53  ? 2998 ASN A ND2   1 
ATOM   11609 N  N     . VAL A 1 2999 ? 215.839 213.997 203.309 1.00 75.27  ? 2999 VAL A N     1 
ATOM   11610 C  CA    . VAL A 1 2999 ? 216.018 213.727 204.735 1.00 78.64  ? 2999 VAL A CA    1 
ATOM   11611 C  C     . VAL A 1 2999 ? 215.683 215.022 205.469 1.00 78.11  ? 2999 VAL A C     1 
ATOM   11612 O  O     . VAL A 1 2999 ? 216.512 215.922 205.605 1.00 80.23  ? 2999 VAL A O     1 
ATOM   11613 C  CB    . VAL A 1 2999 ? 217.425 213.228 205.050 1.00 76.36  ? 2999 VAL A CB    1 
ATOM   11614 C  CG1   . VAL A 1 2999 ? 217.593 213.054 206.546 1.00 75.80  ? 2999 VAL A CG1   1 
ATOM   11615 C  CG2   . VAL A 1 2999 ? 217.698 211.923 204.325 1.00 70.83  ? 2999 VAL A CG2   1 
ATOM   11616 N  N     . LEU A 1 3000 ? 214.444 215.117 205.940 1.00 78.52  ? 3000 LEU A N     1 
ATOM   11617 C  CA    . LEU A 1 3000 ? 214.000 216.263 206.720 1.00 78.39  ? 3000 LEU A CA    1 
ATOM   11618 C  C     . LEU A 1 3000 ? 214.141 216.048 208.221 1.00 78.23  ? 3000 LEU A C     1 
ATOM   11619 O  O     . LEU A 1 3000 ? 213.893 216.981 208.990 1.00 79.00  ? 3000 LEU A O     1 
ATOM   11620 C  CB    . LEU A 1 3000 ? 212.541 216.591 206.393 1.00 78.00  ? 3000 LEU A CB    1 
ATOM   11621 C  CG    . LEU A 1 3000 ? 212.104 216.445 204.936 1.00 79.70  ? 3000 LEU A CG    1 
ATOM   11622 C  CD1   . LEU A 1 3000 ? 210.591 216.479 204.848 1.00 78.87  ? 3000 LEU A CD1   1 
ATOM   11623 C  CD2   . LEU A 1 3000 ? 212.720 217.535 204.075 1.00 78.57  ? 3000 LEU A CD2   1 
ATOM   11624 N  N     . ASP A 1 3001 ? 214.533 214.852 208.654 1.00 81.30  ? 3001 ASP A N     1 
ATOM   11625 C  CA    . ASP A 1 3001 ? 214.576 214.540 210.074 1.00 83.85  ? 3001 ASP A CA    1 
ATOM   11626 C  C     . ASP A 1 3001 ? 215.519 213.365 210.289 1.00 84.94  ? 3001 ASP A C     1 
ATOM   11627 O  O     . ASP A 1 3001 ? 215.746 212.563 209.380 1.00 81.74  ? 3001 ASP A O     1 
ATOM   11628 C  CB    . ASP A 1 3001 ? 213.170 214.224 210.605 1.00 84.29  ? 3001 ASP A CB    1 
ATOM   11629 C  CG    . ASP A 1 3001 ? 213.171 213.787 212.057 1.00 87.35  ? 3001 ASP A CG    1 
ATOM   11630 O  OD1   . ASP A 1 3001 ? 214.083 214.197 212.805 1.00 85.98  ? 3001 ASP A OD1   1 
ATOM   11631 O  OD2   . ASP A 1 3001 ? 212.256 213.034 212.451 1.00 85.93  ? 3001 ASP A OD2   1 
ATOM   11632 N  N     . SER A 1 3002 ? 216.070 213.278 211.503 1.00 86.42  ? 3002 SER A N     1 
ATOM   11633 C  CA    . SER A 1 3002 ? 216.962 212.178 211.848 1.00 86.92  ? 3002 SER A CA    1 
ATOM   11634 C  C     . SER A 1 3002 ? 216.236 210.842 211.926 1.00 86.61  ? 3002 SER A C     1 
ATOM   11635 O  O     . SER A 1 3002 ? 216.877 209.793 211.786 1.00 89.07  ? 3002 SER A O     1 
ATOM   11636 C  CB    . SER A 1 3002 ? 217.661 212.466 213.177 1.00 84.36  ? 3002 SER A CB    1 
ATOM   11637 O  OG    . SER A 1 3002 ? 218.539 211.411 213.529 1.00 84.13  ? 3002 SER A OG    1 
ATOM   11638 N  N     . GLY A 1 3003 ? 214.921 210.852 212.158 1.00 73.00  ? 3003 GLY A N     1 
ATOM   11639 C  CA    . GLY A 1 3003 ? 214.158 209.619 212.135 1.00 73.46  ? 3003 GLY A CA    1 
ATOM   11640 C  C     . GLY A 1 3003 ? 214.187 208.918 210.796 1.00 77.07  ? 3003 GLY A C     1 
ATOM   11641 O  O     . GLY A 1 3003 ? 214.210 207.681 210.754 1.00 80.35  ? 3003 GLY A O     1 
ATOM   11642 N  N     . PHE A 1 3004 ? 214.200 209.683 209.701 1.00 71.40  ? 3004 PHE A N     1 
ATOM   11643 C  CA    . PHE A 1 3004 ? 214.330 209.078 208.381 1.00 71.18  ? 3004 PHE A CA    1 
ATOM   11644 C  C     . PHE A 1 3004 ? 215.624 208.285 208.284 1.00 74.17  ? 3004 PHE A C     1 
ATOM   11645 O  O     . PHE A 1 3004 ? 215.627 207.135 207.829 1.00 74.73  ? 3004 PHE A O     1 
ATOM   11646 C  CB    . PHE A 1 3004 ? 214.297 210.147 207.284 1.00 70.38  ? 3004 PHE A CB    1 
ATOM   11647 C  CG    . PHE A 1 3004 ? 213.036 210.977 207.249 1.00 73.97  ? 3004 PHE A CG    1 
ATOM   11648 C  CD1   . PHE A 1 3004 ? 211.958 210.697 208.071 1.00 76.03  ? 3004 PHE A CD1   1 
ATOM   11649 C  CD2   . PHE A 1 3004 ? 212.932 212.036 206.365 1.00 72.61  ? 3004 PHE A CD2   1 
ATOM   11650 C  CE1   . PHE A 1 3004 ? 210.816 211.469 208.025 1.00 72.84  ? 3004 PHE A CE1   1 
ATOM   11651 C  CE2   . PHE A 1 3004 ? 211.790 212.806 206.311 1.00 73.15  ? 3004 PHE A CE2   1 
ATOM   11652 C  CZ    . PHE A 1 3004 ? 210.731 212.521 207.141 1.00 73.83  ? 3004 PHE A CZ    1 
ATOM   11653 N  N     . LEU A 1 3005 ? 216.733 208.881 208.724 1.00 70.91  ? 3005 LEU A N     1 
ATOM   11654 C  CA    . LEU A 1 3005 ? 218.021 208.204 208.668 1.00 65.84  ? 3005 LEU A CA    1 
ATOM   11655 C  C     . LEU A 1 3005 ? 218.094 207.021 209.620 1.00 67.02  ? 3005 LEU A C     1 
ATOM   11656 O  O     . LEU A 1 3005 ? 218.732 206.021 209.291 1.00 72.81  ? 3005 LEU A O     1 
ATOM   11657 C  CB    . LEU A 1 3005 ? 219.153 209.186 208.963 1.00 69.77  ? 3005 LEU A CB    1 
ATOM   11658 C  CG    . LEU A 1 3005 ? 219.328 210.275 207.909 1.00 74.98  ? 3005 LEU A CG    1 
ATOM   11659 C  CD1   . LEU A 1 3005 ? 220.373 211.290 208.335 1.00 75.01  ? 3005 LEU A CD1   1 
ATOM   11660 C  CD2   . LEU A 1 3005 ? 219.696 209.654 206.572 1.00 72.57  ? 3005 LEU A CD2   1 
ATOM   11661 N  N     . GLU A 1 3006 ? 217.459 207.100 210.790 1.00 63.03  ? 3006 GLU A N     1 
ATOM   11662 C  CA    . GLU A 1 3006 ? 217.441 205.941 211.679 1.00 62.30  ? 3006 GLU A CA    1 
ATOM   11663 C  C     . GLU A 1 3006 ? 216.690 204.773 211.046 1.00 61.98  ? 3006 GLU A C     1 
ATOM   11664 O  O     . GLU A 1 3006 ? 217.175 203.629 211.051 1.00 65.51  ? 3006 GLU A O     1 
ATOM   11665 C  CB    . GLU A 1 3006 ? 216.816 206.315 213.022 1.00 61.31  ? 3006 GLU A CB    1 
ATOM   11666 C  CG    . GLU A 1 3006 ? 216.742 205.165 214.012 1.00 65.41  ? 3006 GLU A CG    1 
ATOM   11667 C  CD    . GLU A 1 3006 ? 218.063 204.914 214.712 1.00 65.99  ? 3006 GLU A CD    1 
ATOM   11668 O  OE1   . GLU A 1 3006 ? 218.947 205.791 214.639 1.00 67.64  ? 3006 GLU A OE1   1 
ATOM   11669 O  OE2   . GLU A 1 3006 ? 218.218 203.843 215.333 1.00 63.84  ? 3006 GLU A OE2   1 
ATOM   11670 N  N     . ARG A 1 3007 ? 215.508 205.044 210.486 1.00 62.64  ? 3007 ARG A N     1 
ATOM   11671 C  CA    . ARG A 1 3007 ? 214.741 203.983 209.842 1.00 62.45  ? 3007 ARG A CA    1 
ATOM   11672 C  C     . ARG A 1 3007 ? 215.486 203.411 208.645 1.00 60.25  ? 3007 ARG A C     1 
ATOM   11673 O  O     . ARG A 1 3007 ? 215.494 202.191 208.438 1.00 57.26  ? 3007 ARG A O     1 
ATOM   11674 C  CB    . ARG A 1 3007 ? 213.368 204.504 209.424 1.00 63.61  ? 3007 ARG A CB    1 
ATOM   11675 C  CG    . ARG A 1 3007 ? 212.422 204.752 210.583 1.00 63.94  ? 3007 ARG A CG    1 
ATOM   11676 C  CD    . ARG A 1 3007 ? 210.987 204.864 210.094 1.00 66.55  ? 3007 ARG A CD    1 
ATOM   11677 N  NE    . ARG A 1 3007 ? 210.005 204.937 211.171 1.00 72.73  ? 3007 ARG A NE    1 
ATOM   11678 C  CZ    . ARG A 1 3007 ? 209.795 203.995 212.082 1.00 72.35  ? 3007 ARG A CZ    1 
ATOM   11679 N  NH1   . ARG A 1 3007 ? 210.473 202.859 212.077 1.00 63.77  ? 3007 ARG A NH1   1 
ATOM   11680 N  NH2   . ARG A 1 3007 ? 208.869 204.192 213.016 1.00 66.61  ? 3007 ARG A NH2   1 
ATOM   11681 N  N     . MET A 1 3008 ? 216.127 204.270 207.847 1.00 60.77  ? 3008 MET A N     1 
ATOM   11682 C  CA    . MET A 1 3008 ? 216.901 203.775 206.715 1.00 56.09  ? 3008 MET A CA    1 
ATOM   11683 C  C     . MET A 1 3008 ? 218.132 203.002 207.163 1.00 55.61  ? 3008 MET A C     1 
ATOM   11684 O  O     . MET A 1 3008 ? 218.539 202.058 206.487 1.00 63.86  ? 3008 MET A O     1 
ATOM   11685 C  CB    . MET A 1 3008 ? 217.301 204.926 205.795 1.00 56.09  ? 3008 MET A CB    1 
ATOM   11686 C  CG    . MET A 1 3008 ? 216.126 205.596 205.110 1.00 61.32  ? 3008 MET A CG    1 
ATOM   11687 S  SD    . MET A 1 3008 ? 215.214 204.449 204.062 1.00 71.89  ? 3008 MET A SD    1 
ATOM   11688 C  CE    . MET A 1 3008 ? 216.403 204.170 202.755 1.00 64.16  ? 3008 MET A CE    1 
ATOM   11689 N  N     . ASN A 1 3009 ? 218.736 203.378 208.290 1.00 49.89  ? 3009 ASN A N     1 
ATOM   11690 C  CA    . ASN A 1 3009 ? 219.849 202.607 208.831 1.00 50.62  ? 3009 ASN A CA    1 
ATOM   11691 C  C     . ASN A 1 3009 ? 219.410 201.191 209.175 1.00 55.44  ? 3009 ASN A C     1 
ATOM   11692 O  O     . ASN A 1 3009 ? 220.047 200.211 208.758 1.00 57.99  ? 3009 ASN A O     1 
ATOM   11693 C  CB    . ASN A 1 3009 ? 220.407 203.318 210.065 1.00 52.30  ? 3009 ASN A CB    1 
ATOM   11694 C  CG    . ASN A 1 3009 ? 221.629 202.636 210.635 1.00 55.18  ? 3009 ASN A CG    1 
ATOM   11695 O  OD1   . ASN A 1 3009 ? 222.707 202.681 210.051 1.00 56.66  ? 3009 ASN A OD1   1 
ATOM   11696 N  ND2   . ASN A 1 3009 ? 221.469 202.008 211.791 1.00 58.21  ? 3009 ASN A ND2   1 
ATOM   11697 N  N     . THR A 1 3010 ? 218.303 201.064 209.912 1.00 55.49  ? 3010 THR A N     1 
ATOM   11698 C  CA    . THR A 1 3010 ? 217.808 199.732 210.251 1.00 54.61  ? 3010 THR A CA    1 
ATOM   11699 C  C     . THR A 1 3010 ? 217.419 198.948 209.002 1.00 52.50  ? 3010 THR A C     1 
ATOM   11700 O  O     . THR A 1 3010 ? 217.712 197.751 208.902 1.00 52.96  ? 3010 THR A O     1 
ATOM   11701 C  CB    . THR A 1 3010 ? 216.623 199.822 211.214 1.00 57.05  ? 3010 THR A CB    1 
ATOM   11702 O  OG1   . THR A 1 3010 ? 215.447 200.219 210.498 1.00 62.70  ? 3010 THR A OG1   1 
ATOM   11703 C  CG2   . THR A 1 3010 ? 216.905 200.807 212.333 1.00 55.51  ? 3010 THR A CG2   1 
ATOM   11704 N  N     . LEU A 1 3011 ? 216.762 199.601 208.040 1.00 52.50  ? 3011 LEU A N     1 
ATOM   11705 C  CA    . LEU A 1 3011 ? 216.349 198.907 206.823 1.00 50.60  ? 3011 LEU A CA    1 
ATOM   11706 C  C     . LEU A 1 3011 ? 217.548 198.444 206.004 1.00 53.63  ? 3011 LEU A C     1 
ATOM   11707 O  O     . LEU A 1 3011 ? 217.566 197.315 205.505 1.00 51.98  ? 3011 LEU A O     1 
ATOM   11708 C  CB    . LEU A 1 3011 ? 215.453 199.814 205.983 1.00 49.41  ? 3011 LEU A CB    1 
ATOM   11709 C  CG    . LEU A 1 3011 ? 215.035 199.237 204.633 1.00 49.34  ? 3011 LEU A CG    1 
ATOM   11710 C  CD1   . LEU A 1 3011 ? 214.065 198.088 204.830 1.00 53.58  ? 3011 LEU A CD1   1 
ATOM   11711 C  CD2   . LEU A 1 3011 ? 214.428 200.312 203.753 1.00 54.36  ? 3011 LEU A CD2   1 
ATOM   11712 N  N     . LEU A 1 3012 ? 218.552 199.306 205.848 1.00 53.33  ? 3012 LEU A N     1 
ATOM   11713 C  CA    . LEU A 1 3012 ? 219.718 198.969 205.043 1.00 47.25  ? 3012 LEU A CA    1 
ATOM   11714 C  C     . LEU A 1 3012 ? 220.523 197.851 205.684 1.00 53.12  ? 3012 LEU A C     1 
ATOM   11715 O  O     . LEU A 1 3012 ? 221.051 196.979 204.984 1.00 54.37  ? 3012 LEU A O     1 
ATOM   11716 C  CB    . LEU A 1 3012 ? 220.586 200.211 204.848 1.00 43.93  ? 3012 LEU A CB    1 
ATOM   11717 C  CG    . LEU A 1 3012 ? 220.398 201.027 203.569 1.00 43.73  ? 3012 LEU A CG    1 
ATOM   11718 C  CD1   . LEU A 1 3012 ? 218.941 201.374 203.346 1.00 50.64  ? 3012 LEU A CD1   1 
ATOM   11719 C  CD2   . LEU A 1 3012 ? 221.226 202.290 203.655 1.00 46.92  ? 3012 LEU A CD2   1 
ATOM   11720 N  N     . ALA A 1 3013 ? 220.634 197.856 207.013 1.00 50.93  ? 3013 ALA A N     1 
ATOM   11721 C  CA    . ALA A 1 3013 ? 221.416 196.816 207.668 1.00 48.81  ? 3013 ALA A CA    1 
ATOM   11722 C  C     . ALA A 1 3013 ? 220.654 195.496 207.734 1.00 50.39  ? 3013 ALA A C     1 
ATOM   11723 O  O     . ALA A 1 3013 ? 221.126 194.474 207.227 1.00 46.74  ? 3013 ALA A O     1 
ATOM   11724 C  CB    . ALA A 1 3013 ? 221.825 197.274 209.064 1.00 49.39  ? 3013 ALA A CB    1 
ATOM   11725 N  N     . ASN A 1 3014 ? 219.470 195.499 208.347 1.00 55.27  ? 3014 ASN A N     1 
ATOM   11726 C  CA    . ASN A 1 3014 ? 218.750 194.260 208.611 1.00 53.43  ? 3014 ASN A CA    1 
ATOM   11727 C  C     . ASN A 1 3014 ? 217.865 193.813 207.457 1.00 54.58  ? 3014 ASN A C     1 
ATOM   11728 O  O     . ASN A 1 3014 ? 217.600 192.613 207.321 1.00 49.99  ? 3014 ASN A O     1 
ATOM   11729 C  CB    . ASN A 1 3014 ? 217.888 194.412 209.867 1.00 49.42  ? 3014 ASN A CB    1 
ATOM   11730 C  CG    . ASN A 1 3014 ? 218.709 194.431 211.136 1.00 52.56  ? 3014 ASN A CG    1 
ATOM   11731 O  OD1   . ASN A 1 3014 ? 218.591 195.345 211.950 1.00 53.47  ? 3014 ASN A OD1   1 
ATOM   11732 N  ND2   . ASN A 1 3014 ? 219.550 193.421 211.312 1.00 50.91  ? 3014 ASN A ND2   1 
ATOM   11733 N  N     . GLY A 1 3015 ? 217.403 194.738 206.623 1.00 53.13  ? 3015 GLY A N     1 
ATOM   11734 C  CA    . GLY A 1 3015 ? 216.398 194.407 205.636 1.00 48.49  ? 3015 GLY A CA    1 
ATOM   11735 C  C     . GLY A 1 3015 ? 214.980 194.448 206.152 1.00 55.83  ? 3015 GLY A C     1 
ATOM   11736 O  O     . GLY A 1 3015 ? 214.060 194.064 205.423 1.00 57.05  ? 3015 GLY A O     1 
ATOM   11737 N  N     . GLU A 1 3016 ? 214.775 194.900 207.386 1.00 62.23  ? 3016 GLU A N     1 
ATOM   11738 C  CA    . GLU A 1 3016 ? 213.451 194.965 207.984 1.00 56.56  ? 3016 GLU A CA    1 
ATOM   11739 C  C     . GLU A 1 3016 ? 213.489 195.938 209.152 1.00 63.39  ? 3016 GLU A C     1 
ATOM   11740 O  O     . GLU A 1 3016 ? 214.486 196.007 209.876 1.00 63.20  ? 3016 GLU A O     1 
ATOM   11741 C  CB    . GLU A 1 3016 ? 212.980 193.574 208.432 1.00 55.78  ? 3016 GLU A CB    1 
ATOM   11742 C  CG    . GLU A 1 3016 ? 213.853 192.901 209.490 1.00 59.54  ? 3016 GLU A CG    1 
ATOM   11743 C  CD    . GLU A 1 3016 ? 213.494 193.299 210.907 1.00 65.20  ? 3016 GLU A CD    1 
ATOM   11744 O  OE1   . GLU A 1 3016 ? 212.366 193.787 211.124 1.00 69.49  ? 3016 GLU A OE1   1 
ATOM   11745 O  OE2   . GLU A 1 3016 ? 214.341 193.120 211.807 1.00 65.05  ? 3016 GLU A OE2   1 
ATOM   11746 N  N     . VAL A 1 3017 ? 212.408 196.693 209.321 1.00 65.93  ? 3017 VAL A N     1 
ATOM   11747 C  CA    . VAL A 1 3017 ? 212.279 197.659 210.408 1.00 61.21  ? 3017 VAL A CA    1 
ATOM   11748 C  C     . VAL A 1 3017 ? 211.314 197.070 211.434 1.00 64.27  ? 3017 VAL A C     1 
ATOM   11749 O  O     . VAL A 1 3017 ? 210.116 196.936 211.133 1.00 62.86  ? 3017 VAL A O     1 
ATOM   11750 C  CB    . VAL A 1 3017 ? 211.791 199.019 209.898 1.00 60.93  ? 3017 VAL A CB    1 
ATOM   11751 C  CG1   . VAL A 1 3017 ? 211.770 200.026 211.030 1.00 62.96  ? 3017 VAL A CG1   1 
ATOM   11752 C  CG2   . VAL A 1 3017 ? 212.672 199.505 208.760 1.00 60.47  ? 3017 VAL A CG2   1 
ATOM   11753 N  N     . PRO A 1 3018 ? 211.778 196.695 212.630 1.00 70.51  ? 3018 PRO A N     1 
ATOM   11754 C  CA    . PRO A 1 3018 ? 210.887 195.995 213.573 1.00 69.92  ? 3018 PRO A CA    1 
ATOM   11755 C  C     . PRO A 1 3018 ? 209.666 196.797 213.989 1.00 69.11  ? 3018 PRO A C     1 
ATOM   11756 O  O     . PRO A 1 3018 ? 208.583 196.222 214.154 1.00 72.44  ? 3018 PRO A O     1 
ATOM   11757 C  CB    . PRO A 1 3018 ? 211.808 195.703 214.767 1.00 66.66  ? 3018 PRO A CB    1 
ATOM   11758 C  CG    . PRO A 1 3018 ? 212.901 196.716 214.662 1.00 68.39  ? 3018 PRO A CG    1 
ATOM   11759 C  CD    . PRO A 1 3018 ? 213.118 196.924 213.196 1.00 65.91  ? 3018 PRO A CD    1 
ATOM   11760 N  N     . GLY A 1 3019 ? 209.802 198.107 214.162 1.00 57.12  ? 3019 GLY A N     1 
ATOM   11761 C  CA    . GLY A 1 3019 ? 208.693 198.917 214.614 1.00 58.74  ? 3019 GLY A CA    1 
ATOM   11762 C  C     . GLY A 1 3019 ? 207.829 199.516 213.532 1.00 63.05  ? 3019 GLY A C     1 
ATOM   11763 O  O     . GLY A 1 3019 ? 206.893 200.257 213.843 1.00 66.04  ? 3019 GLY A O     1 
ATOM   11764 N  N     . LEU A 1 3020 ? 208.112 199.221 212.263 1.00 66.35  ? 3020 LEU A N     1 
ATOM   11765 C  CA    . LEU A 1 3020 ? 207.365 199.840 211.174 1.00 64.89  ? 3020 LEU A CA    1 
ATOM   11766 C  C     . LEU A 1 3020 ? 205.931 199.329 211.126 1.00 65.69  ? 3020 LEU A C     1 
ATOM   11767 O  O     . LEU A 1 3020 ? 204.983 200.117 211.034 1.00 67.02  ? 3020 LEU A O     1 
ATOM   11768 C  CB    . LEU A 1 3020 ? 208.076 199.586 209.846 1.00 59.98  ? 3020 LEU A CB    1 
ATOM   11769 C  CG    . LEU A 1 3020 ? 207.820 200.606 208.739 1.00 58.40  ? 3020 LEU A CG    1 
ATOM   11770 C  CD1   . LEU A 1 3020 ? 208.485 201.925 209.077 1.00 63.68  ? 3020 LEU A CD1   1 
ATOM   11771 C  CD2   . LEU A 1 3020 ? 208.320 200.080 207.409 1.00 56.78  ? 3020 LEU A CD2   1 
ATOM   11772 N  N     . PHE A 1 3021 ? 205.751 198.013 211.189 1.00 67.32  ? 3021 PHE A N     1 
ATOM   11773 C  CA    . PHE A 1 3021 ? 204.430 197.392 211.131 1.00 64.10  ? 3021 PHE A CA    1 
ATOM   11774 C  C     . PHE A 1 3021 ? 204.018 197.018 212.549 1.00 70.32  ? 3021 PHE A C     1 
ATOM   11775 O  O     . PHE A 1 3021 ? 204.569 196.088 213.143 1.00 73.44  ? 3021 PHE A O     1 
ATOM   11776 C  CB    . PHE A 1 3021 ? 204.439 196.167 210.222 1.00 66.38  ? 3021 PHE A CB    1 
ATOM   11777 C  CG    . PHE A 1 3021 ? 204.816 196.462 208.800 1.00 66.76  ? 3021 PHE A CG    1 
ATOM   11778 C  CD1   . PHE A 1 3021 ? 206.143 196.484 208.410 1.00 64.84  ? 3021 PHE A CD1   1 
ATOM   11779 C  CD2   . PHE A 1 3021 ? 203.842 196.701 207.848 1.00 66.24  ? 3021 PHE A CD2   1 
ATOM   11780 C  CE1   . PHE A 1 3021 ? 206.489 196.747 207.102 1.00 63.85  ? 3021 PHE A CE1   1 
ATOM   11781 C  CE2   . PHE A 1 3021 ? 204.184 196.963 206.540 1.00 64.27  ? 3021 PHE A CE2   1 
ATOM   11782 C  CZ    . PHE A 1 3021 ? 205.509 196.986 206.166 1.00 63.54  ? 3021 PHE A CZ    1 
ATOM   11783 N  N     . GLU A 1 3022 ? 203.048 197.747 213.095 1.00 75.08  ? 3022 GLU A N     1 
ATOM   11784 C  CA    . GLU A 1 3022 ? 202.496 197.438 214.404 1.00 73.88  ? 3022 GLU A CA    1 
ATOM   11785 C  C     . GLU A 1 3022 ? 201.029 197.837 214.437 1.00 78.00  ? 3022 GLU A C     1 
ATOM   11786 O  O     . GLU A 1 3022 ? 200.647 198.873 213.887 1.00 77.56  ? 3022 GLU A O     1 
ATOM   11787 C  CB    . GLU A 1 3022 ? 203.270 198.147 215.523 1.00 69.63  ? 3022 GLU A CB    1 
ATOM   11788 C  CG    . GLU A 1 3022 ? 203.544 199.617 215.266 1.00 74.30  ? 3022 GLU A CG    1 
ATOM   11789 C  CD    . GLU A 1 3022 ? 204.582 200.185 216.214 1.00 77.05  ? 3022 GLU A CD    1 
ATOM   11790 O  OE1   . GLU A 1 3022 ? 204.904 199.513 217.215 1.00 77.54  ? 3022 GLU A OE1   1 
ATOM   11791 O  OE2   . GLU A 1 3022 ? 205.077 201.303 215.957 1.00 74.48  ? 3022 GLU A OE2   1 
ATOM   11792 N  N     . GLY A 1 3023 ? 200.217 197.010 215.082 1.00 83.66  ? 3023 GLY A N     1 
ATOM   11793 C  CA    . GLY A 1 3023 ? 198.784 197.253 215.143 1.00 80.16  ? 3023 GLY A CA    1 
ATOM   11794 C  C     . GLY A 1 3023 ? 198.064 196.529 214.024 1.00 83.06  ? 3023 GLY A C     1 
ATOM   11795 O  O     . GLY A 1 3023 ? 198.368 195.374 213.730 1.00 84.89  ? 3023 GLY A O     1 
ATOM   11796 N  N     . ASP A 1 3024 ? 197.103 197.213 213.400 1.00 84.37  ? 3024 ASP A N     1 
ATOM   11797 C  CA    . ASP A 1 3024 ? 196.394 196.622 212.270 1.00 84.62  ? 3024 ASP A CA    1 
ATOM   11798 C  C     . ASP A 1 3024 ? 197.297 196.469 211.052 1.00 85.09  ? 3024 ASP A C     1 
ATOM   11799 O  O     . ASP A 1 3024 ? 197.110 195.539 210.256 1.00 83.14  ? 3024 ASP A O     1 
ATOM   11800 C  CB    . ASP A 1 3024 ? 195.158 197.457 211.931 1.00 85.13  ? 3024 ASP A CB    1 
ATOM   11801 C  CG    . ASP A 1 3024 ? 195.500 198.872 211.492 1.00 88.94  ? 3024 ASP A CG    1 
ATOM   11802 O  OD1   . ASP A 1 3024 ? 196.695 199.238 211.485 1.00 87.92  ? 3024 ASP A OD1   1 
ATOM   11803 O  OD2   . ASP A 1 3024 ? 194.564 199.625 211.151 1.00 89.11  ? 3024 ASP A OD2   1 
ATOM   11804 N  N     . GLU A 1 3025 ? 198.275 197.366 210.893 1.00 81.79  ? 3025 GLU A N     1 
ATOM   11805 C  CA    . GLU A 1 3025 ? 199.205 197.262 209.773 1.00 77.56  ? 3025 GLU A CA    1 
ATOM   11806 C  C     . GLU A 1 3025 ? 199.972 195.950 209.816 1.00 74.93  ? 3025 GLU A C     1 
ATOM   11807 O  O     . GLU A 1 3025 ? 200.219 195.337 208.773 1.00 77.73  ? 3025 GLU A O     1 
ATOM   11808 C  CB    . GLU A 1 3025 ? 200.172 198.446 209.769 1.00 75.37  ? 3025 GLU A CB    1 
ATOM   11809 C  CG    . GLU A 1 3025 ? 199.510 199.797 209.563 1.00 76.33  ? 3025 GLU A CG    1 
ATOM   11810 C  CD    . GLU A 1 3025 ? 199.162 200.058 208.109 1.00 78.46  ? 3025 GLU A CD    1 
ATOM   11811 O  OE1   . GLU A 1 3025 ? 199.500 199.215 207.252 1.00 76.94  ? 3025 GLU A OE1   1 
ATOM   11812 O  OE2   . GLU A 1 3025 ? 198.553 201.108 207.822 1.00 77.89  ? 3025 GLU A OE2   1 
ATOM   11813 N  N     . TYR A 1 3026 ? 200.355 195.501 211.012 1.00 68.91  ? 3026 TYR A N     1 
ATOM   11814 C  CA    . TYR A 1 3026 ? 201.034 194.215 211.124 1.00 72.03  ? 3026 TYR A CA    1 
ATOM   11815 C  C     . TYR A 1 3026 ? 200.128 193.074 210.684 1.00 76.19  ? 3026 TYR A C     1 
ATOM   11816 O  O     . TYR A 1 3026 ? 200.578 192.144 210.008 1.00 73.66  ? 3026 TYR A O     1 
ATOM   11817 C  CB    . TYR A 1 3026 ? 201.519 193.990 212.554 1.00 70.77  ? 3026 TYR A CB    1 
ATOM   11818 C  CG    . TYR A 1 3026 ? 202.459 192.813 212.686 1.00 70.43  ? 3026 TYR A CG    1 
ATOM   11819 C  CD1   . TYR A 1 3026 ? 203.755 192.878 212.199 1.00 72.39  ? 3026 TYR A CD1   1 
ATOM   11820 C  CD2   . TYR A 1 3026 ? 202.046 191.634 213.289 1.00 70.30  ? 3026 TYR A CD2   1 
ATOM   11821 C  CE1   . TYR A 1 3026 ? 204.614 191.806 212.312 1.00 75.61  ? 3026 TYR A CE1   1 
ATOM   11822 C  CE2   . TYR A 1 3026 ? 202.898 190.557 213.407 1.00 69.97  ? 3026 TYR A CE2   1 
ATOM   11823 C  CZ    . TYR A 1 3026 ? 204.181 190.647 212.918 1.00 73.68  ? 3026 TYR A CZ    1 
ATOM   11824 O  OH    . TYR A 1 3026 ? 205.035 189.575 213.033 1.00 70.88  ? 3026 TYR A OH    1 
ATOM   11825 N  N     . ALA A 1 3027 ? 198.847 193.124 211.056 1.00 78.86  ? 3027 ALA A N     1 
ATOM   11826 C  CA    . ALA A 1 3027 ? 197.919 192.070 210.655 1.00 76.34  ? 3027 ALA A CA    1 
ATOM   11827 C  C     . ALA A 1 3027 ? 197.748 192.032 209.141 1.00 81.04  ? 3027 ALA A C     1 
ATOM   11828 O  O     . ALA A 1 3027 ? 197.762 190.956 208.526 1.00 79.03  ? 3027 ALA A O     1 
ATOM   11829 C  CB    . ALA A 1 3027 ? 196.572 192.269 211.348 1.00 72.45  ? 3027 ALA A CB    1 
ATOM   11830 N  N     . THR A 1 3028 ? 197.581 193.203 208.519 1.00 78.82  ? 3028 THR A N     1 
ATOM   11831 C  CA    . THR A 1 3028 ? 197.462 193.242 207.064 1.00 75.69  ? 3028 THR A CA    1 
ATOM   11832 C  C     . THR A 1 3028 ? 198.737 192.746 206.395 1.00 76.81  ? 3028 THR A C     1 
ATOM   11833 O  O     . THR A 1 3028 ? 198.680 191.963 205.437 1.00 78.05  ? 3028 THR A O     1 
ATOM   11834 C  CB    . THR A 1 3028 ? 197.124 194.657 206.590 1.00 76.87  ? 3028 THR A CB    1 
ATOM   11835 O  OG1   . THR A 1 3028 ? 198.269 195.505 206.746 1.00 77.17  ? 3028 THR A OG1   1 
ATOM   11836 C  CG2   . THR A 1 3028 ? 195.953 195.224 207.376 1.00 76.27  ? 3028 THR A CG2   1 
ATOM   11837 N  N     . LEU A 1 3029 ? 199.898 193.179 206.895 1.00 75.16  ? 3029 LEU A N     1 
ATOM   11838 C  CA    . LEU A 1 3029 ? 201.166 192.696 206.365 1.00 77.15  ? 3029 LEU A CA    1 
ATOM   11839 C  C     . LEU A 1 3029 ? 201.279 191.189 206.485 1.00 76.53  ? 3029 LEU A C     1 
ATOM   11840 O  O     . LEU A 1 3029 ? 201.798 190.532 205.579 1.00 77.76  ? 3029 LEU A O     1 
ATOM   11841 C  CB    . LEU A 1 3029 ? 202.333 193.357 207.097 1.00 73.74  ? 3029 LEU A CB    1 
ATOM   11842 C  CG    . LEU A 1 3029 ? 203.719 192.803 206.752 1.00 72.58  ? 3029 LEU A CG    1 
ATOM   11843 C  CD1   . LEU A 1 3029 ? 204.241 193.393 205.454 1.00 75.09  ? 3029 LEU A CD1   1 
ATOM   11844 C  CD2   . LEU A 1 3029 ? 204.704 193.027 207.891 1.00 73.65  ? 3029 LEU A CD2   1 
ATOM   11845 N  N     . MET A 1 3030 ? 200.796 190.622 207.589 1.00 76.10  ? 3030 MET A N     1 
ATOM   11846 C  CA    . MET A 1 3030 ? 200.979 189.196 207.808 1.00 75.38  ? 3030 MET A CA    1 
ATOM   11847 C  C     . MET A 1 3030 ? 200.056 188.398 206.901 1.00 75.26  ? 3030 MET A C     1 
ATOM   11848 O  O     . MET A 1 3030 ? 200.446 187.356 206.359 1.00 73.40  ? 3030 MET A O     1 
ATOM   11849 C  CB    . MET A 1 3030 ? 200.731 188.863 209.275 1.00 75.08  ? 3030 MET A CB    1 
ATOM   11850 C  CG    . MET A 1 3030 ? 201.879 189.307 210.158 1.00 77.59  ? 3030 MET A CG    1 
ATOM   11851 S  SD    . MET A 1 3030 ? 203.483 188.911 209.459 1.00 79.80  ? 3030 MET A SD    1 
ATOM   11852 C  CE    . MET A 1 3030 ? 203.807 187.393 210.300 1.00 75.54  ? 3030 MET A CE    1 
ATOM   11853 N  N     . THR A 1 3031 ? 198.832 188.892 206.696 1.00 81.17  ? 3031 THR A N     1 
ATOM   11854 C  CA    . THR A 1 3031 ? 197.961 188.287 205.694 1.00 82.07  ? 3031 THR A CA    1 
ATOM   11855 C  C     . THR A 1 3031 ? 198.623 188.302 204.322 1.00 80.46  ? 3031 THR A C     1 
ATOM   11856 O  O     . THR A 1 3031 ? 198.765 187.251 203.680 1.00 77.81  ? 3031 THR A O     1 
ATOM   11857 C  CB    . THR A 1 3031 ? 196.617 189.017 205.648 1.00 79.08  ? 3031 THR A CB    1 
ATOM   11858 O  OG1   . THR A 1 3031 ? 195.970 188.918 206.922 1.00 78.96  ? 3031 THR A OG1   1 
ATOM   11859 C  CG2   . THR A 1 3031 ? 195.720 188.408 204.583 1.00 77.35  ? 3031 THR A CG2   1 
ATOM   11860 N  N     . GLN A 1 3032 ? 199.080 189.481 203.881 1.00 75.93  ? 3032 GLN A N     1 
ATOM   11861 C  CA    . GLN A 1 3032 ? 199.710 189.590 202.568 1.00 71.83  ? 3032 GLN A CA    1 
ATOM   11862 C  C     . GLN A 1 3032 ? 200.931 188.692 202.452 1.00 74.23  ? 3032 GLN A C     1 
ATOM   11863 O  O     . GLN A 1 3032 ? 201.177 188.122 201.386 1.00 73.99  ? 3032 GLN A O     1 
ATOM   11864 C  CB    . GLN A 1 3032 ? 200.099 191.039 202.278 1.00 72.28  ? 3032 GLN A CB    1 
ATOM   11865 C  CG    . GLN A 1 3032 ? 198.974 192.039 202.437 1.00 72.57  ? 3032 GLN A CG    1 
ATOM   11866 C  CD    . GLN A 1 3032 ? 199.337 193.404 201.895 1.00 76.96  ? 3032 GLN A CD    1 
ATOM   11867 O  OE1   . GLN A 1 3032 ? 200.119 193.521 200.952 1.00 79.79  ? 3032 GLN A OE1   1 
ATOM   11868 N  NE2   . GLN A 1 3032 ? 198.775 194.448 202.493 1.00 77.27  ? 3032 GLN A NE2   1 
ATOM   11869 N  N     . CYS A 1 3033 ? 201.705 188.552 203.529 1.00 76.18  ? 3033 CYS A N     1 
ATOM   11870 C  CA    . CYS A 1 3033 ? 202.831 187.627 203.515 1.00 77.31  ? 3033 CYS A CA    1 
ATOM   11871 C  C     . CYS A 1 3033 ? 202.353 186.191 203.355 1.00 78.78  ? 3033 CYS A C     1 
ATOM   11872 O  O     . CYS A 1 3033 ? 203.009 185.382 202.690 1.00 76.70  ? 3033 CYS A O     1 
ATOM   11873 C  CB    . CYS A 1 3033 ? 203.653 187.781 204.793 1.00 76.05  ? 3033 CYS A CB    1 
ATOM   11874 S  SG    . CYS A 1 3033 ? 204.656 189.276 204.850 1.00 83.72  ? 3033 CYS A SG    1 
ATOM   11875 N  N     . LYS A 1 3034 ? 201.213 185.856 203.964 1.00 81.40  ? 3034 LYS A N     1 
ATOM   11876 C  CA    . LYS A 1 3034 ? 200.653 184.521 203.782 1.00 78.73  ? 3034 LYS A CA    1 
ATOM   11877 C  C     . LYS A 1 3034 ? 200.320 184.256 202.318 1.00 79.67  ? 3034 LYS A C     1 
ATOM   11878 O  O     . LYS A 1 3034 ? 200.731 183.229 201.759 1.00 79.03  ? 3034 LYS A O     1 
ATOM   11879 C  CB    . LYS A 1 3034 ? 199.414 184.342 204.660 1.00 80.98  ? 3034 LYS A CB    1 
ATOM   11880 C  CG    . LYS A 1 3034 ? 198.777 182.969 204.552 1.00 80.85  ? 3034 LYS A CG    1 
ATOM   11881 C  CD    . LYS A 1 3034 ? 199.683 181.900 205.141 1.00 81.44  ? 3034 LYS A CD    1 
ATOM   11882 C  CE    . LYS A 1 3034 ? 199.113 180.508 204.925 1.00 81.21  ? 3034 LYS A CE    1 
ATOM   11883 N  NZ    . LYS A 1 3034 ? 197.857 180.292 205.690 1.00 80.99  ? 3034 LYS A NZ    1 
ATOM   11884 N  N     . GLU A 1 3035 ? 199.594 185.176 201.669 1.00 80.51  ? 3035 GLU A N     1 
ATOM   11885 C  CA    . GLU A 1 3035 ? 199.300 184.942 200.251 1.00 80.86  ? 3035 GLU A CA    1 
ATOM   11886 C  C     . GLU A 1 3035 ? 200.568 184.962 199.403 1.00 82.52  ? 3035 GLU A C     1 
ATOM   11887 O  O     . GLU A 1 3035 ? 200.671 184.209 198.430 1.00 82.35  ? 3035 GLU A O     1 
ATOM   11888 C  CB    . GLU A 1 3035 ? 198.270 185.915 199.653 1.00 80.10  ? 3035 GLU A CB    1 
ATOM   11889 C  CG    . GLU A 1 3035 ? 196.821 185.756 200.122 1.00 83.59  ? 3035 GLU A CG    1 
ATOM   11890 C  CD    . GLU A 1 3035 ? 196.473 186.571 201.332 1.00 84.97  ? 3035 GLU A CD    1 
ATOM   11891 O  OE1   . GLU A 1 3035 ? 197.317 187.374 201.747 1.00 85.01  ? 3035 GLU A OE1   1 
ATOM   11892 O  OE2   . GLU A 1 3035 ? 195.360 186.401 201.873 1.00 84.22  ? 3035 GLU A OE2   1 
ATOM   11893 N  N     . GLY A 1 3036 ? 201.542 185.807 199.745 1.00 74.86  ? 3036 GLY A N     1 
ATOM   11894 C  CA    . GLY A 1 3036 ? 202.772 185.844 198.971 1.00 72.56  ? 3036 GLY A CA    1 
ATOM   11895 C  C     . GLY A 1 3036 ? 203.550 184.544 199.045 1.00 75.34  ? 3036 GLY A C     1 
ATOM   11896 O  O     . GLY A 1 3036 ? 204.021 184.029 198.027 1.00 74.21  ? 3036 GLY A O     1 
ATOM   11897 N  N     . ALA A 1 3037 ? 203.691 183.993 200.252 1.00 76.44  ? 3037 ALA A N     1 
ATOM   11898 C  CA    . ALA A 1 3037 ? 204.352 182.704 200.401 1.00 74.10  ? 3037 ALA A CA    1 
ATOM   11899 C  C     . ALA A 1 3037 ? 203.564 181.594 199.723 1.00 76.96  ? 3037 ALA A C     1 
ATOM   11900 O  O     . ALA A 1 3037 ? 204.160 180.653 199.187 1.00 77.08  ? 3037 ALA A O     1 
ATOM   11901 C  CB    . ALA A 1 3037 ? 204.564 182.386 201.880 1.00 75.09  ? 3037 ALA A CB    1 
ATOM   11902 N  N     . GLN A 1 3038 ? 202.230 181.680 199.737 1.00 85.88  ? 3038 GLN A N     1 
ATOM   11903 C  CA    . GLN A 1 3038 ? 201.429 180.704 199.005 1.00 85.73  ? 3038 GLN A CA    1 
ATOM   11904 C  C     . GLN A 1 3038 ? 201.701 180.778 197.507 1.00 85.45  ? 3038 GLN A C     1 
ATOM   11905 O  O     . GLN A 1 3038 ? 201.822 179.745 196.838 1.00 84.26  ? 3038 GLN A O     1 
ATOM   11906 C  CB    . GLN A 1 3038 ? 199.945 180.925 199.298 1.00 85.05  ? 3038 GLN A CB    1 
ATOM   11907 C  CG    . GLN A 1 3038 ? 199.020 179.912 198.652 1.00 87.60  ? 3038 GLN A CG    1 
ATOM   11908 C  CD    . GLN A 1 3038 ? 197.568 180.141 199.018 1.00 88.29  ? 3038 GLN A CD    1 
ATOM   11909 O  OE1   . GLN A 1 3038 ? 197.240 181.082 199.740 1.00 88.31  ? 3038 GLN A OE1   1 
ATOM   11910 N  NE2   . GLN A 1 3038 ? 196.688 179.280 198.521 1.00 83.78  ? 3038 GLN A NE2   1 
ATOM   11911 N  N     . LYS A 1 3039 ? 201.799 181.994 196.963 1.00 81.55  ? 3039 LYS A N     1 
ATOM   11912 C  CA    . LYS A 1 3039 ? 202.098 182.153 195.541 1.00 78.30  ? 3039 LYS A CA    1 
ATOM   11913 C  C     . LYS A 1 3039 ? 203.489 181.633 195.206 1.00 76.86  ? 3039 LYS A C     1 
ATOM   11914 O  O     . LYS A 1 3039 ? 203.691 181.016 194.154 1.00 76.00  ? 3039 LYS A O     1 
ATOM   11915 C  CB    . LYS A 1 3039 ? 201.960 183.619 195.128 1.00 76.23  ? 3039 LYS A CB    1 
ATOM   11916 C  CG    . LYS A 1 3039 ? 200.584 184.212 195.379 1.00 78.88  ? 3039 LYS A CG    1 
ATOM   11917 C  CD    . LYS A 1 3039 ? 200.128 185.082 194.222 1.00 78.03  ? 3039 LYS A CD    1 
ATOM   11918 C  CE    . LYS A 1 3039 ? 200.578 186.521 194.407 1.00 78.80  ? 3039 LYS A CE    1 
ATOM   11919 N  NZ    . LYS A 1 3039 ? 200.287 187.354 193.207 1.00 79.35  ? 3039 LYS A NZ    1 
ATOM   11920 N  N     . GLU A 1 3040 ? 204.465 181.880 196.081 1.00 80.94  ? 3040 GLU A N     1 
ATOM   11921 C  CA    . GLU A 1 3040 ? 205.805 181.351 195.842 1.00 80.69  ? 3040 GLU A CA    1 
ATOM   11922 C  C     . GLU A 1 3040 ? 205.826 179.829 195.909 1.00 80.96  ? 3040 GLU A C     1 
ATOM   11923 O  O     . GLU A 1 3040 ? 206.635 179.189 195.228 1.00 80.54  ? 3040 GLU A O     1 
ATOM   11924 C  CB    . GLU A 1 3040 ? 206.795 181.941 196.848 1.00 78.71  ? 3040 GLU A CB    1 
ATOM   11925 C  CG    . GLU A 1 3040 ? 208.198 181.362 196.749 1.00 79.77  ? 3040 GLU A CG    1 
ATOM   11926 C  CD    . GLU A 1 3040 ? 209.202 182.107 197.602 1.00 84.84  ? 3040 GLU A CD    1 
ATOM   11927 O  OE1   . GLU A 1 3040 ? 208.776 182.898 198.467 1.00 84.83  ? 3040 GLU A OE1   1 
ATOM   11928 O  OE2   . GLU A 1 3040 ? 210.418 181.898 197.409 1.00 82.25  ? 3040 GLU A OE2   1 
ATOM   11929 N  N     . GLY A 1 3041 ? 204.938 179.234 196.700 1.00 83.94  ? 3041 GLY A N     1 
ATOM   11930 C  CA    . GLY A 1 3041 ? 204.893 177.799 196.871 1.00 82.08  ? 3041 GLY A CA    1 
ATOM   11931 C  C     . GLY A 1 3041 ? 205.253 177.302 198.253 1.00 85.68  ? 3041 GLY A C     1 
ATOM   11932 O  O     . GLY A 1 3041 ? 205.399 176.088 198.436 1.00 84.03  ? 3041 GLY A O     1 
ATOM   11933 N  N     . LEU A 1 3042 ? 205.396 178.193 199.229 1.00 90.91  ? 3042 LEU A N     1 
ATOM   11934 C  CA    . LEU A 1 3042 ? 205.729 177.826 200.598 1.00 89.48  ? 3042 LEU A CA    1 
ATOM   11935 C  C     . LEU A 1 3042 ? 204.479 177.921 201.460 1.00 88.34  ? 3042 LEU A C     1 
ATOM   11936 O  O     . LEU A 1 3042 ? 203.778 178.938 201.434 1.00 87.17  ? 3042 LEU A O     1 
ATOM   11937 C  CB    . LEU A 1 3042 ? 206.831 178.729 201.162 1.00 88.44  ? 3042 LEU A CB    1 
ATOM   11938 C  CG    . LEU A 1 3042 ? 208.300 178.418 200.852 1.00 88.40  ? 3042 LEU A CG    1 
ATOM   11939 C  CD1   . LEU A 1 3042 ? 208.692 177.078 201.454 1.00 88.02  ? 3042 LEU A CD1   1 
ATOM   11940 C  CD2   . LEU A 1 3042 ? 208.608 178.453 199.359 1.00 87.11  ? 3042 LEU A CD2   1 
ATOM   11941 N  N     . MET A 1 3043 ? 204.201 176.864 202.214 1.00 91.59  ? 3043 MET A N     1 
ATOM   11942 C  CA    . MET A 1 3043 ? 203.065 176.828 203.131 1.00 91.95  ? 3043 MET A CA    1 
ATOM   11943 C  C     . MET A 1 3043 ? 203.595 177.111 204.531 1.00 92.90  ? 3043 MET A C     1 
ATOM   11944 O  O     . MET A 1 3043 ? 204.037 176.203 205.239 1.00 91.41  ? 3043 MET A O     1 
ATOM   11945 C  CB    . MET A 1 3043 ? 202.344 175.487 203.056 1.00 90.12  ? 3043 MET A CB    1 
ATOM   11946 C  CG    . MET A 1 3043 ? 201.896 175.104 201.654 1.00 91.95  ? 3043 MET A CG    1 
ATOM   11947 S  SD    . MET A 1 3043 ? 201.367 176.528 200.682 1.00 102.27 ? 3043 MET A SD    1 
ATOM   11948 C  CE    . MET A 1 3043 ? 201.378 175.839 199.030 1.00 91.45  ? 3043 MET A CE    1 
ATOM   11949 N  N     . LEU A 1 3044 ? 203.551 178.380 204.924 1.00 81.71  ? 3044 LEU A N     1 
ATOM   11950 C  CA    . LEU A 1 3044 ? 204.037 178.829 206.218 1.00 79.12  ? 3044 LEU A CA    1 
ATOM   11951 C  C     . LEU A 1 3044 ? 202.859 179.284 207.068 1.00 81.02  ? 3044 LEU A C     1 
ATOM   11952 O  O     . LEU A 1 3044 ? 201.934 179.930 206.567 1.00 80.53  ? 3044 LEU A O     1 
ATOM   11953 C  CB    . LEU A 1 3044 ? 205.045 179.967 206.052 1.00 78.87  ? 3044 LEU A CB    1 
ATOM   11954 C  CG    . LEU A 1 3044 ? 206.318 179.666 205.262 1.00 80.88  ? 3044 LEU A CG    1 
ATOM   11955 C  CD1   . LEU A 1 3044 ? 207.126 180.934 205.077 1.00 80.25  ? 3044 LEU A CD1   1 
ATOM   11956 C  CD2   . LEU A 1 3044 ? 207.145 178.601 205.963 1.00 81.11  ? 3044 LEU A CD2   1 
ATOM   11957 N  N     . ASP A 1 3045 ? 202.893 178.942 208.356 1.00 80.34  ? 3045 ASP A N     1 
ATOM   11958 C  CA    . ASP A 1 3045 ? 201.760 179.165 209.245 1.00 81.69  ? 3045 ASP A CA    1 
ATOM   11959 C  C     . ASP A 1 3045 ? 202.058 180.197 210.325 1.00 78.83  ? 3045 ASP A C     1 
ATOM   11960 O  O     . ASP A 1 3045 ? 201.340 181.194 210.442 1.00 74.17  ? 3045 ASP A O     1 
ATOM   11961 C  CB    . ASP A 1 3045 ? 201.335 177.835 209.883 1.00 79.49  ? 3045 ASP A CB    1 
ATOM   11962 C  CG    . ASP A 1 3045 ? 200.574 176.943 208.921 1.00 82.31  ? 3045 ASP A CG    1 
ATOM   11963 O  OD1   . ASP A 1 3045 ? 200.177 177.430 207.842 1.00 81.67  ? 3045 ASP A OD1   1 
ATOM   11964 O  OD2   . ASP A 1 3045 ? 200.376 175.753 209.243 1.00 81.45  ? 3045 ASP A OD2   1 
ATOM   11965 N  N     . SER A 1 3046 ? 203.102 179.987 211.120 1.00 81.95  ? 3046 SER A N     1 
ATOM   11966 C  CA    . SER A 1 3046 ? 203.374 180.856 212.255 1.00 79.85  ? 3046 SER A CA    1 
ATOM   11967 C  C     . SER A 1 3046 ? 203.838 182.229 211.791 1.00 78.64  ? 3046 SER A C     1 
ATOM   11968 O  O     . SER A 1 3046 ? 204.446 182.379 210.729 1.00 77.67  ? 3046 SER A O     1 
ATOM   11969 C  CB    . SER A 1 3046 ? 204.430 180.236 213.170 1.00 76.24  ? 3046 SER A CB    1 
ATOM   11970 O  OG    . SER A 1 3046 ? 205.686 180.161 212.522 1.00 75.01  ? 3046 SER A OG    1 
ATOM   11971 N  N     . HIS A 1 3047 ? 203.535 183.241 212.606 1.00 78.23  ? 3047 HIS A N     1 
ATOM   11972 C  CA    . HIS A 1 3047 ? 203.950 184.602 212.296 1.00 72.75  ? 3047 HIS A CA    1 
ATOM   11973 C  C     . HIS A 1 3047 ? 205.462 184.746 212.202 1.00 73.43  ? 3047 HIS A C     1 
ATOM   11974 O  O     . HIS A 1 3047 ? 205.950 185.552 211.405 1.00 77.24  ? 3047 HIS A O     1 
ATOM   11975 C  CB    . HIS A 1 3047 ? 203.413 185.570 213.349 1.00 76.91  ? 3047 HIS A CB    1 
ATOM   11976 C  CG    . HIS A 1 3047 ? 201.985 185.961 213.139 1.00 80.29  ? 3047 HIS A CG    1 
ATOM   11977 N  ND1   . HIS A 1 3047 ? 201.348 186.895 213.926 1.00 78.75  ? 3047 HIS A ND1   1 
ATOM   11978 C  CD2   . HIS A 1 3047 ? 201.071 185.548 212.229 1.00 76.74  ? 3047 HIS A CD2   1 
ATOM   11979 C  CE1   . HIS A 1 3047 ? 200.102 187.041 213.510 1.00 75.19  ? 3047 HIS A CE1   1 
ATOM   11980 N  NE2   . HIS A 1 3047 ? 199.909 186.235 212.483 1.00 74.53  ? 3047 HIS A NE2   1 
ATOM   11981 N  N     . GLU A 1 3048 ? 206.213 183.987 212.995 1.00 77.46  ? 3048 GLU A N     1 
ATOM   11982 C  CA    . GLU A 1 3048 ? 207.661 184.142 213.009 1.00 74.14  ? 3048 GLU A CA    1 
ATOM   11983 C  C     . GLU A 1 3048 ? 208.262 183.778 211.657 1.00 75.44  ? 3048 GLU A C     1 
ATOM   11984 O  O     . GLU A 1 3048 ? 209.060 184.536 211.094 1.00 78.70  ? 3048 GLU A O     1 
ATOM   11985 C  CB    . GLU A 1 3048 ? 208.240 183.280 214.126 1.00 73.60  ? 3048 GLU A CB    1 
ATOM   11986 C  CG    . GLU A 1 3048 ? 207.707 183.688 215.485 1.00 78.76  ? 3048 GLU A CG    1 
ATOM   11987 C  CD    . GLU A 1 3048 ? 208.220 182.824 216.609 1.00 83.77  ? 3048 GLU A CD    1 
ATOM   11988 O  OE1   . GLU A 1 3048 ? 208.692 181.700 216.334 1.00 80.63  ? 3048 GLU A OE1   1 
ATOM   11989 O  OE2   . GLU A 1 3048 ? 208.134 183.268 217.772 1.00 80.81  ? 3048 GLU A OE2   1 
ATOM   11990 N  N     . GLU A 1 3049 ? 207.859 182.633 211.106 1.00 72.67  ? 3049 GLU A N     1 
ATOM   11991 C  CA    . GLU A 1 3049 ? 208.385 182.201 209.816 1.00 67.19  ? 3049 GLU A CA    1 
ATOM   11992 C  C     . GLU A 1 3049 ? 207.866 183.064 208.670 1.00 68.18  ? 3049 GLU A C     1 
ATOM   11993 O  O     . GLU A 1 3049 ? 208.597 183.302 207.701 1.00 72.18  ? 3049 GLU A O     1 
ATOM   11994 C  CB    . GLU A 1 3049 ? 208.063 180.720 209.608 1.00 66.50  ? 3049 GLU A CB    1 
ATOM   11995 C  CG    . GLU A 1 3049 ? 206.587 180.398 209.493 1.00 73.16  ? 3049 GLU A CG    1 
ATOM   11996 C  CD    . GLU A 1 3049 ? 206.325 178.911 209.361 1.00 76.79  ? 3049 GLU A CD    1 
ATOM   11997 O  OE1   . GLU A 1 3049 ? 207.300 178.131 209.382 1.00 74.46  ? 3049 GLU A OE1   1 
ATOM   11998 O  OE2   . GLU A 1 3049 ? 205.143 178.521 209.260 1.00 74.47  ? 3049 GLU A OE2   1 
ATOM   11999 N  N     . LEU A 1 3050 ? 206.631 183.567 208.768 1.00 64.10  ? 3050 LEU A N     1 
ATOM   12000 C  CA    . LEU A 1 3050 ? 206.150 184.513 207.765 1.00 64.41  ? 3050 LEU A CA    1 
ATOM   12001 C  C     . LEU A 1 3050 ? 206.985 185.786 207.766 1.00 64.36  ? 3050 LEU A C     1 
ATOM   12002 O  O     . LEU A 1 3050 ? 207.334 186.309 206.701 1.00 68.85  ? 3050 LEU A O     1 
ATOM   12003 C  CB    . LEU A 1 3050 ? 204.680 184.858 207.998 1.00 64.86  ? 3050 LEU A CB    1 
ATOM   12004 C  CG    . LEU A 1 3050 ? 203.591 184.084 207.256 1.00 64.20  ? 3050 LEU A CG    1 
ATOM   12005 C  CD1   . LEU A 1 3050 ? 203.577 182.638 207.678 1.00 70.30  ? 3050 LEU A CD1   1 
ATOM   12006 C  CD2   . LEU A 1 3050 ? 202.233 184.725 207.477 1.00 66.23  ? 3050 LEU A CD2   1 
ATOM   12007 N  N     . TYR A 1 3051 ? 207.311 186.306 208.951 1.00 58.12  ? 3051 TYR A N     1 
ATOM   12008 C  CA    . TYR A 1 3051 ? 208.118 187.520 209.014 1.00 55.44  ? 3051 TYR A CA    1 
ATOM   12009 C  C     . TYR A 1 3051 ? 209.540 187.264 208.536 1.00 59.14  ? 3051 TYR A C     1 
ATOM   12010 O  O     . TYR A 1 3051 ? 210.157 188.138 207.918 1.00 65.19  ? 3051 TYR A O     1 
ATOM   12011 C  CB    . TYR A 1 3051 ? 208.125 188.085 210.432 1.00 56.83  ? 3051 TYR A CB    1 
ATOM   12012 C  CG    . TYR A 1 3051 ? 208.600 189.518 210.493 1.00 60.09  ? 3051 TYR A CG    1 
ATOM   12013 C  CD1   . TYR A 1 3051 ? 207.739 190.566 210.207 1.00 60.95  ? 3051 TYR A CD1   1 
ATOM   12014 C  CD2   . TYR A 1 3051 ? 209.914 189.821 210.817 1.00 58.43  ? 3051 TYR A CD2   1 
ATOM   12015 C  CE1   . TYR A 1 3051 ? 208.169 191.876 210.255 1.00 60.55  ? 3051 TYR A CE1   1 
ATOM   12016 C  CE2   . TYR A 1 3051 ? 210.353 191.128 210.867 1.00 56.97  ? 3051 TYR A CE2   1 
ATOM   12017 C  CZ    . TYR A 1 3051 ? 209.476 192.151 210.585 1.00 59.59  ? 3051 TYR A CZ    1 
ATOM   12018 O  OH    . TYR A 1 3051 ? 209.907 193.455 210.633 1.00 57.17  ? 3051 TYR A OH    1 
ATOM   12019 N  N     . LYS A 1 3052 ? 210.083 186.077 208.818 1.00 56.03  ? 3052 LYS A N     1 
ATOM   12020 C  CA    . LYS A 1 3052 ? 211.400 185.738 208.287 1.00 52.58  ? 3052 LYS A CA    1 
ATOM   12021 C  C     . LYS A 1 3052 ? 211.380 185.699 206.763 1.00 58.82  ? 3052 LYS A C     1 
ATOM   12022 O  O     . LYS A 1 3052 ? 212.301 186.205 206.108 1.00 62.20  ? 3052 LYS A O     1 
ATOM   12023 C  CB    . LYS A 1 3052 ? 211.873 184.400 208.852 1.00 52.13  ? 3052 LYS A CB    1 
ATOM   12024 C  CG    . LYS A 1 3052 ? 212.039 184.383 210.360 1.00 55.26  ? 3052 LYS A CG    1 
ATOM   12025 C  CD    . LYS A 1 3052 ? 213.113 185.348 210.821 1.00 66.27  ? 3052 LYS A CD    1 
ATOM   12026 C  CE    . LYS A 1 3052 ? 213.278 185.297 212.331 1.00 66.12  ? 3052 LYS A CE    1 
ATOM   12027 N  NZ    . LYS A 1 3052 ? 214.296 186.268 212.817 1.00 60.71  ? 3052 LYS A NZ    1 
ATOM   12028 N  N     . TRP A 1 3053 ? 210.334 185.106 206.181 1.00 59.96  ? 3053 TRP A N     1 
ATOM   12029 C  CA    . TRP A 1 3053 ? 210.213 185.088 204.727 1.00 58.38  ? 3053 TRP A CA    1 
ATOM   12030 C  C     . TRP A 1 3053 ? 210.075 186.498 204.167 1.00 58.69  ? 3053 TRP A C     1 
ATOM   12031 O  O     . TRP A 1 3053 ? 210.662 186.821 203.127 1.00 67.25  ? 3053 TRP A O     1 
ATOM   12032 C  CB    . TRP A 1 3053 ? 209.022 184.228 204.308 1.00 57.00  ? 3053 TRP A CB    1 
ATOM   12033 C  CG    . TRP A 1 3053 ? 208.777 184.229 202.832 1.00 57.95  ? 3053 TRP A CG    1 
ATOM   12034 C  CD1   . TRP A 1 3053 ? 209.376 183.433 201.903 1.00 54.15  ? 3053 TRP A CD1   1 
ATOM   12035 C  CD2   . TRP A 1 3053 ? 207.863 185.066 202.115 1.00 60.27  ? 3053 TRP A CD2   1 
ATOM   12036 N  NE1   . TRP A 1 3053 ? 208.894 183.723 200.651 1.00 55.47  ? 3053 TRP A NE1   1 
ATOM   12037 C  CE2   . TRP A 1 3053 ? 207.963 184.722 200.754 1.00 61.07  ? 3053 TRP A CE2   1 
ATOM   12038 C  CE3   . TRP A 1 3053 ? 206.969 186.072 202.491 1.00 58.74  ? 3053 TRP A CE3   1 
ATOM   12039 C  CZ2   . TRP A 1 3053 ? 207.204 185.348 199.770 1.00 59.60  ? 3053 TRP A CZ2   1 
ATOM   12040 C  CZ3   . TRP A 1 3053 ? 206.218 186.692 201.512 1.00 59.41  ? 3053 TRP A CZ3   1 
ATOM   12041 C  CH2   . TRP A 1 3053 ? 206.340 186.329 200.168 1.00 60.17  ? 3053 TRP A CH2   1 
ATOM   12042 N  N     . PHE A 1 3054 ? 209.297 187.347 204.838 1.00 53.44  ? 3054 PHE A N     1 
ATOM   12043 C  CA    . PHE A 1 3054 ? 209.146 188.730 204.397 1.00 48.04  ? 3054 PHE A CA    1 
ATOM   12044 C  C     . PHE A 1 3054 ? 210.477 189.467 204.430 1.00 52.79  ? 3054 PHE A C     1 
ATOM   12045 O  O     . PHE A 1 3054 ? 210.808 190.211 203.499 1.00 63.94  ? 3054 PHE A O     1 
ATOM   12046 C  CB    . PHE A 1 3054 ? 208.116 189.439 205.273 1.00 50.59  ? 3054 PHE A CB    1 
ATOM   12047 C  CG    . PHE A 1 3054 ? 208.000 190.912 205.013 1.00 53.58  ? 3054 PHE A CG    1 
ATOM   12048 C  CD1   . PHE A 1 3054 ? 207.426 191.379 203.845 1.00 56.66  ? 3054 PHE A CD1   1 
ATOM   12049 C  CD2   . PHE A 1 3054 ? 208.442 191.830 205.948 1.00 53.30  ? 3054 PHE A CD2   1 
ATOM   12050 C  CE1   . PHE A 1 3054 ? 207.309 192.732 203.610 1.00 56.17  ? 3054 PHE A CE1   1 
ATOM   12051 C  CE2   . PHE A 1 3054 ? 208.328 193.184 205.717 1.00 53.57  ? 3054 PHE A CE2   1 
ATOM   12052 C  CZ    . PHE A 1 3054 ? 207.761 193.635 204.547 1.00 55.66  ? 3054 PHE A CZ    1 
ATOM   12053 N  N     . THR A 1 3055 ? 211.254 189.272 205.497 1.00 48.70  ? 3055 THR A N     1 
ATOM   12054 C  CA    . THR A 1 3055 ? 212.563 189.906 205.591 1.00 48.29  ? 3055 THR A CA    1 
ATOM   12055 C  C     . THR A 1 3055 ? 213.491 189.419 204.486 1.00 45.09  ? 3055 THR A C     1 
ATOM   12056 O  O     . THR A 1 3055 ? 214.213 190.216 203.877 1.00 53.24  ? 3055 THR A O     1 
ATOM   12057 C  CB    . THR A 1 3055 ? 213.175 189.641 206.966 1.00 52.42  ? 3055 THR A CB    1 
ATOM   12058 O  OG1   . THR A 1 3055 ? 212.392 190.298 207.969 1.00 56.48  ? 3055 THR A OG1   1 
ATOM   12059 C  CG2   . THR A 1 3055 ? 214.602 190.157 207.028 1.00 54.52  ? 3055 THR A CG2   1 
ATOM   12060 N  N     . SER A 1 3056 ? 213.483 188.113 204.209 1.00 50.99  ? 3056 SER A N     1 
ATOM   12061 C  CA    . SER A 1 3056 ? 214.310 187.590 203.125 1.00 48.82  ? 3056 SER A CA    1 
ATOM   12062 C  C     . SER A 1 3056 ? 213.897 188.166 201.777 1.00 52.85  ? 3056 SER A C     1 
ATOM   12063 O  O     . SER A 1 3056 ? 214.757 188.490 200.950 1.00 55.66  ? 3056 SER A O     1 
ATOM   12064 C  CB    . SER A 1 3056 ? 214.238 186.065 203.093 1.00 47.66  ? 3056 SER A CB    1 
ATOM   12065 O  OG    . SER A 1 3056 ? 213.020 185.625 202.519 1.00 50.64  ? 3056 SER A OG    1 
ATOM   12066 N  N     . GLN A 1 3057 ? 212.590 188.301 201.542 1.00 53.37  ? 3057 GLN A N     1 
ATOM   12067 C  CA    . GLN A 1 3057 ? 212.114 188.882 200.291 1.00 48.31  ? 3057 GLN A CA    1 
ATOM   12068 C  C     . GLN A 1 3057 ? 212.538 190.339 200.157 1.00 50.09  ? 3057 GLN A C     1 
ATOM   12069 O  O     . GLN A 1 3057 ? 212.962 190.770 199.078 1.00 54.05  ? 3057 GLN A O     1 
ATOM   12070 C  CB    . GLN A 1 3057 ? 210.596 188.754 200.207 1.00 45.97  ? 3057 GLN A CB    1 
ATOM   12071 C  CG    . GLN A 1 3057 ? 210.121 187.362 199.868 1.00 50.94  ? 3057 GLN A CG    1 
ATOM   12072 C  CD    . GLN A 1 3057 ? 210.463 186.965 198.452 1.00 52.27  ? 3057 GLN A CD    1 
ATOM   12073 O  OE1   . GLN A 1 3057 ? 211.403 186.209 198.216 1.00 54.14  ? 3057 GLN A OE1   1 
ATOM   12074 N  NE2   . GLN A 1 3057 ? 209.697 187.473 197.497 1.00 51.75  ? 3057 GLN A NE2   1 
ATOM   12075 N  N     . VAL A 1 3058 ? 212.426 191.113 201.238 1.00 47.32  ? 3058 VAL A N     1 
ATOM   12076 C  CA    . VAL A 1 3058 ? 212.847 192.510 201.192 1.00 42.75  ? 3058 VAL A CA    1 
ATOM   12077 C  C     . VAL A 1 3058 ? 214.348 192.605 200.954 1.00 43.21  ? 3058 VAL A C     1 
ATOM   12078 O  O     . VAL A 1 3058 ? 214.820 193.480 200.218 1.00 54.21  ? 3058 VAL A O     1 
ATOM   12079 C  CB    . VAL A 1 3058 ? 212.429 193.242 202.480 1.00 43.20  ? 3058 VAL A CB    1 
ATOM   12080 C  CG1   . VAL A 1 3058 ? 212.982 194.652 202.488 1.00 46.26  ? 3058 VAL A CG1   1 
ATOM   12081 C  CG2   . VAL A 1 3058 ? 210.919 193.275 202.598 1.00 47.05  ? 3058 VAL A CG2   1 
ATOM   12082 N  N     . ILE A 1 3059 ? 215.120 191.706 201.566 1.00 38.26  ? 3059 ILE A N     1 
ATOM   12083 C  CA    . ILE A 1 3059 ? 216.564 191.687 201.352 1.00 38.88  ? 3059 ILE A CA    1 
ATOM   12084 C  C     . ILE A 1 3059 ? 216.883 191.399 199.892 1.00 44.46  ? 3059 ILE A C     1 
ATOM   12085 O  O     . ILE A 1 3059 ? 217.749 192.043 199.288 1.00 51.82  ? 3059 ILE A O     1 
ATOM   12086 C  CB    . ILE A 1 3059 ? 217.222 190.659 202.291 1.00 39.65  ? 3059 ILE A CB    1 
ATOM   12087 C  CG1   . ILE A 1 3059 ? 217.425 191.256 203.682 1.00 43.45  ? 3059 ILE A CG1   1 
ATOM   12088 C  CG2   . ILE A 1 3059 ? 218.542 190.168 201.721 1.00 41.20  ? 3059 ILE A CG2   1 
ATOM   12089 C  CD1   . ILE A 1 3059 ? 217.999 190.282 204.680 1.00 45.74  ? 3059 ILE A CD1   1 
ATOM   12090 N  N     . ARG A 1 3060 ? 216.181 190.434 199.298 1.00 45.48  ? 3060 ARG A N     1 
ATOM   12091 C  CA    . ARG A 1 3060 ? 216.491 190.032 197.930 1.00 43.48  ? 3060 ARG A CA    1 
ATOM   12092 C  C     . ARG A 1 3060 ? 216.058 191.084 196.915 1.00 47.93  ? 3060 ARG A C     1 
ATOM   12093 O  O     . ARG A 1 3060 ? 216.754 191.313 195.919 1.00 52.05  ? 3060 ARG A O     1 
ATOM   12094 C  CB    . ARG A 1 3060 ? 215.831 188.692 197.618 1.00 43.70  ? 3060 ARG A CB    1 
ATOM   12095 C  CG    . ARG A 1 3060 ? 216.633 187.814 196.682 1.00 47.80  ? 3060 ARG A CG    1 
ATOM   12096 C  CD    . ARG A 1 3060 ? 216.077 186.404 196.645 1.00 52.54  ? 3060 ARG A CD    1 
ATOM   12097 N  NE    . ARG A 1 3060 ? 214.622 186.390 196.715 1.00 52.04  ? 3060 ARG A NE    1 
ATOM   12098 C  CZ    . ARG A 1 3060 ? 213.822 186.427 195.659 1.00 53.41  ? 3060 ARG A CZ    1 
ATOM   12099 N  NH1   . ARG A 1 3060 ? 214.303 186.490 194.429 1.00 51.30  ? 3060 ARG A NH1   1 
ATOM   12100 N  NH2   . ARG A 1 3060 ? 212.505 186.400 195.842 1.00 57.28  ? 3060 ARG A NH2   1 
ATOM   12101 N  N     . ASN A 1 3061 ? 214.918 191.735 197.143 1.00 45.35  ? 3061 ASN A N     1 
ATOM   12102 C  CA    . ASN A 1 3061 ? 214.286 192.549 196.110 1.00 39.99  ? 3061 ASN A CA    1 
ATOM   12103 C  C     . ASN A 1 3061 ? 214.576 194.040 196.226 1.00 42.07  ? 3061 ASN A C     1 
ATOM   12104 O  O     . ASN A 1 3061 ? 214.828 194.691 195.210 1.00 48.79  ? 3061 ASN A O     1 
ATOM   12105 C  CB    . ASN A 1 3061 ? 212.772 192.327 196.126 1.00 43.07  ? 3061 ASN A CB    1 
ATOM   12106 C  CG    . ASN A 1 3061 ? 212.382 190.965 195.598 1.00 44.08  ? 3061 ASN A CG    1 
ATOM   12107 O  OD1   . ASN A 1 3061 ? 212.905 190.507 194.584 1.00 46.28  ? 3061 ASN A OD1   1 
ATOM   12108 N  ND2   . ASN A 1 3061 ? 211.461 190.307 196.287 1.00 47.40  ? 3061 ASN A ND2   1 
ATOM   12109 N  N     . LEU A 1 3062 ? 214.543 194.604 197.429 1.00 39.17  ? 3062 LEU A N     1 
ATOM   12110 C  CA    . LEU A 1 3062 ? 214.663 196.048 197.582 1.00 39.62  ? 3062 LEU A CA    1 
ATOM   12111 C  C     . LEU A 1 3062 ? 216.109 196.500 197.411 1.00 46.62  ? 3062 LEU A C     1 
ATOM   12112 O  O     . LEU A 1 3062 ? 217.014 195.982 198.071 1.00 48.42  ? 3062 LEU A O     1 
ATOM   12113 C  CB    . LEU A 1 3062 ? 214.136 196.484 198.948 1.00 44.98  ? 3062 LEU A CB    1 
ATOM   12114 C  CG    . LEU A 1 3062 ? 214.121 197.993 199.191 1.00 43.71  ? 3062 LEU A CG    1 
ATOM   12115 C  CD1   . LEU A 1 3062 ? 213.478 198.715 198.021 1.00 40.70  ? 3062 LEU A CD1   1 
ATOM   12116 C  CD2   . LEU A 1 3062 ? 213.402 198.320 200.484 1.00 40.18  ? 3062 LEU A CD2   1 
ATOM   12117 N  N     . HIS A 1 3063 ? 216.317 197.469 196.523 1.00 37.49  ? 3063 HIS A N     1 
ATOM   12118 C  CA    . HIS A 1 3063 ? 217.610 198.110 196.320 1.00 34.97  ? 3063 HIS A CA    1 
ATOM   12119 C  C     . HIS A 1 3063 ? 217.466 199.594 196.616 1.00 31.50  ? 3063 HIS A C     1 
ATOM   12120 O  O     . HIS A 1 3063 ? 216.587 200.257 196.058 1.00 49.91  ? 3063 HIS A O     1 
ATOM   12121 C  CB    . HIS A 1 3063 ? 218.120 197.911 194.890 1.00 28.99  ? 3063 HIS A CB    1 
ATOM   12122 C  CG    . HIS A 1 3063 ? 218.336 196.480 194.515 1.00 29.11  ? 3063 HIS A CG    1 
ATOM   12123 N  ND1   . HIS A 1 3063 ? 217.394 195.738 193.838 1.00 40.26  ? 3063 HIS A ND1   1 
ATOM   12124 C  CD2   . HIS A 1 3063 ? 219.389 195.654 194.718 1.00 32.89  ? 3063 HIS A CD2   1 
ATOM   12125 C  CE1   . HIS A 1 3063 ? 217.855 194.516 193.643 1.00 34.31  ? 3063 HIS A CE1   1 
ATOM   12126 N  NE2   . HIS A 1 3063 ? 219.064 194.439 194.168 1.00 40.39  ? 3063 HIS A NE2   1 
ATOM   12127 N  N     . VAL A 1 3064 ? 218.329 200.114 197.482 1.00 30.71  ? 3064 VAL A N     1 
ATOM   12128 C  CA    . VAL A 1 3064 ? 218.270 201.504 197.916 1.00 30.08  ? 3064 VAL A CA    1 
ATOM   12129 C  C     . VAL A 1 3064 ? 219.430 202.254 197.279 1.00 36.90  ? 3064 VAL A C     1 
ATOM   12130 O  O     . VAL A 1 3064 ? 220.594 201.878 197.456 1.00 45.18  ? 3064 VAL A O     1 
ATOM   12131 C  CB    . VAL A 1 3064 ? 218.313 201.623 199.446 1.00 32.74  ? 3064 VAL A CB    1 
ATOM   12132 C  CG1   . VAL A 1 3064 ? 218.568 203.060 199.856 1.00 35.54  ? 3064 VAL A CG1   1 
ATOM   12133 C  CG2   . VAL A 1 3064 ? 217.016 201.118 200.051 1.00 40.41  ? 3064 VAL A CG2   1 
ATOM   12134 N  N     . VAL A 1 3065 ? 219.113 203.313 196.541 1.00 41.07  ? 3065 VAL A N     1 
ATOM   12135 C  CA    . VAL A 1 3065 ? 220.110 204.201 195.954 1.00 34.67  ? 3065 VAL A CA    1 
ATOM   12136 C  C     . VAL A 1 3065 ? 220.036 205.527 196.694 1.00 43.02  ? 3065 VAL A C     1 
ATOM   12137 O  O     . VAL A 1 3065 ? 218.974 206.157 196.747 1.00 50.49  ? 3065 VAL A O     1 
ATOM   12138 C  CB    . VAL A 1 3065 ? 219.886 204.396 194.448 1.00 30.09  ? 3065 VAL A CB    1 
ATOM   12139 C  CG1   . VAL A 1 3065 ? 221.051 205.150 193.839 1.00 41.22  ? 3065 VAL A CG1   1 
ATOM   12140 C  CG2   . VAL A 1 3065 ? 219.701 203.058 193.764 1.00 39.27  ? 3065 VAL A CG2   1 
ATOM   12141 N  N     . PHE A 1 3066 ? 221.158 205.947 197.265 1.00 42.38  ? 3066 PHE A N     1 
ATOM   12142 C  CA    . PHE A 1 3066 ? 221.234 207.167 198.056 1.00 35.41  ? 3066 PHE A CA    1 
ATOM   12143 C  C     . PHE A 1 3066 ? 222.213 208.121 197.388 1.00 39.85  ? 3066 PHE A C     1 
ATOM   12144 O  O     . PHE A 1 3066 ? 223.383 207.778 197.191 1.00 51.32  ? 3066 PHE A O     1 
ATOM   12145 C  CB    . PHE A 1 3066 ? 221.663 206.856 199.490 1.00 36.80  ? 3066 PHE A CB    1 
ATOM   12146 C  CG    . PHE A 1 3066 ? 221.109 207.807 200.508 1.00 48.94  ? 3066 PHE A CG    1 
ATOM   12147 C  CD1   . PHE A 1 3066 ? 221.691 209.046 200.709 1.00 54.28  ? 3066 PHE A CD1   1 
ATOM   12148 C  CD2   . PHE A 1 3066 ? 220.000 207.465 201.261 1.00 50.77  ? 3066 PHE A CD2   1 
ATOM   12149 C  CE1   . PHE A 1 3066 ? 221.182 209.923 201.644 1.00 49.53  ? 3066 PHE A CE1   1 
ATOM   12150 C  CE2   . PHE A 1 3066 ? 219.485 208.337 202.196 1.00 49.47  ? 3066 PHE A CE2   1 
ATOM   12151 C  CZ    . PHE A 1 3066 ? 220.077 209.568 202.388 1.00 50.55  ? 3066 PHE A CZ    1 
ATOM   12152 N  N     . THR A 1 3067 ? 221.736 209.312 197.041 1.00 45.15  ? 3067 THR A N     1 
ATOM   12153 C  CA    . THR A 1 3067 ? 222.537 210.314 196.352 1.00 48.22  ? 3067 THR A CA    1 
ATOM   12154 C  C     . THR A 1 3067 ? 222.737 211.518 197.261 1.00 53.17  ? 3067 THR A C     1 
ATOM   12155 O  O     . THR A 1 3067 ? 221.788 211.978 197.904 1.00 56.90  ? 3067 THR A O     1 
ATOM   12156 C  CB    . THR A 1 3067 ? 221.872 210.742 195.042 1.00 46.46  ? 3067 THR A CB    1 
ATOM   12157 O  OG1   . THR A 1 3067 ? 220.643 211.419 195.328 1.00 60.37  ? 3067 THR A OG1   1 
ATOM   12158 C  CG2   . THR A 1 3067 ? 221.582 209.532 194.172 1.00 41.74  ? 3067 THR A CG2   1 
ATOM   12159 N  N     . MET A 1 3068 ? 223.968 212.020 197.318 1.00 51.16  ? 3068 MET A N     1 
ATOM   12160 C  CA    . MET A 1 3068 ? 224.282 213.168 198.154 1.00 49.46  ? 3068 MET A CA    1 
ATOM   12161 C  C     . MET A 1 3068 ? 225.413 213.963 197.519 1.00 54.72  ? 3068 MET A C     1 
ATOM   12162 O  O     . MET A 1 3068 ? 226.178 213.448 196.700 1.00 54.05  ? 3068 MET A O     1 
ATOM   12163 C  CB    . MET A 1 3068 ? 224.671 212.744 199.574 1.00 49.61  ? 3068 MET A CB    1 
ATOM   12164 C  CG    . MET A 1 3068 ? 225.851 211.792 199.629 1.00 56.85  ? 3068 MET A CG    1 
ATOM   12165 S  SD    . MET A 1 3068 ? 226.643 211.759 201.246 1.00 70.32  ? 3068 MET A SD    1 
ATOM   12166 C  CE    . MET A 1 3068 ? 225.209 211.738 202.312 1.00 54.96  ? 3068 MET A CE    1 
ATOM   12167 N  N     . ASN A 1 3069 ? 225.505 215.231 197.907 1.00 55.66  ? 3069 ASN A N     1 
ATOM   12168 C  CA    . ASN A 1 3069 ? 226.574 216.102 197.449 1.00 52.74  ? 3069 ASN A CA    1 
ATOM   12169 C  C     . ASN A 1 3069 ? 227.859 215.825 198.228 1.00 56.61  ? 3069 ASN A C     1 
ATOM   12170 O  O     . ASN A 1 3069 ? 227.812 215.414 199.390 1.00 56.63  ? 3069 ASN A O     1 
ATOM   12171 C  CB    . ASN A 1 3069 ? 226.172 217.563 197.611 1.00 52.18  ? 3069 ASN A CB    1 
ATOM   12172 C  CG    . ASN A 1 3069 ? 225.163 218.005 196.574 1.00 52.87  ? 3069 ASN A CG    1 
ATOM   12173 O  OD1   . ASN A 1 3069 ? 225.308 217.711 195.389 1.00 53.04  ? 3069 ASN A OD1   1 
ATOM   12174 N  ND2   . ASN A 1 3069 ? 224.132 218.712 197.014 1.00 56.21  ? 3069 ASN A ND2   1 
ATOM   12175 N  N     . PRO A 1 3070 ? 229.023 216.048 197.611 1.00 57.12  ? 3070 PRO A N     1 
ATOM   12176 C  CA    . PRO A 1 3070 ? 230.296 215.689 198.267 1.00 53.39  ? 3070 PRO A CA    1 
ATOM   12177 C  C     . PRO A 1 3070 ? 230.753 216.728 199.285 1.00 61.06  ? 3070 PRO A C     1 
ATOM   12178 O  O     . PRO A 1 3070 ? 231.767 217.414 199.130 1.00 66.26  ? 3070 PRO A O     1 
ATOM   12179 C  CB    . PRO A 1 3070 ? 231.251 215.568 197.077 1.00 51.12  ? 3070 PRO A CB    1 
ATOM   12180 C  CG    . PRO A 1 3070 ? 230.727 216.526 196.081 1.00 52.36  ? 3070 PRO A CG    1 
ATOM   12181 C  CD    . PRO A 1 3070 ? 229.235 216.594 196.260 1.00 57.46  ? 3070 PRO A CD    1 
ATOM   12182 N  N     . SER A 1 3071 ? 229.989 216.854 200.365 1.00 70.96  ? 3071 SER A N     1 
ATOM   12183 C  CA    . SER A 1 3071 ? 230.368 217.736 201.455 1.00 70.99  ? 3071 SER A CA    1 
ATOM   12184 C  C     . SER A 1 3071 ? 231.443 217.083 202.316 1.00 75.45  ? 3071 SER A C     1 
ATOM   12185 O  O     . SER A 1 3071 ? 231.503 215.858 202.451 1.00 76.25  ? 3071 SER A O     1 
ATOM   12186 C  CB    . SER A 1 3071 ? 229.155 218.088 202.314 1.00 68.68  ? 3071 SER A CB    1 
ATOM   12187 O  OG    . SER A 1 3071 ? 229.512 218.983 203.352 1.00 72.81  ? 3071 SER A OG    1 
ATOM   12188 N  N     . SER A 1 3072 ? 232.303 217.919 202.899 1.00 83.96  ? 3072 SER A N     1 
ATOM   12189 C  CA    . SER A 1 3072 ? 233.382 217.403 203.735 1.00 85.12  ? 3072 SER A CA    1 
ATOM   12190 C  C     . SER A 1 3072 ? 232.858 216.980 205.103 1.00 83.45  ? 3072 SER A C     1 
ATOM   12191 O  O     . SER A 1 3072 ? 232.985 215.816 205.499 1.00 78.91  ? 3072 SER A O     1 
ATOM   12192 C  CB    . SER A 1 3072 ? 234.483 218.455 203.876 1.00 83.95  ? 3072 SER A CB    1 
ATOM   12193 O  OG    . SER A 1 3072 ? 234.950 218.874 202.605 1.00 82.20  ? 3072 SER A OG    1 
ATOM   12194 N  N     . GLU A 1 3073 ? 232.264 217.919 205.842 1.00 77.49  ? 3073 GLU A N     1 
ATOM   12195 C  CA    . GLU A 1 3073 ? 231.723 217.598 207.156 1.00 77.56  ? 3073 GLU A CA    1 
ATOM   12196 C  C     . GLU A 1 3073 ? 230.426 216.805 207.070 1.00 80.12  ? 3073 GLU A C     1 
ATOM   12197 O  O     . GLU A 1 3073 ? 230.096 216.079 208.014 1.00 81.81  ? 3073 GLU A O     1 
ATOM   12198 C  CB    . GLU A 1 3073 ? 231.507 218.880 207.963 1.00 80.10  ? 3073 GLU A CB    1 
ATOM   12199 C  CG    . GLU A 1 3073 ? 230.279 219.680 207.560 1.00 81.19  ? 3073 GLU A CG    1 
ATOM   12200 C  CD    . GLU A 1 3073 ? 230.607 220.815 206.610 1.00 83.89  ? 3073 GLU A CD    1 
ATOM   12201 O  OE1   . GLU A 1 3073 ? 231.795 220.974 206.258 1.00 84.22  ? 3073 GLU A OE1   1 
ATOM   12202 O  OE2   . GLU A 1 3073 ? 229.677 221.547 206.213 1.00 81.98  ? 3073 GLU A OE2   1 
ATOM   12203 N  N     . GLY A 1 3074 ? 229.686 216.925 205.967 1.00 74.95  ? 3074 GLY A N     1 
ATOM   12204 C  CA    . GLY A 1 3074 ? 228.459 216.159 205.825 1.00 71.83  ? 3074 GLY A CA    1 
ATOM   12205 C  C     . GLY A 1 3074 ? 228.710 214.665 205.757 1.00 73.70  ? 3074 GLY A C     1 
ATOM   12206 O  O     . GLY A 1 3074 ? 227.952 213.873 206.322 1.00 70.46  ? 3074 GLY A O     1 
ATOM   12207 N  N     . LEU A 1 3075 ? 229.776 214.260 205.063 1.00 71.21  ? 3075 LEU A N     1 
ATOM   12208 C  CA    . LEU A 1 3075 ? 230.133 212.847 205.010 1.00 67.46  ? 3075 LEU A CA    1 
ATOM   12209 C  C     . LEU A 1 3075 ? 230.499 212.319 206.391 1.00 64.41  ? 3075 LEU A C     1 
ATOM   12210 O  O     . LEU A 1 3075 ? 230.099 211.210 206.765 1.00 63.98  ? 3075 LEU A O     1 
ATOM   12211 C  CB    . LEU A 1 3075 ? 231.285 212.637 204.030 1.00 69.70  ? 3075 LEU A CB    1 
ATOM   12212 C  CG    . LEU A 1 3075 ? 231.321 211.289 203.311 1.00 69.86  ? 3075 LEU A CG    1 
ATOM   12213 C  CD1   . LEU A 1 3075 ? 230.037 211.069 202.533 1.00 67.08  ? 3075 LEU A CD1   1 
ATOM   12214 C  CD2   . LEU A 1 3075 ? 232.523 211.216 202.394 1.00 63.86  ? 3075 LEU A CD2   1 
ATOM   12215 N  N     . LYS A 1 3076 ? 231.254 213.099 207.166 1.00 67.69  ? 3076 LYS A N     1 
ATOM   12216 C  CA    . LYS A 1 3076 ? 231.598 212.687 208.522 1.00 66.47  ? 3076 LYS A CA    1 
ATOM   12217 C  C     . LYS A 1 3076 ? 230.359 212.598 209.403 1.00 65.42  ? 3076 LYS A C     1 
ATOM   12218 O  O     . LYS A 1 3076 ? 230.248 211.695 210.240 1.00 70.23  ? 3076 LYS A O     1 
ATOM   12219 C  CB    . LYS A 1 3076 ? 232.618 213.655 209.119 1.00 69.06  ? 3076 LYS A CB    1 
ATOM   12220 C  CG    . LYS A 1 3076 ? 233.781 213.964 208.194 1.00 68.45  ? 3076 LYS A CG    1 
ATOM   12221 C  CD    . LYS A 1 3076 ? 235.078 214.123 208.965 1.00 72.34  ? 3076 LYS A CD    1 
ATOM   12222 C  CE    . LYS A 1 3076 ? 235.968 215.177 208.328 1.00 70.25  ? 3076 LYS A CE    1 
ATOM   12223 N  NZ    . LYS A 1 3076 ? 237.211 215.404 209.113 1.00 69.93  ? 3076 LYS A NZ    1 
ATOM   12224 N  N     . ASP A 1 3077 ? 229.423 213.534 209.238 1.00 64.97  ? 3077 ASP A N     1 
ATOM   12225 C  CA    . ASP A 1 3077 ? 228.179 213.490 210.001 1.00 68.06  ? 3077 ASP A CA    1 
ATOM   12226 C  C     . ASP A 1 3077 ? 227.373 212.240 209.659 1.00 69.67  ? 3077 ASP A C     1 
ATOM   12227 O  O     . ASP A 1 3077 ? 226.851 211.559 210.550 1.00 69.52  ? 3077 ASP A O     1 
ATOM   12228 C  CB    . ASP A 1 3077 ? 227.364 214.756 209.729 1.00 72.31  ? 3077 ASP A CB    1 
ATOM   12229 C  CG    . ASP A 1 3077 ? 226.155 214.891 210.639 1.00 76.71  ? 3077 ASP A CG    1 
ATOM   12230 O  OD1   . ASP A 1 3077 ? 225.915 213.993 211.472 1.00 77.11  ? 3077 ASP A OD1   1 
ATOM   12231 O  OD2   . ASP A 1 3077 ? 225.438 215.905 210.518 1.00 74.55  ? 3077 ASP A OD2   1 
ATOM   12232 N  N     . ARG A 1 3078 ? 227.265 211.921 208.367 1.00 69.03  ? 3078 ARG A N     1 
ATOM   12233 C  CA    . ARG A 1 3078 ? 226.515 210.740 207.954 1.00 68.14  ? 3078 ARG A CA    1 
ATOM   12234 C  C     . ARG A 1 3078 ? 227.221 209.444 208.322 1.00 67.62  ? 3078 ARG A C     1 
ATOM   12235 O  O     . ARG A 1 3078 ? 226.557 208.410 208.453 1.00 67.47  ? 3078 ARG A O     1 
ATOM   12236 C  CB    . ARG A 1 3078 ? 226.249 210.777 206.450 1.00 69.69  ? 3078 ARG A CB    1 
ATOM   12237 C  CG    . ARG A 1 3078 ? 225.432 211.971 206.002 1.00 67.99  ? 3078 ARG A CG    1 
ATOM   12238 C  CD    . ARG A 1 3078 ? 224.007 211.879 206.512 1.00 73.94  ? 3078 ARG A CD    1 
ATOM   12239 N  NE    . ARG A 1 3078 ? 223.211 213.029 206.102 1.00 75.89  ? 3078 ARG A NE    1 
ATOM   12240 C  CZ    . ARG A 1 3078 ? 222.509 213.092 204.980 1.00 75.78  ? 3078 ARG A CZ    1 
ATOM   12241 N  NH1   . ARG A 1 3078 ? 222.467 212.077 204.134 1.00 72.23  ? 3078 ARG A NH1   1 
ATOM   12242 N  NH2   . ARG A 1 3078 ? 221.831 214.201 204.701 1.00 74.26  ? 3078 ARG A NH2   1 
ATOM   12243 N  N     . ALA A 1 3079 ? 228.544 209.470 208.487 1.00 62.98  ? 3079 ALA A N     1 
ATOM   12244 C  CA    . ALA A 1 3079 ? 229.259 208.273 208.913 1.00 61.93  ? 3079 ALA A CA    1 
ATOM   12245 C  C     . ALA A 1 3079 ? 228.868 207.834 210.317 1.00 63.45  ? 3079 ALA A C     1 
ATOM   12246 O  O     . ALA A 1 3079 ? 229.121 206.683 210.685 1.00 66.57  ? 3079 ALA A O     1 
ATOM   12247 C  CB    . ALA A 1 3079 ? 230.768 208.507 208.841 1.00 61.01  ? 3079 ALA A CB    1 
ATOM   12248 N  N     . ALA A 1 3080 ? 228.261 208.718 211.103 1.00 60.01  ? 3080 ALA A N     1 
ATOM   12249 C  CA    . ALA A 1 3080 ? 227.782 208.397 212.442 1.00 62.79  ? 3080 ALA A CA    1 
ATOM   12250 C  C     . ALA A 1 3080 ? 226.267 208.379 212.548 1.00 56.55  ? 3080 ALA A C     1 
ATOM   12251 O  O     . ALA A 1 3080 ? 225.716 207.550 213.273 1.00 57.93  ? 3080 ALA A O     1 
ATOM   12252 C  CB    . ALA A 1 3080 ? 228.346 209.396 213.458 1.00 59.42  ? 3080 ALA A CB    1 
ATOM   12253 N  N     . THR A 1 3081 ? 225.578 209.279 211.844 1.00 58.93  ? 3081 THR A N     1 
ATOM   12254 C  CA    . THR A 1 3081 ? 224.119 209.284 211.887 1.00 57.88  ? 3081 THR A CA    1 
ATOM   12255 C  C     . THR A 1 3081 ? 223.543 208.040 211.223 1.00 61.58  ? 3081 THR A C     1 
ATOM   12256 O  O     . THR A 1 3081 ? 222.544 207.484 211.694 1.00 61.30  ? 3081 THR A O     1 
ATOM   12257 C  CB    . THR A 1 3081 ? 223.578 210.547 211.219 1.00 64.63  ? 3081 THR A CB    1 
ATOM   12258 O  OG1   . THR A 1 3081 ? 224.207 211.698 211.795 1.00 63.29  ? 3081 THR A OG1   1 
ATOM   12259 C  CG2   . THR A 1 3081 ? 222.079 210.651 211.432 1.00 64.32  ? 3081 THR A CG2   1 
ATOM   12260 N  N     . SER A 1 3082 ? 224.148 207.597 210.123 1.00 59.25  ? 3082 SER A N     1 
ATOM   12261 C  CA    . SER A 1 3082 ? 223.741 206.382 209.418 1.00 50.71  ? 3082 SER A CA    1 
ATOM   12262 C  C     . SER A 1 3082 ? 224.984 205.548 209.145 1.00 51.20  ? 3082 SER A C     1 
ATOM   12263 O  O     . SER A 1 3082 ? 225.545 205.589 208.042 1.00 55.03  ? 3082 SER A O     1 
ATOM   12264 C  CB    . SER A 1 3082 ? 222.997 206.711 208.124 1.00 56.24  ? 3082 SER A CB    1 
ATOM   12265 O  OG    . SER A 1 3082 ? 222.373 205.558 207.588 1.00 57.55  ? 3082 SER A OG    1 
ATOM   12266 N  N     . PRO A 1 3083 ? 225.455 204.789 210.137 1.00 52.12  ? 3083 PRO A N     1 
ATOM   12267 C  CA    . PRO A 1 3083 ? 226.652 203.962 209.919 1.00 47.43  ? 3083 PRO A CA    1 
ATOM   12268 C  C     . PRO A 1 3083 ? 226.476 202.896 208.851 1.00 49.66  ? 3083 PRO A C     1 
ATOM   12269 O  O     . PRO A 1 3083 ? 227.471 202.461 208.259 1.00 53.58  ? 3083 PRO A O     1 
ATOM   12270 C  CB    . PRO A 1 3083 ? 226.902 203.343 211.301 1.00 44.32  ? 3083 PRO A CB    1 
ATOM   12271 C  CG    . PRO A 1 3083 ? 225.578 203.391 211.978 1.00 48.74  ? 3083 PRO A CG    1 
ATOM   12272 C  CD    . PRO A 1 3083 ? 224.932 204.651 211.504 1.00 52.97  ? 3083 PRO A CD    1 
ATOM   12273 N  N     . ALA A 1 3084 ? 225.244 202.453 208.590 1.00 49.40  ? 3084 ALA A N     1 
ATOM   12274 C  CA    . ALA A 1 3084 ? 225.022 201.447 207.559 1.00 44.71  ? 3084 ALA A CA    1 
ATOM   12275 C  C     . ALA A 1 3084 ? 225.260 201.994 206.160 1.00 51.35  ? 3084 ALA A C     1 
ATOM   12276 O  O     . ALA A 1 3084 ? 225.457 201.211 205.226 1.00 55.09  ? 3084 ALA A O     1 
ATOM   12277 C  CB    . ALA A 1 3084 ? 223.606 200.883 207.657 1.00 44.24  ? 3084 ALA A CB    1 
ATOM   12278 N  N     . LEU A 1 3085 ? 225.248 203.316 205.993 1.00 51.35  ? 3085 LEU A N     1 
ATOM   12279 C  CA    . LEU A 1 3085 ? 225.490 203.919 204.690 1.00 47.12  ? 3085 LEU A CA    1 
ATOM   12280 C  C     . LEU A 1 3085 ? 226.910 203.697 204.193 1.00 49.34  ? 3085 LEU A C     1 
ATOM   12281 O  O     . LEU A 1 3085 ? 227.169 203.904 203.004 1.00 57.72  ? 3085 LEU A O     1 
ATOM   12282 C  CB    . LEU A 1 3085 ? 225.201 205.419 204.744 1.00 47.47  ? 3085 LEU A CB    1 
ATOM   12283 C  CG    . LEU A 1 3085 ? 223.817 205.898 204.303 1.00 47.05  ? 3085 LEU A CG    1 
ATOM   12284 C  CD1   . LEU A 1 3085 ? 223.730 207.410 204.401 1.00 51.96  ? 3085 LEU A CD1   1 
ATOM   12285 C  CD2   . LEU A 1 3085 ? 223.512 205.438 202.892 1.00 54.13  ? 3085 LEU A CD2   1 
ATOM   12286 N  N     . PHE A 1 3086 ? 227.830 203.283 205.062 1.00 47.07  ? 3086 PHE A N     1 
ATOM   12287 C  CA    . PHE A 1 3086 ? 229.229 203.149 204.694 1.00 53.17  ? 3086 PHE A CA    1 
ATOM   12288 C  C     . PHE A 1 3086 ? 229.775 201.738 204.848 1.00 58.36  ? 3086 PHE A C     1 
ATOM   12289 O  O     . PHE A 1 3086 ? 230.917 201.494 204.445 1.00 57.55  ? 3086 PHE A O     1 
ATOM   12290 C  CB    . PHE A 1 3086 ? 230.088 204.121 205.518 1.00 51.90  ? 3086 PHE A CB    1 
ATOM   12291 C  CG    . PHE A 1 3086 ? 229.805 205.565 205.223 1.00 57.15  ? 3086 PHE A CG    1 
ATOM   12292 C  CD1   . PHE A 1 3086 ? 228.741 206.213 205.827 1.00 53.89  ? 3086 PHE A CD1   1 
ATOM   12293 C  CD2   . PHE A 1 3086 ? 230.590 206.270 204.329 1.00 58.16  ? 3086 PHE A CD2   1 
ATOM   12294 C  CE1   . PHE A 1 3086 ? 228.471 207.537 205.549 1.00 53.82  ? 3086 PHE A CE1   1 
ATOM   12295 C  CE2   . PHE A 1 3086 ? 230.325 207.595 204.050 1.00 53.91  ? 3086 PHE A CE2   1 
ATOM   12296 C  CZ    . PHE A 1 3086 ? 229.265 208.229 204.662 1.00 54.96  ? 3086 PHE A CZ    1 
ATOM   12297 N  N     . ASN A 1 3087 ? 229.007 200.808 205.412 1.00 49.25  ? 3087 ASN A N     1 
ATOM   12298 C  CA    . ASN A 1 3087 ? 229.403 199.410 205.463 1.00 50.25  ? 3087 ASN A CA    1 
ATOM   12299 C  C     . ASN A 1 3087 ? 228.353 198.456 204.914 1.00 52.28  ? 3087 ASN A C     1 
ATOM   12300 O  O     . ASN A 1 3087 ? 228.629 197.256 204.812 1.00 55.61  ? 3087 ASN A O     1 
ATOM   12301 C  CB    . ASN A 1 3087 ? 229.777 199.006 206.900 1.00 48.65  ? 3087 ASN A CB    1 
ATOM   12302 C  CG    . ASN A 1 3087 ? 228.612 199.099 207.867 1.00 58.70  ? 3087 ASN A CG    1 
ATOM   12303 O  OD1   . ASN A 1 3087 ? 227.473 199.347 207.477 1.00 64.23  ? 3087 ASN A OD1   1 
ATOM   12304 N  ND2   . ASN A 1 3087 ? 228.899 198.903 209.147 1.00 58.19  ? 3087 ASN A ND2   1 
ATOM   12305 N  N     . ARG A 1 3088 ? 227.162 198.947 204.565 1.00 43.78  ? 3088 ARG A N     1 
ATOM   12306 C  CA    . ARG A 1 3088 ? 226.169 198.156 203.854 1.00 45.05  ? 3088 ARG A CA    1 
ATOM   12307 C  C     . ARG A 1 3088 ? 225.912 198.652 202.440 1.00 48.66  ? 3088 ARG A C     1 
ATOM   12308 O  O     . ARG A 1 3088 ? 225.419 197.879 201.613 1.00 54.40  ? 3088 ARG A O     1 
ATOM   12309 C  CB    . ARG A 1 3088 ? 224.838 198.139 204.620 1.00 47.10  ? 3088 ARG A CB    1 
ATOM   12310 C  CG    . ARG A 1 3088 ? 224.933 197.618 206.043 1.00 51.29  ? 3088 ARG A CG    1 
ATOM   12311 C  CD    . ARG A 1 3088 ? 225.722 196.322 206.107 1.00 52.24  ? 3088 ARG A CD    1 
ATOM   12312 N  NE    . ARG A 1 3088 ? 225.310 195.489 207.230 1.00 55.68  ? 3088 ARG A NE    1 
ATOM   12313 C  CZ    . ARG A 1 3088 ? 224.752 194.293 207.109 1.00 59.48  ? 3088 ARG A CZ    1 
ATOM   12314 N  NH1   . ARG A 1 3088 ? 224.531 193.750 205.923 1.00 52.64  ? 3088 ARG A NH1   1 
ATOM   12315 N  NH2   . ARG A 1 3088 ? 224.405 193.625 208.205 1.00 55.76  ? 3088 ARG A NH2   1 
ATOM   12316 N  N     . CYS A 1 3089 ? 226.230 199.906 202.146 1.00 45.80  ? 3089 CYS A N     1 
ATOM   12317 C  CA    . CYS A 1 3089 ? 226.112 200.469 200.812 1.00 38.60  ? 3089 CYS A CA    1 
ATOM   12318 C  C     . CYS A 1 3089 ? 227.446 200.383 200.083 1.00 44.80  ? 3089 CYS A C     1 
ATOM   12319 O  O     . CYS A 1 3089 ? 228.506 200.219 200.690 1.00 50.81  ? 3089 CYS A O     1 
ATOM   12320 C  CB    . CYS A 1 3089 ? 225.650 201.926 200.877 1.00 34.56  ? 3089 CYS A CB    1 
ATOM   12321 S  SG    . CYS A 1 3089 ? 223.937 202.148 201.376 1.00 53.15  ? 3089 CYS A SG    1 
ATOM   12322 N  N     . VAL A 1 3090 ? 227.379 200.496 198.762 1.00 37.12  ? 3090 VAL A N     1 
ATOM   12323 C  CA    . VAL A 1 3090 ? 228.562 200.525 197.913 1.00 32.66  ? 3090 VAL A CA    1 
ATOM   12324 C  C     . VAL A 1 3090 ? 228.785 201.972 197.501 1.00 38.22  ? 3090 VAL A C     1 
ATOM   12325 O  O     . VAL A 1 3090 ? 228.045 202.515 196.675 1.00 46.75  ? 3090 VAL A O     1 
ATOM   12326 C  CB    . VAL A 1 3090 ? 228.408 199.609 196.694 1.00 29.76  ? 3090 VAL A CB    1 
ATOM   12327 C  CG1   . VAL A 1 3090 ? 229.582 199.785 195.749 1.00 30.02  ? 3090 VAL A CG1   1 
ATOM   12328 C  CG2   . VAL A 1 3090 ? 228.293 198.166 197.138 1.00 40.84  ? 3090 VAL A CG2   1 
ATOM   12329 N  N     . LEU A 1 3091 ? 229.801 202.603 198.080 1.00 37.42  ? 3091 LEU A N     1 
ATOM   12330 C  CA    . LEU A 1 3091 ? 230.069 204.008 197.817 1.00 30.53  ? 3091 LEU A CA    1 
ATOM   12331 C  C     . LEU A 1 3091 ? 230.703 204.167 196.443 1.00 38.99  ? 3091 LEU A C     1 
ATOM   12332 O  O     . LEU A 1 3091 ? 231.688 203.497 196.121 1.00 42.76  ? 3091 LEU A O     1 
ATOM   12333 C  CB    . LEU A 1 3091 ? 230.983 204.586 198.897 1.00 33.48  ? 3091 LEU A CB    1 
ATOM   12334 C  CG    . LEU A 1 3091 ? 231.072 206.109 199.032 1.00 36.57  ? 3091 LEU A CG    1 
ATOM   12335 C  CD1   . LEU A 1 3091 ? 231.376 206.481 200.467 1.00 42.16  ? 3091 LEU A CD1   1 
ATOM   12336 C  CD2   . LEU A 1 3091 ? 232.121 206.697 198.108 1.00 37.13  ? 3091 LEU A CD2   1 
ATOM   12337 N  N     . ASN A 1 3092 ? 230.134 205.058 195.636 1.00 40.08  ? 3092 ASN A N     1 
ATOM   12338 C  CA    . ASN A 1 3092 ? 230.680 205.407 194.329 1.00 35.21  ? 3092 ASN A CA    1 
ATOM   12339 C  C     . ASN A 1 3092 ? 230.818 206.920 194.275 1.00 38.30  ? 3092 ASN A C     1 
ATOM   12340 O  O     . ASN A 1 3092 ? 229.816 207.639 194.332 1.00 43.06  ? 3092 ASN A O     1 
ATOM   12341 C  CB    . ASN A 1 3092 ? 229.789 204.898 193.198 1.00 31.52  ? 3092 ASN A CB    1 
ATOM   12342 C  CG    . ASN A 1 3092 ? 230.043 203.444 192.867 1.00 43.94  ? 3092 ASN A CG    1 
ATOM   12343 O  OD1   . ASN A 1 3092 ? 231.041 202.864 193.290 1.00 49.01  ? 3092 ASN A OD1   1 
ATOM   12344 N  ND2   . ASN A 1 3092 ? 229.138 202.846 192.106 1.00 52.70  ? 3092 ASN A ND2   1 
ATOM   12345 N  N     . TRP A 1 3093 ? 232.051 207.402 194.173 1.00 33.14  ? 3093 TRP A N     1 
ATOM   12346 C  CA    . TRP A 1 3093 ? 232.309 208.837 194.113 1.00 28.71  ? 3093 TRP A CA    1 
ATOM   12347 C  C     . TRP A 1 3093 ? 232.197 209.292 192.665 1.00 38.55  ? 3093 TRP A C     1 
ATOM   12348 O  O     . TRP A 1 3093 ? 233.145 209.169 191.886 1.00 46.92  ? 3093 TRP A O     1 
ATOM   12349 C  CB    . TRP A 1 3093 ? 233.679 209.167 194.689 1.00 35.85  ? 3093 TRP A CB    1 
ATOM   12350 C  CG    . TRP A 1 3093 ? 233.781 210.574 195.166 1.00 38.03  ? 3093 TRP A CG    1 
ATOM   12351 C  CD1   . TRP A 1 3093 ? 234.047 211.676 194.412 1.00 39.09  ? 3093 TRP A CD1   1 
ATOM   12352 C  CD2   . TRP A 1 3093 ? 233.607 211.038 196.507 1.00 37.26  ? 3093 TRP A CD2   1 
ATOM   12353 N  NE1   . TRP A 1 3093 ? 234.054 212.798 195.200 1.00 33.73  ? 3093 TRP A NE1   1 
ATOM   12354 C  CE2   . TRP A 1 3093 ? 233.785 212.433 196.492 1.00 36.63  ? 3093 TRP A CE2   1 
ATOM   12355 C  CE3   . TRP A 1 3093 ? 233.318 210.409 197.720 1.00 36.94  ? 3093 TRP A CE3   1 
ATOM   12356 C  CZ2   . TRP A 1 3093 ? 233.690 213.208 197.642 1.00 38.02  ? 3093 TRP A CZ2   1 
ATOM   12357 C  CZ3   . TRP A 1 3093 ? 233.221 211.181 198.859 1.00 41.67  ? 3093 TRP A CZ3   1 
ATOM   12358 C  CH2   . TRP A 1 3093 ? 233.405 212.565 198.813 1.00 39.46  ? 3093 TRP A CH2   1 
ATOM   12359 N  N     . PHE A 1 3094 ? 231.028 209.815 192.296 1.00 36.54  ? 3094 PHE A N     1 
ATOM   12360 C  CA    . PHE A 1 3094 ? 230.866 210.385 190.965 1.00 31.50  ? 3094 PHE A CA    1 
ATOM   12361 C  C     . PHE A 1 3094 ? 231.666 211.674 190.829 1.00 40.26  ? 3094 PHE A C     1 
ATOM   12362 O  O     . PHE A 1 3094 ? 232.492 211.813 189.920 1.00 45.12  ? 3094 PHE A O     1 
ATOM   12363 C  CB    . PHE A 1 3094 ? 229.387 210.643 190.676 1.00 37.75  ? 3094 PHE A CB    1 
ATOM   12364 C  CG    . PHE A 1 3094 ? 228.628 209.429 190.220 1.00 40.05  ? 3094 PHE A CG    1 
ATOM   12365 C  CD1   . PHE A 1 3094 ? 228.995 208.161 190.634 1.00 44.32  ? 3094 PHE A CD1   1 
ATOM   12366 C  CD2   . PHE A 1 3094 ? 227.542 209.561 189.373 1.00 40.02  ? 3094 PHE A CD2   1 
ATOM   12367 C  CE1   . PHE A 1 3094 ? 228.294 207.050 190.212 1.00 45.03  ? 3094 PHE A CE1   1 
ATOM   12368 C  CE2   . PHE A 1 3094 ? 226.838 208.453 188.948 1.00 44.30  ? 3094 PHE A CE2   1 
ATOM   12369 C  CZ    . PHE A 1 3094 ? 227.214 207.197 189.369 1.00 49.45  ? 3094 PHE A CZ    1 
ATOM   12370 N  N     . GLY A 1 3095 ? 231.440 212.623 191.733 1.00 37.31  ? 3095 GLY A N     1 
ATOM   12371 C  CA    . GLY A 1 3095 ? 232.115 213.899 191.679 1.00 33.07  ? 3095 GLY A CA    1 
ATOM   12372 C  C     . GLY A 1 3095 ? 231.594 214.763 190.542 1.00 44.22  ? 3095 GLY A C     1 
ATOM   12373 O  O     . GLY A 1 3095 ? 230.631 214.437 189.850 1.00 50.10  ? 3095 GLY A O     1 
ATOM   12374 N  N     . ASP A 1 3096 ? 232.264 215.895 190.361 1.00 45.12  ? 3096 ASP A N     1 
ATOM   12375 C  CA    . ASP A 1 3096 ? 231.962 216.764 189.238 1.00 41.56  ? 3096 ASP A CA    1 
ATOM   12376 C  C     . ASP A 1 3096 ? 232.510 216.158 187.951 1.00 39.67  ? 3096 ASP A C     1 
ATOM   12377 O  O     . ASP A 1 3096 ? 233.431 215.336 187.965 1.00 39.70  ? 3096 ASP A O     1 
ATOM   12378 C  CB    . ASP A 1 3096 ? 232.546 218.160 189.464 1.00 42.95  ? 3096 ASP A CB    1 
ATOM   12379 C  CG    . ASP A 1 3096 ? 231.954 219.205 188.533 1.00 55.17  ? 3096 ASP A CG    1 
ATOM   12380 O  OD1   . ASP A 1 3096 ? 231.976 218.999 187.301 1.00 48.92  ? 3096 ASP A OD1   1 
ATOM   12381 O  OD2   . ASP A 1 3096 ? 231.466 220.239 189.035 1.00 54.56  ? 3096 ASP A OD2   1 
ATOM   12382 N  N     . TRP A 1 3097 ? 231.918 216.560 186.829 1.00 38.37  ? 3097 TRP A N     1 
ATOM   12383 C  CA    . TRP A 1 3097 ? 232.417 216.123 185.534 1.00 38.69  ? 3097 TRP A CA    1 
ATOM   12384 C  C     . TRP A 1 3097 ? 233.863 216.565 185.363 1.00 41.71  ? 3097 TRP A C     1 
ATOM   12385 O  O     . TRP A 1 3097 ? 234.194 217.738 185.557 1.00 42.35  ? 3097 TRP A O     1 
ATOM   12386 C  CB    . TRP A 1 3097 ? 231.556 216.691 184.407 1.00 32.26  ? 3097 TRP A CB    1 
ATOM   12387 C  CG    . TRP A 1 3097 ? 230.192 216.093 184.313 1.00 39.61  ? 3097 TRP A CG    1 
ATOM   12388 C  CD1   . TRP A 1 3097 ? 229.646 215.163 185.143 1.00 42.93  ? 3097 TRP A CD1   1 
ATOM   12389 C  CD2   . TRP A 1 3097 ? 229.195 216.388 183.329 1.00 41.06  ? 3097 TRP A CD2   1 
ATOM   12390 N  NE1   . TRP A 1 3097 ? 228.369 214.859 184.739 1.00 35.93  ? 3097 TRP A NE1   1 
ATOM   12391 C  CE2   . TRP A 1 3097 ? 228.069 215.598 183.627 1.00 32.89  ? 3097 TRP A CE2   1 
ATOM   12392 C  CE3   . TRP A 1 3097 ? 229.144 217.245 182.227 1.00 39.17  ? 3097 TRP A CE3   1 
ATOM   12393 C  CZ2   . TRP A 1 3097 ? 226.907 215.638 182.862 1.00 33.62  ? 3097 TRP A CZ2   1 
ATOM   12394 C  CZ3   . TRP A 1 3097 ? 227.990 217.283 181.470 1.00 40.43  ? 3097 TRP A CZ3   1 
ATOM   12395 C  CH2   . TRP A 1 3097 ? 226.888 216.484 181.790 1.00 35.93  ? 3097 TRP A CH2   1 
ATOM   12396 N  N     . SER A 1 3098 ? 234.725 215.622 185.001 1.00 45.70  ? 3098 SER A N     1 
ATOM   12397 C  CA    . SER A 1 3098 ? 236.129 215.941 184.824 1.00 45.03  ? 3098 SER A CA    1 
ATOM   12398 C  C     . SER A 1 3098 ? 236.328 216.759 183.552 1.00 46.55  ? 3098 SER A C     1 
ATOM   12399 O  O     . SER A 1 3098 ? 235.398 216.995 182.776 1.00 49.50  ? 3098 SER A O     1 
ATOM   12400 C  CB    . SER A 1 3098 ? 236.965 214.663 184.779 1.00 51.27  ? 3098 SER A CB    1 
ATOM   12401 O  OG    . SER A 1 3098 ? 236.617 213.868 183.660 1.00 51.50  ? 3098 SER A OG    1 
ATOM   12402 N  N     . THR A 1 3099 ? 237.568 217.205 183.347 1.00 50.11  ? 3099 THR A N     1 
ATOM   12403 C  CA    . THR A 1 3099 ? 237.892 217.948 182.135 1.00 40.43  ? 3099 THR A CA    1 
ATOM   12404 C  C     . THR A 1 3099 ? 237.656 217.094 180.896 1.00 46.13  ? 3099 THR A C     1 
ATOM   12405 O  O     . THR A 1 3099 ? 237.194 217.594 179.865 1.00 54.01  ? 3099 THR A O     1 
ATOM   12406 C  CB    . THR A 1 3099 ? 239.339 218.436 182.192 1.00 45.34  ? 3099 THR A CB    1 
ATOM   12407 O  OG1   . THR A 1 3099 ? 239.498 219.326 183.303 1.00 50.53  ? 3099 THR A OG1   1 
ATOM   12408 C  CG2   . THR A 1 3099 ? 239.708 219.170 180.918 1.00 49.66  ? 3099 THR A CG2   1 
ATOM   12409 N  N     . GLU A 1 3100 ? 237.958 215.797 180.983 1.00 49.41  ? 3100 GLU A N     1 
ATOM   12410 C  CA    . GLU A 1 3100 ? 237.666 214.895 179.874 1.00 47.00  ? 3100 GLU A CA    1 
ATOM   12411 C  C     . GLU A 1 3100 ? 236.168 214.799 179.623 1.00 46.17  ? 3100 GLU A C     1 
ATOM   12412 O  O     . GLU A 1 3100 ? 235.723 214.797 178.469 1.00 51.85  ? 3100 GLU A O     1 
ATOM   12413 C  CB    . GLU A 1 3100 ? 238.253 213.513 180.154 1.00 52.65  ? 3100 GLU A CB    1 
ATOM   12414 C  CG    . GLU A 1 3100 ? 238.067 212.523 179.017 1.00 57.27  ? 3100 GLU A CG    1 
ATOM   12415 C  CD    . GLU A 1 3100 ? 238.703 211.178 179.301 1.00 60.60  ? 3100 GLU A CD    1 
ATOM   12416 O  OE1   . GLU A 1 3100 ? 239.274 211.008 180.399 1.00 60.74  ? 3100 GLU A OE1   1 
ATOM   12417 O  OE2   . GLU A 1 3100 ? 238.634 210.290 178.426 1.00 56.66  ? 3100 GLU A OE2   1 
ATOM   12418 N  N     . ALA A 1 3101 ? 235.372 214.720 180.692 1.00 45.99  ? 3101 ALA A N     1 
ATOM   12419 C  CA    . ALA A 1 3101 ? 233.924 214.649 180.534 1.00 42.35  ? 3101 ALA A CA    1 
ATOM   12420 C  C     . ALA A 1 3101 ? 233.372 215.922 179.907 1.00 43.22  ? 3101 ALA A C     1 
ATOM   12421 O  O     . ALA A 1 3101 ? 232.529 215.863 179.005 1.00 48.42  ? 3101 ALA A O     1 
ATOM   12422 C  CB    . ALA A 1 3101 ? 233.263 214.388 181.886 1.00 44.73  ? 3101 ALA A CB    1 
ATOM   12423 N  N     . LEU A 1 3102 ? 233.838 217.084 180.372 1.00 45.86  ? 3102 LEU A N     1 
ATOM   12424 C  CA    . LEU A 1 3102 ? 233.398 218.348 179.791 1.00 33.39  ? 3102 LEU A CA    1 
ATOM   12425 C  C     . LEU A 1 3102 ? 233.796 218.448 178.326 1.00 32.98  ? 3102 LEU A C     1 
ATOM   12426 O  O     . LEU A 1 3102 ? 232.999 218.887 177.489 1.00 43.58  ? 3102 LEU A O     1 
ATOM   12427 C  CB    . LEU A 1 3102 ? 233.980 219.521 180.579 1.00 32.58  ? 3102 LEU A CB    1 
ATOM   12428 C  CG    . LEU A 1 3102 ? 233.563 219.680 182.038 1.00 29.87  ? 3102 LEU A CG    1 
ATOM   12429 C  CD1   . LEU A 1 3102 ? 234.308 220.838 182.668 1.00 38.88  ? 3102 LEU A CD1   1 
ATOM   12430 C  CD2   . LEU A 1 3102 ? 232.067 219.890 182.144 1.00 33.31  ? 3102 LEU A CD2   1 
ATOM   12431 N  N     . TYR A 1 3103 ? 235.025 218.043 177.998 1.00 32.16  ? 3103 TYR A N     1 
ATOM   12432 C  CA    . TYR A 1 3103 ? 235.469 218.083 176.611 1.00 38.97  ? 3103 TYR A CA    1 
ATOM   12433 C  C     . TYR A 1 3103 ? 234.619 217.179 175.733 1.00 42.83  ? 3103 TYR A C     1 
ATOM   12434 O  O     . TYR A 1 3103 ? 234.231 217.566 174.626 1.00 45.89  ? 3103 TYR A O     1 
ATOM   12435 C  CB    . TYR A 1 3103 ? 236.939 217.682 176.515 1.00 43.76  ? 3103 TYR A CB    1 
ATOM   12436 C  CG    . TYR A 1 3103 ? 237.469 217.685 175.100 1.00 48.58  ? 3103 TYR A CG    1 
ATOM   12437 C  CD1   . TYR A 1 3103 ? 237.933 218.854 174.516 1.00 42.65  ? 3103 TYR A CD1   1 
ATOM   12438 C  CD2   . TYR A 1 3103 ? 237.500 216.521 174.346 1.00 53.28  ? 3103 TYR A CD2   1 
ATOM   12439 C  CE1   . TYR A 1 3103 ? 238.411 218.863 173.225 1.00 44.84  ? 3103 TYR A CE1   1 
ATOM   12440 C  CE2   . TYR A 1 3103 ? 237.978 216.521 173.054 1.00 46.24  ? 3103 TYR A CE2   1 
ATOM   12441 C  CZ    . TYR A 1 3103 ? 238.431 217.694 172.499 1.00 50.25  ? 3103 TYR A CZ    1 
ATOM   12442 O  OH    . TYR A 1 3103 ? 238.909 217.698 171.210 1.00 61.48  ? 3103 TYR A OH    1 
ATOM   12443 N  N     . GLN A 1 3104 ? 234.323 215.968 176.206 1.00 47.91  ? 3104 GLN A N     1 
ATOM   12444 C  CA    . GLN A 1 3104 ? 233.522 215.046 175.411 1.00 43.67  ? 3104 GLN A CA    1 
ATOM   12445 C  C     . GLN A 1 3104 ? 232.101 215.562 175.225 1.00 41.81  ? 3104 GLN A C     1 
ATOM   12446 O  O     . GLN A 1 3104 ? 231.546 215.472 174.125 1.00 54.42  ? 3104 GLN A O     1 
ATOM   12447 C  CB    . GLN A 1 3104 ? 233.518 213.665 176.060 1.00 46.83  ? 3104 GLN A CB    1 
ATOM   12448 C  CG    . GLN A 1 3104 ? 234.852 212.951 175.974 1.00 44.55  ? 3104 GLN A CG    1 
ATOM   12449 C  CD    . GLN A 1 3104 ? 234.769 211.518 176.443 1.00 52.31  ? 3104 GLN A CD    1 
ATOM   12450 O  OE1   . GLN A 1 3104 ? 235.446 211.125 177.391 1.00 54.07  ? 3104 GLN A OE1   1 
ATOM   12451 N  NE2   . GLN A 1 3104 ? 233.934 210.727 175.782 1.00 49.94  ? 3104 GLN A NE2   1 
ATOM   12452 N  N     . VAL A 1 3105 ? 231.499 216.115 176.282 1.00 30.11  ? 3105 VAL A N     1 
ATOM   12453 C  CA    . VAL A 1 3105 ? 230.152 216.667 176.158 1.00 37.94  ? 3105 VAL A CA    1 
ATOM   12454 C  C     . VAL A 1 3105 ? 230.134 217.820 175.164 1.00 43.61  ? 3105 VAL A C     1 
ATOM   12455 O  O     . VAL A 1 3105 ? 229.252 217.900 174.298 1.00 46.38  ? 3105 VAL A O     1 
ATOM   12456 C  CB    . VAL A 1 3105 ? 229.618 217.103 177.535 1.00 40.22  ? 3105 VAL A CB    1 
ATOM   12457 C  CG1   . VAL A 1 3105 ? 228.323 217.873 177.376 1.00 41.93  ? 3105 VAL A CG1   1 
ATOM   12458 C  CG2   . VAL A 1 3105 ? 229.396 215.898 178.418 1.00 39.64  ? 3105 VAL A CG2   1 
ATOM   12459 N  N     . GLY A 1 3106 ? 231.106 218.729 175.267 1.00 41.95  ? 3106 GLY A N     1 
ATOM   12460 C  CA    . GLY A 1 3106 ? 231.156 219.845 174.339 1.00 38.97  ? 3106 GLY A CA    1 
ATOM   12461 C  C     . GLY A 1 3106 ? 231.370 219.403 172.905 1.00 42.51  ? 3106 GLY A C     1 
ATOM   12462 O  O     . GLY A 1 3106 ? 230.701 219.892 171.990 1.00 50.70  ? 3106 GLY A O     1 
ATOM   12463 N  N     . LYS A 1 3107 ? 232.287 218.458 172.690 1.00 42.24  ? 3107 LYS A N     1 
ATOM   12464 C  CA    . LYS A 1 3107 ? 232.562 217.986 171.339 1.00 39.89  ? 3107 LYS A CA    1 
ATOM   12465 C  C     . LYS A 1 3107 ? 231.354 217.275 170.744 1.00 44.07  ? 3107 LYS A C     1 
ATOM   12466 O  O     . LYS A 1 3107 ? 231.057 217.439 169.556 1.00 49.24  ? 3107 LYS A O     1 
ATOM   12467 C  CB    . LYS A 1 3107 ? 233.780 217.064 171.345 1.00 41.51  ? 3107 LYS A CB    1 
ATOM   12468 C  CG    . LYS A 1 3107 ? 234.375 216.825 169.973 1.00 47.52  ? 3107 LYS A CG    1 
ATOM   12469 C  CD    . LYS A 1 3107 ? 235.890 216.897 170.008 1.00 48.68  ? 3107 LYS A CD    1 
ATOM   12470 C  CE    . LYS A 1 3107 ? 236.490 216.435 168.692 1.00 54.27  ? 3107 LYS A CE    1 
ATOM   12471 N  NZ    . LYS A 1 3107 ? 236.266 217.426 167.605 1.00 52.98  ? 3107 LYS A NZ    1 
ATOM   12472 N  N     . GLU A 1 3108 ? 230.644 216.481 171.549 1.00 42.30  ? 3108 GLU A N     1 
ATOM   12473 C  CA    . GLU A 1 3108 ? 229.472 215.785 171.033 1.00 47.22  ? 3108 GLU A CA    1 
ATOM   12474 C  C     . GLU A 1 3108 ? 228.331 216.747 170.737 1.00 52.38  ? 3108 GLU A C     1 
ATOM   12475 O  O     . GLU A 1 3108 ? 227.638 216.594 169.725 1.00 55.25  ? 3108 GLU A O     1 
ATOM   12476 C  CB    . GLU A 1 3108 ? 229.017 214.704 172.010 1.00 50.87  ? 3108 GLU A CB    1 
ATOM   12477 C  CG    . GLU A 1 3108 ? 229.998 213.563 172.174 1.00 55.01  ? 3108 GLU A CG    1 
ATOM   12478 C  CD    . GLU A 1 3108 ? 230.142 212.744 170.907 1.00 56.61  ? 3108 GLU A CD    1 
ATOM   12479 O  OE1   . GLU A 1 3108 ? 229.151 212.632 170.154 1.00 50.70  ? 3108 GLU A OE1   1 
ATOM   12480 O  OE2   . GLU A 1 3108 ? 231.245 212.212 170.662 1.00 61.00  ? 3108 GLU A OE2   1 
ATOM   12481 N  N     . PHE A 1 3109 ? 228.107 217.741 171.598 1.00 50.83  ? 3109 PHE A N     1 
ATOM   12482 C  CA    . PHE A 1 3109 ? 226.944 218.589 171.374 1.00 51.01  ? 3109 PHE A CA    1 
ATOM   12483 C  C     . PHE A 1 3109 ? 227.205 219.597 170.258 1.00 51.19  ? 3109 PHE A C     1 
ATOM   12484 O  O     . PHE A 1 3109 ? 226.301 219.914 169.478 1.00 56.65  ? 3109 PHE A O     1 
ATOM   12485 C  CB    . PHE A 1 3109 ? 226.541 219.310 172.659 1.00 47.98  ? 3109 PHE A CB    1 
ATOM   12486 C  CG    . PHE A 1 3109 ? 225.310 220.153 172.505 1.00 53.59  ? 3109 PHE A CG    1 
ATOM   12487 C  CD1   . PHE A 1 3109 ? 224.062 219.558 172.461 1.00 53.95  ? 3109 PHE A CD1   1 
ATOM   12488 C  CD2   . PHE A 1 3109 ? 225.393 221.520 172.347 1.00 62.29  ? 3109 PHE A CD2   1 
ATOM   12489 C  CE1   . PHE A 1 3109 ? 222.922 220.317 172.307 1.00 55.92  ? 3109 PHE A CE1   1 
ATOM   12490 C  CE2   . PHE A 1 3109 ? 224.258 222.284 172.190 1.00 62.92  ? 3109 PHE A CE2   1 
ATOM   12491 C  CZ    . PHE A 1 3109 ? 223.020 221.681 172.169 1.00 58.35  ? 3109 PHE A CZ    1 
ATOM   12492 N  N     . THR A 1 3110 ? 228.434 220.109 170.162 1.00 50.36  ? 3110 THR A N     1 
ATOM   12493 C  CA    . THR A 1 3110 ? 228.777 221.071 169.120 1.00 52.07  ? 3110 THR A CA    1 
ATOM   12494 C  C     . THR A 1 3110 ? 229.189 220.417 167.809 1.00 53.43  ? 3110 THR A C     1 
ATOM   12495 O  O     . THR A 1 3110 ? 229.713 221.112 166.934 1.00 58.29  ? 3110 THR A O     1 
ATOM   12496 C  CB    . THR A 1 3110 ? 229.906 221.996 169.584 1.00 55.14  ? 3110 THR A CB    1 
ATOM   12497 O  OG1   . THR A 1 3110 ? 231.122 221.248 169.710 1.00 54.56  ? 3110 THR A OG1   1 
ATOM   12498 C  CG2   . THR A 1 3110 ? 229.564 222.642 170.913 1.00 47.27  ? 3110 THR A CG2   1 
ATOM   12499 N  N     . SER A 1 3111 ? 228.975 219.109 167.653 1.00 56.85  ? 3111 SER A N     1 
ATOM   12500 C  CA    . SER A 1 3111 ? 229.309 218.446 166.398 1.00 60.19  ? 3111 SER A CA    1 
ATOM   12501 C  C     . SER A 1 3111 ? 228.496 219.022 165.243 1.00 61.71  ? 3111 SER A C     1 
ATOM   12502 O  O     . SER A 1 3111 ? 229.009 219.199 164.133 1.00 53.56  ? 3111 SER A O     1 
ATOM   12503 C  CB    . SER A 1 3111 ? 229.075 216.941 166.528 1.00 58.40  ? 3111 SER A CB    1 
ATOM   12504 O  OG    . SER A 1 3111 ? 227.701 216.668 166.735 1.00 61.40  ? 3111 SER A OG    1 
ATOM   12505 N  N     . LYS A 1 3112 ? 227.220 219.327 165.498 1.00 69.61  ? 3112 LYS A N     1 
ATOM   12506 C  CA    . LYS A 1 3112 ? 226.342 219.871 164.465 1.00 67.05  ? 3112 LYS A CA    1 
ATOM   12507 C  C     . LYS A 1 3112 ? 226.794 221.260 164.036 1.00 70.14  ? 3112 LYS A C     1 
ATOM   12508 O  O     . LYS A 1 3112 ? 226.623 221.653 162.875 1.00 67.46  ? 3112 LYS A O     1 
ATOM   12509 C  CB    . LYS A 1 3112 ? 224.907 219.916 164.989 1.00 65.26  ? 3112 LYS A CB    1 
ATOM   12510 C  CG    . LYS A 1 3112 ? 224.332 218.577 165.417 1.00 68.42  ? 3112 LYS A CG    1 
ATOM   12511 C  CD    . LYS A 1 3112 ? 224.371 217.570 164.297 1.00 67.53  ? 3112 LYS A CD    1 
ATOM   12512 C  CE    . LYS A 1 3112 ? 223.139 216.655 164.330 1.00 70.47  ? 3112 LYS A CE    1 
ATOM   12513 N  NZ    . LYS A 1 3112 ? 221.868 217.427 164.351 1.00 65.13  ? 3112 LYS A NZ    1 
ATOM   12514 N  N     . MET A 1 3113 ? 227.356 222.019 164.972 1.00 70.85  ? 3113 MET A N     1 
ATOM   12515 C  CA    . MET A 1 3113 ? 227.846 223.362 164.707 1.00 63.12  ? 3113 MET A CA    1 
ATOM   12516 C  C     . MET A 1 3113 ? 228.959 223.330 163.667 1.00 69.07  ? 3113 MET A C     1 
ATOM   12517 O  O     . MET A 1 3113 ? 229.780 222.409 163.644 1.00 72.55  ? 3113 MET A O     1 
ATOM   12518 C  CB    . MET A 1 3113 ? 228.355 223.964 166.017 1.00 57.72  ? 3113 MET A CB    1 
ATOM   12519 C  CG    . MET A 1 3113 ? 227.263 224.207 167.041 1.00 60.71  ? 3113 MET A CG    1 
ATOM   12520 S  SD    . MET A 1 3113 ? 227.874 224.830 168.618 1.00 71.64  ? 3113 MET A SD    1 
ATOM   12521 C  CE    . MET A 1 3113 ? 228.376 226.482 168.156 1.00 61.04  ? 3113 MET A CE    1 
ATOM   12522 N  N     . ASP A 1 3114 ? 228.978 224.334 162.790 1.00 70.16  ? 3114 ASP A N     1 
ATOM   12523 C  CA    . ASP A 1 3114 ? 230.008 224.443 161.757 1.00 71.40  ? 3114 ASP A CA    1 
ATOM   12524 C  C     . ASP A 1 3114 ? 231.177 225.234 162.340 1.00 71.60  ? 3114 ASP A C     1 
ATOM   12525 O  O     . ASP A 1 3114 ? 231.395 226.408 162.034 1.00 70.78  ? 3114 ASP A O     1 
ATOM   12526 C  CB    . ASP A 1 3114 ? 229.445 225.102 160.505 1.00 73.41  ? 3114 ASP A CB    1 
ATOM   12527 C  CG    . ASP A 1 3114 ? 230.431 225.107 159.354 1.00 78.28  ? 3114 ASP A CG    1 
ATOM   12528 O  OD1   . ASP A 1 3114 ? 230.643 224.037 158.747 1.00 79.28  ? 3114 ASP A OD1   1 
ATOM   12529 O  OD2   . ASP A 1 3114 ? 231.009 226.177 159.069 1.00 75.49  ? 3114 ASP A OD2   1 
ATOM   12530 N  N     . LEU A 1 3115 ? 231.940 224.568 163.209 1.00 67.22  ? 3115 LEU A N     1 
ATOM   12531 C  CA    . LEU A 1 3115 ? 232.997 225.205 163.985 1.00 69.59  ? 3115 LEU A CA    1 
ATOM   12532 C  C     . LEU A 1 3115 ? 234.386 224.948 163.414 1.00 69.63  ? 3115 LEU A C     1 
ATOM   12533 O  O     . LEU A 1 3115 ? 235.387 225.205 164.091 1.00 68.78  ? 3115 LEU A O     1 
ATOM   12534 C  CB    . LEU A 1 3115 ? 232.938 224.741 165.440 1.00 67.16  ? 3115 LEU A CB    1 
ATOM   12535 C  CG    . LEU A 1 3115 ? 231.668 225.088 166.213 1.00 63.41  ? 3115 LEU A CG    1 
ATOM   12536 C  CD1   . LEU A 1 3115 ? 231.755 224.561 167.626 1.00 65.81  ? 3115 LEU A CD1   1 
ATOM   12537 C  CD2   . LEU A 1 3115 ? 231.414 226.585 166.215 1.00 64.46  ? 3115 LEU A CD2   1 
ATOM   12538 N  N     . GLU A 1 3116 ? 234.476 224.445 162.186 1.00 79.58  ? 3116 GLU A N     1 
ATOM   12539 C  CA    . GLU A 1 3116 ? 235.765 224.218 161.548 1.00 78.52  ? 3116 GLU A CA    1 
ATOM   12540 C  C     . GLU A 1 3116 ? 236.097 225.402 160.649 1.00 78.64  ? 3116 GLU A C     1 
ATOM   12541 O  O     . GLU A 1 3116 ? 235.277 225.821 159.825 1.00 77.90  ? 3116 GLU A O     1 
ATOM   12542 C  CB    . GLU A 1 3116 ? 235.789 222.903 160.759 1.00 75.61  ? 3116 GLU A CB    1 
ATOM   12543 C  CG    . GLU A 1 3116 ? 234.932 222.842 159.500 1.00 76.65  ? 3116 GLU A CG    1 
ATOM   12544 C  CD    . GLU A 1 3116 ? 233.490 222.465 159.777 1.00 78.95  ? 3116 GLU A CD    1 
ATOM   12545 O  OE1   . GLU A 1 3116 ? 233.067 222.537 160.949 1.00 81.92  ? 3116 GLU A OE1   1 
ATOM   12546 O  OE2   . GLU A 1 3116 ? 232.780 222.089 158.820 1.00 75.38  ? 3116 GLU A OE2   1 
ATOM   12547 N  N     . LYS A 1 3117 ? 237.284 225.957 160.842 1.00 83.49  ? 3117 LYS A N     1 
ATOM   12548 C  CA    . LYS A 1 3117 ? 237.757 227.103 160.074 1.00 82.49  ? 3117 LYS A CA    1 
ATOM   12549 C  C     . LYS A 1 3117 ? 239.105 226.753 159.469 1.00 84.36  ? 3117 LYS A C     1 
ATOM   12550 O  O     . LYS A 1 3117 ? 240.110 226.692 160.203 1.00 83.58  ? 3117 LYS A O     1 
ATOM   12551 C  CB    . LYS A 1 3117 ? 237.869 228.342 160.961 1.00 81.02  ? 3117 LYS A CB    1 
ATOM   12552 C  CG    . LYS A 1 3117 ? 238.428 229.554 160.252 1.00 84.59  ? 3117 LYS A CG    1 
ATOM   12553 C  CD    . LYS A 1 3117 ? 238.439 230.775 161.155 1.00 84.71  ? 3117 LYS A CD    1 
ATOM   12554 C  CE    . LYS A 1 3117 ? 239.230 230.524 162.427 1.00 86.58  ? 3117 LYS A CE    1 
ATOM   12555 N  NZ    . LYS A 1 3117 ? 239.238 231.718 163.317 1.00 83.90  ? 3117 LYS A NZ    1 
ATOM   12556 N  N     . PRO A 1 3118 ? 239.185 226.497 158.162 1.00 91.67  ? 3118 PRO A N     1 
ATOM   12557 C  CA    . PRO A 1 3118 ? 240.487 226.167 157.562 1.00 90.22  ? 3118 PRO A CA    1 
ATOM   12558 C  C     . PRO A 1 3118 ? 241.516 227.273 157.714 1.00 90.25  ? 3118 PRO A C     1 
ATOM   12559 O  O     . PRO A 1 3118 ? 242.721 226.995 157.683 1.00 87.40  ? 3118 PRO A O     1 
ATOM   12560 C  CB    . PRO A 1 3118 ? 240.138 225.917 156.089 1.00 87.63  ? 3118 PRO A CB    1 
ATOM   12561 C  CG    . PRO A 1 3118 ? 238.686 225.561 156.099 1.00 88.19  ? 3118 PRO A CG    1 
ATOM   12562 C  CD    . PRO A 1 3118 ? 238.080 226.376 157.197 1.00 89.57  ? 3118 PRO A CD    1 
ATOM   12563 N  N     . ASN A 1 3119 ? 241.076 228.521 157.880 1.00 89.62  ? 3119 ASN A N     1 
ATOM   12564 C  CA    . ASN A 1 3119 ? 241.994 229.639 158.053 1.00 88.02  ? 3119 ASN A CA    1 
ATOM   12565 C  C     . ASN A 1 3119 ? 242.571 229.718 159.459 1.00 88.97  ? 3119 ASN A C     1 
ATOM   12566 O  O     . ASN A 1 3119 ? 243.437 230.564 159.704 1.00 91.80  ? 3119 ASN A O     1 
ATOM   12567 C  CB    . ASN A 1 3119 ? 241.286 230.952 157.719 1.00 88.48  ? 3119 ASN A CB    1 
ATOM   12568 C  CG    . ASN A 1 3119 ? 240.556 230.898 156.394 1.00 92.17  ? 3119 ASN A CG    1 
ATOM   12569 O  OD1   . ASN A 1 3119 ? 241.165 230.704 155.342 1.00 90.77  ? 3119 ASN A OD1   1 
ATOM   12570 N  ND2   . ASN A 1 3119 ? 239.239 231.064 156.440 1.00 90.05  ? 3119 ASN A ND2   1 
ATOM   12571 N  N     . TYR A 1 3120 ? 242.106 228.877 160.383 1.00 80.27  ? 3120 TYR A N     1 
ATOM   12572 C  CA    . TYR A 1 3120 ? 242.590 228.912 161.757 1.00 78.48  ? 3120 TYR A CA    1 
ATOM   12573 C  C     . TYR A 1 3120 ? 244.084 228.631 161.814 1.00 75.48  ? 3120 TYR A C     1 
ATOM   12574 O  O     . TYR A 1 3120 ? 244.581 227.697 161.178 1.00 73.35  ? 3120 TYR A O     1 
ATOM   12575 C  CB    . TYR A 1 3120 ? 241.830 227.890 162.605 1.00 75.93  ? 3120 TYR A CB    1 
ATOM   12576 C  CG    . TYR A 1 3120 ? 242.278 227.823 164.048 1.00 74.01  ? 3120 TYR A CG    1 
ATOM   12577 C  CD1   . TYR A 1 3120 ? 242.158 228.922 164.886 1.00 75.90  ? 3120 TYR A CD1   1 
ATOM   12578 C  CD2   . TYR A 1 3120 ? 242.823 226.660 164.570 1.00 73.41  ? 3120 TYR A CD2   1 
ATOM   12579 C  CE1   . TYR A 1 3120 ? 242.567 228.862 166.203 1.00 75.57  ? 3120 TYR A CE1   1 
ATOM   12580 C  CE2   . TYR A 1 3120 ? 243.235 226.592 165.884 1.00 71.28  ? 3120 TYR A CE2   1 
ATOM   12581 C  CZ    . TYR A 1 3120 ? 243.104 227.695 166.695 1.00 73.52  ? 3120 TYR A CZ    1 
ATOM   12582 O  OH    . TYR A 1 3120 ? 243.514 227.629 168.006 1.00 76.67  ? 3120 TYR A OH    1 
ATOM   12583 N  N     . ILE A 1 3121 ? 244.799 229.451 162.577 1.00 74.82  ? 3121 ILE A N     1 
ATOM   12584 C  CA    . ILE A 1 3121 ? 246.235 229.310 162.772 1.00 75.79  ? 3121 ILE A CA    1 
ATOM   12585 C  C     . ILE A 1 3121 ? 246.472 228.994 164.240 1.00 77.30  ? 3121 ILE A C     1 
ATOM   12586 O  O     . ILE A 1 3121 ? 246.086 229.774 165.119 1.00 77.72  ? 3121 ILE A O     1 
ATOM   12587 C  CB    . ILE A 1 3121 ? 246.991 230.579 162.352 1.00 80.25  ? 3121 ILE A CB    1 
ATOM   12588 C  CG1   . ILE A 1 3121 ? 246.722 230.893 160.879 1.00 80.05  ? 3121 ILE A CG1   1 
ATOM   12589 C  CG2   . ILE A 1 3121 ? 248.480 230.422 162.613 1.00 77.86  ? 3121 ILE A CG2   1 
ATOM   12590 C  CD1   . ILE A 1 3121 ? 247.173 229.808 159.929 1.00 78.23  ? 3121 ILE A CD1   1 
ATOM   12591 N  N     . VAL A 1 3122 ? 247.109 227.863 164.505 1.00 76.64  ? 3122 VAL A N     1 
ATOM   12592 C  CA    . VAL A 1 3122 ? 247.346 227.454 165.893 1.00 75.84  ? 3122 VAL A CA    1 
ATOM   12593 C  C     . VAL A 1 3122 ? 248.372 228.388 166.522 1.00 77.31  ? 3122 VAL A C     1 
ATOM   12594 O  O     . VAL A 1 3122 ? 249.441 228.618 165.930 1.00 78.57  ? 3122 VAL A O     1 
ATOM   12595 C  CB    . VAL A 1 3122 ? 247.816 226.003 165.949 1.00 75.25  ? 3122 VAL A CB    1 
ATOM   12596 C  CG1   . VAL A 1 3122 ? 247.735 225.482 167.372 1.00 77.52  ? 3122 VAL A CG1   1 
ATOM   12597 C  CG2   . VAL A 1 3122 ? 246.982 225.142 165.016 1.00 73.47  ? 3122 VAL A CG2   1 
ATOM   12598 N  N     . PRO A 1 3123 ? 248.102 228.950 167.697 1.00 80.38  ? 3123 PRO A N     1 
ATOM   12599 C  CA    . PRO A 1 3123 ? 249.100 229.793 168.359 1.00 82.83  ? 3123 PRO A CA    1 
ATOM   12600 C  C     . PRO A 1 3123 ? 250.320 228.984 168.768 1.00 80.73  ? 3123 PRO A C     1 
ATOM   12601 O  O     . PRO A 1 3123 ? 250.267 227.764 168.936 1.00 82.51  ? 3123 PRO A O     1 
ATOM   12602 C  CB    . PRO A 1 3123 ? 248.355 230.333 169.584 1.00 81.34  ? 3123 PRO A CB    1 
ATOM   12603 C  CG    . PRO A 1 3123 ? 247.272 229.335 169.831 1.00 79.42  ? 3123 PRO A CG    1 
ATOM   12604 C  CD    . PRO A 1 3123 ? 246.855 228.858 168.474 1.00 76.36  ? 3123 PRO A CD    1 
ATOM   12605 N  N     . ASP A 1 3124 ? 251.443 229.693 168.914 1.00 90.05  ? 3124 ASP A N     1 
ATOM   12606 C  CA    . ASP A 1 3124 ? 252.681 229.034 169.317 1.00 94.27  ? 3124 ASP A CA    1 
ATOM   12607 C  C     . ASP A 1 3124 ? 252.533 228.374 170.682 1.00 95.42  ? 3124 ASP A C     1 
ATOM   12608 O  O     . ASP A 1 3124 ? 252.992 227.245 170.888 1.00 93.63  ? 3124 ASP A O     1 
ATOM   12609 C  CB    . ASP A 1 3124 ? 253.835 230.037 169.318 1.00 94.39  ? 3124 ASP A CB    1 
ATOM   12610 C  CG    . ASP A 1 3124 ? 253.549 231.259 170.169 1.00 96.01  ? 3124 ASP A CG    1 
ATOM   12611 O  OD1   . ASP A 1 3124 ? 252.420 231.377 170.691 1.00 91.69  ? 3124 ASP A OD1   1 
ATOM   12612 O  OD2   . ASP A 1 3124 ? 254.455 232.106 170.315 1.00 94.57  ? 3124 ASP A OD2   1 
ATOM   12613 N  N     . TYR A 1 3125 ? 251.894 229.059 171.625 1.00 94.05  ? 3125 TYR A N     1 
ATOM   12614 C  CA    . TYR A 1 3125 ? 251.548 228.487 172.919 1.00 93.98  ? 3125 TYR A CA    1 
ATOM   12615 C  C     . TYR A 1 3125 ? 250.036 228.323 172.978 1.00 96.66  ? 3125 TYR A C     1 
ATOM   12616 O  O     . TYR A 1 3125 ? 249.296 229.306 172.866 1.00 95.85  ? 3125 TYR A O     1 
ATOM   12617 C  CB    . TYR A 1 3125 ? 252.040 229.369 174.066 1.00 93.03  ? 3125 TYR A CB    1 
ATOM   12618 C  CG    . TYR A 1 3125 ? 251.294 229.148 175.362 1.00 95.34  ? 3125 TYR A CG    1 
ATOM   12619 C  CD1   . TYR A 1 3125 ? 251.512 228.008 176.125 1.00 94.31  ? 3125 TYR A CD1   1 
ATOM   12620 C  CD2   . TYR A 1 3125 ? 250.369 230.077 175.822 1.00 93.60  ? 3125 TYR A CD2   1 
ATOM   12621 C  CE1   . TYR A 1 3125 ? 250.833 227.800 177.310 1.00 96.40  ? 3125 TYR A CE1   1 
ATOM   12622 C  CE2   . TYR A 1 3125 ? 249.684 229.877 177.006 1.00 95.00  ? 3125 TYR A CE2   1 
ATOM   12623 C  CZ    . TYR A 1 3125 ? 249.920 228.737 177.746 1.00 97.38  ? 3125 TYR A CZ    1 
ATOM   12624 O  OH    . TYR A 1 3125 ? 249.241 228.533 178.925 1.00 96.25  ? 3125 TYR A OH    1 
ATOM   12625 N  N     . MET A 1 3126 ? 249.585 227.089 173.152 1.00 89.86  ? 3126 MET A N     1 
ATOM   12626 C  CA    . MET A 1 3126 ? 248.159 226.806 173.212 1.00 89.54  ? 3126 MET A CA    1 
ATOM   12627 C  C     . MET A 1 3126 ? 247.708 226.712 174.658 1.00 87.80  ? 3126 MET A C     1 
ATOM   12628 O  O     . MET A 1 3126 ? 248.295 225.943 175.433 1.00 86.85  ? 3126 MET A O     1 
ATOM   12629 C  CB    . MET A 1 3126 ? 247.840 225.503 172.485 1.00 87.82  ? 3126 MET A CB    1 
ATOM   12630 C  CG    . MET A 1 3126 ? 246.383 225.085 172.575 1.00 89.72  ? 3126 MET A CG    1 
ATOM   12631 S  SD    . MET A 1 3126 ? 245.370 225.812 171.275 1.00 95.33  ? 3126 MET A SD    1 
ATOM   12632 C  CE    . MET A 1 3126 ? 243.753 225.750 172.039 1.00 89.30  ? 3126 MET A CE    1 
ATOM   12633 N  N     . PRO A 1 3127 ? 246.689 227.469 175.067 1.00 79.02  ? 3127 PRO A N     1 
ATOM   12634 C  CA    . PRO A 1 3127 ? 246.206 227.364 176.449 1.00 79.56  ? 3127 PRO A CA    1 
ATOM   12635 C  C     . PRO A 1 3127 ? 245.502 226.039 176.681 1.00 83.34  ? 3127 PRO A C     1 
ATOM   12636 O  O     . PRO A 1 3127 ? 244.270 225.980 176.746 1.00 82.77  ? 3127 PRO A O     1 
ATOM   12637 C  CB    . PRO A 1 3127 ? 245.239 228.549 176.585 1.00 78.38  ? 3127 PRO A CB    1 
ATOM   12638 C  CG    . PRO A 1 3127 ? 245.355 229.332 175.304 1.00 78.08  ? 3127 PRO A CG    1 
ATOM   12639 C  CD    . PRO A 1 3127 ? 245.883 228.403 174.270 1.00 76.15  ? 3127 PRO A CD    1 
ATOM   12640 N  N     . VAL A 1 3128 ? 246.283 224.968 176.802 1.00 80.80  ? 3128 VAL A N     1 
ATOM   12641 C  CA    . VAL A 1 3128 ? 245.721 223.625 176.870 1.00 76.16  ? 3128 VAL A CA    1 
ATOM   12642 C  C     . VAL A 1 3128 ? 245.037 223.433 178.217 1.00 77.56  ? 3128 VAL A C     1 
ATOM   12643 O  O     . VAL A 1 3128 ? 245.674 223.508 179.273 1.00 76.20  ? 3128 VAL A O     1 
ATOM   12644 C  CB    . VAL A 1 3128 ? 246.807 222.567 176.641 1.00 78.50  ? 3128 VAL A CB    1 
ATOM   12645 C  CG1   . VAL A 1 3128 ? 246.312 221.198 177.066 1.00 75.83  ? 3128 VAL A CG1   1 
ATOM   12646 C  CG2   . VAL A 1 3128 ? 247.227 222.553 175.181 1.00 74.91  ? 3128 VAL A CG2   1 
ATOM   12647 N  N     . VAL A 1 3129 ? 243.731 223.192 178.180 1.00 70.11  ? 3129 VAL A N     1 
ATOM   12648 C  CA    . VAL A 1 3129 ? 242.968 222.827 179.363 1.00 66.53  ? 3129 VAL A CA    1 
ATOM   12649 C  C     . VAL A 1 3129 ? 242.742 221.323 179.435 1.00 65.63  ? 3129 VAL A C     1 
ATOM   12650 O  O     . VAL A 1 3129 ? 242.923 220.715 180.490 1.00 65.08  ? 3129 VAL A O     1 
ATOM   12651 C  CB    . VAL A 1 3129 ? 241.629 223.595 179.388 1.00 57.67  ? 3129 VAL A CB    1 
ATOM   12652 C  CG1   . VAL A 1 3129 ? 240.810 223.197 180.600 1.00 61.53  ? 3129 VAL A CG1   1 
ATOM   12653 C  CG2   . VAL A 1 3129 ? 241.883 225.089 179.380 1.00 59.70  ? 3129 VAL A CG2   1 
ATOM   12654 N  N     . TYR A 1 3130 ? 242.356 220.714 178.318 1.00 61.89  ? 3130 TYR A N     1 
ATOM   12655 C  CA    . TYR A 1 3130 ? 242.201 219.267 178.226 1.00 62.17  ? 3130 TYR A CA    1 
ATOM   12656 C  C     . TYR A 1 3130 ? 243.565 218.665 177.911 1.00 68.56  ? 3130 TYR A C     1 
ATOM   12657 O  O     . TYR A 1 3130 ? 244.115 218.891 176.829 1.00 70.65  ? 3130 TYR A O     1 
ATOM   12658 C  CB    . TYR A 1 3130 ? 241.173 218.901 177.160 1.00 63.45  ? 3130 TYR A CB    1 
ATOM   12659 C  CG    . TYR A 1 3130 ? 240.918 217.418 177.038 1.00 61.98  ? 3130 TYR A CG    1 
ATOM   12660 C  CD1   . TYR A 1 3130 ? 240.870 216.608 178.162 1.00 59.17  ? 3130 TYR A CD1   1 
ATOM   12661 C  CD2   . TYR A 1 3130 ? 240.725 216.829 175.798 1.00 64.02  ? 3130 TYR A CD2   1 
ATOM   12662 C  CE1   . TYR A 1 3130 ? 240.639 215.254 178.052 1.00 63.04  ? 3130 TYR A CE1   1 
ATOM   12663 C  CE2   . TYR A 1 3130 ? 240.493 215.477 175.680 1.00 63.32  ? 3130 TYR A CE2   1 
ATOM   12664 C  CZ    . TYR A 1 3130 ? 240.448 214.695 176.810 1.00 65.91  ? 3130 TYR A CZ    1 
ATOM   12665 O  OH    . TYR A 1 3130 ? 240.217 213.345 176.694 1.00 67.77  ? 3130 TYR A OH    1 
ATOM   12666 N  N     . ASP A 1 3131 ? 244.106 217.895 178.858 1.00 76.50  ? 3131 ASP A N     1 
ATOM   12667 C  CA    . ASP A 1 3131 ? 245.467 217.386 178.719 1.00 74.72  ? 3131 ASP A CA    1 
ATOM   12668 C  C     . ASP A 1 3131 ? 245.611 216.452 177.525 1.00 73.22  ? 3131 ASP A C     1 
ATOM   12669 O  O     . ASP A 1 3131 ? 246.707 216.325 176.968 1.00 74.92  ? 3131 ASP A O     1 
ATOM   12670 C  CB    . ASP A 1 3131 ? 245.887 216.674 180.004 1.00 75.35  ? 3131 ASP A CB    1 
ATOM   12671 C  CG    . ASP A 1 3131 ? 246.061 217.630 181.167 1.00 77.12  ? 3131 ASP A CG    1 
ATOM   12672 O  OD1   . ASP A 1 3131 ? 246.405 218.806 180.924 1.00 76.17  ? 3131 ASP A OD1   1 
ATOM   12673 O  OD2   . ASP A 1 3131 ? 245.849 217.209 182.323 1.00 74.07  ? 3131 ASP A OD2   1 
ATOM   12674 N  N     . LYS A 1 3132 ? 244.527 215.794 177.116 1.00 70.23  ? 3132 LYS A N     1 
ATOM   12675 C  CA    . LYS A 1 3132 ? 244.555 214.862 175.998 1.00 71.23  ? 3132 LYS A CA    1 
ATOM   12676 C  C     . LYS A 1 3132 ? 244.130 215.510 174.686 1.00 72.36  ? 3132 LYS A C     1 
ATOM   12677 O  O     . LYS A 1 3132 ? 243.775 214.801 173.739 1.00 71.48  ? 3132 LYS A O     1 
ATOM   12678 C  CB    . LYS A 1 3132 ? 243.673 213.651 176.301 1.00 70.94  ? 3132 LYS A CB    1 
ATOM   12679 C  CG    . LYS A 1 3132 ? 244.211 212.753 177.403 1.00 74.36  ? 3132 LYS A CG    1 
ATOM   12680 C  CD    . LYS A 1 3132 ? 243.142 211.802 177.913 1.00 73.74  ? 3132 LYS A CD    1 
ATOM   12681 C  CE    . LYS A 1 3132 ? 243.353 211.470 179.380 1.00 72.72  ? 3132 LYS A CE    1 
ATOM   12682 N  NZ    . LYS A 1 3132 ? 242.615 212.405 180.274 1.00 69.80  ? 3132 LYS A NZ    1 
ATOM   12683 N  N     . LEU A 1 3133 ? 244.150 216.837 174.614 1.00 70.20  ? 3133 LEU A N     1 
ATOM   12684 C  CA    . LEU A 1 3133 ? 243.797 217.518 173.378 1.00 73.66  ? 3133 LEU A CA    1 
ATOM   12685 C  C     . LEU A 1 3133 ? 244.844 217.226 172.304 1.00 77.70  ? 3133 LEU A C     1 
ATOM   12686 O  O     . LEU A 1 3133 ? 246.040 217.161 172.607 1.00 77.28  ? 3133 LEU A O     1 
ATOM   12687 C  CB    . LEU A 1 3133 ? 243.688 219.025 173.612 1.00 70.68  ? 3133 LEU A CB    1 
ATOM   12688 C  CG    . LEU A 1 3133 ? 243.223 219.900 172.446 1.00 72.27  ? 3133 LEU A CG    1 
ATOM   12689 C  CD1   . LEU A 1 3133 ? 241.710 219.893 172.347 1.00 69.57  ? 3133 LEU A CD1   1 
ATOM   12690 C  CD2   . LEU A 1 3133 ? 243.746 221.319 172.593 1.00 72.28  ? 3133 LEU A CD2   1 
ATOM   12691 N  N     . PRO A 1 3134 ? 244.429 217.028 171.053 1.00 78.26  ? 3134 PRO A N     1 
ATOM   12692 C  CA    . PRO A 1 3134 ? 245.402 216.752 169.989 1.00 77.03  ? 3134 PRO A CA    1 
ATOM   12693 C  C     . PRO A 1 3134 ? 246.422 217.873 169.853 1.00 76.75  ? 3134 PRO A C     1 
ATOM   12694 O  O     . PRO A 1 3134 ? 246.099 219.054 169.999 1.00 74.81  ? 3134 PRO A O     1 
ATOM   12695 C  CB    . PRO A 1 3134 ? 244.527 216.629 168.738 1.00 75.94  ? 3134 PRO A CB    1 
ATOM   12696 C  CG    . PRO A 1 3134 ? 243.216 216.155 169.260 1.00 76.54  ? 3134 PRO A CG    1 
ATOM   12697 C  CD    . PRO A 1 3134 ? 243.043 216.830 170.594 1.00 75.15  ? 3134 PRO A CD    1 
ATOM   12698 N  N     . GLN A 1 3135 ? 247.669 217.485 169.581 1.00 89.24  ? 3135 GLN A N     1 
ATOM   12699 C  CA    . GLN A 1 3135 ? 248.758 218.459 169.524 1.00 90.00  ? 3135 GLN A CA    1 
ATOM   12700 C  C     . GLN A 1 3135 ? 248.591 219.472 168.397 1.00 92.75  ? 3135 GLN A C     1 
ATOM   12701 O  O     . GLN A 1 3135 ? 248.914 220.652 168.615 1.00 91.31  ? 3135 GLN A O     1 
ATOM   12702 C  CB    . GLN A 1 3135 ? 250.103 217.727 169.445 1.00 89.41  ? 3135 GLN A CB    1 
ATOM   12703 C  CG    . GLN A 1 3135 ? 250.258 216.604 170.456 1.00 91.95  ? 3135 GLN A CG    1 
ATOM   12704 C  CD    . GLN A 1 3135 ? 250.053 217.072 171.883 1.00 94.21  ? 3135 GLN A CD    1 
ATOM   12705 O  OE1   . GLN A 1 3135 ? 250.607 218.088 172.300 1.00 92.21  ? 3135 GLN A OE1   1 
ATOM   12706 N  NE2   . GLN A 1 3135 ? 249.252 216.331 172.640 1.00 92.09  ? 3135 GLN A NE2   1 
ATOM   12707 N  N     . PRO A 1 3136 ? 248.194 219.098 167.180 1.00 89.38  ? 3136 PRO A N     1 
ATOM   12708 C  CA    . PRO A 1 3136 ? 247.732 220.104 166.207 1.00 83.67  ? 3136 PRO A CA    1 
ATOM   12709 C  C     . PRO A 1 3136 ? 246.232 220.322 166.313 1.00 85.74  ? 3136 PRO A C     1 
ATOM   12710 O  O     . PRO A 1 3136 ? 245.466 219.753 165.519 1.00 84.57  ? 3136 PRO A O     1 
ATOM   12711 C  CB    . PRO A 1 3136 ? 248.099 219.482 164.852 1.00 85.84  ? 3136 PRO A CB    1 
ATOM   12712 C  CG    . PRO A 1 3136 ? 248.079 218.025 165.109 1.00 87.32  ? 3136 PRO A CG    1 
ATOM   12713 C  CD    . PRO A 1 3136 ? 248.566 217.837 166.510 1.00 86.06  ? 3136 PRO A CD    1 
ATOM   12714 N  N     . PRO A 1 3137 ? 245.763 221.127 167.266 1.00 80.02  ? 3137 PRO A N     1 
ATOM   12715 C  CA    . PRO A 1 3137 ? 244.314 221.232 167.476 1.00 77.32  ? 3137 PRO A CA    1 
ATOM   12716 C  C     . PRO A 1 3137 ? 243.649 222.004 166.346 1.00 77.08  ? 3137 PRO A C     1 
ATOM   12717 O  O     . PRO A 1 3137 ? 244.129 223.060 165.929 1.00 79.21  ? 3137 PRO A O     1 
ATOM   12718 C  CB    . PRO A 1 3137 ? 244.205 221.976 168.810 1.00 74.50  ? 3137 PRO A CB    1 
ATOM   12719 C  CG    . PRO A 1 3137 ? 245.419 222.833 168.848 1.00 76.32  ? 3137 PRO A CG    1 
ATOM   12720 C  CD    . PRO A 1 3137 ? 246.485 222.189 167.986 1.00 76.26  ? 3137 PRO A CD    1 
ATOM   12721 N  N     . SER A 1 3138 ? 242.541 221.465 165.848 1.00 64.70  ? 3138 SER A N     1 
ATOM   12722 C  CA    . SER A 1 3138 ? 241.753 222.160 164.846 1.00 68.58  ? 3138 SER A CA    1 
ATOM   12723 C  C     . SER A 1 3138 ? 240.949 223.275 165.509 1.00 71.74  ? 3138 SER A C     1 
ATOM   12724 O  O     . SER A 1 3138 ? 241.037 223.508 166.717 1.00 75.61  ? 3138 SER A O     1 
ATOM   12725 C  CB    . SER A 1 3138 ? 240.842 221.181 164.110 1.00 68.22  ? 3138 SER A CB    1 
ATOM   12726 O  OG    . SER A 1 3138 ? 239.935 220.559 165.001 1.00 67.79  ? 3138 SER A OG    1 
ATOM   12727 N  N     . HIS A 1 3139 ? 240.156 223.987 164.706 1.00 65.52  ? 3139 HIS A N     1 
ATOM   12728 C  CA    . HIS A 1 3139 ? 239.337 225.059 165.260 1.00 63.74  ? 3139 HIS A CA    1 
ATOM   12729 C  C     . HIS A 1 3139 ? 238.278 224.512 166.209 1.00 65.66  ? 3139 HIS A C     1 
ATOM   12730 O  O     . HIS A 1 3139 ? 238.024 225.097 167.267 1.00 67.02  ? 3139 HIS A O     1 
ATOM   12731 C  CB    . HIS A 1 3139 ? 238.686 225.862 164.137 1.00 64.77  ? 3139 HIS A CB    1 
ATOM   12732 C  CG    . HIS A 1 3139 ? 238.057 227.139 164.599 1.00 64.29  ? 3139 HIS A CG    1 
ATOM   12733 N  ND1   . HIS A 1 3139 ? 236.767 227.494 164.271 1.00 66.37  ? 3139 HIS A ND1   1 
ATOM   12734 C  CD2   . HIS A 1 3139 ? 238.538 228.139 165.373 1.00 66.65  ? 3139 HIS A CD2   1 
ATOM   12735 C  CE1   . HIS A 1 3139 ? 236.483 228.662 164.819 1.00 67.84  ? 3139 HIS A CE1   1 
ATOM   12736 N  NE2   . HIS A 1 3139 ? 237.540 229.075 165.493 1.00 67.84  ? 3139 HIS A NE2   1 
ATOM   12737 N  N     . ARG A 1 3140 ? 237.646 223.394 165.845 1.00 60.66  ? 3140 ARG A N     1 
ATOM   12738 C  CA    . ARG A 1 3140 ? 236.598 222.821 166.685 1.00 53.69  ? 3140 ARG A CA    1 
ATOM   12739 C  C     . ARG A 1 3140 ? 237.150 222.371 168.032 1.00 58.60  ? 3140 ARG A C     1 
ATOM   12740 O  O     . ARG A 1 3140 ? 236.530 222.604 169.079 1.00 66.07  ? 3140 ARG A O     1 
ATOM   12741 C  CB    . ARG A 1 3140 ? 235.940 221.650 165.958 1.00 57.63  ? 3140 ARG A CB    1 
ATOM   12742 C  CG    . ARG A 1 3140 ? 234.678 221.130 166.614 1.00 63.62  ? 3140 ARG A CG    1 
ATOM   12743 C  CD    . ARG A 1 3140 ? 234.096 219.978 165.818 1.00 56.92  ? 3140 ARG A CD    1 
ATOM   12744 N  NE    . ARG A 1 3140 ? 233.566 220.419 164.535 1.00 59.36  ? 3140 ARG A NE    1 
ATOM   12745 C  CZ    . ARG A 1 3140 ? 232.359 220.938 164.362 1.00 62.62  ? 3140 ARG A CZ    1 
ATOM   12746 N  NH1   . ARG A 1 3140 ? 231.525 221.099 165.374 1.00 65.74  ? 3140 ARG A NH1   1 
ATOM   12747 N  NH2   . ARG A 1 3140 ? 231.978 221.302 163.141 1.00 60.45  ? 3140 ARG A NH2   1 
ATOM   12748 N  N     . GLU A 1 3141 ? 238.315 221.723 168.026 1.00 60.81  ? 3141 GLU A N     1 
ATOM   12749 C  CA    . GLU A 1 3141 ? 238.922 221.280 169.275 1.00 56.80  ? 3141 GLU A CA    1 
ATOM   12750 C  C     . GLU A 1 3141 ? 239.307 222.465 170.150 1.00 60.17  ? 3141 GLU A C     1 
ATOM   12751 O  O     . GLU A 1 3141 ? 239.118 222.428 171.371 1.00 64.67  ? 3141 GLU A O     1 
ATOM   12752 C  CB    . GLU A 1 3141 ? 240.134 220.399 168.980 1.00 59.02  ? 3141 GLU A CB    1 
ATOM   12753 C  CG    . GLU A 1 3141 ? 239.798 219.164 168.161 1.00 63.19  ? 3141 GLU A CG    1 
ATOM   12754 C  CD    . GLU A 1 3141 ? 241.029 218.454 167.639 1.00 69.24  ? 3141 GLU A CD    1 
ATOM   12755 O  OE1   . GLU A 1 3141 ? 242.149 218.908 167.942 1.00 73.19  ? 3141 GLU A OE1   1 
ATOM   12756 O  OE2   . GLU A 1 3141 ? 240.875 217.443 166.923 1.00 66.55  ? 3141 GLU A OE2   1 
ATOM   12757 N  N     . ALA A 1 3142 ? 239.838 223.529 169.545 1.00 55.23  ? 3142 ALA A N     1 
ATOM   12758 C  CA    . ALA A 1 3142 ? 240.158 224.730 170.309 1.00 52.11  ? 3142 ALA A CA    1 
ATOM   12759 C  C     . ALA A 1 3142 ? 238.901 225.371 170.883 1.00 50.97  ? 3142 ALA A C     1 
ATOM   12760 O  O     . ALA A 1 3142 ? 238.920 225.892 172.002 1.00 53.59  ? 3142 ALA A O     1 
ATOM   12761 C  CB    . ALA A 1 3142 ? 240.918 225.723 169.433 1.00 55.20  ? 3142 ALA A CB    1 
ATOM   12762 N  N     . ILE A 1 3143 ? 237.798 225.339 170.132 1.00 53.89  ? 3143 ILE A N     1 
ATOM   12763 C  CA    . ILE A 1 3143 ? 236.536 225.888 170.622 1.00 47.82  ? 3143 ILE A CA    1 
ATOM   12764 C  C     . ILE A 1 3143 ? 236.051 225.109 171.839 1.00 51.67  ? 3143 ILE A C     1 
ATOM   12765 O  O     . ILE A 1 3143 ? 235.623 225.689 172.845 1.00 54.15  ? 3143 ILE A O     1 
ATOM   12766 C  CB    . ILE A 1 3143 ? 235.485 225.888 169.498 1.00 45.15  ? 3143 ILE A CB    1 
ATOM   12767 C  CG1   . ILE A 1 3143 ? 235.751 227.030 168.516 1.00 47.48  ? 3143 ILE A CG1   1 
ATOM   12768 C  CG2   . ILE A 1 3143 ? 234.084 225.986 170.075 1.00 49.18  ? 3143 ILE A CG2   1 
ATOM   12769 C  CD1   . ILE A 1 3143 ? 235.370 228.389 169.041 1.00 52.32  ? 3143 ILE A CD1   1 
ATOM   12770 N  N     . VAL A 1 3144 ? 236.107 223.778 171.766 1.00 48.43  ? 3144 VAL A N     1 
ATOM   12771 C  CA    . VAL A 1 3144 ? 235.661 222.966 172.896 1.00 42.58  ? 3144 VAL A CA    1 
ATOM   12772 C  C     . VAL A 1 3144 ? 236.586 223.159 174.094 1.00 50.41  ? 3144 VAL A C     1 
ATOM   12773 O  O     . VAL A 1 3144 ? 236.139 223.176 175.250 1.00 54.14  ? 3144 VAL A O     1 
ATOM   12774 C  CB    . VAL A 1 3144 ? 235.553 221.487 172.486 1.00 43.12  ? 3144 VAL A CB    1 
ATOM   12775 C  CG1   . VAL A 1 3144 ? 235.019 220.662 173.638 1.00 48.37  ? 3144 VAL A CG1   1 
ATOM   12776 C  CG2   . VAL A 1 3144 ? 234.650 221.342 171.278 1.00 44.74  ? 3144 VAL A CG2   1 
ATOM   12777 N  N     . ASN A 1 3145 ? 237.888 223.311 173.842 1.00 47.57  ? 3145 ASN A N     1 
ATOM   12778 C  CA    . ASN A 1 3145 ? 238.826 223.596 174.921 1.00 44.04  ? 3145 ASN A CA    1 
ATOM   12779 C  C     . ASN A 1 3145 ? 238.506 224.932 175.583 1.00 50.33  ? 3145 ASN A C     1 
ATOM   12780 O  O     . ASN A 1 3145 ? 238.574 225.062 176.812 1.00 51.03  ? 3145 ASN A O     1 
ATOM   12781 C  CB    . ASN A 1 3145 ? 240.253 223.585 174.374 1.00 43.71  ? 3145 ASN A CB    1 
ATOM   12782 C  CG    . ASN A 1 3145 ? 241.297 223.612 175.463 1.00 51.22  ? 3145 ASN A CG    1 
ATOM   12783 O  OD1   . ASN A 1 3145 ? 241.407 222.680 176.256 1.00 59.38  ? 3145 ASN A OD1   1 
ATOM   12784 N  ND2   . ASN A 1 3145 ? 242.078 224.683 175.504 1.00 54.56  ? 3145 ASN A ND2   1 
ATOM   12785 N  N     . SER A 1 3146 ? 238.148 225.935 174.779 1.00 46.58  ? 3146 SER A N     1 
ATOM   12786 C  CA    . SER A 1 3146 ? 237.730 227.221 175.323 1.00 39.00  ? 3146 SER A CA    1 
ATOM   12787 C  C     . SER A 1 3146 ? 236.464 227.082 176.157 1.00 47.43  ? 3146 SER A C     1 
ATOM   12788 O  O     . SER A 1 3146 ? 236.321 227.746 177.188 1.00 52.35  ? 3146 SER A O     1 
ATOM   12789 C  CB    . SER A 1 3146 ? 237.516 228.221 174.190 1.00 43.50  ? 3146 SER A CB    1 
ATOM   12790 O  OG    . SER A 1 3146 ? 238.734 228.504 173.527 1.00 51.65  ? 3146 SER A OG    1 
ATOM   12791 N  N     . CYS A 1 3147 ? 235.530 226.236 175.720 1.00 40.21  ? 3147 CYS A N     1 
ATOM   12792 C  CA    . CYS A 1 3147 ? 234.321 225.998 176.506 1.00 22.09  ? 3147 CYS A CA    1 
ATOM   12793 C  C     . CYS A 1 3147 ? 234.654 225.385 177.863 1.00 35.59  ? 3147 CYS A C     1 
ATOM   12794 O  O     . CYS A 1 3147 ? 234.099 225.788 178.896 1.00 49.33  ? 3147 CYS A O     1 
ATOM   12795 C  CB    . CYS A 1 3147 ? 233.365 225.093 175.733 1.00 34.91  ? 3147 CYS A CB    1 
ATOM   12796 S  SG    . CYS A 1 3147 ? 232.609 225.857 174.286 1.00 45.65  ? 3147 CYS A SG    1 
ATOM   12797 N  N     . VAL A 1 3148 ? 235.560 224.406 177.879 1.00 43.09  ? 3148 VAL A N     1 
ATOM   12798 C  CA    . VAL A 1 3148 ? 235.964 223.791 179.142 1.00 36.64  ? 3148 VAL A CA    1 
ATOM   12799 C  C     . VAL A 1 3148 ? 236.634 224.819 180.047 1.00 44.12  ? 3148 VAL A C     1 
ATOM   12800 O  O     . VAL A 1 3148 ? 236.380 224.867 181.260 1.00 53.89  ? 3148 VAL A O     1 
ATOM   12801 C  CB    . VAL A 1 3148 ? 236.878 222.581 178.881 1.00 31.54  ? 3148 VAL A CB    1 
ATOM   12802 C  CG1   . VAL A 1 3148 ? 237.319 221.964 180.190 1.00 40.24  ? 3148 VAL A CG1   1 
ATOM   12803 C  CG2   . VAL A 1 3148 ? 236.160 221.554 178.030 1.00 35.12  ? 3148 VAL A CG2   1 
ATOM   12804 N  N     . PHE A 1 3149 ? 237.499 225.661 179.473 1.00 35.92  ? 3149 PHE A N     1 
ATOM   12805 C  CA    . PHE A 1 3149 ? 238.135 226.713 180.260 1.00 32.19  ? 3149 PHE A CA    1 
ATOM   12806 C  C     . PHE A 1 3149 ? 237.102 227.673 180.830 1.00 36.13  ? 3149 PHE A C     1 
ATOM   12807 O  O     . PHE A 1 3149 ? 237.222 228.119 181.978 1.00 41.44  ? 3149 PHE A O     1 
ATOM   12808 C  CB    . PHE A 1 3149 ? 239.147 227.475 179.408 1.00 44.01  ? 3149 PHE A CB    1 
ATOM   12809 C  CG    . PHE A 1 3149 ? 239.755 228.656 180.109 1.00 51.28  ? 3149 PHE A CG    1 
ATOM   12810 C  CD1   . PHE A 1 3149 ? 240.806 228.485 180.992 1.00 49.52  ? 3149 PHE A CD1   1 
ATOM   12811 C  CD2   . PHE A 1 3149 ? 239.271 229.936 179.895 1.00 44.63  ? 3149 PHE A CD2   1 
ATOM   12812 C  CE1   . PHE A 1 3149 ? 241.366 229.565 181.642 1.00 43.93  ? 3149 PHE A CE1   1 
ATOM   12813 C  CE2   . PHE A 1 3149 ? 239.827 231.017 180.544 1.00 43.71  ? 3149 PHE A CE2   1 
ATOM   12814 C  CZ    . PHE A 1 3149 ? 240.876 230.832 181.417 1.00 46.95  ? 3149 PHE A CZ    1 
ATOM   12815 N  N     . VAL A 1 3150 ? 236.089 228.018 180.034 1.00 39.16  ? 3150 VAL A N     1 
ATOM   12816 C  CA    . VAL A 1 3150 ? 235.030 228.907 180.500 1.00 35.77  ? 3150 VAL A CA    1 
ATOM   12817 C  C     . VAL A 1 3150 ? 234.308 228.289 181.686 1.00 35.64  ? 3150 VAL A C     1 
ATOM   12818 O  O     . VAL A 1 3150 ? 233.990 228.975 182.664 1.00 43.73  ? 3150 VAL A O     1 
ATOM   12819 C  CB    . VAL A 1 3150 ? 234.060 229.226 179.348 1.00 29.70  ? 3150 VAL A CB    1 
ATOM   12820 C  CG1   . VAL A 1 3150 ? 232.737 229.721 179.890 1.00 31.81  ? 3150 VAL A CG1   1 
ATOM   12821 C  CG2   . VAL A 1 3150 ? 234.671 230.253 178.412 1.00 33.73  ? 3150 VAL A CG2   1 
ATOM   12822 N  N     . HIS A 1 3151 ? 234.040 226.984 181.622 1.00 36.30  ? 3151 HIS A N     1 
ATOM   12823 C  CA    . HIS A 1 3151 ? 233.407 226.324 182.761 1.00 38.41  ? 3151 HIS A CA    1 
ATOM   12824 C  C     . HIS A 1 3151 ? 234.295 226.378 184.000 1.00 46.30  ? 3151 HIS A C     1 
ATOM   12825 O  O     . HIS A 1 3151 ? 233.810 226.628 185.108 1.00 51.56  ? 3151 HIS A O     1 
ATOM   12826 C  CB    . HIS A 1 3151 ? 233.055 224.878 182.421 1.00 35.67  ? 3151 HIS A CB    1 
ATOM   12827 C  CG    . HIS A 1 3151 ? 232.246 224.195 183.480 1.00 39.87  ? 3151 HIS A CG    1 
ATOM   12828 N  ND1   . HIS A 1 3151 ? 230.907 224.455 183.677 1.00 41.49  ? 3151 HIS A ND1   1 
ATOM   12829 C  CD2   . HIS A 1 3151 ? 232.590 223.273 184.409 1.00 44.05  ? 3151 HIS A CD2   1 
ATOM   12830 C  CE1   . HIS A 1 3151 ? 230.459 223.717 184.676 1.00 37.28  ? 3151 HIS A CE1   1 
ATOM   12831 N  NE2   . HIS A 1 3151 ? 231.460 222.991 185.138 1.00 44.48  ? 3151 HIS A NE2   1 
ATOM   12832 N  N     . GLN A 1 3152 ? 235.601 226.148 183.833 1.00 42.59  ? 3152 GLN A N     1 
ATOM   12833 C  CA    . GLN A 1 3152 ? 236.492 226.113 184.994 1.00 40.67  ? 3152 GLN A CA    1 
ATOM   12834 C  C     . GLN A 1 3152 ? 236.700 227.498 185.610 1.00 50.94  ? 3152 GLN A C     1 
ATOM   12835 O  O     . GLN A 1 3152 ? 236.975 227.611 186.818 1.00 52.51  ? 3152 GLN A O     1 
ATOM   12836 C  CB    . GLN A 1 3152 ? 237.832 225.495 184.602 1.00 38.28  ? 3152 GLN A CB    1 
ATOM   12837 C  CG    . GLN A 1 3152 ? 237.710 224.099 184.016 1.00 47.48  ? 3152 GLN A CG    1 
ATOM   12838 C  CD    . GLN A 1 3152 ? 239.043 223.386 183.925 1.00 51.57  ? 3152 GLN A CD    1 
ATOM   12839 O  OE1   . GLN A 1 3152 ? 240.068 223.998 183.630 1.00 49.53  ? 3152 GLN A OE1   1 
ATOM   12840 N  NE2   . GLN A 1 3152 ? 239.034 222.082 184.172 1.00 44.27  ? 3152 GLN A NE2   1 
ATOM   12841 N  N     . THR A 1 3153 ? 236.591 228.557 184.803 1.00 51.28  ? 3153 THR A N     1 
ATOM   12842 C  CA    . THR A 1 3153 ? 236.734 229.904 185.349 1.00 38.48  ? 3153 THR A CA    1 
ATOM   12843 C  C     . THR A 1 3153 ? 235.671 230.207 186.391 1.00 40.04  ? 3153 THR A C     1 
ATOM   12844 O  O     . THR A 1 3153 ? 235.906 231.013 187.294 1.00 51.54  ? 3153 THR A O     1 
ATOM   12845 C  CB    . THR A 1 3153 ? 236.681 230.954 184.241 1.00 43.72  ? 3153 THR A CB    1 
ATOM   12846 O  OG1   . THR A 1 3153 ? 235.459 230.820 183.503 1.00 45.10  ? 3153 THR A OG1   1 
ATOM   12847 C  CG2   . THR A 1 3153 ? 237.866 230.819 183.318 1.00 48.28  ? 3153 THR A CG2   1 
ATOM   12848 N  N     . LEU A 1 3154 ? 234.502 229.574 186.295 1.00 42.86  ? 3154 LEU A N     1 
ATOM   12849 C  CA    . LEU A 1 3154 ? 233.473 229.796 187.305 1.00 44.28  ? 3154 LEU A CA    1 
ATOM   12850 C  C     . LEU A 1 3154 ? 233.854 229.162 188.635 1.00 42.56  ? 3154 LEU A C     1 
ATOM   12851 O  O     . LEU A 1 3154 ? 233.595 229.738 189.695 1.00 51.53  ? 3154 LEU A O     1 
ATOM   12852 C  CB    . LEU A 1 3154 ? 232.122 229.275 186.823 1.00 42.60  ? 3154 LEU A CB    1 
ATOM   12853 C  CG    . LEU A 1 3154 ? 231.325 230.222 185.925 1.00 40.35  ? 3154 LEU A CG    1 
ATOM   12854 C  CD1   . LEU A 1 3154 ? 230.960 231.467 186.707 1.00 43.56  ? 3154 LEU A CD1   1 
ATOM   12855 C  CD2   . LEU A 1 3154 ? 232.047 230.589 184.643 1.00 39.85  ? 3154 LEU A CD2   1 
ATOM   12856 N  N     . HIS A 1 3155 ? 234.473 227.982 188.604 1.00 50.23  ? 3155 HIS A N     1 
ATOM   12857 C  CA    . HIS A 1 3155 ? 234.999 227.406 189.837 1.00 53.24  ? 3155 HIS A CA    1 
ATOM   12858 C  C     . HIS A 1 3155 ? 236.074 228.299 190.438 1.00 55.56  ? 3155 HIS A C     1 
ATOM   12859 O  O     . HIS A 1 3155 ? 236.108 228.515 191.657 1.00 55.51  ? 3155 HIS A O     1 
ATOM   12860 C  CB    . HIS A 1 3155 ? 235.550 226.006 189.574 1.00 50.33  ? 3155 HIS A CB    1 
ATOM   12861 C  CG    . HIS A 1 3155 ? 234.492 224.980 189.316 1.00 51.32  ? 3155 HIS A CG    1 
ATOM   12862 N  ND1   . HIS A 1 3155 ? 234.395 224.294 188.125 1.00 48.84  ? 3155 HIS A ND1   1 
ATOM   12863 C  CD2   . HIS A 1 3155 ? 233.487 224.521 190.098 1.00 51.79  ? 3155 HIS A CD2   1 
ATOM   12864 C  CE1   . HIS A 1 3155 ? 233.375 223.458 188.184 1.00 52.06  ? 3155 HIS A CE1   1 
ATOM   12865 N  NE2   . HIS A 1 3155 ? 232.807 223.576 189.371 1.00 58.04  ? 3155 HIS A NE2   1 
ATOM   12866 N  N     . GLN A 1 3156 ? 236.957 228.838 189.593 1.00 57.98  ? 3156 GLN A N     1 
ATOM   12867 C  CA    . GLN A 1 3156 ? 237.989 229.742 190.102 1.00 53.24  ? 3156 GLN A CA    1 
ATOM   12868 C  C     . GLN A 1 3156 ? 237.381 231.005 190.714 1.00 59.80  ? 3156 GLN A C     1 
ATOM   12869 O  O     . GLN A 1 3156 ? 237.813 231.459 191.782 1.00 62.52  ? 3156 GLN A O     1 
ATOM   12870 C  CB    . GLN A 1 3156 ? 238.971 230.100 188.990 1.00 51.63  ? 3156 GLN A CB    1 
ATOM   12871 C  CG    . GLN A 1 3156 ? 240.016 229.029 188.734 1.00 58.11  ? 3156 GLN A CG    1 
ATOM   12872 C  CD    . GLN A 1 3156 ? 240.619 229.122 187.350 1.00 63.17  ? 3156 GLN A CD    1 
ATOM   12873 O  OE1   . GLN A 1 3156 ? 240.698 230.202 186.766 1.00 63.68  ? 3156 GLN A OE1   1 
ATOM   12874 N  NE2   . GLN A 1 3156 ? 241.052 227.986 186.815 1.00 58.36  ? 3156 GLN A NE2   1 
ATOM   12875 N  N     . ALA A 1 3157 ? 236.373 231.582 190.055 1.00 63.77  ? 3157 ALA A N     1 
ATOM   12876 C  CA    . ALA A 1 3157 ? 235.734 232.790 190.570 1.00 60.20  ? 3157 ALA A CA    1 
ATOM   12877 C  C     . ALA A 1 3157 ? 234.977 232.510 191.861 1.00 57.58  ? 3157 ALA A C     1 
ATOM   12878 O  O     . ALA A 1 3157 ? 234.949 233.350 192.768 1.00 66.93  ? 3157 ALA A O     1 
ATOM   12879 C  CB    . ALA A 1 3157 ? 234.798 233.379 189.517 1.00 56.87  ? 3157 ALA A CB    1 
ATOM   12880 N  N     . ASN A 1 3158 ? 234.339 231.344 191.957 1.00 56.57  ? 3158 ASN A N     1 
ATOM   12881 C  CA    . ASN A 1 3158 ? 233.664 230.977 193.195 1.00 60.15  ? 3158 ASN A CA    1 
ATOM   12882 C  C     . ASN A 1 3158 ? 234.663 230.796 194.329 1.00 65.18  ? 3158 ASN A C     1 
ATOM   12883 O  O     . ASN A 1 3158 ? 234.385 231.172 195.472 1.00 68.21  ? 3158 ASN A O     1 
ATOM   12884 C  CB    . ASN A 1 3158 ? 232.843 229.709 192.984 1.00 61.28  ? 3158 ASN A CB    1 
ATOM   12885 C  CG    . ASN A 1 3158 ? 231.506 229.991 192.340 1.00 63.84  ? 3158 ASN A CG    1 
ATOM   12886 O  OD1   . ASN A 1 3158 ? 230.522 230.268 193.019 1.00 64.62  ? 3158 ASN A OD1   1 
ATOM   12887 N  ND2   . ASN A 1 3158 ? 231.469 229.938 191.016 1.00 67.45  ? 3158 ASN A ND2   1 
ATOM   12888 N  N     . ALA A 1 3159 ? 235.832 230.224 194.033 1.00 70.98  ? 3159 ALA A N     1 
ATOM   12889 C  CA    . ALA A 1 3159 ? 236.882 230.147 195.045 1.00 69.26  ? 3159 ALA A CA    1 
ATOM   12890 C  C     . ALA A 1 3159 ? 237.314 231.538 195.494 1.00 70.64  ? 3159 ALA A C     1 
ATOM   12891 O  O     . ALA A 1 3159 ? 237.497 231.786 196.693 1.00 73.46  ? 3159 ALA A O     1 
ATOM   12892 C  CB    . ALA A 1 3159 ? 238.075 229.360 194.505 1.00 66.09  ? 3159 ALA A CB    1 
ATOM   12893 N  N     . ARG A 1 3160 ? 237.476 232.461 194.541 1.00 70.52  ? 3160 ARG A N     1 
ATOM   12894 C  CA    . ARG A 1 3160 ? 237.864 233.827 194.889 1.00 69.39  ? 3160 ARG A CA    1 
ATOM   12895 C  C     . ARG A 1 3160 ? 236.806 234.513 195.750 1.00 70.98  ? 3160 ARG A C     1 
ATOM   12896 O  O     . ARG A 1 3160 ? 237.142 235.259 196.677 1.00 75.02  ? 3160 ARG A O     1 
ATOM   12897 C  CB    . ARG A 1 3160 ? 238.140 234.638 193.622 1.00 71.08  ? 3160 ARG A CB    1 
ATOM   12898 C  CG    . ARG A 1 3160 ? 239.479 234.326 192.970 1.00 71.17  ? 3160 ARG A CG    1 
ATOM   12899 C  CD    . ARG A 1 3160 ? 239.834 235.341 191.891 1.00 73.08  ? 3160 ARG A CD    1 
ATOM   12900 N  NE    . ARG A 1 3160 ? 239.505 234.866 190.551 1.00 80.91  ? 3160 ARG A NE    1 
ATOM   12901 C  CZ    . ARG A 1 3160 ? 238.636 235.448 189.736 1.00 78.56  ? 3160 ARG A CZ    1 
ATOM   12902 N  NH1   . ARG A 1 3160 ? 237.986 236.546 190.088 1.00 75.72  ? 3160 ARG A NH1   1 
ATOM   12903 N  NH2   . ARG A 1 3160 ? 238.416 234.918 188.536 1.00 68.60  ? 3160 ARG A NH2   1 
ATOM   12904 N  N     . LEU A 1 3161 ? 235.524 234.295 195.446 1.00 69.97  ? 3161 LEU A N     1 
ATOM   12905 C  CA    . LEU A 1 3161 ? 234.460 234.802 196.313 1.00 69.71  ? 3161 LEU A CA    1 
ATOM   12906 C  C     . LEU A 1 3161 ? 234.525 234.177 197.701 1.00 71.64  ? 3161 LEU A C     1 
ATOM   12907 O  O     . LEU A 1 3161 ? 234.333 234.867 198.708 1.00 74.77  ? 3161 LEU A O     1 
ATOM   12908 C  CB    . LEU A 1 3161 ? 233.087 234.549 195.688 1.00 74.56  ? 3161 LEU A CB    1 
ATOM   12909 C  CG    . LEU A 1 3161 ? 232.656 235.252 194.403 1.00 73.61  ? 3161 LEU A CG    1 
ATOM   12910 C  CD1   . LEU A 1 3161 ? 231.325 234.703 193.933 1.00 75.21  ? 3161 LEU A CD1   1 
ATOM   12911 C  CD2   . LEU A 1 3161 ? 232.502 236.738 194.698 1.00 68.18  ? 3161 LEU A CD2   1 
ATOM   12912 N  N     . ALA A 1 3162 ? 234.784 232.871 197.775 1.00 72.19  ? 3162 ALA A N     1 
ATOM   12913 C  CA    . ALA A 1 3162 ? 234.802 232.200 199.069 1.00 77.32  ? 3162 ALA A CA    1 
ATOM   12914 C  C     . ALA A 1 3162 ? 235.926 232.727 199.951 1.00 80.09  ? 3162 ALA A C     1 
ATOM   12915 O  O     . ALA A 1 3162 ? 235.731 232.951 201.151 1.00 73.61  ? 3162 ALA A O     1 
ATOM   12916 C  CB    . ALA A 1 3162 ? 234.923 230.689 198.873 1.00 75.83  ? 3162 ALA A CB    1 
ATOM   12917 N  N     . LYS A 1 3163 ? 237.110 232.942 199.375 1.00 85.24  ? 3163 LYS A N     1 
ATOM   12918 C  CA    . LYS A 1 3163 ? 238.221 233.454 200.169 1.00 84.51  ? 3163 LYS A CA    1 
ATOM   12919 C  C     . LYS A 1 3163 ? 238.054 234.924 200.538 1.00 84.68  ? 3163 LYS A C     1 
ATOM   12920 O  O     . LYS A 1 3163 ? 238.754 235.403 201.435 1.00 87.72  ? 3163 LYS A O     1 
ATOM   12921 C  CB    . LYS A 1 3163 ? 239.546 233.236 199.436 1.00 81.19  ? 3163 LYS A CB    1 
ATOM   12922 C  CG    . LYS A 1 3163 ? 240.158 231.852 199.653 1.00 83.25  ? 3163 LYS A CG    1 
ATOM   12923 C  CD    . LYS A 1 3163 ? 239.398 230.756 198.919 1.00 85.26  ? 3163 LYS A CD    1 
ATOM   12924 C  CE    . LYS A 1 3163 ? 240.072 229.403 199.075 1.00 87.03  ? 3163 LYS A CE    1 
ATOM   12925 N  NZ    . LYS A 1 3163 ? 239.263 228.317 198.459 1.00 84.46  ? 3163 LYS A NZ    1 
ATOM   12926 N  N     . ARG A 1 3164 ? 237.149 235.648 199.883 1.00 78.77  ? 3164 ARG A N     1 
ATOM   12927 C  CA    . ARG A 1 3164 ? 236.857 237.022 200.270 1.00 79.37  ? 3164 ARG A CA    1 
ATOM   12928 C  C     . ARG A 1 3164 ? 235.599 237.142 201.122 1.00 81.53  ? 3164 ARG A C     1 
ATOM   12929 O  O     . ARG A 1 3164 ? 235.121 238.260 201.342 1.00 82.75  ? 3164 ARG A O     1 
ATOM   12930 C  CB    . ARG A 1 3164 ? 236.740 237.926 199.031 1.00 74.61  ? 3164 ARG A CB    1 
ATOM   12931 C  CG    . ARG A 1 3164 ? 238.061 238.130 198.293 1.00 76.97  ? 3164 ARG A CG    1 
ATOM   12932 C  CD    . ARG A 1 3164 ? 237.946 239.092 197.119 1.00 81.07  ? 3164 ARG A CD    1 
ATOM   12933 N  NE    . ARG A 1 3164 ? 237.158 238.564 196.011 1.00 84.42  ? 3164 ARG A NE    1 
ATOM   12934 C  CZ    . ARG A 1 3164 ? 235.984 239.051 195.630 1.00 81.52  ? 3164 ARG A CZ    1 
ATOM   12935 N  NH1   . ARG A 1 3164 ? 235.433 240.087 196.242 1.00 79.43  ? 3164 ARG A NH1   1 
ATOM   12936 N  NH2   . ARG A 1 3164 ? 235.357 238.500 194.594 1.00 80.67  ? 3164 ARG A NH2   1 
ATOM   12937 N  N     . GLY A 1 3165 ? 235.050 236.028 201.599 1.00 73.53  ? 3165 GLY A N     1 
ATOM   12938 C  CA    . GLY A 1 3165 ? 233.905 236.071 202.483 1.00 71.73  ? 3165 GLY A CA    1 
ATOM   12939 C  C     . GLY A 1 3165 ? 232.574 236.270 201.801 1.00 74.18  ? 3165 GLY A C     1 
ATOM   12940 O  O     . GLY A 1 3165 ? 231.548 236.341 202.488 1.00 74.23  ? 3165 GLY A O     1 
ATOM   12941 N  N     . GLY A 1 3166 ? 232.552 236.365 200.473 1.00 77.45  ? 3166 GLY A N     1 
ATOM   12942 C  CA    . GLY A 1 3166 ? 231.306 236.521 199.758 1.00 74.60  ? 3166 GLY A CA    1 
ATOM   12943 C  C     . GLY A 1 3166 ? 230.543 235.219 199.649 1.00 74.84  ? 3166 GLY A C     1 
ATOM   12944 O  O     . GLY A 1 3166 ? 230.967 234.167 200.127 1.00 73.77  ? 3166 GLY A O     1 
ATOM   12945 N  N     . ARG A 1 3167 ? 229.384 235.299 199.004 1.00 71.58  ? 3167 ARG A N     1 
ATOM   12946 C  CA    . ARG A 1 3167 ? 228.521 234.142 198.828 1.00 72.94  ? 3167 ARG A CA    1 
ATOM   12947 C  C     . ARG A 1 3167 ? 228.705 233.562 197.434 1.00 71.55  ? 3167 ARG A C     1 
ATOM   12948 O  O     . ARG A 1 3167 ? 228.767 234.302 196.447 1.00 69.31  ? 3167 ARG A O     1 
ATOM   12949 C  CB    . ARG A 1 3167 ? 227.061 234.523 199.061 1.00 68.91  ? 3167 ARG A CB    1 
ATOM   12950 C  CG    . ARG A 1 3167 ? 226.092 233.357 199.009 1.00 71.55  ? 3167 ARG A CG    1 
ATOM   12951 C  CD    . ARG A 1 3167 ? 224.699 233.861 199.292 1.00 70.77  ? 3167 ARG A CD    1 
ATOM   12952 N  NE    . ARG A 1 3167 ? 224.624 234.380 200.650 1.00 74.64  ? 3167 ARG A NE    1 
ATOM   12953 C  CZ    . ARG A 1 3167 ? 224.444 235.658 200.952 1.00 76.98  ? 3167 ARG A CZ    1 
ATOM   12954 N  NH1   . ARG A 1 3167 ? 224.347 236.582 200.010 1.00 71.91  ? 3167 ARG A NH1   1 
ATOM   12955 N  NH2   . ARG A 1 3167 ? 224.382 236.021 202.230 1.00 74.78  ? 3167 ARG A NH2   1 
ATOM   12956 N  N     . THR A 1 3168 ? 228.796 232.239 197.362 1.00 67.03  ? 3168 THR A N     1 
ATOM   12957 C  CA    . THR A 1 3168 ? 229.026 231.524 196.117 1.00 68.48  ? 3168 THR A CA    1 
ATOM   12958 C  C     . THR A 1 3168 ? 227.852 230.599 195.838 1.00 67.00  ? 3168 THR A C     1 
ATOM   12959 O  O     . THR A 1 3168 ? 227.209 230.101 196.766 1.00 66.86  ? 3168 THR A O     1 
ATOM   12960 C  CB    . THR A 1 3168 ? 230.316 230.705 196.179 1.00 68.41  ? 3168 THR A CB    1 
ATOM   12961 O  OG1   . THR A 1 3168 ? 230.138 229.601 197.073 1.00 68.52  ? 3168 THR A OG1   1 
ATOM   12962 C  CG2   . THR A 1 3168 ? 231.457 231.559 196.681 1.00 71.14  ? 3168 THR A CG2   1 
ATOM   12963 N  N     . MET A 1 3169 ? 227.576 230.378 194.558 1.00 58.84  ? 3169 MET A N     1 
ATOM   12964 C  CA    . MET A 1 3169 ? 226.576 229.415 194.125 1.00 60.26  ? 3169 MET A CA    1 
ATOM   12965 C  C     . MET A 1 3169 ? 227.271 228.256 193.426 1.00 60.09  ? 3169 MET A C     1 
ATOM   12966 O  O     . MET A 1 3169 ? 228.257 228.454 192.711 1.00 66.23  ? 3169 MET A O     1 
ATOM   12967 C  CB    . MET A 1 3169 ? 225.548 230.061 193.194 1.00 58.21  ? 3169 MET A CB    1 
ATOM   12968 C  CG    . MET A 1 3169 ? 224.581 230.986 193.908 1.00 58.86  ? 3169 MET A CG    1 
ATOM   12969 S  SD    . MET A 1 3169 ? 224.038 230.309 195.486 1.00 72.20  ? 3169 MET A SD    1 
ATOM   12970 C  CE    . MET A 1 3169 ? 222.747 231.467 195.923 1.00 60.89  ? 3169 MET A CE    1 
ATOM   12971 N  N     . ALA A 1 3170 ? 226.761 227.049 193.650 1.00 47.23  ? 3170 ALA A N     1 
ATOM   12972 C  CA    . ALA A 1 3170 ? 227.398 225.854 193.115 1.00 51.56  ? 3170 ALA A CA    1 
ATOM   12973 C  C     . ALA A 1 3170 ? 227.394 225.871 191.593 1.00 51.34  ? 3170 ALA A C     1 
ATOM   12974 O  O     . ALA A 1 3170 ? 226.382 226.189 190.963 1.00 51.65  ? 3170 ALA A O     1 
ATOM   12975 C  CB    . ALA A 1 3170 ? 226.685 224.605 193.631 1.00 52.65  ? 3170 ALA A CB    1 
ATOM   12976 N  N     . ILE A 1 3171 ? 228.535 225.531 191.004 1.00 43.61  ? 3171 ILE A N     1 
ATOM   12977 C  CA    . ILE A 1 3171 ? 228.676 225.407 189.559 1.00 40.98  ? 3171 ILE A CA    1 
ATOM   12978 C  C     . ILE A 1 3171 ? 228.518 223.933 189.216 1.00 47.82  ? 3171 ILE A C     1 
ATOM   12979 O  O     . ILE A 1 3171 ? 229.410 223.121 189.483 1.00 50.43  ? 3171 ILE A O     1 
ATOM   12980 C  CB    . ILE A 1 3171 ? 230.019 225.958 189.068 1.00 38.35  ? 3171 ILE A CB    1 
ATOM   12981 C  CG1   . ILE A 1 3171 ? 230.158 227.429 189.455 1.00 42.85  ? 3171 ILE A CG1   1 
ATOM   12982 C  CG2   . ILE A 1 3171 ? 230.145 225.793 187.567 1.00 47.56  ? 3171 ILE A CG2   1 
ATOM   12983 C  CD1   . ILE A 1 3171 ? 229.152 228.332 188.783 1.00 43.23  ? 3171 ILE A CD1   1 
ATOM   12984 N  N     . THR A 1 3172 ? 227.386 223.589 188.626 1.00 39.26  ? 3172 THR A N     1 
ATOM   12985 C  CA    . THR A 1 3172 ? 227.014 222.222 188.318 1.00 36.35  ? 3172 THR A CA    1 
ATOM   12986 C  C     . THR A 1 3172 ? 227.184 221.937 186.833 1.00 40.37  ? 3172 THR A C     1 
ATOM   12987 O  O     . THR A 1 3172 ? 227.274 222.862 186.020 1.00 43.74  ? 3172 THR A O     1 
ATOM   12988 C  CB    . THR A 1 3172 ? 225.560 221.964 188.733 1.00 36.13  ? 3172 THR A CB    1 
ATOM   12989 O  OG1   . THR A 1 3172 ? 224.679 222.706 187.883 1.00 50.90  ? 3172 THR A OG1   1 
ATOM   12990 C  CG2   . THR A 1 3172 ? 225.340 222.386 190.173 1.00 39.88  ? 3172 THR A CG2   1 
ATOM   12991 N  N     . PRO A 1 3173 ? 227.255 220.662 186.442 1.00 34.27  ? 3173 PRO A N     1 
ATOM   12992 C  CA    . PRO A 1 3173 ? 227.322 220.340 185.008 1.00 24.38  ? 3173 PRO A CA    1 
ATOM   12993 C  C     . PRO A 1 3173 ? 226.133 220.850 184.220 1.00 34.13  ? 3173 PRO A C     1 
ATOM   12994 O  O     . PRO A 1 3173 ? 226.249 221.033 183.002 1.00 43.30  ? 3173 PRO A O     1 
ATOM   12995 C  CB    . PRO A 1 3173 ? 227.383 218.809 185.000 1.00 29.61  ? 3173 PRO A CB    1 
ATOM   12996 C  CG    . PRO A 1 3173 ? 227.995 218.463 186.303 1.00 31.84  ? 3173 PRO A CG    1 
ATOM   12997 C  CD    . PRO A 1 3173 ? 227.481 219.471 187.278 1.00 35.72  ? 3173 PRO A CD    1 
ATOM   12998 N  N     . ARG A 1 3174 ? 224.990 221.075 184.870 1.00 38.77  ? 3174 ARG A N     1 
ATOM   12999 C  CA    . ARG A 1 3174 ? 223.853 221.671 184.181 1.00 34.39  ? 3174 ARG A CA    1 
ATOM   13000 C  C     . ARG A 1 3174 ? 224.176 223.077 183.693 1.00 39.89  ? 3174 ARG A C     1 
ATOM   13001 O  O     . ARG A 1 3174 ? 223.656 223.508 182.658 1.00 47.61  ? 3174 ARG A O     1 
ATOM   13002 C  CB    . ARG A 1 3174 ? 222.636 221.680 185.100 1.00 34.80  ? 3174 ARG A CB    1 
ATOM   13003 C  CG    . ARG A 1 3174 ? 222.069 220.298 185.356 1.00 43.82  ? 3174 ARG A CG    1 
ATOM   13004 C  CD    . ARG A 1 3174 ? 220.684 220.368 185.968 1.00 42.96  ? 3174 ARG A CD    1 
ATOM   13005 N  NE    . ARG A 1 3174 ? 219.680 220.797 185.004 1.00 37.07  ? 3174 ARG A NE    1 
ATOM   13006 C  CZ    . ARG A 1 3174 ? 218.376 220.790 185.235 1.00 43.01  ? 3174 ARG A CZ    1 
ATOM   13007 N  NH1   . ARG A 1 3174 ? 217.881 220.383 186.391 1.00 39.76  ? 3174 ARG A NH1   1 
ATOM   13008 N  NH2   . ARG A 1 3174 ? 217.546 221.197 184.279 1.00 46.51  ? 3174 ARG A NH2   1 
ATOM   13009 N  N     . HIS A 1 3175 ? 225.044 223.796 184.410 1.00 39.46  ? 3175 HIS A N     1 
ATOM   13010 C  CA    . HIS A 1 3175 ? 225.533 225.075 183.909 1.00 30.30  ? 3175 HIS A CA    1 
ATOM   13011 C  C     . HIS A 1 3175 ? 226.270 224.895 182.591 1.00 31.79  ? 3175 HIS A C     1 
ATOM   13012 O  O     . HIS A 1 3175 ? 226.073 225.671 181.650 1.00 43.51  ? 3175 HIS A O     1 
ATOM   13013 C  CB    . HIS A 1 3175 ? 226.456 225.731 184.935 1.00 37.00  ? 3175 HIS A CB    1 
ATOM   13014 C  CG    . HIS A 1 3175 ? 225.745 226.304 186.120 1.00 34.21  ? 3175 HIS A CG    1 
ATOM   13015 N  ND1   . HIS A 1 3175 ? 224.999 225.534 186.986 1.00 39.54  ? 3175 HIS A ND1   1 
ATOM   13016 C  CD2   . HIS A 1 3175 ? 225.680 227.571 186.591 1.00 36.82  ? 3175 HIS A CD2   1 
ATOM   13017 C  CE1   . HIS A 1 3175 ? 224.500 226.303 187.936 1.00 42.15  ? 3175 HIS A CE1   1 
ATOM   13018 N  NE2   . HIS A 1 3175 ? 224.898 227.544 187.719 1.00 44.77  ? 3175 HIS A NE2   1 
ATOM   13019 N  N     . TYR A 1 3176 ? 227.123 223.873 182.505 1.00 28.55  ? 3176 TYR A N     1 
ATOM   13020 C  CA    . TYR A 1 3176 ? 227.845 223.604 181.267 1.00 24.74  ? 3176 TYR A CA    1 
ATOM   13021 C  C     . TYR A 1 3176 ? 226.893 223.214 180.145 1.00 31.97  ? 3176 TYR A C     1 
ATOM   13022 O  O     . TYR A 1 3176 ? 227.073 223.635 178.996 1.00 45.34  ? 3176 TYR A O     1 
ATOM   13023 C  CB    . TYR A 1 3176 ? 228.878 222.504 181.496 1.00 33.41  ? 3176 TYR A CB    1 
ATOM   13024 C  CG    . TYR A 1 3176 ? 229.821 222.295 180.336 1.00 34.10  ? 3176 TYR A CG    1 
ATOM   13025 C  CD1   . TYR A 1 3176 ? 230.790 223.236 180.027 1.00 30.16  ? 3176 TYR A CD1   1 
ATOM   13026 C  CD2   . TYR A 1 3176 ? 229.744 221.153 179.553 1.00 33.16  ? 3176 TYR A CD2   1 
ATOM   13027 C  CE1   . TYR A 1 3176 ? 231.652 223.047 178.973 1.00 28.36  ? 3176 TYR A CE1   1 
ATOM   13028 C  CE2   . TYR A 1 3176 ? 230.604 220.958 178.496 1.00 31.79  ? 3176 TYR A CE2   1 
ATOM   13029 C  CZ    . TYR A 1 3176 ? 231.555 221.908 178.210 1.00 30.81  ? 3176 TYR A CZ    1 
ATOM   13030 O  OH    . TYR A 1 3176 ? 232.414 221.715 177.156 1.00 39.08  ? 3176 TYR A OH    1 
ATOM   13031 N  N     . LEU A 1 3177 ? 225.886 222.398 180.455 1.00 36.31  ? 3177 LEU A N     1 
ATOM   13032 C  CA    . LEU A 1 3177 ? 224.916 222.012 179.437 1.00 33.55  ? 3177 LEU A CA    1 
ATOM   13033 C  C     . LEU A 1 3177 ? 224.159 223.226 178.916 1.00 38.02  ? 3177 LEU A C     1 
ATOM   13034 O  O     . LEU A 1 3177 ? 223.954 223.366 177.704 1.00 47.83  ? 3177 LEU A O     1 
ATOM   13035 C  CB    . LEU A 1 3177 ? 223.950 220.971 179.999 1.00 43.78  ? 3177 LEU A CB    1 
ATOM   13036 C  CG    . LEU A 1 3177 ? 224.581 219.669 180.494 1.00 39.64  ? 3177 LEU A CG    1 
ATOM   13037 C  CD1   . LEU A 1 3177 ? 223.612 218.911 181.383 1.00 40.79  ? 3177 LEU A CD1   1 
ATOM   13038 C  CD2   . LEU A 1 3177 ? 225.026 218.808 179.326 1.00 30.83  ? 3177 LEU A CD2   1 
ATOM   13039 N  N     . ASP A 1 3178 ? 223.752 224.126 179.815 1.00 39.23  ? 3178 ASP A N     1 
ATOM   13040 C  CA    . ASP A 1 3178 ? 223.107 225.362 179.385 1.00 37.05  ? 3178 ASP A CA    1 
ATOM   13041 C  C     . ASP A 1 3178 ? 224.047 226.211 178.544 1.00 38.86  ? 3178 ASP A C     1 
ATOM   13042 O  O     . ASP A 1 3178 ? 223.627 226.812 177.554 1.00 47.03  ? 3178 ASP A O     1 
ATOM   13043 C  CB    . ASP A 1 3178 ? 222.625 226.164 180.589 1.00 32.50  ? 3178 ASP A CB    1 
ATOM   13044 C  CG    . ASP A 1 3178 ? 221.396 225.574 181.222 1.00 54.75  ? 3178 ASP A CG    1 
ATOM   13045 O  OD1   . ASP A 1 3178 ? 220.677 224.815 180.540 1.00 56.31  ? 3178 ASP A OD1   1 
ATOM   13046 O  OD2   . ASP A 1 3178 ? 221.139 225.884 182.399 1.00 58.26  ? 3178 ASP A OD2   1 
ATOM   13047 N  N     . PHE A 1 3179 ? 225.318 226.288 178.935 1.00 30.22  ? 3179 PHE A N     1 
ATOM   13048 C  CA    . PHE A 1 3179 ? 226.279 227.086 178.183 1.00 21.99  ? 3179 PHE A CA    1 
ATOM   13049 C  C     . PHE A 1 3179 ? 226.422 226.569 176.759 1.00 32.00  ? 3179 PHE A C     1 
ATOM   13050 O  O     . PHE A 1 3179 ? 226.369 227.342 175.797 1.00 45.56  ? 3179 PHE A O     1 
ATOM   13051 C  CB    . PHE A 1 3179 ? 227.623 227.085 178.916 1.00 28.18  ? 3179 PHE A CB    1 
ATOM   13052 C  CG    . PHE A 1 3179 ? 228.792 227.523 178.075 1.00 31.08  ? 3179 PHE A CG    1 
ATOM   13053 C  CD1   . PHE A 1 3179 ? 228.716 228.644 177.268 1.00 36.04  ? 3179 PHE A CD1   1 
ATOM   13054 C  CD2   . PHE A 1 3179 ? 229.978 226.815 178.112 1.00 31.88  ? 3179 PHE A CD2   1 
ATOM   13055 C  CE1   . PHE A 1 3179 ? 229.793 229.036 176.505 1.00 35.35  ? 3179 PHE A CE1   1 
ATOM   13056 C  CE2   . PHE A 1 3179 ? 231.055 227.206 177.353 1.00 34.32  ? 3179 PHE A CE2   1 
ATOM   13057 C  CZ    . PHE A 1 3179 ? 230.963 228.316 176.549 1.00 34.77  ? 3179 PHE A CZ    1 
ATOM   13058 N  N     . ILE A 1 3180 ? 226.583 225.257 176.600 1.00 38.28  ? 3180 ILE A N     1 
ATOM   13059 C  CA    . ILE A 1 3180 ? 226.792 224.705 175.264 1.00 34.16  ? 3180 ILE A CA    1 
ATOM   13060 C  C     . ILE A 1 3180 ? 225.510 224.787 174.436 1.00 44.70  ? 3180 ILE A C     1 
ATOM   13061 O  O     . ILE A 1 3180 ? 225.551 225.054 173.226 1.00 51.61  ? 3180 ILE A O     1 
ATOM   13062 C  CB    . ILE A 1 3180 ? 227.339 223.271 175.361 1.00 30.92  ? 3180 ILE A CB    1 
ATOM   13063 C  CG1   . ILE A 1 3180 ? 228.507 223.228 176.338 1.00 39.98  ? 3180 ILE A CG1   1 
ATOM   13064 C  CG2   . ILE A 1 3180 ? 227.878 222.833 174.037 1.00 49.51  ? 3180 ILE A CG2   1 
ATOM   13065 C  CD1   . ILE A 1 3180 ? 229.725 223.980 175.855 1.00 40.88  ? 3180 ILE A CD1   1 
ATOM   13066 N  N     . ASN A 1 3181 ? 224.350 224.571 175.067 1.00 42.99  ? 3181 ASN A N     1 
ATOM   13067 C  CA    . ASN A 1 3181 ? 223.084 224.725 174.357 1.00 38.98  ? 3181 ASN A CA    1 
ATOM   13068 C  C     . ASN A 1 3181 ? 222.876 226.164 173.898 1.00 46.13  ? 3181 ASN A C     1 
ATOM   13069 O  O     . ASN A 1 3181 ? 222.430 226.407 172.769 1.00 54.83  ? 3181 ASN A O     1 
ATOM   13070 C  CB    . ASN A 1 3181 ? 221.931 224.271 175.249 1.00 41.72  ? 3181 ASN A CB    1 
ATOM   13071 C  CG    . ASN A 1 3181 ? 220.703 223.867 174.458 1.00 56.53  ? 3181 ASN A CG    1 
ATOM   13072 O  OD1   . ASN A 1 3181 ? 220.550 224.236 173.294 1.00 57.52  ? 3181 ASN A OD1   1 
ATOM   13073 N  ND2   . ASN A 1 3181 ? 219.815 223.110 175.091 1.00 51.00  ? 3181 ASN A ND2   1 
ATOM   13074 N  N     . HIS A 1 3182 ? 223.189 227.131 174.764 1.00 38.68  ? 3182 HIS A N     1 
ATOM   13075 C  CA    . HIS A 1 3182 ? 223.101 228.536 174.388 1.00 34.33  ? 3182 HIS A CA    1 
ATOM   13076 C  C     . HIS A 1 3182 ? 224.061 228.854 173.256 1.00 30.56  ? 3182 HIS A C     1 
ATOM   13077 O  O     . HIS A 1 3182 ? 223.733 229.629 172.355 1.00 48.45  ? 3182 HIS A O     1 
ATOM   13078 C  CB    . HIS A 1 3182 ? 223.400 229.420 175.599 1.00 43.33  ? 3182 HIS A CB    1 
ATOM   13079 C  CG    . HIS A 1 3182 ? 222.211 229.691 176.465 1.00 41.17  ? 3182 HIS A CG    1 
ATOM   13080 N  ND1   . HIS A 1 3182 ? 222.229 229.505 177.830 1.00 34.06  ? 3182 HIS A ND1   1 
ATOM   13081 C  CD2   . HIS A 1 3182 ? 220.973 230.148 176.164 1.00 44.21  ? 3182 HIS A CD2   1 
ATOM   13082 C  CE1   . HIS A 1 3182 ? 221.051 229.827 178.332 1.00 43.92  ? 3182 HIS A CE1   1 
ATOM   13083 N  NE2   . HIS A 1 3182 ? 220.271 230.221 177.342 1.00 47.40  ? 3182 HIS A NE2   1 
ATOM   13084 N  N     . TYR A 1 3183 ? 225.260 228.269 173.295 1.00 37.94  ? 3183 TYR A N     1 
ATOM   13085 C  CA    . TYR A 1 3183 ? 226.221 228.464 172.216 1.00 38.32  ? 3183 TYR A CA    1 
ATOM   13086 C  C     . TYR A 1 3183 ? 225.650 227.998 170.887 1.00 43.43  ? 3183 TYR A C     1 
ATOM   13087 O  O     . TYR A 1 3183 ? 225.687 228.736 169.896 1.00 53.36  ? 3183 TYR A O     1 
ATOM   13088 C  CB    . TYR A 1 3183 ? 227.514 227.718 172.544 1.00 36.96  ? 3183 TYR A CB    1 
ATOM   13089 C  CG    . TYR A 1 3183 ? 228.667 228.006 171.614 1.00 39.78  ? 3183 TYR A CG    1 
ATOM   13090 C  CD1   . TYR A 1 3183 ? 228.691 229.153 170.839 1.00 43.09  ? 3183 TYR A CD1   1 
ATOM   13091 C  CD2   . TYR A 1 3183 ? 229.736 227.129 171.516 1.00 45.93  ? 3183 TYR A CD2   1 
ATOM   13092 C  CE1   . TYR A 1 3183 ? 229.740 229.417 169.991 1.00 42.70  ? 3183 TYR A CE1   1 
ATOM   13093 C  CE2   . TYR A 1 3183 ? 230.791 227.386 170.669 1.00 45.77  ? 3183 TYR A CE2   1 
ATOM   13094 C  CZ    . TYR A 1 3183 ? 230.787 228.532 169.910 1.00 46.00  ? 3183 TYR A CZ    1 
ATOM   13095 O  OH    . TYR A 1 3183 ? 231.836 228.798 169.064 1.00 54.39  ? 3183 TYR A OH    1 
ATOM   13096 N  N     . ALA A 1 3184 ? 225.090 226.788 170.855 1.00 45.38  ? 3184 ALA A N     1 
ATOM   13097 C  CA    . ALA A 1 3184 ? 224.514 226.277 169.613 1.00 48.49  ? 3184 ALA A CA    1 
ATOM   13098 C  C     . ALA A 1 3184 ? 223.351 227.141 169.131 1.00 50.27  ? 3184 ALA A C     1 
ATOM   13099 O  O     . ALA A 1 3184 ? 223.282 227.493 167.944 1.00 52.28  ? 3184 ALA A O     1 
ATOM   13100 C  CB    . ALA A 1 3184 ? 224.061 224.832 169.804 1.00 52.20  ? 3184 ALA A CB    1 
ATOM   13101 N  N     . ASN A 1 3185 ? 222.431 227.499 170.037 1.00 51.42  ? 3185 ASN A N     1 
ATOM   13102 C  CA    . ASN A 1 3185 ? 221.272 228.300 169.645 1.00 46.42  ? 3185 ASN A CA    1 
ATOM   13103 C  C     . ASN A 1 3185 ? 221.687 229.671 169.123 1.00 48.86  ? 3185 ASN A C     1 
ATOM   13104 O  O     . ASN A 1 3185 ? 221.196 230.118 168.078 1.00 56.74  ? 3185 ASN A O     1 
ATOM   13105 C  CB    . ASN A 1 3185 ? 220.310 228.457 170.821 1.00 42.14  ? 3185 ASN A CB    1 
ATOM   13106 C  CG    . ASN A 1 3185 ? 219.648 227.154 171.212 1.00 54.73  ? 3185 ASN A CG    1 
ATOM   13107 O  OD1   . ASN A 1 3185 ? 219.785 226.145 170.524 1.00 57.27  ? 3185 ASN A OD1   1 
ATOM   13108 N  ND2   . ASN A 1 3185 ? 218.919 227.170 172.321 1.00 54.34  ? 3185 ASN A ND2   1 
ATOM   13109 N  N     . LEU A 1 3186 ? 222.585 230.353 169.839 1.00 46.68  ? 3186 LEU A N     1 
ATOM   13110 C  CA    . LEU A 1 3186 ? 223.053 231.665 169.414 1.00 42.66  ? 3186 LEU A CA    1 
ATOM   13111 C  C     . LEU A 1 3186 ? 223.795 231.583 168.092 1.00 48.02  ? 3186 LEU A C     1 
ATOM   13112 O  O     . LEU A 1 3186 ? 223.617 232.446 167.229 1.00 60.40  ? 3186 LEU A O     1 
ATOM   13113 C  CB    . LEU A 1 3186 ? 223.948 232.276 170.487 1.00 49.48  ? 3186 LEU A CB    1 
ATOM   13114 C  CG    . LEU A 1 3186 ? 223.229 232.805 171.725 1.00 51.73  ? 3186 LEU A CG    1 
ATOM   13115 C  CD1   . LEU A 1 3186 ? 224.239 233.265 172.755 1.00 51.83  ? 3186 LEU A CD1   1 
ATOM   13116 C  CD2   . LEU A 1 3186 ? 222.272 233.935 171.356 1.00 52.08  ? 3186 LEU A CD2   1 
ATOM   13117 N  N     . PHE A 1 3187 ? 224.633 230.560 167.914 1.00 51.09  ? 3187 PHE A N     1 
ATOM   13118 C  CA    . PHE A 1 3187 ? 225.352 230.401 166.657 1.00 52.54  ? 3187 PHE A CA    1 
ATOM   13119 C  C     . PHE A 1 3187 ? 224.384 230.260 165.491 1.00 60.26  ? 3187 PHE A C     1 
ATOM   13120 O  O     . PHE A 1 3187 ? 224.496 230.978 164.489 1.00 64.14  ? 3187 PHE A O     1 
ATOM   13121 C  CB    . PHE A 1 3187 ? 226.267 229.179 166.759 1.00 56.96  ? 3187 PHE A CB    1 
ATOM   13122 C  CG    . PHE A 1 3187 ? 227.413 229.176 165.790 1.00 58.69  ? 3187 PHE A CG    1 
ATOM   13123 C  CD1   . PHE A 1 3187 ? 228.504 230.002 165.981 1.00 63.81  ? 3187 PHE A CD1   1 
ATOM   13124 C  CD2   . PHE A 1 3187 ? 227.421 228.306 164.715 1.00 57.95  ? 3187 PHE A CD2   1 
ATOM   13125 C  CE1   . PHE A 1 3187 ? 229.565 229.982 165.103 1.00 57.51  ? 3187 PHE A CE1   1 
ATOM   13126 C  CE2   . PHE A 1 3187 ? 228.485 228.278 163.839 1.00 54.82  ? 3187 PHE A CE2   1 
ATOM   13127 C  CZ    . PHE A 1 3187 ? 229.555 229.120 164.030 1.00 53.89  ? 3187 PHE A CZ    1 
ATOM   13128 N  N     . HIS A 1 3188 ? 223.405 229.359 165.618 1.00 58.90  ? 3188 HIS A N     1 
ATOM   13129 C  CA    . HIS A 1 3188 ? 222.455 229.161 164.528 1.00 57.25  ? 3188 HIS A CA    1 
ATOM   13130 C  C     . HIS A 1 3188 ? 221.647 230.423 164.251 1.00 61.80  ? 3188 HIS A C     1 
ATOM   13131 O  O     . HIS A 1 3188 ? 221.486 230.817 163.087 1.00 71.22  ? 3188 HIS A O     1 
ATOM   13132 C  CB    . HIS A 1 3188 ? 221.528 227.990 164.845 1.00 62.41  ? 3188 HIS A CB    1 
ATOM   13133 C  CG    . HIS A 1 3188 ? 222.247 226.696 165.066 1.00 72.05  ? 3188 HIS A CG    1 
ATOM   13134 N  ND1   . HIS A 1 3188 ? 221.772 225.716 165.911 1.00 72.13  ? 3188 HIS A ND1   1 
ATOM   13135 C  CD2   . HIS A 1 3188 ? 223.413 226.227 164.563 1.00 65.25  ? 3188 HIS A CD2   1 
ATOM   13136 C  CE1   . HIS A 1 3188 ? 222.610 224.695 165.910 1.00 66.51  ? 3188 HIS A CE1   1 
ATOM   13137 N  NE2   . HIS A 1 3188 ? 223.614 224.980 165.101 1.00 65.13  ? 3188 HIS A NE2   1 
ATOM   13138 N  N     . GLU A 1 3189 ? 221.141 231.076 165.301 1.00 61.50  ? 3189 GLU A N     1 
ATOM   13139 C  CA    . GLU A 1 3189 ? 220.322 232.270 165.111 1.00 63.19  ? 3189 GLU A CA    1 
ATOM   13140 C  C     . GLU A 1 3189 ? 221.120 233.396 164.462 1.00 64.79  ? 3189 GLU A C     1 
ATOM   13141 O  O     . GLU A 1 3189 ? 220.640 234.059 163.532 1.00 71.25  ? 3189 GLU A O     1 
ATOM   13142 C  CB    . GLU A 1 3189 ? 219.744 232.719 166.452 1.00 57.37  ? 3189 GLU A CB    1 
ATOM   13143 C  CG    . GLU A 1 3189 ? 219.256 234.153 166.470 1.00 63.91  ? 3189 GLU A CG    1 
ATOM   13144 C  CD    . GLU A 1 3189 ? 219.081 234.697 167.873 1.00 65.80  ? 3189 GLU A CD    1 
ATOM   13145 O  OE1   . GLU A 1 3189 ? 218.340 234.078 168.664 1.00 67.85  ? 3189 GLU A OE1   1 
ATOM   13146 O  OE2   . GLU A 1 3189 ? 219.681 235.747 168.184 1.00 62.06  ? 3189 GLU A OE2   1 
ATOM   13147 N  N     . LYS A 1 3190 ? 222.346 233.625 164.938 1.00 57.74  ? 3190 LYS A N     1 
ATOM   13148 C  CA    . LYS A 1 3190 ? 223.155 234.708 164.400 1.00 58.28  ? 3190 LYS A CA    1 
ATOM   13149 C  C     . LYS A 1 3190 ? 223.573 234.429 162.963 1.00 63.20  ? 3190 LYS A C     1 
ATOM   13150 O  O     . LYS A 1 3190 ? 223.599 235.348 162.137 1.00 75.35  ? 3190 LYS A O     1 
ATOM   13151 C  CB    . LYS A 1 3190 ? 224.377 234.940 165.287 1.00 60.52  ? 3190 LYS A CB    1 
ATOM   13152 C  CG    . LYS A 1 3190 ? 224.058 235.502 166.664 1.00 61.12  ? 3190 LYS A CG    1 
ATOM   13153 C  CD    . LYS A 1 3190 ? 223.349 236.842 166.575 1.00 65.63  ? 3190 LYS A CD    1 
ATOM   13154 C  CE    . LYS A 1 3190 ? 223.009 237.381 167.956 1.00 65.88  ? 3190 LYS A CE    1 
ATOM   13155 N  NZ    . LYS A 1 3190 ? 222.474 238.770 167.904 1.00 63.25  ? 3190 LYS A NZ    1 
ATOM   13156 N  N     . ARG A 1 3191 ? 223.906 233.175 162.635 1.00 65.26  ? 3191 ARG A N     1 
ATOM   13157 C  CA    . ARG A 1 3191 ? 224.222 232.863 161.244 1.00 68.84  ? 3191 ARG A CA    1 
ATOM   13158 C  C     . ARG A 1 3191 ? 223.018 233.079 160.342 1.00 69.19  ? 3191 ARG A C     1 
ATOM   13159 O  O     . ARG A 1 3191 ? 223.155 233.630 159.244 1.00 72.33  ? 3191 ARG A O     1 
ATOM   13160 C  CB    . ARG A 1 3191 ? 224.735 231.432 161.095 1.00 71.03  ? 3191 ARG A CB    1 
ATOM   13161 C  CG    . ARG A 1 3191 ? 226.055 231.153 161.767 1.00 69.61  ? 3191 ARG A CG    1 
ATOM   13162 C  CD    . ARG A 1 3191 ? 226.452 229.708 161.568 1.00 71.45  ? 3191 ARG A CD    1 
ATOM   13163 N  NE    . ARG A 1 3191 ? 226.740 229.407 160.171 1.00 72.47  ? 3191 ARG A NE    1 
ATOM   13164 C  CZ    . ARG A 1 3191 ? 225.974 228.654 159.394 1.00 75.39  ? 3191 ARG A CZ    1 
ATOM   13165 N  NH1   . ARG A 1 3191 ? 224.847 228.125 159.840 1.00 72.84  ? 3191 ARG A NH1   1 
ATOM   13166 N  NH2   . ARG A 1 3191 ? 226.348 228.427 158.139 1.00 75.49  ? 3191 ARG A NH2   1 
ATOM   13167 N  N     . SER A 1 3192 ? 221.830 232.652 160.779 1.00 65.31  ? 3192 SER A N     1 
ATOM   13168 C  CA    . SER A 1 3192 ? 220.641 232.878 159.963 1.00 66.26  ? 3192 SER A CA    1 
ATOM   13169 C  C     . SER A 1 3192 ? 220.405 234.367 159.738 1.00 73.71  ? 3192 SER A C     1 
ATOM   13170 O  O     . SER A 1 3192 ? 220.156 234.803 158.604 1.00 77.05  ? 3192 SER A O     1 
ATOM   13171 C  CB    . SER A 1 3192 ? 219.421 232.235 160.620 1.00 65.66  ? 3192 SER A CB    1 
ATOM   13172 O  OG    . SER A 1 3192 ? 219.584 230.833 160.729 1.00 68.67  ? 3192 SER A OG    1 
ATOM   13173 N  N     . GLU A 1 3193 ? 220.498 235.166 160.806 1.00 74.55  ? 3193 GLU A N     1 
ATOM   13174 C  CA    . GLU A 1 3193 ? 220.267 236.601 160.676 1.00 68.18  ? 3193 GLU A CA    1 
ATOM   13175 C  C     . GLU A 1 3193 ? 221.293 237.250 159.756 1.00 65.46  ? 3193 GLU A C     1 
ATOM   13176 O  O     . GLU A 1 3193 ? 220.934 238.060 158.894 1.00 75.17  ? 3193 GLU A O     1 
ATOM   13177 C  CB    . GLU A 1 3193 ? 220.289 237.261 162.053 1.00 67.83  ? 3193 GLU A CB    1 
ATOM   13178 C  CG    . GLU A 1 3193 ? 219.098 236.914 162.922 1.00 70.64  ? 3193 GLU A CG    1 
ATOM   13179 C  CD    . GLU A 1 3193 ? 219.136 237.612 164.264 1.00 74.90  ? 3193 GLU A CD    1 
ATOM   13180 O  OE1   . GLU A 1 3193 ? 220.143 238.290 164.554 1.00 76.52  ? 3193 GLU A OE1   1 
ATOM   13181 O  OE2   . GLU A 1 3193 ? 218.158 237.483 165.029 1.00 75.26  ? 3193 GLU A OE2   1 
ATOM   13182 N  N     . LEU A 1 3194 ? 222.572 236.901 159.914 1.00 64.99  ? 3194 LEU A N     1 
ATOM   13183 C  CA    . LEU A 1 3194 ? 223.611 237.509 159.091 1.00 72.13  ? 3194 LEU A CA    1 
ATOM   13184 C  C     . LEU A 1 3194 ? 223.476 237.099 157.630 1.00 76.26  ? 3194 LEU A C     1 
ATOM   13185 O  O     . LEU A 1 3194 ? 223.681 237.920 156.729 1.00 79.71  ? 3194 LEU A O     1 
ATOM   13186 C  CB    . LEU A 1 3194 ? 224.990 237.133 159.631 1.00 74.36  ? 3194 LEU A CB    1 
ATOM   13187 C  CG    . LEU A 1 3194 ? 226.190 237.747 158.912 1.00 72.94  ? 3194 LEU A CG    1 
ATOM   13188 C  CD1   . LEU A 1 3194 ? 226.163 239.258 159.036 1.00 77.13  ? 3194 LEU A CD1   1 
ATOM   13189 C  CD2   . LEU A 1 3194 ? 227.483 237.187 159.472 1.00 74.95  ? 3194 LEU A CD2   1 
ATOM   13190 N  N     . GLU A 1 3195 ? 223.138 235.833 157.373 1.00 79.44  ? 3195 GLU A N     1 
ATOM   13191 C  CA    . GLU A 1 3195 ? 222.954 235.383 155.999 1.00 77.42  ? 3195 GLU A CA    1 
ATOM   13192 C  C     . GLU A 1 3195 ? 221.786 236.101 155.338 1.00 80.69  ? 3195 GLU A C     1 
ATOM   13193 O  O     . GLU A 1 3195 ? 221.888 236.538 154.184 1.00 82.82  ? 3195 GLU A O     1 
ATOM   13194 C  CB    . GLU A 1 3195 ? 222.745 233.870 155.974 1.00 77.87  ? 3195 GLU A CB    1 
ATOM   13195 C  CG    . GLU A 1 3195 ? 224.027 233.072 156.151 1.00 78.75  ? 3195 GLU A CG    1 
ATOM   13196 C  CD    . GLU A 1 3195 ? 223.768 231.606 156.434 1.00 83.06  ? 3195 GLU A CD    1 
ATOM   13197 O  OE1   . GLU A 1 3195 ? 222.603 231.172 156.315 1.00 84.22  ? 3195 GLU A OE1   1 
ATOM   13198 O  OE2   . GLU A 1 3195 ? 224.729 230.888 156.782 1.00 83.90  ? 3195 GLU A OE2   1 
ATOM   13199 N  N     . GLU A 1 3196 ? 220.668 236.242 156.056 1.00 84.76  ? 3196 GLU A N     1 
ATOM   13200 C  CA    . GLU A 1 3196 ? 219.530 236.967 155.498 1.00 80.80  ? 3196 GLU A CA    1 
ATOM   13201 C  C     . GLU A 1 3196 ? 219.879 238.430 155.244 1.00 82.67  ? 3196 GLU A C     1 
ATOM   13202 O  O     . GLU A 1 3196 ? 219.500 238.995 154.209 1.00 87.59  ? 3196 GLU A O     1 
ATOM   13203 C  CB    . GLU A 1 3196 ? 218.328 236.845 156.433 1.00 80.43  ? 3196 GLU A CB    1 
ATOM   13204 C  CG    . GLU A 1 3196 ? 217.145 237.709 156.043 1.00 85.06  ? 3196 GLU A CG    1 
ATOM   13205 C  CD    . GLU A 1 3196 ? 215.905 237.412 156.865 1.00 88.52  ? 3196 GLU A CD    1 
ATOM   13206 O  OE1   . GLU A 1 3196 ? 215.949 237.591 158.100 1.00 88.06  ? 3196 GLU A OE1   1 
ATOM   13207 O  OE2   . GLU A 1 3196 ? 214.885 237.001 156.275 1.00 88.02  ? 3196 GLU A OE2   1 
ATOM   13208 N  N     . GLN A 1 3197 ? 220.607 239.056 156.173 1.00 81.56  ? 3197 GLN A N     1 
ATOM   13209 C  CA    . GLN A 1 3197 ? 221.041 240.436 155.979 1.00 82.40  ? 3197 GLN A CA    1 
ATOM   13210 C  C     . GLN A 1 3197 ? 221.899 240.576 154.728 1.00 79.97  ? 3197 GLN A C     1 
ATOM   13211 O  O     . GLN A 1 3197 ? 221.679 241.478 153.910 1.00 84.23  ? 3197 GLN A O     1 
ATOM   13212 C  CB    . GLN A 1 3197 ? 221.814 240.907 157.211 1.00 85.20  ? 3197 GLN A CB    1 
ATOM   13213 C  CG    . GLN A 1 3197 ? 222.254 242.359 157.182 1.00 86.91  ? 3197 GLN A CG    1 
ATOM   13214 C  CD    . GLN A 1 3197 ? 222.965 242.768 158.458 1.00 88.25  ? 3197 GLN A CD    1 
ATOM   13215 O  OE1   . GLN A 1 3197 ? 223.164 241.952 159.357 1.00 83.37  ? 3197 GLN A OE1   1 
ATOM   13216 N  NE2   . GLN A 1 3197 ? 223.356 244.034 158.541 1.00 84.87  ? 3197 GLN A NE2   1 
ATOM   13217 N  N     . GLN A 1 3198 ? 222.883 239.691 154.564 1.00 84.47  ? 3198 GLN A N     1 
ATOM   13218 C  CA    . GLN A 1 3198 ? 223.756 239.768 153.399 1.00 88.62  ? 3198 GLN A CA    1 
ATOM   13219 C  C     . GLN A 1 3198 ? 222.971 239.559 152.111 1.00 87.65  ? 3198 GLN A C     1 
ATOM   13220 O  O     . GLN A 1 3198 ? 223.203 240.256 151.118 1.00 86.76  ? 3198 GLN A O     1 
ATOM   13221 C  CB    . GLN A 1 3198 ? 224.885 238.747 153.520 1.00 90.65  ? 3198 GLN A CB    1 
ATOM   13222 C  CG    . GLN A 1 3198 ? 225.846 238.741 152.345 1.00 88.77  ? 3198 GLN A CG    1 
ATOM   13223 C  CD    . GLN A 1 3198 ? 226.917 239.808 152.459 1.00 91.20  ? 3198 GLN A CD    1 
ATOM   13224 O  OE1   . GLN A 1 3198 ? 226.805 240.733 153.262 1.00 91.28  ? 3198 GLN A OE1   1 
ATOM   13225 N  NE2   . GLN A 1 3198 ? 227.962 239.685 151.649 1.00 88.28  ? 3198 GLN A NE2   1 
ATOM   13226 N  N     . MET A 1 3199 ? 222.032 238.608 152.113 1.00 91.22  ? 3199 MET A N     1 
ATOM   13227 C  CA    . MET A 1 3199 ? 221.179 238.408 150.946 1.00 91.73  ? 3199 MET A CA    1 
ATOM   13228 C  C     . MET A 1 3199 ? 220.413 239.678 150.598 1.00 94.27  ? 3199 MET A C     1 
ATOM   13229 O  O     . MET A 1 3199 ? 220.371 240.089 149.428 1.00 95.63  ? 3199 MET A O     1 
ATOM   13230 C  CB    . MET A 1 3199 ? 220.208 237.256 151.207 1.00 88.38  ? 3199 MET A CB    1 
ATOM   13231 C  CG    . MET A 1 3199 ? 219.350 236.880 150.015 1.00 90.21  ? 3199 MET A CG    1 
ATOM   13232 S  SD    . MET A 1 3199 ? 220.318 236.260 148.630 1.00 105.62 ? 3199 MET A SD    1 
ATOM   13233 C  CE    . MET A 1 3199 ? 220.796 234.651 149.255 1.00 90.38  ? 3199 MET A CE    1 
ATOM   13234 N  N     . HIS A 1 3200 ? 219.807 240.316 151.603 1.00 87.02  ? 3200 HIS A N     1 
ATOM   13235 C  CA    . HIS A 1 3200 ? 219.008 241.510 151.348 1.00 83.63  ? 3200 HIS A CA    1 
ATOM   13236 C  C     . HIS A 1 3200 ? 219.861 242.643 150.791 1.00 84.87  ? 3200 HIS A C     1 
ATOM   13237 O  O     . HIS A 1 3200 ? 219.470 243.306 149.824 1.00 87.32  ? 3200 HIS A O     1 
ATOM   13238 C  CB    . HIS A 1 3200 ? 218.290 241.947 152.624 1.00 81.31  ? 3200 HIS A CB    1 
ATOM   13239 C  CG    . HIS A 1 3200 ? 217.185 241.026 153.037 1.00 85.27  ? 3200 HIS A CG    1 
ATOM   13240 N  ND1   . HIS A 1 3200 ? 216.448 240.298 152.129 1.00 83.95  ? 3200 HIS A ND1   1 
ATOM   13241 C  CD2   . HIS A 1 3200 ? 216.684 240.724 154.258 1.00 87.51  ? 3200 HIS A CD2   1 
ATOM   13242 C  CE1   . HIS A 1 3200 ? 215.544 239.582 152.773 1.00 83.19  ? 3200 HIS A CE1   1 
ATOM   13243 N  NE2   . HIS A 1 3200 ? 215.666 239.823 154.065 1.00 86.23  ? 3200 HIS A NE2   1 
ATOM   13244 N  N     . LEU A 1 3201 ? 221.036 242.879 151.380 1.00 86.58  ? 3201 LEU A N     1 
ATOM   13245 C  CA    . LEU A 1 3201 ? 221.902 243.937 150.857 1.00 84.58  ? 3201 LEU A CA    1 
ATOM   13246 C  C     . LEU A 1 3201 ? 222.408 243.626 149.453 1.00 84.90  ? 3201 LEU A C     1 
ATOM   13247 O  O     . LEU A 1 3201 ? 222.510 244.531 148.617 1.00 89.37  ? 3201 LEU A O     1 
ATOM   13248 C  CB    . LEU A 1 3201 ? 223.072 244.228 151.797 1.00 85.00  ? 3201 LEU A CB    1 
ATOM   13249 C  CG    . LEU A 1 3201 ? 222.804 245.085 153.040 1.00 87.08  ? 3201 LEU A CG    1 
ATOM   13250 C  CD1   . LEU A 1 3201 ? 221.997 244.411 154.130 1.00 87.13  ? 3201 LEU A CD1   1 
ATOM   13251 C  CD2   . LEU A 1 3201 ? 224.122 245.610 153.581 1.00 85.92  ? 3201 LEU A CD2   1 
ATOM   13252 N  N     . ASN A 1 3202 ? 222.764 242.371 149.170 1.00 83.60  ? 3202 ASN A N     1 
ATOM   13253 C  CA    . ASN A 1 3202 ? 223.221 242.058 147.817 1.00 87.82  ? 3202 ASN A CA    1 
ATOM   13254 C  C     . ASN A 1 3202 ? 222.114 242.302 146.798 1.00 88.01  ? 3202 ASN A C     1 
ATOM   13255 O  O     . ASN A 1 3202 ? 222.357 242.861 145.719 1.00 84.94  ? 3202 ASN A O     1 
ATOM   13256 C  CB    . ASN A 1 3202 ? 223.736 240.621 147.722 1.00 89.12  ? 3202 ASN A CB    1 
ATOM   13257 C  CG    . ASN A 1 3202 ? 225.057 240.420 148.442 1.00 90.74  ? 3202 ASN A CG    1 
ATOM   13258 O  OD1   . ASN A 1 3202 ? 225.147 239.653 149.396 1.00 90.50  ? 3202 ASN A OD1   1 
ATOM   13259 N  ND2   . ASN A 1 3202 ? 226.093 241.116 147.984 1.00 87.32  ? 3202 ASN A ND2   1 
ATOM   13260 N  N     . VAL A 1 3203 ? 220.884 241.905 147.133 1.00 88.52  ? 3203 VAL A N     1 
ATOM   13261 C  CA    . VAL A 1 3203 ? 219.757 242.183 146.247 1.00 87.55  ? 3203 VAL A CA    1 
ATOM   13262 C  C     . VAL A 1 3203 ? 219.586 243.689 146.067 1.00 86.91  ? 3203 VAL A C     1 
ATOM   13263 O  O     . VAL A 1 3203 ? 219.352 244.183 144.955 1.00 89.09  ? 3203 VAL A O     1 
ATOM   13264 C  CB    . VAL A 1 3203 ? 218.477 241.521 146.788 1.00 86.32  ? 3203 VAL A CB    1 
ATOM   13265 C  CG1   . VAL A 1 3203 ? 217.239 242.144 146.165 1.00 84.75  ? 3203 VAL A CG1   1 
ATOM   13266 C  CG2   . VAL A 1 3203 ? 218.512 240.023 146.527 1.00 86.27  ? 3203 VAL A CG2   1 
ATOM   13267 N  N     . GLY A 1 3204 ? 219.711 244.443 147.160 1.00 85.23  ? 3204 GLY A N     1 
ATOM   13268 C  CA    . GLY A 1 3204 ? 219.531 245.884 147.072 1.00 83.00  ? 3204 GLY A CA    1 
ATOM   13269 C  C     . GLY A 1 3204 ? 220.555 246.556 146.177 1.00 83.11  ? 3204 GLY A C     1 
ATOM   13270 O  O     . GLY A 1 3204 ? 220.210 247.379 145.323 1.00 88.23  ? 3204 GLY A O     1 
ATOM   13271 N  N     . LEU A 1 3205 ? 221.834 246.212 146.355 1.00 85.69  ? 3205 LEU A N     1 
ATOM   13272 C  CA    . LEU A 1 3205 ? 222.865 246.810 145.509 1.00 87.04  ? 3205 LEU A CA    1 
ATOM   13273 C  C     . LEU A 1 3205 ? 222.734 246.377 144.057 1.00 89.45  ? 3205 LEU A C     1 
ATOM   13274 O  O     . LEU A 1 3205 ? 222.997 247.175 143.152 1.00 87.70  ? 3205 LEU A O     1 
ATOM   13275 C  CB    . LEU A 1 3205 ? 224.276 246.516 146.022 1.00 84.01  ? 3205 LEU A CB    1 
ATOM   13276 C  CG    . LEU A 1 3205 ? 224.838 247.316 147.202 1.00 86.48  ? 3205 LEU A CG    1 
ATOM   13277 C  CD1   . LEU A 1 3205 ? 224.213 246.984 148.539 1.00 88.22  ? 3205 LEU A CD1   1 
ATOM   13278 C  CD2   . LEU A 1 3205 ? 226.354 247.153 147.243 1.00 88.11  ? 3205 LEU A CD2   1 
ATOM   13279 N  N     . ARG A 1 3206 ? 222.354 245.123 143.794 1.00 89.32  ? 3206 ARG A N     1 
ATOM   13280 C  CA    . ARG A 1 3206 ? 222.205 244.734 142.394 1.00 89.43  ? 3206 ARG A CA    1 
ATOM   13281 C  C     . ARG A 1 3206 ? 221.053 245.498 141.747 1.00 89.53  ? 3206 ARG A C     1 
ATOM   13282 O  O     . ARG A 1 3206 ? 221.146 245.918 140.587 1.00 88.68  ? 3206 ARG A O     1 
ATOM   13283 C  CB    . ARG A 1 3206 ? 222.017 243.221 142.245 1.00 88.27  ? 3206 ARG A CB    1 
ATOM   13284 C  CG    . ARG A 1 3206 ? 220.724 242.659 142.784 1.00 89.63  ? 3206 ARG A CG    1 
ATOM   13285 C  CD    . ARG A 1 3206 ? 220.678 241.146 142.682 1.00 87.00  ? 3206 ARG A CD    1 
ATOM   13286 N  NE    . ARG A 1 3206 ? 221.630 240.496 143.573 1.00 92.18  ? 3206 ARG A NE    1 
ATOM   13287 C  CZ    . ARG A 1 3206 ? 221.887 239.196 143.568 1.00 91.11  ? 3206 ARG A CZ    1 
ATOM   13288 N  NH1   . ARG A 1 3206 ? 221.277 238.374 142.729 1.00 88.94  ? 3206 ARG A NH1   1 
ATOM   13289 N  NH2   . ARG A 1 3206 ? 222.777 238.707 144.427 1.00 88.78  ? 3206 ARG A NH2   1 
ATOM   13290 N  N     . LYS A 1 3207 ? 219.968 245.725 142.497 1.00 92.07  ? 3207 LYS A N     1 
ATOM   13291 C  CA    . LYS A 1 3207 ? 218.873 246.532 141.964 1.00 91.47  ? 3207 LYS A CA    1 
ATOM   13292 C  C     . LYS A 1 3207 ? 219.319 247.964 141.686 1.00 91.68  ? 3207 LYS A C     1 
ATOM   13293 O  O     . LYS A 1 3207 ? 218.982 248.538 140.641 1.00 94.25  ? 3207 LYS A O     1 
ATOM   13294 C  CB    . LYS A 1 3207 ? 217.687 246.518 142.927 1.00 88.88  ? 3207 LYS A CB    1 
ATOM   13295 C  CG    . LYS A 1 3207 ? 217.020 245.162 143.073 1.00 90.51  ? 3207 LYS A CG    1 
ATOM   13296 C  CD    . LYS A 1 3207 ? 216.284 244.762 141.808 1.00 90.79  ? 3207 LYS A CD    1 
ATOM   13297 C  CE    . LYS A 1 3207 ? 215.448 243.514 142.035 1.00 91.36  ? 3207 LYS A CE    1 
ATOM   13298 N  NZ    . LYS A 1 3207 ? 214.465 243.693 143.140 1.00 91.85  ? 3207 LYS A NZ    1 
ATOM   13299 N  N     . ILE A 1 3208 ? 220.078 248.563 142.607 1.00 90.54  ? 3208 ILE A N     1 
ATOM   13300 C  CA    . ILE A 1 3208 ? 220.491 249.953 142.416 1.00 90.10  ? 3208 ILE A CA    1 
ATOM   13301 C  C     . ILE A 1 3208 ? 221.477 250.063 141.254 1.00 90.50  ? 3208 ILE A C     1 
ATOM   13302 O  O     . ILE A 1 3208 ? 221.472 251.045 140.502 1.00 91.77  ? 3208 ILE A O     1 
ATOM   13303 C  CB    . ILE A 1 3208 ? 221.071 250.533 143.718 1.00 90.84  ? 3208 ILE A CB    1 
ATOM   13304 C  CG1   . ILE A 1 3208 ? 220.008 250.556 144.813 1.00 90.49  ? 3208 ILE A CG1   1 
ATOM   13305 C  CG2   . ILE A 1 3208 ? 221.558 251.953 143.497 1.00 89.68  ? 3208 ILE A CG2   1 
ATOM   13306 C  CD1   . ILE A 1 3208 ? 220.568 250.868 146.179 1.00 88.04  ? 3208 ILE A CD1   1 
ATOM   13307 N  N     . LYS A 1 3209 ? 222.340 249.057 141.088 1.00 91.15  ? 3209 LYS A N     1 
ATOM   13308 C  CA    . LYS A 1 3209 ? 223.258 249.053 139.952 1.00 94.70  ? 3209 LYS A CA    1 
ATOM   13309 C  C     . LYS A 1 3209 ? 222.502 248.894 138.637 1.00 93.98  ? 3209 LYS A C     1 
ATOM   13310 O  O     . LYS A 1 3209 ? 222.873 249.499 137.620 1.00 91.92  ? 3209 LYS A O     1 
ATOM   13311 C  CB    . LYS A 1 3209 ? 224.296 247.942 140.113 1.00 93.71  ? 3209 LYS A CB    1 
ATOM   13312 C  CG    . LYS A 1 3209 ? 225.325 247.888 138.993 1.00 90.30  ? 3209 LYS A CG    1 
ATOM   13313 C  CD    . LYS A 1 3209 ? 225.891 249.274 138.718 1.00 92.94  ? 3209 LYS A CD    1 
ATOM   13314 C  CE    . LYS A 1 3209 ? 226.563 249.352 137.360 1.00 93.83  ? 3209 LYS A CE    1 
ATOM   13315 N  NZ    . LYS A 1 3209 ? 226.910 250.758 137.009 1.00 93.42  ? 3209 LYS A NZ    1 
ATOM   13316 N  N     . GLU A 1 3210 ? 221.445 248.078 138.637 1.00 94.05  ? 3210 GLU A N     1 
ATOM   13317 C  CA    . GLU A 1 3210 ? 220.573 248.000 137.471 1.00 95.40  ? 3210 GLU A CA    1 
ATOM   13318 C  C     . GLU A 1 3210 ? 219.977 249.364 137.154 1.00 97.26  ? 3210 GLU A C     1 
ATOM   13319 O  O     . GLU A 1 3210 ? 219.930 249.780 135.990 1.00 97.35  ? 3210 GLU A O     1 
ATOM   13320 C  CB    . GLU A 1 3210 ? 219.464 246.977 137.720 1.00 93.53  ? 3210 GLU A CB    1 
ATOM   13321 C  CG    . GLU A 1 3210 ? 218.996 246.241 136.481 1.00 96.12  ? 3210 GLU A CG    1 
ATOM   13322 C  CD    . GLU A 1 3210 ? 218.093 245.069 136.812 1.00 98.21  ? 3210 GLU A CD    1 
ATOM   13323 O  OE1   . GLU A 1 3210 ? 217.763 244.889 138.004 1.00 96.71  ? 3210 GLU A OE1   1 
ATOM   13324 O  OE2   . GLU A 1 3210 ? 217.715 244.327 135.882 1.00 98.56  ? 3210 GLU A OE2   1 
ATOM   13325 N  N     . THR A 1 3211 ? 219.530 250.078 138.189 1.00 96.25  ? 3211 THR A N     1 
ATOM   13326 C  CA    . THR A 1 3211 ? 219.005 251.428 138.001 1.00 94.66  ? 3211 THR A CA    1 
ATOM   13327 C  C     . THR A 1 3211 ? 220.057 252.352 137.395 1.00 94.66  ? 3211 THR A C     1 
ATOM   13328 O  O     . THR A 1 3211 ? 219.755 253.153 136.503 1.00 96.08  ? 3211 THR A O     1 
ATOM   13329 C  CB    . THR A 1 3211 ? 218.503 251.980 139.337 1.00 96.52  ? 3211 THR A CB    1 
ATOM   13330 O  OG1   . THR A 1 3211 ? 217.367 251.224 139.774 1.00 93.05  ? 3211 THR A OG1   1 
ATOM   13331 C  CG2   . THR A 1 3211 ? 218.122 253.447 139.215 1.00 96.04  ? 3211 THR A CG2   1 
ATOM   13332 N  N     . VAL A 1 3212 ? 221.300 252.257 137.873 1.00 92.62  ? 3212 VAL A N     1 
ATOM   13333 C  CA    . VAL A 1 3212 ? 222.369 253.120 137.366 1.00 95.20  ? 3212 VAL A CA    1 
ATOM   13334 C  C     . VAL A 1 3212 ? 222.643 252.835 135.893 1.00 95.29  ? 3212 VAL A C     1 
ATOM   13335 O  O     . VAL A 1 3212 ? 222.793 253.757 135.078 1.00 94.27  ? 3212 VAL A O     1 
ATOM   13336 C  CB    . VAL A 1 3212 ? 223.640 252.951 138.221 1.00 95.15  ? 3212 VAL A CB    1 
ATOM   13337 C  CG1   . VAL A 1 3212 ? 224.857 253.477 137.477 1.00 92.65  ? 3212 VAL A CG1   1 
ATOM   13338 C  CG2   . VAL A 1 3212 ? 223.480 253.661 139.553 1.00 93.20  ? 3212 VAL A CG2   1 
ATOM   13339 N  N     . ASP A 1 3213 ? 222.722 251.555 135.526 1.00 98.61  ? 3213 ASP A N     1 
ATOM   13340 C  CA    . ASP A 1 3213 ? 222.928 251.216 134.120 1.00 98.94  ? 3213 ASP A CA    1 
ATOM   13341 C  C     . ASP A 1 3213 ? 221.775 251.712 133.256 1.00 100.26 ? 3213 ASP A C     1 
ATOM   13342 O  O     . ASP A 1 3213 ? 221.996 252.246 132.155 1.00 98.78  ? 3213 ASP A O     1 
ATOM   13343 C  CB    . ASP A 1 3213 ? 223.101 249.705 133.962 1.00 99.83  ? 3213 ASP A CB    1 
ATOM   13344 C  CG    . ASP A 1 3213 ? 223.386 249.299 132.530 1.00 102.29 ? 3213 ASP A CG    1 
ATOM   13345 O  OD1   . ASP A 1 3213 ? 224.511 249.553 132.051 1.00 102.33 ? 3213 ASP A OD1   1 
ATOM   13346 O  OD2   . ASP A 1 3213 ? 222.487 248.722 131.884 1.00 101.28 ? 3213 ASP A OD2   1 
ATOM   13347 N  N     . GLN A 1 3214 ? 220.542 251.555 133.744 1.00 102.07 ? 3214 GLN A N     1 
ATOM   13348 C  CA    . GLN A 1 3214 ? 219.383 252.012 132.989 1.00 100.26 ? 3214 GLN A CA    1 
ATOM   13349 C  C     . GLN A 1 3214 ? 219.403 253.521 132.801 1.00 100.58 ? 3214 GLN A C     1 
ATOM   13350 O  O     . GLN A 1 3214 ? 219.075 254.015 131.720 1.00 100.09 ? 3214 GLN A O     1 
ATOM   13351 C  CB    . GLN A 1 3214 ? 218.096 251.569 133.681 1.00 98.43  ? 3214 GLN A CB    1 
ATOM   13352 C  CG    . GLN A 1 3214 ? 217.888 250.067 133.660 1.00 100.72 ? 3214 GLN A CG    1 
ATOM   13353 C  CD    . GLN A 1 3214 ? 218.233 249.448 132.320 1.00 102.44 ? 3214 GLN A CD    1 
ATOM   13354 O  OE1   . GLN A 1 3214 ? 217.668 249.814 131.289 1.00 101.54 ? 3214 GLN A OE1   1 
ATOM   13355 N  NE2   . GLN A 1 3214 ? 219.170 248.508 132.327 1.00 101.11 ? 3214 GLN A NE2   1 
ATOM   13356 N  N     . VAL A 1 3215 ? 219.788 254.276 133.834 1.00 99.78  ? 3215 VAL A N     1 
ATOM   13357 C  CA    . VAL A 1 3215 ? 219.802 255.727 133.685 1.00 99.67  ? 3215 VAL A CA    1 
ATOM   13358 C  C     . VAL A 1 3215 ? 220.942 256.179 132.780 1.00 100.31 ? 3215 VAL A C     1 
ATOM   13359 O  O     . VAL A 1 3215 ? 220.801 257.182 132.073 1.00 99.18  ? 3215 VAL A O     1 
ATOM   13360 C  CB    . VAL A 1 3215 ? 219.871 256.443 135.050 1.00 97.60  ? 3215 VAL A CB    1 
ATOM   13361 C  CG1   . VAL A 1 3215 ? 218.682 256.057 135.898 1.00 97.48  ? 3215 VAL A CG1   1 
ATOM   13362 C  CG2   . VAL A 1 3215 ? 221.174 256.181 135.768 1.00 98.87  ? 3215 VAL A CG2   1 
ATOM   13363 N  N     . GLU A 1 3216 ? 222.069 255.461 132.770 1.00 102.36 ? 3216 GLU A N     1 
ATOM   13364 C  CA    . GLU A 1 3216 ? 223.130 255.785 131.819 1.00 103.48 ? 3216 GLU A CA    1 
ATOM   13365 C  C     . GLU A 1 3216 ? 222.652 255.596 130.382 1.00 104.09 ? 3216 GLU A C     1 
ATOM   13366 O  O     . GLU A 1 3216 ? 222.803 256.493 129.535 1.00 102.54 ? 3216 GLU A O     1 
ATOM   13367 C  CB    . GLU A 1 3216 ? 224.364 254.927 132.101 1.00 103.65 ? 3216 GLU A CB    1 
ATOM   13368 C  CG    . GLU A 1 3216 ? 225.635 255.408 131.417 1.00 102.85 ? 3216 GLU A CG    1 
ATOM   13369 C  CD    . GLU A 1 3216 ? 225.863 254.749 130.070 1.00 104.22 ? 3216 GLU A CD    1 
ATOM   13370 O  OE1   . GLU A 1 3216 ? 225.395 253.607 129.879 1.00 103.47 ? 3216 GLU A OE1   1 
ATOM   13371 O  OE2   . GLU A 1 3216 ? 226.511 255.372 129.204 1.00 102.69 ? 3216 GLU A OE2   1 
ATOM   13372 N  N     . GLU A 1 3217 ? 222.053 254.437 130.090 1.00 103.59 ? 3217 GLU A N     1 
ATOM   13373 C  CA    . GLU A 1 3217 ? 221.526 254.232 128.744 1.00 104.16 ? 3217 GLU A CA    1 
ATOM   13374 C  C     . GLU A 1 3217 ? 220.387 255.199 128.433 1.00 104.63 ? 3217 GLU A C     1 
ATOM   13375 O  O     . GLU A 1 3217 ? 220.204 255.583 127.273 1.00 103.73 ? 3217 GLU A O     1 
ATOM   13376 C  CB    . GLU A 1 3217 ? 221.069 252.783 128.555 1.00 103.80 ? 3217 GLU A CB    1 
ATOM   13377 C  CG    . GLU A 1 3217 ? 219.626 252.505 128.945 1.00 105.76 ? 3217 GLU A CG    1 
ATOM   13378 C  CD    . GLU A 1 3217 ? 219.185 251.103 128.579 1.00 106.07 ? 3217 GLU A CD    1 
ATOM   13379 O  OE1   . GLU A 1 3217 ? 220.051 250.284 128.205 1.00 104.72 ? 3217 GLU A OE1   1 
ATOM   13380 O  OE2   . GLU A 1 3217 ? 217.970 250.823 128.658 1.00 103.77 ? 3217 GLU A OE2   1 
ATOM   13381 N  N     . LEU A 1 3218 ? 219.641 255.632 129.453 1.00 101.46 ? 3218 LEU A N     1 
ATOM   13382 C  CA    . LEU A 1 3218 ? 218.556 256.582 129.239 1.00 102.65 ? 3218 LEU A CA    1 
ATOM   13383 C  C     . LEU A 1 3218 ? 219.092 257.962 128.885 1.00 104.49 ? 3218 LEU A C     1 
ATOM   13384 O  O     . LEU A 1 3218 ? 218.513 258.659 128.049 1.00 103.59 ? 3218 LEU A O     1 
ATOM   13385 C  CB    . LEU A 1 3218 ? 217.674 256.649 130.484 1.00 104.64 ? 3218 LEU A CB    1 
ATOM   13386 C  CG    . LEU A 1 3218 ? 216.379 257.457 130.390 1.00 105.47 ? 3218 LEU A CG    1 
ATOM   13387 C  CD1   . LEU A 1 3218 ? 215.418 256.833 129.390 1.00 101.81 ? 3218 LEU A CD1   1 
ATOM   13388 C  CD2   . LEU A 1 3218 ? 215.735 257.568 131.759 1.00 101.51 ? 3218 LEU A CD2   1 
ATOM   13389 N  N     . ARG A 1 3219 ? 220.189 258.380 129.518 1.00 106.08 ? 3219 ARG A N     1 
ATOM   13390 C  CA    . ARG A 1 3219 ? 220.826 259.636 129.134 1.00 106.56 ? 3219 ARG A CA    1 
ATOM   13391 C  C     . ARG A 1 3219 ? 221.378 259.559 127.715 1.00 107.52 ? 3219 ARG A C     1 
ATOM   13392 O  O     . ARG A 1 3219 ? 221.282 260.526 126.944 1.00 107.09 ? 3219 ARG A O     1 
ATOM   13393 C  CB    . ARG A 1 3219 ? 221.933 259.991 130.127 1.00 104.28 ? 3219 ARG A CB    1 
ATOM   13394 C  CG    . ARG A 1 3219 ? 221.448 260.778 131.332 1.00 104.22 ? 3219 ARG A CG    1 
ATOM   13395 C  CD    . ARG A 1 3219 ? 222.572 261.579 131.966 1.00 105.09 ? 3219 ARG A CD    1 
ATOM   13396 N  NE    . ARG A 1 3219 ? 223.795 260.798 132.099 1.00 108.33 ? 3219 ARG A NE    1 
ATOM   13397 C  CZ    . ARG A 1 3219 ? 224.279 260.355 133.251 1.00 107.29 ? 3219 ARG A CZ    1 
ATOM   13398 N  NH1   . ARG A 1 3219 ? 223.664 260.596 134.397 1.00 104.09 ? 3219 ARG A NH1   1 
ATOM   13399 N  NH2   . ARG A 1 3219 ? 225.408 259.652 133.254 1.00 106.73 ? 3219 ARG A NH2   1 
ATOM   13400 N  N     . ARG A 1 3220 ? 221.959 258.412 127.349 1.00 104.76 ? 3220 ARG A N     1 
ATOM   13401 C  CA    . ARG A 1 3220 ? 222.413 258.243 125.970 1.00 105.18 ? 3220 ARG A CA    1 
ATOM   13402 C  C     . ARG A 1 3220 ? 221.246 258.354 124.990 1.00 105.83 ? 3220 ARG A C     1 
ATOM   13403 O  O     . ARG A 1 3220 ? 221.352 259.018 123.949 1.00 104.34 ? 3220 ARG A O     1 
ATOM   13404 C  CB    . ARG A 1 3220 ? 223.126 256.901 125.808 1.00 105.11 ? 3220 ARG A CB    1 
ATOM   13405 C  CG    . ARG A 1 3220 ? 223.342 256.485 124.363 1.00 104.37 ? 3220 ARG A CG    1 
ATOM   13406 C  CD    . ARG A 1 3220 ? 223.201 254.982 124.198 1.00 104.27 ? 3220 ARG A CD    1 
ATOM   13407 N  NE    . ARG A 1 3220 ? 222.031 254.469 124.900 1.00 106.00 ? 3220 ARG A NE    1 
ATOM   13408 C  CZ    . ARG A 1 3220 ? 220.790 254.534 124.437 1.00 107.07 ? 3220 ARG A CZ    1 
ATOM   13409 N  NH1   . ARG A 1 3220 ? 220.518 255.083 123.264 1.00 106.92 ? 3220 ARG A NH1   1 
ATOM   13410 N  NH2   . ARG A 1 3220 ? 219.798 254.036 125.168 1.00 104.26 ? 3220 ARG A NH2   1 
ATOM   13411 N  N     . ASP A 1 3221 ? 220.117 257.721 125.318 1.00 105.21 ? 3221 ASP A N     1 
ATOM   13412 C  CA    . ASP A 1 3221 ? 218.937 257.813 124.464 1.00 105.90 ? 3221 ASP A CA    1 
ATOM   13413 C  C     . ASP A 1 3221 ? 218.373 259.228 124.431 1.00 106.16 ? 3221 ASP A C     1 
ATOM   13414 O  O     . ASP A 1 3221 ? 217.823 259.648 123.410 1.00 104.13 ? 3221 ASP A O     1 
ATOM   13415 C  CB    . ASP A 1 3221 ? 217.869 256.828 124.933 1.00 106.00 ? 3221 ASP A CB    1 
ATOM   13416 C  CG    . ASP A 1 3221 ? 216.756 256.655 123.923 1.00 107.31 ? 3221 ASP A CG    1 
ATOM   13417 O  OD1   . ASP A 1 3221 ? 215.776 257.427 123.979 1.00 108.87 ? 3221 ASP A OD1   1 
ATOM   13418 O  OD2   . ASP A 1 3221 ? 216.862 255.749 123.070 1.00 106.08 ? 3221 ASP A OD2   1 
ATOM   13419 N  N     . LEU A 1 3222 ? 218.487 259.969 125.535 1.00 103.71 ? 3222 LEU A N     1 
ATOM   13420 C  CA    . LEU A 1 3222 ? 218.071 261.367 125.546 1.00 103.64 ? 3222 LEU A CA    1 
ATOM   13421 C  C     . LEU A 1 3222 ? 218.905 262.194 124.579 1.00 105.83 ? 3222 LEU A C     1 
ATOM   13422 O  O     . LEU A 1 3222 ? 218.370 263.025 123.834 1.00 104.54 ? 3222 LEU A O     1 
ATOM   13423 C  CB    . LEU A 1 3222 ? 218.177 261.931 126.964 1.00 102.92 ? 3222 LEU A CB    1 
ATOM   13424 C  CG    . LEU A 1 3222 ? 218.007 263.441 127.145 1.00 104.37 ? 3222 LEU A CG    1 
ATOM   13425 C  CD1   . LEU A 1 3222 ? 216.583 263.869 126.843 1.00 103.11 ? 3222 LEU A CD1   1 
ATOM   13426 C  CD2   . LEU A 1 3222 ? 218.407 263.862 128.552 1.00 102.05 ? 3222 LEU A CD2   1 
ATOM   13427 N  N     . ARG A 1 3223 ? 220.222 261.977 124.574 1.00 106.21 ? 3223 ARG A N     1 
ATOM   13428 C  CA    . ARG A 1 3223 ? 221.073 262.677 123.614 1.00 105.58 ? 3223 ARG A CA    1 
ATOM   13429 C  C     . ARG A 1 3223 ? 220.718 262.292 122.180 1.00 105.42 ? 3223 ARG A C     1 
ATOM   13430 O  O     . ARG A 1 3223 ? 220.677 263.151 121.287 1.00 102.88 ? 3223 ARG A O     1 
ATOM   13431 C  CB    . ARG A 1 3223 ? 222.546 262.385 123.900 1.00 105.48 ? 3223 ARG A CB    1 
ATOM   13432 C  CG    . ARG A 1 3223 ? 223.508 263.120 122.979 1.00 105.85 ? 3223 ARG A CG    1 
ATOM   13433 C  CD    . ARG A 1 3223 ? 224.861 262.431 122.915 1.00 103.94 ? 3223 ARG A CD    1 
ATOM   13434 N  NE    . ARG A 1 3223 ? 224.737 260.979 122.913 1.00 106.72 ? 3223 ARG A NE    1 
ATOM   13435 C  CZ    . ARG A 1 3223 ? 224.460 260.251 121.839 1.00 105.70 ? 3223 ARG A CZ    1 
ATOM   13436 N  NH1   . ARG A 1 3223 ? 224.258 260.812 120.658 1.00 102.36 ? 3223 ARG A NH1   1 
ATOM   13437 N  NH2   . ARG A 1 3223 ? 224.385 258.929 121.953 1.00 104.16 ? 3223 ARG A NH2   1 
ATOM   13438 N  N     . ILE A 1 3224 ? 220.457 261.003 121.945 1.00 104.74 ? 3224 ILE A N     1 
ATOM   13439 C  CA    . ILE A 1 3224 ? 220.071 260.551 120.609 1.00 106.82 ? 3224 ILE A CA    1 
ATOM   13440 C  C     . ILE A 1 3224 ? 218.771 261.219 120.173 1.00 106.82 ? 3224 ILE A C     1 
ATOM   13441 O  O     . ILE A 1 3224 ? 218.633 261.662 119.025 1.00 104.75 ? 3224 ILE A O     1 
ATOM   13442 C  CB    . ILE A 1 3224 ? 219.959 259.015 120.578 1.00 106.50 ? 3224 ILE A CB    1 
ATOM   13443 C  CG1   . ILE A 1 3224 ? 221.350 258.381 120.533 1.00 105.16 ? 3224 ILE A CG1   1 
ATOM   13444 C  CG2   . ILE A 1 3224 ? 219.120 258.556 119.395 1.00 104.16 ? 3224 ILE A CG2   1 
ATOM   13445 C  CD1   . ILE A 1 3224 ? 221.332 256.870 120.465 1.00 103.97 ? 3224 ILE A CD1   1 
ATOM   13446 N  N     . LYS A 1 3225 ? 217.797 261.297 121.082 1.00 107.40 ? 3225 LYS A N     1 
ATOM   13447 C  CA    . LYS A 1 3225 ? 216.523 261.934 120.766 1.00 108.15 ? 3225 LYS A CA    1 
ATOM   13448 C  C     . LYS A 1 3225 ? 216.702 263.420 120.488 1.00 108.11 ? 3225 LYS A C     1 
ATOM   13449 O  O     . LYS A 1 3225 ? 216.034 263.977 119.612 1.00 106.75 ? 3225 LYS A O     1 
ATOM   13450 C  CB    . LYS A 1 3225 ? 215.530 261.716 121.907 1.00 107.13 ? 3225 LYS A CB    1 
ATOM   13451 C  CG    . LYS A 1 3225 ? 214.788 260.392 121.835 1.00 107.56 ? 3225 LYS A CG    1 
ATOM   13452 C  CD    . LYS A 1 3225 ? 213.795 260.376 120.683 1.00 106.44 ? 3225 LYS A CD    1 
ATOM   13453 C  CE    . LYS A 1 3225 ? 212.759 261.477 120.828 1.00 106.35 ? 3225 LYS A CE    1 
ATOM   13454 N  NZ    . LYS A 1 3225 ? 212.200 261.531 122.207 1.00 105.10 ? 3225 LYS A NZ    1 
ATOM   13455 N  N     . SER A 1 3226 ? 217.589 264.084 121.234 1.00 107.05 ? 3226 SER A N     1 
ATOM   13456 C  CA    . SER A 1 3226 ? 217.862 265.493 120.964 1.00 107.48 ? 3226 SER A CA    1 
ATOM   13457 C  C     . SER A 1 3226 ? 218.460 265.680 119.574 1.00 109.20 ? 3226 SER A C     1 
ATOM   13458 O  O     . SER A 1 3226 ? 218.078 266.603 118.842 1.00 106.21 ? 3226 SER A O     1 
ATOM   13459 C  CB    . SER A 1 3226 ? 218.795 266.064 122.032 1.00 105.96 ? 3226 SER A CB    1 
ATOM   13460 O  OG    . SER A 1 3226 ? 220.123 265.603 121.849 1.00 106.83 ? 3226 SER A OG    1 
ATOM   13461 N  N     . GLN A 1 3227 ? 219.399 264.810 119.192 1.00 109.50 ? 3227 GLN A N     1 
ATOM   13462 C  CA    . GLN A 1 3227 ? 219.974 264.892 117.850 1.00 107.76 ? 3227 GLN A CA    1 
ATOM   13463 C  C     . GLN A 1 3227 ? 218.914 264.659 116.778 1.00 107.80 ? 3227 GLN A C     1 
ATOM   13464 O  O     . GLN A 1 3227 ? 218.877 265.364 115.759 1.00 105.02 ? 3227 GLN A O     1 
ATOM   13465 C  CB    . GLN A 1 3227 ? 221.114 263.884 117.705 1.00 106.70 ? 3227 GLN A CB    1 
ATOM   13466 C  CG    . GLN A 1 3227 ? 221.728 263.836 116.316 1.00 106.08 ? 3227 GLN A CG    1 
ATOM   13467 C  CD    . GLN A 1 3227 ? 221.176 262.702 115.474 1.00 107.12 ? 3227 GLN A CD    1 
ATOM   13468 O  OE1   . GLN A 1 3227 ? 220.404 261.874 115.958 1.00 106.26 ? 3227 GLN A OE1   1 
ATOM   13469 N  NE2   . GLN A 1 3227 ? 221.570 262.659 114.207 1.00 104.63 ? 3227 GLN A NE2   1 
ATOM   13470 N  N     . GLU A 1 3228 ? 218.046 263.666 116.990 1.00 108.68 ? 3228 GLU A N     1 
ATOM   13471 C  CA    . GLU A 1 3228 ? 216.984 263.392 116.027 1.00 108.67 ? 3228 GLU A CA    1 
ATOM   13472 C  C     . GLU A 1 3228 ? 216.027 264.571 115.916 1.00 109.09 ? 3228 GLU A C     1 
ATOM   13473 O  O     . GLU A 1 3228 ? 215.577 264.914 114.817 1.00 107.20 ? 3228 GLU A O     1 
ATOM   13474 C  CB    . GLU A 1 3228 ? 216.230 262.122 116.423 1.00 107.32 ? 3228 GLU A CB    1 
ATOM   13475 C  CG    . GLU A 1 3228 ? 215.053 261.792 115.520 1.00 107.63 ? 3228 GLU A CG    1 
ATOM   13476 C  CD    . GLU A 1 3228 ? 214.170 260.701 116.090 1.00 109.32 ? 3228 GLU A CD    1 
ATOM   13477 O  OE1   . GLU A 1 3228 ? 214.393 260.300 117.252 1.00 109.12 ? 3228 GLU A OE1   1 
ATOM   13478 O  OE2   . GLU A 1 3228 ? 213.255 260.242 115.375 1.00 108.45 ? 3228 GLU A OE2   1 
ATOM   13479 N  N     . LEU A 1 3229 ? 215.704 265.202 117.047 1.00 106.86 ? 3229 LEU A N     1 
ATOM   13480 C  CA    . LEU A 1 3229 ? 214.847 266.381 117.029 1.00 106.78 ? 3229 LEU A CA    1 
ATOM   13481 C  C     . LEU A 1 3229 ? 215.497 267.520 116.258 1.00 105.77 ? 3229 LEU A C     1 
ATOM   13482 O  O     . LEU A 1 3229 ? 214.829 268.218 115.485 1.00 104.92 ? 3229 LEU A O     1 
ATOM   13483 C  CB    . LEU A 1 3229 ? 214.533 266.818 118.459 1.00 107.46 ? 3229 LEU A CB    1 
ATOM   13484 C  CG    . LEU A 1 3229 ? 213.720 268.102 118.616 1.00 106.94 ? 3229 LEU A CG    1 
ATOM   13485 C  CD1   . LEU A 1 3229 ? 212.425 268.012 117.824 1.00 105.39 ? 3229 LEU A CD1   1 
ATOM   13486 C  CD2   . LEU A 1 3229 ? 213.444 268.379 120.085 1.00 103.98 ? 3229 LEU A CD2   1 
ATOM   13487 N  N     . GLU A 1 3230 ? 216.801 267.729 116.461 1.00 104.53 ? 3230 GLU A N     1 
ATOM   13488 C  CA    . GLU A 1 3230 ? 217.503 268.767 115.715 1.00 105.33 ? 3230 GLU A CA    1 
ATOM   13489 C  C     . GLU A 1 3230 ? 217.437 268.503 114.216 1.00 104.37 ? 3230 GLU A C     1 
ATOM   13490 O  O     . GLU A 1 3230 ? 217.118 269.405 113.430 1.00 101.69 ? 3230 GLU A O     1 
ATOM   13491 C  CB    . GLU A 1 3230 ? 218.956 268.860 116.179 1.00 104.11 ? 3230 GLU A CB    1 
ATOM   13492 C  CG    . GLU A 1 3230 ? 219.138 269.530 117.530 1.00 103.26 ? 3230 GLU A CG    1 
ATOM   13493 C  CD    . GLU A 1 3230 ? 220.594 269.624 117.940 1.00 104.58 ? 3230 GLU A CD    1 
ATOM   13494 O  OE1   . GLU A 1 3230 ? 221.465 269.232 117.136 1.00 105.95 ? 3230 GLU A OE1   1 
ATOM   13495 O  OE2   . GLU A 1 3230 ? 220.868 270.090 119.065 1.00 103.88 ? 3230 GLU A OE2   1 
ATOM   13496 N  N     . VAL A 1 3231 ? 217.711 267.262 113.807 1.00 105.35 ? 3231 VAL A N     1 
ATOM   13497 C  CA    . VAL A 1 3231 ? 217.679 266.932 112.384 1.00 106.28 ? 3231 VAL A CA    1 
ATOM   13498 C  C     . VAL A 1 3231 ? 216.277 267.126 111.816 1.00 105.26 ? 3231 VAL A C     1 
ATOM   13499 O  O     . VAL A 1 3231 ? 216.106 267.700 110.732 1.00 103.22 ? 3231 VAL A O     1 
ATOM   13500 C  CB    . VAL A 1 3231 ? 218.191 265.498 112.157 1.00 104.96 ? 3231 VAL A CB    1 
ATOM   13501 C  CG1   . VAL A 1 3231 ? 218.030 265.100 110.699 1.00 103.29 ? 3231 VAL A CG1   1 
ATOM   13502 C  CG2   . VAL A 1 3231 ? 219.646 265.384 112.581 1.00 103.09 ? 3231 VAL A CG2   1 
ATOM   13503 N  N     . LYS A 1 3232 ? 215.253 266.661 112.538 1.00 102.88 ? 3232 LYS A N     1 
ATOM   13504 C  CA    . LYS A 1 3232 ? 213.885 266.758 112.038 1.00 102.29 ? 3232 LYS A CA    1 
ATOM   13505 C  C     . LYS A 1 3232 ? 213.426 268.206 111.923 1.00 100.49 ? 3232 LYS A C     1 
ATOM   13506 O  O     . LYS A 1 3232 ? 212.792 268.581 110.929 1.00 99.24  ? 3232 LYS A O     1 
ATOM   13507 C  CB    . LYS A 1 3232 ? 212.939 265.963 112.937 1.00 101.62 ? 3232 LYS A CB    1 
ATOM   13508 C  CG    . LYS A 1 3232 ? 213.088 264.455 112.803 1.00 101.84 ? 3232 LYS A CG    1 
ATOM   13509 C  CD    . LYS A 1 3232 ? 212.290 263.928 111.621 1.00 101.02 ? 3232 LYS A CD    1 
ATOM   13510 C  CE    . LYS A 1 3232 ? 212.038 262.435 111.746 1.00 100.86 ? 3232 LYS A CE    1 
ATOM   13511 N  NZ    . LYS A 1 3232 ? 210.968 261.977 110.817 1.00 99.35  ? 3232 LYS A NZ    1 
ATOM   13512 N  N     . ASN A 1 3233 ? 213.727 269.040 112.924 1.00 100.96 ? 3233 ASN A N     1 
ATOM   13513 C  CA    . ASN A 1 3233 ? 213.293 270.431 112.844 1.00 102.76 ? 3233 ASN A CA    1 
ATOM   13514 C  C     . ASN A 1 3233 ? 214.058 271.183 111.763 1.00 103.25 ? 3233 ASN A C     1 
ATOM   13515 O  O     . ASN A 1 3233 ? 213.485 272.037 111.075 1.00 99.49  ? 3233 ASN A O     1 
ATOM   13516 C  CB    . ASN A 1 3233 ? 213.417 271.122 114.208 1.00 101.69 ? 3233 ASN A CB    1 
ATOM   13517 C  CG    . ASN A 1 3233 ? 214.851 271.230 114.705 1.00 103.46 ? 3233 ASN A CG    1 
ATOM   13518 O  OD1   . ASN A 1 3233 ? 215.748 271.675 113.989 1.00 102.10 ? 3233 ASN A OD1   1 
ATOM   13519 N  ND2   . ASN A 1 3233 ? 215.063 270.842 115.956 1.00 101.62 ? 3233 ASN A ND2   1 
ATOM   13520 N  N     . ALA A 1 3234 ? 215.347 270.873 111.581 1.00 103.47 ? 3234 ALA A N     1 
ATOM   13521 C  CA    . ALA A 1 3234 ? 216.091 271.484 110.484 1.00 102.79 ? 3234 ALA A CA    1 
ATOM   13522 C  C     . ALA A 1 3234 ? 215.495 271.098 109.135 1.00 102.35 ? 3234 ALA A C     1 
ATOM   13523 O  O     . ALA A 1 3234 ? 215.336 271.949 108.251 1.00 96.79  ? 3234 ALA A O     1 
ATOM   13524 C  CB    . ALA A 1 3234 ? 217.563 271.081 110.558 1.00 98.55  ? 3234 ALA A CB    1 
ATOM   13525 N  N     . ALA A 1 3235 ? 215.146 269.819 108.964 1.00 103.33 ? 3235 ALA A N     1 
ATOM   13526 C  CA    . ALA A 1 3235 ? 214.541 269.377 107.712 1.00 101.69 ? 3235 ALA A CA    1 
ATOM   13527 C  C     . ALA A 1 3235 ? 213.194 270.051 107.477 1.00 101.73 ? 3235 ALA A C     1 
ATOM   13528 O  O     . ALA A 1 3235 ? 212.888 270.468 106.354 1.00 100.22 ? 3235 ALA A O     1 
ATOM   13529 C  CB    . ALA A 1 3235 ? 214.389 267.856 107.709 1.00 97.58  ? 3235 ALA A CB    1 
ATOM   13530 N  N     . ALA A 1 3236 ? 212.374 270.162 108.526 1.00 102.41 ? 3236 ALA A N     1 
ATOM   13531 C  CA    . ALA A 1 3236 ? 211.073 270.807 108.380 1.00 103.46 ? 3236 ALA A CA    1 
ATOM   13532 C  C     . ALA A 1 3236 ? 211.221 272.281 108.020 1.00 103.99 ? 3236 ALA A C     1 
ATOM   13533 O  O     . ALA A 1 3236 ? 210.498 272.792 107.156 1.00 100.17 ? 3236 ALA A O     1 
ATOM   13534 C  CB    . ALA A 1 3236 ? 210.258 270.646 109.663 1.00 101.28 ? 3236 ALA A CB    1 
ATOM   13535 N  N     . ASN A 1 3237 ? 212.152 272.981 108.674 1.00 107.82 ? 3237 ASN A N     1 
ATOM   13536 C  CA    . ASN A 1 3237 ? 212.377 274.388 108.358 1.00 107.61 ? 3237 ASN A CA    1 
ATOM   13537 C  C     . ASN A 1 3237 ? 212.879 274.559 106.930 1.00 107.71 ? 3237 ASN A C     1 
ATOM   13538 O  O     . ASN A 1 3237 ? 212.465 275.489 106.227 1.00 104.85 ? 3237 ASN A O     1 
ATOM   13539 C  CB    . ASN A 1 3237 ? 213.365 274.998 109.352 1.00 105.85 ? 3237 ASN A CB    1 
ATOM   13540 C  CG    . ASN A 1 3237 ? 212.823 275.030 110.766 1.00 107.18 ? 3237 ASN A CG    1 
ATOM   13541 O  OD1   . ASN A 1 3237 ? 211.802 274.410 111.066 1.00 107.16 ? 3237 ASN A OD1   1 
ATOM   13542 N  ND2   . ASN A 1 3237 ? 213.506 275.754 111.645 1.00 105.83 ? 3237 ASN A ND2   1 
ATOM   13543 N  N     . ASP A 1 3238 ? 213.777 273.677 106.485 1.00 109.31 ? 3238 ASP A N     1 
ATOM   13544 C  CA    . ASP A 1 3238 ? 214.269 273.758 105.113 1.00 109.33 ? 3238 ASP A CA    1 
ATOM   13545 C  C     . ASP A 1 3238 ? 213.153 273.498 104.109 1.00 108.92 ? 3238 ASP A C     1 
ATOM   13546 O  O     . ASP A 1 3238 ? 213.069 274.170 103.074 1.00 107.77 ? 3238 ASP A O     1 
ATOM   13547 C  CB    . ASP A 1 3238 ? 215.421 272.775 104.910 1.00 108.82 ? 3238 ASP A CB    1 
ATOM   13548 C  CG    . ASP A 1 3238 ? 216.735 273.300 105.454 1.00 110.50 ? 3238 ASP A CG    1 
ATOM   13549 O  OD1   . ASP A 1 3238 ? 216.766 274.459 105.919 1.00 110.68 ? 3238 ASP A OD1   1 
ATOM   13550 O  OD2   . ASP A 1 3238 ? 217.738 272.555 105.416 1.00 109.31 ? 3238 ASP A OD2   1 
ATOM   13551 N  N     . LYS A 1 3239 ? 212.285 272.523 104.395 1.00 109.45 ? 3239 LYS A N     1 
ATOM   13552 C  CA    . LYS A 1 3239 ? 211.165 272.248 103.500 1.00 110.27 ? 3239 LYS A CA    1 
ATOM   13553 C  C     . LYS A 1 3239 ? 210.168 273.399 103.476 1.00 110.29 ? 3239 LYS A C     1 
ATOM   13554 O  O     . LYS A 1 3239 ? 209.548 273.657 102.437 1.00 109.51 ? 3239 LYS A O     1 
ATOM   13555 C  CB    . LYS A 1 3239 ? 210.468 270.950 103.906 1.00 109.63 ? 3239 LYS A CB    1 
ATOM   13556 C  CG    . LYS A 1 3239 ? 211.138 269.694 103.371 1.00 110.39 ? 3239 LYS A CG    1 
ATOM   13557 C  CD    . LYS A 1 3239 ? 210.169 268.521 103.344 1.00 110.02 ? 3239 LYS A CD    1 
ATOM   13558 C  CE    . LYS A 1 3239 ? 210.851 267.252 102.859 1.00 109.42 ? 3239 LYS A CE    1 
ATOM   13559 N  NZ    . LYS A 1 3239 ? 209.908 266.099 102.809 1.00 108.32 ? 3239 LYS A NZ    1 
ATOM   13560 N  N     . LEU A 1 3240 ? 209.995 274.096 104.602 1.00 108.20 ? 3240 LEU A N     1 
ATOM   13561 C  CA    . LEU A 1 3240 ? 209.098 275.246 104.635 1.00 109.19 ? 3240 LEU A CA    1 
ATOM   13562 C  C     . LEU A 1 3240 ? 209.587 276.391 103.756 1.00 107.84 ? 3240 LEU A C     1 
ATOM   13563 O  O     . LEU A 1 3240 ? 208.792 277.270 103.408 1.00 105.85 ? 3240 LEU A O     1 
ATOM   13564 C  CB    . LEU A 1 3240 ? 208.920 275.737 106.073 1.00 108.98 ? 3240 LEU A CB    1 
ATOM   13565 C  CG    . LEU A 1 3240 ? 207.920 274.968 106.940 1.00 109.16 ? 3240 LEU A CG    1 
ATOM   13566 C  CD1   . LEU A 1 3240 ? 208.033 275.394 108.396 1.00 105.55 ? 3240 LEU A CD1   1 
ATOM   13567 C  CD2   . LEU A 1 3240 ? 206.501 275.165 106.429 1.00 107.90 ? 3240 LEU A CD2   1 
ATOM   13568 N  N     . LYS A 1 3241 ? 210.872 276.404 103.394 1.00 108.98 ? 3241 LYS A N     1 
ATOM   13569 C  CA    . LYS A 1 3241 ? 211.405 277.447 102.526 1.00 110.13 ? 3241 LYS A CA    1 
ATOM   13570 C  C     . LYS A 1 3241 ? 211.072 277.221 101.058 1.00 109.84 ? 3241 LYS A C     1 
ATOM   13571 O  O     . LYS A 1 3241 ? 211.354 278.101 100.236 1.00 107.59 ? 3241 LYS A O     1 
ATOM   13572 C  CB    . LYS A 1 3241 ? 212.921 277.552 102.703 1.00 108.05 ? 3241 LYS A CB    1 
ATOM   13573 C  CG    . LYS A 1 3241 ? 213.345 278.228 103.997 1.00 107.47 ? 3241 LYS A CG    1 
ATOM   13574 C  CD    . LYS A 1 3241 ? 214.659 277.665 104.509 1.00 107.41 ? 3241 LYS A CD    1 
ATOM   13575 C  CE    . LYS A 1 3241 ? 214.814 277.899 106.003 1.00 107.59 ? 3241 LYS A CE    1 
ATOM   13576 N  NZ    . LYS A 1 3241 ? 215.968 277.144 106.566 1.00 106.54 ? 3241 LYS A NZ    1 
ATOM   13577 N  N     . LYS A 1 3242 ? 210.491 276.078 100.708 1.00 107.64 ? 3242 LYS A N     1 
ATOM   13578 C  CA    . LYS A 1 3242 ? 210.083 275.817 99.333  1.00 106.79 ? 3242 LYS A CA    1 
ATOM   13579 C  C     . LYS A 1 3242 ? 208.747 276.487 99.033  1.00 104.40 ? 3242 LYS A C     1 
ATOM   13580 O  O     . LYS A 1 3242 ? 208.066 276.971 99.938  0.00 104.35 ? 3242 LYS A O     1 
ATOM   13581 C  CB    . LYS A 1 3242 ? 209.988 274.312 99.071  1.00 105.90 ? 3242 LYS A CB    1 
ATOM   13582 C  CG    . LYS A 1 3242 ? 211.303 273.662 98.672  1.00 104.85 ? 3242 LYS A CG    1 
ATOM   13583 C  CD    . LYS A 1 3242 ? 211.129 272.169 98.440  1.00 105.53 ? 3242 LYS A CD    1 
ATOM   13584 C  CE    . LYS A 1 3242 ? 212.438 271.516 98.029  1.00 105.01 ? 3242 LYS A CE    1 
ATOM   13585 N  NZ    . LYS A 1 3242 ? 212.357 270.029 98.074  1.00 104.12 ? 3242 LYS A NZ    1 
ATOM   13586 N  N     . GLU A 1 3449 ? 200.387 270.445 103.573 1.00 111.34 ? 3449 GLU A N     1 
ATOM   13587 C  CA    . GLU A 1 3449 ? 200.035 269.133 104.103 1.00 113.65 ? 3449 GLU A CA    1 
ATOM   13588 C  C     . GLU A 1 3449 ? 201.258 268.410 104.659 1.00 114.28 ? 3449 GLU A C     1 
ATOM   13589 O  O     . GLU A 1 3449 ? 201.317 268.098 105.848 1.00 111.80 ? 3449 GLU A O     1 
ATOM   13590 C  CB    . GLU A 1 3449 ? 199.369 268.279 103.022 1.00 113.78 ? 3449 GLU A CB    1 
ATOM   13591 C  CG    . GLU A 1 3449 ? 198.208 268.958 102.316 1.00 113.76 ? 3449 GLU A CG    1 
ATOM   13592 C  CD    . GLU A 1 3449 ? 197.665 268.132 101.165 1.00 114.35 ? 3449 GLU A CD    1 
ATOM   13593 O  OE1   . GLU A 1 3449 ? 198.182 267.018 100.937 1.00 113.39 ? 3449 GLU A OE1   1 
ATOM   13594 O  OE2   . GLU A 1 3449 ? 196.720 268.595 100.491 1.00 112.89 ? 3449 GLU A OE2   1 
ATOM   13595 N  N     . GLU A 1 3450 ? 202.231 268.143 103.784 1.00 113.46 ? 3450 GLU A N     1 
ATOM   13596 C  CA    . GLU A 1 3450 ? 203.428 267.418 104.202 1.00 113.41 ? 3450 GLU A CA    1 
ATOM   13597 C  C     . GLU A 1 3450 ? 204.215 268.201 105.245 1.00 113.06 ? 3450 GLU A C     1 
ATOM   13598 O  O     . GLU A 1 3450 ? 204.700 267.628 106.228 1.00 111.49 ? 3450 GLU A O     1 
ATOM   13599 C  CB    . GLU A 1 3450 ? 204.301 267.107 102.986 1.00 113.31 ? 3450 GLU A CB    1 
ATOM   13600 C  CG    . GLU A 1 3450 ? 205.391 266.082 103.246 1.00 112.71 ? 3450 GLU A CG    1 
ATOM   13601 C  CD    . GLU A 1 3450 ? 206.055 265.606 101.969 1.00 113.18 ? 3450 GLU A CD    1 
ATOM   13602 O  OE1   . GLU A 1 3450 ? 205.629 266.042 100.878 1.00 112.01 ? 3450 GLU A OE1   1 
ATOM   13603 O  OE2   . GLU A 1 3450 ? 207.001 264.795 102.055 1.00 112.65 ? 3450 GLU A OE2   1 
ATOM   13604 N  N     . TYR A 1 3451 ? 204.354 269.514 105.047 1.00 108.99 ? 3451 TYR A N     1 
ATOM   13605 C  CA    . TYR A 1 3451 ? 205.043 270.340 106.033 1.00 108.84 ? 3451 TYR A CA    1 
ATOM   13606 C  C     . TYR A 1 3451 ? 204.294 270.352 107.361 1.00 108.87 ? 3451 TYR A C     1 
ATOM   13607 O  O     . TYR A 1 3451 ? 204.915 270.386 108.431 1.00 106.41 ? 3451 TYR A O     1 
ATOM   13608 C  CB    . TYR A 1 3451 ? 205.218 271.760 105.496 1.00 108.19 ? 3451 TYR A CB    1 
ATOM   13609 C  CG    . TYR A 1 3451 ? 205.700 271.817 104.063 1.00 110.10 ? 3451 TYR A CG    1 
ATOM   13610 C  CD1   . TYR A 1 3451 ? 206.790 271.063 103.645 1.00 108.80 ? 3451 TYR A CD1   1 
ATOM   13611 C  CD2   . TYR A 1 3451 ? 205.066 272.624 103.128 1.00 108.78 ? 3451 TYR A CD2   1 
ATOM   13612 C  CE1   . TYR A 1 3451 ? 207.234 271.111 102.336 1.00 108.74 ? 3451 TYR A CE1   1 
ATOM   13613 C  CE2   . TYR A 1 3451 ? 205.502 272.679 101.818 1.00 108.80 ? 3451 TYR A CE2   1 
ATOM   13614 C  CZ    . TYR A 1 3451 ? 206.586 271.922 101.428 1.00 109.22 ? 3451 TYR A CZ    1 
ATOM   13615 O  OH    . TYR A 1 3451 ? 207.022 271.975 100.124 1.00 105.54 ? 3451 TYR A OH    1 
ATOM   13616 N  N     . ALA A 1 3452 ? 202.960 270.325 107.311 1.00 106.09 ? 3452 ALA A N     1 
ATOM   13617 C  CA    . ALA A 1 3452 ? 202.176 270.237 108.538 1.00 104.20 ? 3452 ALA A CA    1 
ATOM   13618 C  C     . ALA A 1 3452 ? 202.453 268.932 109.274 1.00 103.24 ? 3452 ALA A C     1 
ATOM   13619 O  O     . ALA A 1 3452 ? 202.593 268.920 110.502 1.00 99.96  ? 3452 ALA A O     1 
ATOM   13620 C  CB    . ALA A 1 3452 ? 200.687 270.374 108.223 1.00 102.43 ? 3452 ALA A CB    1 
ATOM   13621 N  N     . VAL A 1 3453 ? 202.547 267.822 108.538 1.00 105.81 ? 3453 VAL A N     1 
ATOM   13622 C  CA    . VAL A 1 3453 ? 202.874 266.543 109.160 1.00 107.74 ? 3453 VAL A CA    1 
ATOM   13623 C  C     . VAL A 1 3453 ? 204.271 266.588 109.770 1.00 106.49 ? 3453 VAL A C     1 
ATOM   13624 O  O     . VAL A 1 3453 ? 204.498 266.080 110.876 1.00 103.75 ? 3453 VAL A O     1 
ATOM   13625 C  CB    . VAL A 1 3453 ? 202.737 265.402 108.136 1.00 104.64 ? 3453 VAL A CB    1 
ATOM   13626 C  CG1   . VAL A 1 3453 ? 203.151 264.075 108.755 1.00 102.41 ? 3453 VAL A CG1   1 
ATOM   13627 C  CG2   . VAL A 1 3453 ? 201.311 265.326 107.614 1.00 102.26 ? 3453 VAL A CG2   1 
ATOM   13628 N  N     . LEU A 1 3454 ? 205.227 267.193 109.061 1.00 104.07 ? 3454 LEU A N     1 
ATOM   13629 C  CA    . LEU A 1 3454 ? 206.591 267.278 109.575 1.00 105.86 ? 3454 LEU A CA    1 
ATOM   13630 C  C     . LEU A 1 3454 ? 206.652 268.097 110.860 1.00 105.98 ? 3454 LEU A C     1 
ATOM   13631 O  O     . LEU A 1 3454 ? 207.306 267.700 111.830 1.00 104.71 ? 3454 LEU A O     1 
ATOM   13632 C  CB    . LEU A 1 3454 ? 207.519 267.868 108.511 1.00 105.51 ? 3454 LEU A CB    1 
ATOM   13633 C  CG    . LEU A 1 3454 ? 208.333 266.865 107.688 1.00 105.17 ? 3454 LEU A CG    1 
ATOM   13634 C  CD1   . LEU A 1 3454 ? 207.440 266.034 106.779 1.00 103.29 ? 3454 LEU A CD1   1 
ATOM   13635 C  CD2   . LEU A 1 3454 ? 209.406 267.582 106.882 1.00 103.68 ? 3454 LEU A CD2   1 
ATOM   13636 N  N     . ILE A 1 3455 ? 205.969 269.244 110.893 1.00 101.33 ? 3455 ILE A N     1 
ATOM   13637 C  CA    . ILE A 1 3455 ? 206.015 270.062 112.103 1.00 102.08 ? 3455 ILE A CA    1 
ATOM   13638 C  C     . ILE A 1 3455 ? 205.243 269.394 113.239 1.00 102.22 ? 3455 ILE A C     1 
ATOM   13639 O  O     . ILE A 1 3455 ? 205.626 269.515 114.410 1.00 98.54  ? 3455 ILE A O     1 
ATOM   13640 C  CB    . ILE A 1 3455 ? 205.513 271.493 111.828 1.00 102.06 ? 3455 ILE A CB    1 
ATOM   13641 C  CG1   . ILE A 1 3455 ? 204.055 271.496 111.370 1.00 102.55 ? 3455 ILE A CG1   1 
ATOM   13642 C  CG2   . ILE A 1 3455 ? 206.404 272.178 110.800 1.00 99.90  ? 3455 ILE A CG2   1 
ATOM   13643 C  CD1   . ILE A 1 3455 ? 203.575 272.840 110.861 1.00 98.37  ? 3455 ILE A CD1   1 
ATOM   13644 N  N     . SER A 1 3456 ? 204.165 268.669 112.926 1.00 100.80 ? 3456 SER A N     1 
ATOM   13645 C  CA    . SER A 1 3456 ? 203.444 267.940 113.966 1.00 100.68 ? 3456 SER A CA    1 
ATOM   13646 C  C     . SER A 1 3456 ? 204.310 266.847 114.580 1.00 101.46 ? 3456 SER A C     1 
ATOM   13647 O  O     . SER A 1 3456 ? 204.347 266.691 115.808 1.00 98.50  ? 3456 SER A O     1 
ATOM   13648 C  CB    . SER A 1 3456 ? 202.157 267.348 113.393 1.00 99.18  ? 3456 SER A CB    1 
ATOM   13649 O  OG    . SER A 1 3456 ? 202.436 266.263 112.525 1.00 97.82  ? 3456 SER A OG    1 
ATOM   13650 N  N     . GLU A 1 3457 ? 205.022 266.083 113.747 1.00 103.00 ? 3457 GLU A N     1 
ATOM   13651 C  CA    . GLU A 1 3457 ? 205.896 265.051 114.294 1.00 103.16 ? 3457 GLU A CA    1 
ATOM   13652 C  C     . GLU A 1 3457 ? 207.087 265.664 115.020 1.00 103.79 ? 3457 GLU A C     1 
ATOM   13653 O  O     . GLU A 1 3457 ? 207.581 265.082 115.991 1.00 102.35 ? 3457 GLU A O     1 
ATOM   13654 C  CB    . GLU A 1 3457 ? 206.358 264.092 113.194 1.00 101.00 ? 3457 GLU A CB    1 
ATOM   13655 C  CG    . GLU A 1 3457 ? 207.394 264.649 112.237 1.00 102.08 ? 3457 GLU A CG    1 
ATOM   13656 C  CD    . GLU A 1 3457 ? 207.710 263.695 111.104 1.00 103.89 ? 3457 GLU A CD    1 
ATOM   13657 O  OE1   . GLU A 1 3457 ? 207.048 262.640 111.013 1.00 104.25 ? 3457 GLU A OE1   1 
ATOM   13658 O  OE2   . GLU A 1 3457 ? 208.625 263.996 110.309 1.00 102.91 ? 3457 GLU A OE2   1 
ATOM   13659 N  N     . ALA A 1 3458 ? 207.546 266.842 114.587 1.00 100.92 ? 3458 ALA A N     1 
ATOM   13660 C  CA    . ALA A 1 3458 ? 208.591 267.541 115.328 1.00 102.10 ? 3458 ALA A CA    1 
ATOM   13661 C  C     . ALA A 1 3458 ? 208.105 267.950 116.713 1.00 102.50 ? 3458 ALA A C     1 
ATOM   13662 O  O     . ALA A 1 3458 ? 208.844 267.827 117.696 1.00 97.78  ? 3458 ALA A O     1 
ATOM   13663 C  CB    . ALA A 1 3458 ? 209.066 268.761 114.540 1.00 98.84  ? 3458 ALA A CB    1 
ATOM   13664 N  N     . GLN A 1 3459 ? 206.866 268.438 116.812 1.00 101.86 ? 3459 GLN A N     1 
ATOM   13665 C  CA    . GLN A 1 3459 ? 206.307 268.776 118.119 1.00 101.90 ? 3459 GLN A CA    1 
ATOM   13666 C  C     . GLN A 1 3459 ? 206.137 267.533 118.986 1.00 101.85 ? 3459 GLN A C     1 
ATOM   13667 O  O     . GLN A 1 3459 ? 206.363 267.575 120.203 1.00 99.51  ? 3459 GLN A O     1 
ATOM   13668 C  CB    . GLN A 1 3459 ? 204.972 269.501 117.948 1.00 100.76 ? 3459 GLN A CB    1 
ATOM   13669 C  CG    . GLN A 1 3459 ? 204.470 270.177 119.212 1.00 100.81 ? 3459 GLN A CG    1 
ATOM   13670 C  CD    . GLN A 1 3459 ? 203.167 270.921 118.997 1.00 100.92 ? 3459 GLN A CD    1 
ATOM   13671 O  OE1   . GLN A 1 3459 ? 203.061 271.765 118.107 1.00 100.13 ? 3459 GLN A OE1   1 
ATOM   13672 N  NE2   . GLN A 1 3459 ? 202.166 270.612 119.814 1.00 98.85  ? 3459 GLN A NE2   1 
ATOM   13673 N  N     . ALA A 1 3460 ? 205.728 266.417 118.377 1.00 100.34 ? 3460 ALA A N     1 
ATOM   13674 C  CA    . ALA A 1 3460 ? 205.624 265.166 119.123 1.00 101.30 ? 3460 ALA A CA    1 
ATOM   13675 C  C     . ALA A 1 3460 ? 206.984 264.726 119.653 1.00 100.82 ? 3460 ALA A C     1 
ATOM   13676 O  O     . ALA A 1 3460 ? 207.099 264.275 120.801 1.00 99.13  ? 3460 ALA A O     1 
ATOM   13677 C  CB    . ALA A 1 3460 ? 205.013 264.077 118.242 1.00 97.04  ? 3460 ALA A CB    1 
ATOM   13678 N  N     . ILE A 1 3461 ? 208.027 264.851 118.829 1.00 101.93 ? 3461 ILE A N     1 
ATOM   13679 C  CA    . ILE A 1 3461 ? 209.377 264.518 119.270 1.00 104.70 ? 3461 ILE A CA    1 
ATOM   13680 C  C     . ILE A 1 3461 ? 209.826 265.465 120.378 1.00 103.54 ? 3461 ILE A C     1 
ATOM   13681 O  O     . ILE A 1 3461 ? 210.517 265.057 121.316 1.00 101.67 ? 3461 ILE A O     1 
ATOM   13682 C  CB    . ILE A 1 3461 ? 210.346 264.533 118.073 1.00 103.90 ? 3461 ILE A CB    1 
ATOM   13683 C  CG1   . ILE A 1 3461 ? 210.018 263.391 117.109 1.00 100.69 ? 3461 ILE A CG1   1 
ATOM   13684 C  CG2   . ILE A 1 3461 ? 211.789 264.419 118.538 1.00 101.39 ? 3461 ILE A CG2   1 
ATOM   13685 C  CD1   . ILE A 1 3461 ? 209.980 262.029 117.765 1.00 99.56  ? 3461 ILE A CD1   1 
ATOM   13686 N  N     . LYS A 1 3462 ? 209.440 266.740 120.289 1.00 100.14 ? 3462 LYS A N     1 
ATOM   13687 C  CA    . LYS A 1 3462 ? 209.753 267.687 121.356 1.00 101.12 ? 3462 LYS A CA    1 
ATOM   13688 C  C     . LYS A 1 3462 ? 209.121 267.260 122.675 1.00 101.05 ? 3462 LYS A C     1 
ATOM   13689 O  O     . LYS A 1 3462 ? 209.777 267.279 123.725 1.00 99.31  ? 3462 LYS A O     1 
ATOM   13690 C  CB    . LYS A 1 3462 ? 209.274 269.089 120.973 1.00 99.72  ? 3462 LYS A CB    1 
ATOM   13691 C  CG    . LYS A 1 3462 ? 210.137 269.798 119.946 1.00 100.89 ? 3462 LYS A CG    1 
ATOM   13692 C  CD    . LYS A 1 3462 ? 209.402 270.977 119.326 1.00 100.85 ? 3462 LYS A CD    1 
ATOM   13693 C  CE    . LYS A 1 3462 ? 210.228 271.630 118.228 1.00 100.27 ? 3462 LYS A CE    1 
ATOM   13694 N  NZ    . LYS A 1 3462 ? 210.494 270.699 117.097 1.00 100.34 ? 3462 LYS A NZ    1 
ATOM   13695 N  N     . ALA A 1 3463 ? 207.844 266.875 122.639 1.00 98.81  ? 3463 ALA A N     1 
ATOM   13696 C  CA    . ALA A 1 3463 ? 207.170 266.425 123.855 1.00 99.35  ? 3463 ALA A CA    1 
ATOM   13697 C  C     . ALA A 1 3463 ? 207.809 265.154 124.405 1.00 98.77  ? 3463 ALA A C     1 
ATOM   13698 O  O     . ALA A 1 3463 ? 207.985 265.014 125.624 1.00 95.43  ? 3463 ALA A O     1 
ATOM   13699 C  CB    . ALA A 1 3463 ? 205.683 266.206 123.582 1.00 95.95  ? 3463 ALA A CB    1 
ATOM   13700 N  N     . ASP A 1 3464 ? 208.161 264.218 123.521 1.00 100.69 ? 3464 ASP A N     1 
ATOM   13701 C  CA    . ASP A 1 3464 ? 208.815 262.991 123.965 1.00 101.95 ? 3464 ASP A CA    1 
ATOM   13702 C  C     . ASP A 1 3464 ? 210.168 263.285 124.602 1.00 100.93 ? 3464 ASP A C     1 
ATOM   13703 O  O     . ASP A 1 3464 ? 210.529 262.683 125.619 1.00 98.72  ? 3464 ASP A O     1 
ATOM   13704 C  CB    . ASP A 1 3464 ? 208.969 262.025 122.791 1.00 100.64 ? 3464 ASP A CB    1 
ATOM   13705 C  CG    . ASP A 1 3464 ? 209.216 260.600 123.239 1.00 102.04 ? 3464 ASP A CG    1 
ATOM   13706 O  OD1   . ASP A 1 3464 ? 209.044 260.317 124.443 1.00 101.13 ? 3464 ASP A OD1   1 
ATOM   13707 O  OD2   . ASP A 1 3464 ? 209.583 259.763 122.388 1.00 101.45 ? 3464 ASP A OD2   1 
ATOM   13708 N  N     . LEU A 1 3465 ? 210.931 264.211 124.015 1.00 98.48  ? 3465 LEU A N     1 
ATOM   13709 C  CA    . LEU A 1 3465 ? 212.217 264.594 124.587 1.00 98.98  ? 3465 LEU A CA    1 
ATOM   13710 C  C     . LEU A 1 3465 ? 212.040 265.261 125.944 1.00 98.32  ? 3465 LEU A C     1 
ATOM   13711 O  O     . LEU A 1 3465 ? 212.837 265.037 126.862 1.00 93.56  ? 3465 LEU A O     1 
ATOM   13712 C  CB    . LEU A 1 3465 ? 212.959 265.522 123.625 1.00 99.12  ? 3465 LEU A CB    1 
ATOM   13713 C  CG    . LEU A 1 3465 ? 214.340 266.000 124.071 1.00 100.18 ? 3465 LEU A CG    1 
ATOM   13714 C  CD1   . LEU A 1 3465 ? 215.408 265.030 123.603 1.00 98.14  ? 3465 LEU A CD1   1 
ATOM   13715 C  CD2   . LEU A 1 3465 ? 214.618 267.401 123.550 1.00 97.15  ? 3465 LEU A CD2   1 
ATOM   13716 N  N     . ALA A 1 3466 ? 211.008 266.097 126.084 1.00 99.10  ? 3466 ALA A N     1 
ATOM   13717 C  CA    . ALA A 1 3466 ? 210.729 266.709 127.379 1.00 98.73  ? 3466 ALA A CA    1 
ATOM   13718 C  C     . ALA A 1 3466 ? 210.417 265.651 128.429 1.00 100.69 ? 3466 ALA A C     1 
ATOM   13719 O  O     . ALA A 1 3466 ? 210.925 265.711 129.556 1.00 98.03  ? 3466 ALA A O     1 
ATOM   13720 C  CB    . ALA A 1 3466 ? 209.574 267.703 127.255 1.00 91.93  ? 3466 ALA A CB    1 
ATOM   13721 N  N     . ALA A 1 3467 ? 209.592 264.664 128.072 1.00 98.70  ? 3467 ALA A N     1 
ATOM   13722 C  CA    . ALA A 1 3467 ? 209.289 263.585 129.008 1.00 96.22  ? 3467 ALA A CA    1 
ATOM   13723 C  C     . ALA A 1 3467 ? 210.542 262.794 129.367 1.00 96.67  ? 3467 ALA A C     1 
ATOM   13724 O  O     . ALA A 1 3467 ? 210.752 262.444 130.536 1.00 94.15  ? 3467 ALA A O     1 
ATOM   13725 C  CB    . ALA A 1 3467 ? 208.221 262.664 128.421 1.00 92.58  ? 3467 ALA A CB    1 
ATOM   13726 N  N     . VAL A 1 3468 ? 211.391 262.513 128.376 1.00 97.44  ? 3468 VAL A N     1 
ATOM   13727 C  CA    . VAL A 1 3468 ? 212.596 261.726 128.620 1.00 98.92  ? 3468 VAL A CA    1 
ATOM   13728 C  C     . VAL A 1 3468 ? 213.550 262.478 129.543 1.00 100.06 ? 3468 VAL A C     1 
ATOM   13729 O  O     . VAL A 1 3468 ? 214.123 261.897 130.471 1.00 98.89  ? 3468 VAL A O     1 
ATOM   13730 C  CB    . VAL A 1 3468 ? 213.270 261.348 127.289 1.00 97.94  ? 3468 VAL A CB    1 
ATOM   13731 C  CG1   . VAL A 1 3468 ? 214.691 260.863 127.527 1.00 95.64  ? 3468 VAL A CG1   1 
ATOM   13732 C  CG2   . VAL A 1 3468 ? 212.460 260.281 126.572 1.00 96.06  ? 3468 VAL A CG2   1 
ATOM   13733 N  N     . GLU A 1 3469 ? 213.733 263.781 129.310 1.00 96.98  ? 3469 GLU A N     1 
ATOM   13734 C  CA    . GLU A 1 3469 ? 214.635 264.546 130.167 1.00 96.46  ? 3469 GLU A CA    1 
ATOM   13735 C  C     . GLU A 1 3469 ? 214.063 264.726 131.569 1.00 95.74  ? 3469 GLU A C     1 
ATOM   13736 O  O     . GLU A 1 3469 ? 214.821 264.739 132.547 1.00 92.18  ? 3469 GLU A O     1 
ATOM   13737 C  CB    . GLU A 1 3469 ? 214.962 265.902 129.535 1.00 95.87  ? 3469 GLU A CB    1 
ATOM   13738 C  CG    . GLU A 1 3469 ? 213.799 266.872 129.438 1.00 95.57  ? 3469 GLU A CG    1 
ATOM   13739 C  CD    . GLU A 1 3469 ? 214.163 268.144 128.698 1.00 97.19  ? 3469 GLU A CD    1 
ATOM   13740 O  OE1   . GLU A 1 3469 ? 215.099 268.843 129.140 1.00 96.95  ? 3469 GLU A OE1   1 
ATOM   13741 O  OE2   . GLU A 1 3469 ? 213.515 268.445 127.673 1.00 95.12  ? 3469 GLU A OE2   1 
ATOM   13742 N  N     . ALA A 1 3470 ? 212.737 264.849 131.694 1.00 96.65  ? 3470 ALA A N     1 
ATOM   13743 C  CA    . ALA A 1 3470 ? 212.133 264.887 133.022 1.00 98.63  ? 3470 ALA A CA    1 
ATOM   13744 C  C     . ALA A 1 3470 ? 212.373 263.580 133.768 1.00 97.93  ? 3470 ALA A C     1 
ATOM   13745 O  O     . ALA A 1 3470 ? 212.713 263.587 134.958 1.00 94.35  ? 3470 ALA A O     1 
ATOM   13746 C  CB    . ALA A 1 3470 ? 210.637 265.179 132.910 1.00 94.77  ? 3470 ALA A CB    1 
ATOM   13747 N  N     . LYS A 1 3471 ? 212.213 262.447 133.078 1.00 96.93  ? 3471 LYS A N     1 
ATOM   13748 C  CA    . LYS A 1 3471 ? 212.501 261.159 133.700 1.00 96.23  ? 3471 LYS A CA    1 
ATOM   13749 C  C     . LYS A 1 3471 ? 213.974 261.034 134.069 1.00 96.26  ? 3471 LYS A C     1 
ATOM   13750 O  O     . LYS A 1 3471 ? 214.303 260.464 135.114 1.00 94.73  ? 3471 LYS A O     1 
ATOM   13751 C  CB    . LYS A 1 3471 ? 212.083 260.020 132.770 1.00 95.02  ? 3471 LYS A CB    1 
ATOM   13752 C  CG    . LYS A 1 3471 ? 212.614 258.655 133.176 1.00 95.75  ? 3471 LYS A CG    1 
ATOM   13753 C  CD    . LYS A 1 3471 ? 212.071 257.555 132.280 1.00 96.23  ? 3471 LYS A CD    1 
ATOM   13754 C  CE    . LYS A 1 3471 ? 210.600 257.293 132.551 1.00 96.52  ? 3471 LYS A CE    1 
ATOM   13755 N  NZ    . LYS A 1 3471 ? 210.117 256.087 131.823 1.00 96.26  ? 3471 LYS A NZ    1 
ATOM   13756 N  N     . VAL A 1 3472 ? 214.867 261.558 133.226 1.00 97.92  ? 3472 VAL A N     1 
ATOM   13757 C  CA    . VAL A 1 3472 ? 216.299 261.507 133.517 1.00 98.31  ? 3472 VAL A CA    1 
ATOM   13758 C  C     . VAL A 1 3472 ? 216.615 262.303 134.777 1.00 99.70  ? 3472 VAL A C     1 
ATOM   13759 O  O     . VAL A 1 3472 ? 217.382 261.857 135.639 1.00 97.60  ? 3472 VAL A O     1 
ATOM   13760 C  CB    . VAL A 1 3472 ? 217.108 262.016 132.310 1.00 97.13  ? 3472 VAL A CB    1 
ATOM   13761 C  CG1   . VAL A 1 3472 ? 218.518 262.394 132.733 1.00 94.91  ? 3472 VAL A CG1   1 
ATOM   13762 C  CG2   . VAL A 1 3472 ? 217.141 260.964 131.217 1.00 96.98  ? 3472 VAL A CG2   1 
ATOM   13763 N  N     . ASN A 1 3473 ? 216.037 263.500 134.898 1.00 98.97  ? 3473 ASN A N     1 
ATOM   13764 C  CA    . ASN A 1 3473 ? 216.241 264.297 136.106 1.00 97.73  ? 3473 ASN A CA    1 
ATOM   13765 C  C     . ASN A 1 3473 ? 215.672 263.596 137.334 1.00 95.14  ? 3473 ASN A C     1 
ATOM   13766 O  O     . ASN A 1 3473 ? 216.296 263.597 138.403 1.00 94.08  ? 3473 ASN A O     1 
ATOM   13767 C  CB    . ASN A 1 3473 ? 215.615 265.680 135.937 1.00 97.24  ? 3473 ASN A CB    1 
ATOM   13768 C  CG    . ASN A 1 3473 ? 216.495 266.623 135.142 1.00 99.00  ? 3473 ASN A CG    1 
ATOM   13769 O  OD1   . ASN A 1 3473 ? 217.633 266.293 134.807 1.00 99.99  ? 3473 ASN A OD1   1 
ATOM   13770 N  ND2   . ASN A 1 3473 ? 215.972 267.804 134.836 1.00 96.88  ? 3473 ASN A ND2   1 
ATOM   13771 N  N     . ARG A 1 3474 ? 214.489 262.990 137.200 1.00 95.09  ? 3474 ARG A N     1 
ATOM   13772 C  CA    . ARG A 1 3474 ? 213.896 262.255 138.313 1.00 96.10  ? 3474 ARG A CA    1 
ATOM   13773 C  C     . ARG A 1 3474 ? 214.796 261.107 138.753 1.00 95.80  ? 3474 ARG A C     1 
ATOM   13774 O  O     . ARG A 1 3474 ? 215.000 260.884 139.952 1.00 95.54  ? 3474 ARG A O     1 
ATOM   13775 C  CB    . ARG A 1 3474 ? 212.517 261.734 137.906 1.00 93.43  ? 3474 ARG A CB    1 
ATOM   13776 C  CG    . ARG A 1 3474 ? 211.581 261.403 139.052 1.00 93.92  ? 3474 ARG A CG    1 
ATOM   13777 C  CD    . ARG A 1 3474 ? 210.313 260.748 138.521 1.00 95.84  ? 3474 ARG A CD    1 
ATOM   13778 N  NE    . ARG A 1 3474 ? 209.423 260.302 139.585 1.00 97.91  ? 3474 ARG A NE    1 
ATOM   13779 C  CZ    . ARG A 1 3474 ? 208.505 261.064 140.164 1.00 96.36  ? 3474 ARG A CZ    1 
ATOM   13780 N  NH1   . ARG A 1 3474 ? 208.323 262.323 139.801 1.00 95.60  ? 3474 ARG A NH1   1 
ATOM   13781 N  NH2   . ARG A 1 3474 ? 207.750 260.549 141.130 1.00 93.21  ? 3474 ARG A NH2   1 
ATOM   13782 N  N     . SER A 1 3475 ? 215.360 260.379 137.790 1.00 95.54  ? 3475 SER A N     1 
ATOM   13783 C  CA    . SER A 1 3475 ? 216.210 259.240 138.114 1.00 95.31  ? 3475 SER A CA    1 
ATOM   13784 C  C     . SER A 1 3475 ? 217.544 259.687 138.703 1.00 92.93  ? 3475 SER A C     1 
ATOM   13785 O  O     . SER A 1 3475 ? 218.099 259.011 139.577 1.00 94.36  ? 3475 SER A O     1 
ATOM   13786 C  CB    . SER A 1 3475 ? 216.423 258.391 136.866 1.00 94.82  ? 3475 SER A CB    1 
ATOM   13787 O  OG    . SER A 1 3475 ? 216.895 259.180 135.789 1.00 94.75  ? 3475 SER A OG    1 
ATOM   13788 N  N     . THR A 1 3476 ? 218.081 260.816 138.236 1.00 86.40  ? 3476 THR A N     1 
ATOM   13789 C  CA    . THR A 1 3476 ? 219.293 261.356 138.844 1.00 90.54  ? 3476 THR A CA    1 
ATOM   13790 C  C     . THR A 1 3476 ? 219.036 261.790 140.282 1.00 91.99  ? 3476 THR A C     1 
ATOM   13791 O  O     . THR A 1 3476 ? 219.885 261.593 141.160 1.00 88.80  ? 3476 THR A O     1 
ATOM   13792 C  CB    . THR A 1 3476 ? 219.824 262.526 138.017 1.00 91.48  ? 3476 THR A CB    1 
ATOM   13793 O  OG1   . THR A 1 3476 ? 219.740 262.202 136.624 1.00 91.50  ? 3476 THR A OG1   1 
ATOM   13794 C  CG2   . THR A 1 3476 ? 221.273 262.817 138.379 1.00 86.85  ? 3476 THR A CG2   1 
ATOM   13795 N  N     . ALA A 1 3477 ? 217.866 262.380 140.541 1.00 91.56  ? 3477 ALA A N     1 
ATOM   13796 C  CA    . ALA A 1 3477 ? 217.493 262.708 141.913 1.00 91.64  ? 3477 ALA A CA    1 
ATOM   13797 C  C     . ALA A 1 3477 ? 217.366 261.449 142.761 1.00 92.18  ? 3477 ALA A C     1 
ATOM   13798 O  O     . ALA A 1 3477 ? 217.773 261.432 143.928 1.00 88.68  ? 3477 ALA A O     1 
ATOM   13799 C  CB    . ALA A 1 3477 ? 216.188 263.503 141.927 1.00 87.37  ? 3477 ALA A CB    1 
ATOM   13800 N  N     . LEU A 1 3478 ? 216.798 260.384 142.189 1.00 89.92  ? 3478 LEU A N     1 
ATOM   13801 C  CA    . LEU A 1 3478 ? 216.717 259.111 142.901 1.00 88.73  ? 3478 LEU A CA    1 
ATOM   13802 C  C     . LEU A 1 3478 ? 218.103 258.578 143.244 1.00 87.12  ? 3478 LEU A C     1 
ATOM   13803 O  O     . LEU A 1 3478 ? 218.338 258.109 144.365 1.00 87.22  ? 3478 LEU A O     1 
ATOM   13804 C  CB    . LEU A 1 3478 ? 215.951 258.090 142.061 1.00 89.45  ? 3478 LEU A CB    1 
ATOM   13805 C  CG    . LEU A 1 3478 ? 215.730 256.723 142.706 1.00 92.77  ? 3478 LEU A CG    1 
ATOM   13806 C  CD1   . LEU A 1 3478 ? 214.883 256.859 143.960 1.00 89.27  ? 3478 LEU A CD1   1 
ATOM   13807 C  CD2   . LEU A 1 3478 ? 215.095 255.758 141.719 1.00 90.01  ? 3478 LEU A CD2   1 
ATOM   13808 N  N     . LEU A 1 3479 ? 219.033 258.636 142.288 1.00 87.17  ? 3479 LEU A N     1 
ATOM   13809 C  CA    . LEU A 1 3479 ? 220.392 258.169 142.547 1.00 87.52  ? 3479 LEU A CA    1 
ATOM   13810 C  C     . LEU A 1 3479 ? 221.068 259.002 143.627 1.00 88.81  ? 3479 LEU A C     1 
ATOM   13811 O  O     . LEU A 1 3479 ? 221.763 258.459 144.493 1.00 90.64  ? 3479 LEU A O     1 
ATOM   13812 C  CB    . LEU A 1 3479 ? 221.224 258.195 141.266 1.00 87.23  ? 3479 LEU A CB    1 
ATOM   13813 C  CG    . LEU A 1 3479 ? 220.924 257.139 140.205 1.00 92.35  ? 3479 LEU A CG    1 
ATOM   13814 C  CD1   . LEU A 1 3479 ? 222.036 257.120 139.168 1.00 88.30  ? 3479 LEU A CD1   1 
ATOM   13815 C  CD2   . LEU A 1 3479 ? 220.750 255.771 140.843 1.00 90.25  ? 3479 LEU A CD2   1 
ATOM   13816 N  N     . LYS A 1 3480 ? 220.888 260.323 143.588 1.00 89.15  ? 3480 LYS A N     1 
ATOM   13817 C  CA    . LYS A 1 3480 ? 221.483 261.169 144.617 1.00 92.45  ? 3480 LYS A CA    1 
ATOM   13818 C  C     . LYS A 1 3480 ? 220.888 260.870 145.988 1.00 90.53  ? 3480 LYS A C     1 
ATOM   13819 O  O     . LYS A 1 3480 ? 221.605 260.860 146.996 1.00 85.71  ? 3480 LYS A O     1 
ATOM   13820 C  CB    . LYS A 1 3480 ? 221.307 262.645 144.262 1.00 91.23  ? 3480 LYS A CB    1 
ATOM   13821 C  CG    . LYS A 1 3480 ? 222.175 263.113 143.105 1.00 89.79  ? 3480 LYS A CG    1 
ATOM   13822 C  CD    . LYS A 1 3480 ? 222.146 264.627 142.968 1.00 88.97  ? 3480 LYS A CD    1 
ATOM   13823 C  CE    . LYS A 1 3480 ? 220.793 265.114 142.481 1.00 90.01  ? 3480 LYS A CE    1 
ATOM   13824 N  NZ    . LYS A 1 3480 ? 220.555 264.766 141.055 1.00 89.22  ? 3480 LYS A NZ    1 
ATOM   13825 N  N     . SER A 1 3481 ? 219.576 260.626 146.046 1.00 88.23  ? 3481 SER A N     1 
ATOM   13826 C  CA    . SER A 1 3481 ? 218.938 260.286 147.314 1.00 87.01  ? 3481 SER A CA    1 
ATOM   13827 C  C     . SER A 1 3481 ? 219.440 258.950 147.849 1.00 88.54  ? 3481 SER A C     1 
ATOM   13828 O  O     . SER A 1 3481 ? 219.620 258.789 149.061 1.00 87.83  ? 3481 SER A O     1 
ATOM   13829 C  CB    . SER A 1 3481 ? 217.420 260.257 147.144 1.00 86.27  ? 3481 SER A CB    1 
ATOM   13830 O  OG    . SER A 1 3481 ? 216.948 261.467 146.581 1.00 87.91  ? 3481 SER A OG    1 
ATOM   13831 N  N     . LEU A 1 3482 ? 219.670 257.984 146.963 1.00 87.68  ? 3482 LEU A N     1 
ATOM   13832 C  CA    . LEU A 1 3482 ? 220.121 256.658 147.364 1.00 86.82  ? 3482 LEU A CA    1 
ATOM   13833 C  C     . LEU A 1 3482 ? 221.640 256.529 147.417 1.00 85.85  ? 3482 LEU A C     1 
ATOM   13834 O  O     . LEU A 1 3482 ? 222.142 255.427 147.658 1.00 85.68  ? 3482 LEU A O     1 
ATOM   13835 C  CB    . LEU A 1 3482 ? 219.548 255.601 146.415 1.00 82.80  ? 3482 LEU A CB    1 
ATOM   13836 C  CG    . LEU A 1 3482 ? 218.036 255.384 146.499 1.00 84.14  ? 3482 LEU A CG    1 
ATOM   13837 C  CD1   . LEU A 1 3482 ? 217.616 254.173 145.683 1.00 82.59  ? 3482 LEU A CD1   1 
ATOM   13838 C  CD2   . LEU A 1 3482 ? 217.599 255.236 147.946 1.00 83.60  ? 3482 LEU A CD2   1 
ATOM   13839 N  N     . SER A 1 3483 ? 222.378 257.617 147.187 1.00 85.03  ? 3483 SER A N     1 
ATOM   13840 C  CA    . SER A 1 3483 ? 223.837 257.544 147.215 1.00 86.08  ? 3483 SER A CA    1 
ATOM   13841 C  C     . SER A 1 3483 ? 224.355 257.188 148.603 1.00 88.35  ? 3483 SER A C     1 
ATOM   13842 O  O     . SER A 1 3483 ? 225.305 256.407 148.736 1.00 89.03  ? 3483 SER A O     1 
ATOM   13843 C  CB    . SER A 1 3483 ? 224.438 258.868 146.745 1.00 87.03  ? 3483 SER A CB    1 
ATOM   13844 O  OG    . SER A 1 3483 ? 225.848 258.862 146.881 1.00 83.62  ? 3483 SER A OG    1 
ATOM   13845 N  N     . ALA A 1 3484 ? 223.758 257.763 149.650 1.00 90.92  ? 3484 ALA A N     1 
ATOM   13846 C  CA    . ALA A 1 3484 ? 224.181 257.435 151.009 1.00 89.37  ? 3484 ALA A CA    1 
ATOM   13847 C  C     . ALA A 1 3484 ? 223.907 255.972 151.330 1.00 89.82  ? 3484 ALA A C     1 
ATOM   13848 O  O     . ALA A 1 3484 ? 224.717 255.308 151.991 1.00 87.77  ? 3484 ALA A O     1 
ATOM   13849 C  CB    . ALA A 1 3484 ? 223.479 258.347 152.014 1.00 86.15  ? 3484 ALA A CB    1 
ATOM   13850 N  N     . GLU A 1 3485 ? 222.766 255.454 150.874 1.00 91.42  ? 3485 GLU A N     1 
ATOM   13851 C  CA    . GLU A 1 3485 ? 222.470 254.041 151.074 1.00 91.81  ? 3485 GLU A CA    1 
ATOM   13852 C  C     . GLU A 1 3485 ? 223.482 253.160 150.356 1.00 91.27  ? 3485 GLU A C     1 
ATOM   13853 O  O     . GLU A 1 3485 ? 223.886 252.124 150.894 1.00 93.60  ? 3485 GLU A O     1 
ATOM   13854 C  CB    . GLU A 1 3485 ? 221.047 253.727 150.605 1.00 89.19  ? 3485 GLU A CB    1 
ATOM   13855 C  CG    . GLU A 1 3485 ? 219.966 254.739 151.017 1.00 90.98  ? 3485 GLU A CG    1 
ATOM   13856 C  CD    . GLU A 1 3485 ? 220.111 255.298 152.432 1.00 94.64  ? 3485 GLU A CD    1 
ATOM   13857 O  OE1   . GLU A 1 3485 ? 219.639 256.431 152.661 1.00 93.58  ? 3485 GLU A OE1   1 
ATOM   13858 O  OE2   . GLU A 1 3485 ? 220.635 254.602 153.328 1.00 92.88  ? 3485 GLU A OE2   1 
ATOM   13859 N  N     . ARG A 1 3486 ? 223.907 253.560 149.154 1.00 92.66  ? 3486 ARG A N     1 
ATOM   13860 C  CA    . ARG A 1 3486 ? 224.973 252.844 148.459 1.00 91.98  ? 3486 ARG A CA    1 
ATOM   13861 C  C     . ARG A 1 3486 ? 226.210 252.694 149.333 1.00 93.43  ? 3486 ARG A C     1 
ATOM   13862 O  O     . ARG A 1 3486 ? 226.707 251.580 149.527 1.00 94.70  ? 3486 ARG A O     1 
ATOM   13863 C  CB    . ARG A 1 3486 ? 225.327 253.561 147.155 1.00 92.27  ? 3486 ARG A CB    1 
ATOM   13864 C  CG    . ARG A 1 3486 ? 226.468 252.915 146.373 1.00 90.85  ? 3486 ARG A CG    1 
ATOM   13865 C  CD    . ARG A 1 3486 ? 226.163 252.646 144.906 1.00 92.23  ? 3486 ARG A CD    1 
ATOM   13866 N  NE    . ARG A 1 3486 ? 225.372 251.439 144.705 1.00 94.99  ? 3486 ARG A NE    1 
ATOM   13867 C  CZ    . ARG A 1 3486 ? 224.830 251.084 143.548 1.00 95.13  ? 3486 ARG A CZ    1 
ATOM   13868 N  NH1   . ARG A 1 3486 ? 224.919 251.856 142.477 1.00 94.15  ? 3486 ARG A NH1   1 
ATOM   13869 N  NH2   . ARG A 1 3486 ? 224.195 249.920 143.460 1.00 93.22  ? 3486 ARG A NH2   1 
ATOM   13870 N  N     . GLU A 1 3487 ? 226.714 253.799 149.887 1.00 97.17  ? 3487 GLU A N     1 
ATOM   13871 C  CA    . GLU A 1 3487 ? 227.966 253.716 150.633 1.00 97.13  ? 3487 GLU A CA    1 
ATOM   13872 C  C     . GLU A 1 3487 ? 227.780 252.977 151.954 1.00 99.12  ? 3487 GLU A C     1 
ATOM   13873 O  O     . GLU A 1 3487 ? 228.638 252.176 152.344 1.00 97.88  ? 3487 GLU A O     1 
ATOM   13874 C  CB    . GLU A 1 3487 ? 228.557 255.112 150.857 1.00 96.87  ? 3487 GLU A CB    1 
ATOM   13875 C  CG    . GLU A 1 3487 ? 227.749 256.042 151.746 1.00 97.85  ? 3487 GLU A CG    1 
ATOM   13876 C  CD    . GLU A 1 3487 ? 228.422 257.389 151.937 1.00 99.40  ? 3487 GLU A CD    1 
ATOM   13877 O  OE1   . GLU A 1 3487 ? 229.492 257.610 151.332 1.00 98.60  ? 3487 GLU A OE1   1 
ATOM   13878 O  OE2   . GLU A 1 3487 ? 227.884 258.225 152.692 1.00 99.61  ? 3487 GLU A OE2   1 
ATOM   13879 N  N     . ARG A 1 3488 ? 226.660 253.209 152.647 1.00 98.75  ? 3488 ARG A N     1 
ATOM   13880 C  CA    . ARG A 1 3488 ? 226.433 252.508 153.909 1.00 96.22  ? 3488 ARG A CA    1 
ATOM   13881 C  C     . ARG A 1 3488 ? 226.325 251.004 153.695 1.00 95.90  ? 3488 ARG A C     1 
ATOM   13882 O  O     . ARG A 1 3488 ? 226.949 250.220 154.423 1.00 97.36  ? 3488 ARG A O     1 
ATOM   13883 C  CB    . ARG A 1 3488 ? 225.175 253.037 154.599 1.00 95.35  ? 3488 ARG A CB    1 
ATOM   13884 C  CG    . ARG A 1 3488 ? 224.853 252.305 155.893 1.00 95.03  ? 3488 ARG A CG    1 
ATOM   13885 C  CD    . ARG A 1 3488 ? 223.418 252.522 156.347 1.00 96.77  ? 3488 ARG A CD    1 
ATOM   13886 N  NE    . ARG A 1 3488 ? 222.934 253.867 156.061 1.00 99.40  ? 3488 ARG A NE    1 
ATOM   13887 C  CZ    . ARG A 1 3488 ? 221.666 254.240 156.166 1.00 97.15  ? 3488 ARG A CZ    1 
ATOM   13888 N  NH1   . ARG A 1 3488 ? 220.725 253.392 156.545 1.00 93.15  ? 3488 ARG A NH1   1 
ATOM   13889 N  NH2   . ARG A 1 3488 ? 221.334 255.497 155.884 1.00 95.50  ? 3488 ARG A NH2   1 
ATOM   13890 N  N     . TRP A 1 3489 ? 225.558 250.579 152.688 1.00 92.05  ? 3489 TRP A N     1 
ATOM   13891 C  CA    . TRP A 1 3489 ? 225.389 249.153 152.443 1.00 92.64  ? 3489 TRP A CA    1 
ATOM   13892 C  C     . TRP A 1 3489 ? 226.665 248.527 151.895 1.00 95.06  ? 3489 TRP A C     1 
ATOM   13893 O  O     . TRP A 1 3489 ? 226.967 247.369 152.198 1.00 97.48  ? 3489 TRP A O     1 
ATOM   13894 C  CB    . TRP A 1 3489 ? 224.217 248.922 151.494 1.00 91.99  ? 3489 TRP A CB    1 
ATOM   13895 C  CG    . TRP A 1 3489 ? 222.900 249.357 152.058 1.00 92.36  ? 3489 TRP A CG    1 
ATOM   13896 C  CD1   . TRP A 1 3489 ? 222.605 249.585 153.370 1.00 93.20  ? 3489 TRP A CD1   1 
ATOM   13897 C  CD2   . TRP A 1 3489 ? 221.696 249.612 151.327 1.00 93.79  ? 3489 TRP A CD2   1 
ATOM   13898 N  NE1   . TRP A 1 3489 ? 221.293 249.968 153.500 1.00 93.59  ? 3489 TRP A NE1   1 
ATOM   13899 C  CE2   . TRP A 1 3489 ? 220.713 249.992 152.260 1.00 94.24  ? 3489 TRP A CE2   1 
ATOM   13900 C  CE3   . TRP A 1 3489 ? 221.355 249.557 149.973 1.00 94.21  ? 3489 TRP A CE3   1 
ATOM   13901 C  CZ2   . TRP A 1 3489 ? 219.413 250.315 151.883 1.00 94.24  ? 3489 TRP A CZ2   1 
ATOM   13902 C  CZ3   . TRP A 1 3489 ? 220.065 249.878 149.601 1.00 94.50  ? 3489 TRP A CZ3   1 
ATOM   13903 C  CH2   . TRP A 1 3489 ? 219.109 250.252 150.552 1.00 93.87  ? 3489 TRP A CH2   1 
ATOM   13904 N  N     . GLU A 1 3490 ? 227.432 249.271 151.093 1.00 95.70  ? 3490 GLU A N     1 
ATOM   13905 C  CA    . GLU A 1 3490 ? 228.719 248.761 150.635 1.00 95.98  ? 3490 GLU A CA    1 
ATOM   13906 C  C     . GLU A 1 3490 ? 229.665 248.541 151.805 1.00 97.10  ? 3490 GLU A C     1 
ATOM   13907 O  O     . GLU A 1 3490 ? 230.353 247.515 151.873 1.00 98.10  ? 3490 GLU A O     1 
ATOM   13908 C  CB    . GLU A 1 3490 ? 229.339 249.724 149.622 1.00 97.63  ? 3490 GLU A CB    1 
ATOM   13909 C  CG    . GLU A 1 3490 ? 228.843 249.538 148.198 1.00 99.53  ? 3490 GLU A CG    1 
ATOM   13910 C  CD    . GLU A 1 3490 ? 229.514 250.478 147.215 1.00 100.63 ? 3490 GLU A CD    1 
ATOM   13911 O  OE1   . GLU A 1 3490 ? 229.567 251.696 147.491 1.00 101.08 ? 3490 GLU A OE1   1 
ATOM   13912 O  OE2   . GLU A 1 3490 ? 229.989 249.999 146.164 1.00 98.78  ? 3490 GLU A OE2   1 
ATOM   13913 N  N     . LYS A 1 3491 ? 229.709 249.491 152.743 1.00 96.61  ? 3491 LYS A N     1 
ATOM   13914 C  CA    . LYS A 1 3491 ? 230.551 249.321 153.921 1.00 97.78  ? 3491 LYS A CA    1 
ATOM   13915 C  C     . LYS A 1 3491 ? 230.089 248.139 154.763 1.00 97.79  ? 3491 LYS A C     1 
ATOM   13916 O  O     . LYS A 1 3491 ? 230.915 247.360 155.254 1.00 97.85  ? 3491 LYS A O     1 
ATOM   13917 C  CB    . LYS A 1 3491 ? 230.557 250.604 154.751 1.00 94.06  ? 3491 LYS A CB    1 
ATOM   13918 C  CG    . LYS A 1 3491 ? 231.374 251.731 154.142 1.00 96.19  ? 3491 LYS A CG    1 
ATOM   13919 C  CD    . LYS A 1 3491 ? 232.746 251.249 153.702 1.00 95.46  ? 3491 LYS A CD    1 
ATOM   13920 C  CE    . LYS A 1 3491 ? 233.386 252.231 152.734 1.00 95.84  ? 3491 LYS A CE    1 
ATOM   13921 N  NZ    . LYS A 1 3491 ? 232.624 252.333 151.458 1.00 94.03  ? 3491 LYS A NZ    1 
ATOM   13922 N  N     . THR A 1 3492 ? 228.774 247.989 154.942 1.00 91.30  ? 3492 THR A N     1 
ATOM   13923 C  CA    . THR A 1 3492 ? 228.262 246.880 155.742 1.00 91.48  ? 3492 THR A CA    1 
ATOM   13924 C  C     . THR A 1 3492 ? 228.574 245.534 155.095 1.00 90.46  ? 3492 THR A C     1 
ATOM   13925 O  O     . THR A 1 3492 ? 229.013 244.598 155.773 1.00 92.18  ? 3492 THR A O     1 
ATOM   13926 C  CB    . THR A 1 3492 ? 226.756 247.037 155.956 1.00 90.63  ? 3492 THR A CB    1 
ATOM   13927 O  OG1   . THR A 1 3492 ? 226.509 248.151 156.824 1.00 87.31  ? 3492 THR A OG1   1 
ATOM   13928 C  CG2   . THR A 1 3492 ? 226.171 245.784 156.586 1.00 89.82  ? 3492 THR A CG2   1 
ATOM   13929 N  N     . SER A 1 3493 ? 228.369 245.422 153.780 1.00 88.66  ? 3493 SER A N     1 
ATOM   13930 C  CA    . SER A 1 3493 ? 228.583 244.150 153.099 1.00 90.06  ? 3493 SER A CA    1 
ATOM   13931 C  C     . SER A 1 3493 ? 230.064 243.840 152.922 1.00 91.02  ? 3493 SER A C     1 
ATOM   13932 O  O     . SER A 1 3493 ? 230.435 242.670 152.778 1.00 88.71  ? 3493 SER A O     1 
ATOM   13933 C  CB    . SER A 1 3493 ? 227.878 244.156 151.743 1.00 90.34  ? 3493 SER A CB    1 
ATOM   13934 O  OG    . SER A 1 3493 ? 228.225 243.011 150.984 1.00 92.08  ? 3493 SER A OG    1 
ATOM   13935 N  N     . GLU A 1 3494 ? 230.920 244.864 152.916 1.00 95.83  ? 3494 GLU A N     1 
ATOM   13936 C  CA    . GLU A 1 3494 ? 232.353 244.619 152.797 1.00 97.22  ? 3494 GLU A CA    1 
ATOM   13937 C  C     . GLU A 1 3494 ? 232.895 243.868 154.005 1.00 98.55  ? 3494 GLU A C     1 
ATOM   13938 O  O     . GLU A 1 3494 ? 233.841 243.083 153.873 1.00 99.12  ? 3494 GLU A O     1 
ATOM   13939 C  CB    . GLU A 1 3494 ? 233.097 245.943 152.615 1.00 97.66  ? 3494 GLU A CB    1 
ATOM   13940 C  CG    . GLU A 1 3494 ? 234.590 245.794 152.360 1.00 100.08 ? 3494 GLU A CG    1 
ATOM   13941 C  CD    . GLU A 1 3494 ? 235.413 245.875 153.632 1.00 101.24 ? 3494 GLU A CD    1 
ATOM   13942 O  OE1   . GLU A 1 3494 ? 234.874 246.328 154.664 1.00 98.49  ? 3494 GLU A OE1   1 
ATOM   13943 O  OE2   . GLU A 1 3494 ? 236.598 245.484 153.600 1.00 98.88  ? 3494 GLU A OE2   1 
ATOM   13944 N  N     . THR A 1 3495 ? 232.312 244.086 155.180 1.00 97.94  ? 3495 THR A N     1 
ATOM   13945 C  CA    . THR A 1 3495 ? 232.758 243.452 156.411 1.00 98.17  ? 3495 THR A CA    1 
ATOM   13946 C  C     . THR A 1 3495 ? 232.101 242.099 156.656 1.00 97.20  ? 3495 THR A C     1 
ATOM   13947 O  O     . THR A 1 3495 ? 232.390 241.466 157.676 1.00 98.35  ? 3495 THR A O     1 
ATOM   13948 C  CB    . THR A 1 3495 ? 232.490 244.372 157.606 1.00 98.64  ? 3495 THR A CB    1 
ATOM   13949 O  OG1   . THR A 1 3495 ? 231.083 244.416 157.873 1.00 94.39  ? 3495 THR A OG1   1 
ATOM   13950 C  CG2   . THR A 1 3495 ? 232.988 245.779 157.314 1.00 97.32  ? 3495 THR A CG2   1 
ATOM   13951 N  N     . PHE A 1 3496 ? 231.236 241.643 155.744 1.00 91.92  ? 3496 PHE A N     1 
ATOM   13952 C  CA    . PHE A 1 3496 ? 230.470 240.419 155.973 1.00 92.61  ? 3496 PHE A CA    1 
ATOM   13953 C  C     . PHE A 1 3496 ? 231.379 239.243 156.304 1.00 94.62  ? 3496 PHE A C     1 
ATOM   13954 O  O     . PHE A 1 3496 ? 231.067 238.435 157.188 1.00 95.62  ? 3496 PHE A O     1 
ATOM   13955 C  CB    . PHE A 1 3496 ? 229.615 240.106 154.745 1.00 93.49  ? 3496 PHE A CB    1 
ATOM   13956 C  CG    . PHE A 1 3496 ? 229.157 238.676 154.666 1.00 93.25  ? 3496 PHE A CG    1 
ATOM   13957 C  CD1   . PHE A 1 3496 ? 228.064 238.245 155.398 1.00 92.14  ? 3496 PHE A CD1   1 
ATOM   13958 C  CD2   . PHE A 1 3496 ? 229.808 237.768 153.847 1.00 92.02  ? 3496 PHE A CD2   1 
ATOM   13959 C  CE1   . PHE A 1 3496 ? 227.635 236.934 155.324 1.00 91.15  ? 3496 PHE A CE1   1 
ATOM   13960 C  CE2   . PHE A 1 3496 ? 229.384 236.456 153.770 1.00 92.04  ? 3496 PHE A CE2   1 
ATOM   13961 C  CZ    . PHE A 1 3496 ? 228.295 236.040 154.510 1.00 91.94  ? 3496 PHE A CZ    1 
ATOM   13962 N  N     . LYS A 1 3497 ? 232.512 239.131 155.608 1.00 94.41  ? 3497 LYS A N     1 
ATOM   13963 C  CA    . LYS A 1 3497 ? 233.463 238.072 155.923 1.00 94.70  ? 3497 LYS A CA    1 
ATOM   13964 C  C     . LYS A 1 3497 ? 234.016 238.235 157.333 1.00 94.26  ? 3497 LYS A C     1 
ATOM   13965 O  O     . LYS A 1 3497 ? 234.273 237.241 158.022 1.00 94.74  ? 3497 LYS A O     1 
ATOM   13966 C  CB    . LYS A 1 3497 ? 234.595 238.059 154.896 1.00 93.94  ? 3497 LYS A CB    1 
ATOM   13967 C  CG    . LYS A 1 3497 ? 235.439 236.796 154.925 1.00 94.57  ? 3497 LYS A CG    1 
ATOM   13968 C  CD    . LYS A 1 3497 ? 235.151 235.917 153.719 1.00 95.23  ? 3497 LYS A CD    1 
ATOM   13969 C  CE    . LYS A 1 3497 ? 236.101 234.732 153.655 1.00 94.65  ? 3497 LYS A CE    1 
ATOM   13970 N  NZ    . LYS A 1 3497 ? 236.016 234.022 152.349 1.00 92.83  ? 3497 LYS A NZ    1 
ATOM   13971 N  N     . ASN A 1 3498 ? 234.200 239.479 157.783 1.00 94.29  ? 3498 ASN A N     1 
ATOM   13972 C  CA    . ASN A 1 3498 ? 234.718 239.703 159.129 1.00 92.66  ? 3498 ASN A CA    1 
ATOM   13973 C  C     . ASN A 1 3498 ? 233.699 239.302 160.190 1.00 92.27  ? 3498 ASN A C     1 
ATOM   13974 O  O     . ASN A 1 3498 ? 234.066 238.735 161.225 1.00 93.30  ? 3498 ASN A O     1 
ATOM   13975 C  CB    . ASN A 1 3498 ? 235.133 241.163 159.302 1.00 93.95  ? 3498 ASN A CB    1 
ATOM   13976 C  CG    . ASN A 1 3498 ? 235.889 241.402 160.595 1.00 96.84  ? 3498 ASN A CG    1 
ATOM   13977 O  OD1   . ASN A 1 3498 ? 235.433 242.140 161.468 1.00 98.85  ? 3498 ASN A OD1   1 
ATOM   13978 N  ND2   . ASN A 1 3498 ? 237.052 240.775 160.724 1.00 93.41  ? 3498 ASN A ND2   1 
ATOM   13979 N  N     . GLN A 1 3499 ? 232.415 239.596 159.961 1.00 91.39  ? 3499 GLN A N     1 
ATOM   13980 C  CA    . GLN A 1 3499 ? 231.392 239.114 160.886 1.00 92.12  ? 3499 GLN A CA    1 
ATOM   13981 C  C     . GLN A 1 3499 ? 231.325 237.594 160.882 1.00 92.20  ? 3499 GLN A C     1 
ATOM   13982 O  O     . GLN A 1 3499 ? 231.173 236.969 161.939 1.00 92.96  ? 3499 GLN A O     1 
ATOM   13983 C  CB    . GLN A 1 3499 ? 230.018 239.702 160.556 1.00 90.58  ? 3499 GLN A CB    1 
ATOM   13984 C  CG    . GLN A 1 3499 ? 229.802 241.139 161.006 1.00 92.81  ? 3499 GLN A CG    1 
ATOM   13985 C  CD    . GLN A 1 3499 ? 230.503 242.150 160.131 1.00 96.39  ? 3499 GLN A CD    1 
ATOM   13986 O  OE1   . GLN A 1 3499 ? 230.194 242.275 158.947 1.00 93.86  ? 3499 GLN A OE1   1 
ATOM   13987 N  NE2   . GLN A 1 3499 ? 231.457 242.876 160.704 1.00 93.25  ? 3499 GLN A NE2   1 
ATOM   13988 N  N     . MET A 1 3500 ? 231.427 236.979 159.703 1.00 91.10  ? 3500 MET A N     1 
ATOM   13989 C  CA    . MET A 1 3500 ? 231.399 235.522 159.632 1.00 91.04  ? 3500 MET A CA    1 
ATOM   13990 C  C     . MET A 1 3500 ? 232.606 234.911 160.337 1.00 90.37  ? 3500 MET A C     1 
ATOM   13991 O  O     . MET A 1 3500 ? 232.530 233.791 160.854 1.00 90.69  ? 3500 MET A O     1 
ATOM   13992 C  CB    . MET A 1 3500 ? 231.335 235.070 158.174 1.00 93.56  ? 3500 MET A CB    1 
ATOM   13993 C  CG    . MET A 1 3500 ? 231.143 233.573 157.999 1.00 94.84  ? 3500 MET A CG    1 
ATOM   13994 S  SD    . MET A 1 3500 ? 229.541 233.013 158.608 1.00 102.65 ? 3500 MET A SD    1 
ATOM   13995 C  CE    . MET A 1 3500 ? 229.889 231.287 158.940 1.00 93.77  ? 3500 MET A CE    1 
ATOM   13996 N  N     . SER A 1 3501 ? 233.732 235.625 160.358 1.00 82.73  ? 3501 SER A N     1 
ATOM   13997 C  CA    . SER A 1 3501 ? 234.920 235.109 161.029 1.00 84.05  ? 3501 SER A CA    1 
ATOM   13998 C  C     . SER A 1 3501 ? 234.786 235.155 162.547 1.00 87.91  ? 3501 SER A C     1 
ATOM   13999 O  O     . SER A 1 3501 ? 235.269 234.250 163.236 1.00 87.01  ? 3501 SER A O     1 
ATOM   14000 C  CB    . SER A 1 3501 ? 236.152 235.896 160.586 1.00 82.61  ? 3501 SER A CB    1 
ATOM   14001 O  OG    . SER A 1 3501 ? 237.312 235.453 161.266 1.00 86.84  ? 3501 SER A OG    1 
ATOM   14002 N  N     . THR A 1 3502 ? 234.141 236.188 163.085 1.00 78.41  ? 3502 THR A N     1 
ATOM   14003 C  CA    . THR A 1 3502 ? 234.110 236.432 164.520 1.00 70.34  ? 3502 THR A CA    1 
ATOM   14004 C  C     . THR A 1 3502 ? 232.840 235.930 165.190 1.00 67.32  ? 3502 THR A C     1 
ATOM   14005 O  O     . THR A 1 3502 ? 232.655 236.164 166.388 1.00 68.68  ? 3502 THR A O     1 
ATOM   14006 C  CB    . THR A 1 3502 ? 234.276 237.925 164.806 1.00 71.78  ? 3502 THR A CB    1 
ATOM   14007 O  OG1   . THR A 1 3502 ? 233.219 238.653 164.170 1.00 73.58  ? 3502 THR A OG1   1 
ATOM   14008 C  CG2   . THR A 1 3502 ? 235.613 238.425 164.286 1.00 71.39  ? 3502 THR A CG2   1 
ATOM   14009 N  N     . ILE A 1 3503 ? 231.957 235.255 164.453 1.00 64.58  ? 3503 ILE A N     1 
ATOM   14010 C  CA    . ILE A 1 3503 ? 230.679 234.863 165.039 1.00 65.31  ? 3503 ILE A CA    1 
ATOM   14011 C  C     . ILE A 1 3503 ? 230.867 233.760 166.074 1.00 63.71  ? 3503 ILE A C     1 
ATOM   14012 O  O     . ILE A 1 3503 ? 230.154 233.723 167.083 1.00 61.51  ? 3503 ILE A O     1 
ATOM   14013 C  CB    . ILE A 1 3503 ? 229.688 234.451 163.935 1.00 61.60  ? 3503 ILE A CB    1 
ATOM   14014 C  CG1   . ILE A 1 3503 ? 228.424 233.853 164.541 1.00 61.08  ? 3503 ILE A CG1   1 
ATOM   14015 C  CG2   . ILE A 1 3503 ? 230.317 233.449 162.998 1.00 66.75  ? 3503 ILE A CG2   1 
ATOM   14016 C  CD1   . ILE A 1 3503 ? 227.268 233.857 163.595 1.00 65.98  ? 3503 ILE A CD1   1 
ATOM   14017 N  N     . ALA A 1 3504 ? 231.824 232.854 165.857 1.00 62.07  ? 3504 ALA A N     1 
ATOM   14018 C  CA    . ALA A 1 3504 ? 232.040 231.767 166.808 1.00 51.27  ? 3504 ALA A CA    1 
ATOM   14019 C  C     . ALA A 1 3504 ? 232.466 232.293 168.172 1.00 55.20  ? 3504 ALA A C     1 
ATOM   14020 O  O     . ALA A 1 3504 ? 231.892 231.909 169.197 1.00 60.04  ? 3504 ALA A O     1 
ATOM   14021 C  CB    . ALA A 1 3504 ? 233.080 230.791 166.261 1.00 49.65  ? 3504 ALA A CB    1 
ATOM   14022 N  N     . GLY A 1 3505 ? 233.460 233.182 168.207 1.00 51.74  ? 3505 GLY A N     1 
ATOM   14023 C  CA    . GLY A 1 3505 ? 233.909 233.724 169.478 1.00 45.52  ? 3505 GLY A CA    1 
ATOM   14024 C  C     . GLY A 1 3505 ? 232.860 234.585 170.154 1.00 46.65  ? 3505 GLY A C     1 
ATOM   14025 O  O     . GLY A 1 3505 ? 232.673 234.509 171.372 1.00 57.98  ? 3505 GLY A O     1 
ATOM   14026 N  N     . ASP A 1 3506 ? 232.164 235.418 169.376 1.00 48.84  ? 3506 ASP A N     1 
ATOM   14027 C  CA    . ASP A 1 3506 ? 231.110 236.253 169.942 1.00 47.46  ? 3506 ASP A CA    1 
ATOM   14028 C  C     . ASP A 1 3506 ? 230.000 235.407 170.547 1.00 53.21  ? 3506 ASP A C     1 
ATOM   14029 O  O     . ASP A 1 3506 ? 229.530 235.691 171.655 1.00 53.40  ? 3506 ASP A O     1 
ATOM   14030 C  CB    . ASP A 1 3506 ? 230.543 237.183 168.872 1.00 54.22  ? 3506 ASP A CB    1 
ATOM   14031 C  CG    . ASP A 1 3506 ? 231.411 238.397 168.637 1.00 64.42  ? 3506 ASP A CG    1 
ATOM   14032 O  OD1   . ASP A 1 3506 ? 232.020 238.889 169.609 1.00 65.72  ? 3506 ASP A OD1   1 
ATOM   14033 O  OD2   . ASP A 1 3506 ? 231.482 238.862 167.480 1.00 64.12  ? 3506 ASP A OD2   1 
ATOM   14034 N  N     . CYS A 1 3507 ? 229.570 234.363 169.837 1.00 51.71  ? 3507 CYS A N     1 
ATOM   14035 C  CA    . CYS A 1 3507 ? 228.517 233.501 170.358 1.00 46.77  ? 3507 CYS A CA    1 
ATOM   14036 C  C     . CYS A 1 3507 ? 228.989 232.712 171.569 1.00 50.81  ? 3507 CYS A C     1 
ATOM   14037 O  O     . CYS A 1 3507 ? 228.216 232.507 172.508 1.00 56.69  ? 3507 CYS A O     1 
ATOM   14038 C  CB    . CYS A 1 3507 ? 228.015 232.563 169.264 1.00 48.56  ? 3507 CYS A CB    1 
ATOM   14039 S  SG    . CYS A 1 3507 ? 226.944 233.362 168.053 1.00 66.51  ? 3507 CYS A SG    1 
ATOM   14040 N  N     . LEU A 1 3508 ? 230.249 232.267 171.575 1.00 41.00  ? 3508 LEU A N     1 
ATOM   14041 C  CA    . LEU A 1 3508 ? 230.776 231.587 172.753 1.00 36.31  ? 3508 LEU A CA    1 
ATOM   14042 C  C     . LEU A 1 3508 ? 230.750 232.506 173.967 1.00 41.84  ? 3508 LEU A C     1 
ATOM   14043 O  O     . LEU A 1 3508 ? 230.292 232.111 175.046 1.00 56.12  ? 3508 LEU A O     1 
ATOM   14044 C  CB    . LEU A 1 3508 ? 232.197 231.094 172.478 1.00 39.91  ? 3508 LEU A CB    1 
ATOM   14045 C  CG    . LEU A 1 3508 ? 232.840 230.092 173.442 1.00 40.36  ? 3508 LEU A CG    1 
ATOM   14046 C  CD1   . LEU A 1 3508 ? 233.778 229.174 172.681 1.00 40.21  ? 3508 LEU A CD1   1 
ATOM   14047 C  CD2   . LEU A 1 3508 ? 233.588 230.792 174.562 1.00 43.34  ? 3508 LEU A CD2   1 
ATOM   14048 N  N     . LEU A 1 3509 ? 231.222 233.745 173.802 1.00 40.18  ? 3509 LEU A N     1 
ATOM   14049 C  CA    . LEU A 1 3509 ? 231.225 234.693 174.911 1.00 36.15  ? 3509 LEU A CA    1 
ATOM   14050 C  C     . LEU A 1 3509 ? 229.810 235.001 175.383 1.00 42.54  ? 3509 LEU A C     1 
ATOM   14051 O  O     . LEU A 1 3509 ? 229.549 235.054 176.590 1.00 45.55  ? 3509 LEU A O     1 
ATOM   14052 C  CB    . LEU A 1 3509 ? 231.936 235.979 174.499 1.00 42.17  ? 3509 LEU A CB    1 
ATOM   14053 C  CG    . LEU A 1 3509 ? 233.438 235.900 174.240 1.00 41.01  ? 3509 LEU A CG    1 
ATOM   14054 C  CD1   . LEU A 1 3509 ? 233.960 237.253 173.808 1.00 42.19  ? 3509 LEU A CD1   1 
ATOM   14055 C  CD2   . LEU A 1 3509 ? 234.164 235.415 175.475 1.00 41.16  ? 3509 LEU A CD2   1 
ATOM   14056 N  N     . SER A 1 3510 ? 228.884 235.207 174.445 1.00 37.48  ? 3510 SER A N     1 
ATOM   14057 C  CA    . SER A 1 3510 ? 227.513 235.537 174.815 1.00 32.25  ? 3510 SER A CA    1 
ATOM   14058 C  C     . SER A 1 3510 ? 226.837 234.378 175.536 1.00 42.01  ? 3510 SER A C     1 
ATOM   14059 O  O     . SER A 1 3510 ? 226.131 234.586 176.529 1.00 52.60  ? 3510 SER A O     1 
ATOM   14060 C  CB    . SER A 1 3510 ? 226.724 235.933 173.571 1.00 40.86  ? 3510 SER A CB    1 
ATOM   14061 O  OG    . SER A 1 3510 ? 227.447 236.871 172.794 1.00 46.75  ? 3510 SER A OG    1 
ATOM   14062 N  N     . ALA A 1 3511 ? 227.037 233.151 175.050 1.00 31.97  ? 3511 ALA A N     1 
ATOM   14063 C  CA    . ALA A 1 3511 ? 226.471 231.984 175.714 1.00 28.11  ? 3511 ALA A CA    1 
ATOM   14064 C  C     . ALA A 1 3511 ? 227.049 231.811 177.109 1.00 35.28  ? 3511 ALA A C     1 
ATOM   14065 O  O     . ALA A 1 3511 ? 226.322 231.489 178.055 1.00 38.70  ? 3511 ALA A O     1 
ATOM   14066 C  CB    . ALA A 1 3511 ? 226.726 230.737 174.877 1.00 36.68  ? 3511 ALA A CB    1 
ATOM   14067 N  N     . ALA A 1 3512 ? 228.360 232.016 177.254 1.00 34.55  ? 3512 ALA A N     1 
ATOM   14068 C  CA    . ALA A 1 3512 ? 228.974 231.938 178.572 1.00 28.44  ? 3512 ALA A CA    1 
ATOM   14069 C  C     . ALA A 1 3512 ? 228.382 232.977 179.512 1.00 36.72  ? 3512 ALA A C     1 
ATOM   14070 O  O     . ALA A 1 3512 ? 228.081 232.676 180.673 1.00 41.79  ? 3512 ALA A O     1 
ATOM   14071 C  CB    . ALA A 1 3512 ? 230.485 232.118 178.452 1.00 30.42  ? 3512 ALA A CB    1 
ATOM   14072 N  N     . PHE A 1 3513 ? 228.194 234.205 179.025 1.00 38.02  ? 3513 PHE A N     1 
ATOM   14073 C  CA    . PHE A 1 3513 ? 227.622 235.251 179.864 1.00 33.80  ? 3513 PHE A CA    1 
ATOM   14074 C  C     . PHE A 1 3513 ? 226.196 234.914 180.279 1.00 36.65  ? 3513 PHE A C     1 
ATOM   14075 O  O     . PHE A 1 3513 ? 225.821 235.099 181.442 1.00 47.95  ? 3513 PHE A O     1 
ATOM   14076 C  CB    . PHE A 1 3513 ? 227.664 236.593 179.136 1.00 32.08  ? 3513 PHE A CB    1 
ATOM   14077 C  CG    . PHE A 1 3513 ? 227.406 237.767 180.031 1.00 40.19  ? 3513 PHE A CG    1 
ATOM   14078 C  CD1   . PHE A 1 3513 ? 228.413 238.278 180.829 1.00 41.42  ? 3513 PHE A CD1   1 
ATOM   14079 C  CD2   . PHE A 1 3513 ? 226.152 238.349 180.086 1.00 36.96  ? 3513 PHE A CD2   1 
ATOM   14080 C  CE1   . PHE A 1 3513 ? 228.177 239.349 181.658 1.00 44.57  ? 3513 PHE A CE1   1 
ATOM   14081 C  CE2   . PHE A 1 3513 ? 225.911 239.421 180.914 1.00 38.82  ? 3513 PHE A CE2   1 
ATOM   14082 C  CZ    . PHE A 1 3513 ? 226.925 239.921 181.701 1.00 45.18  ? 3513 PHE A CZ    1 
ATOM   14083 N  N     . ILE A 1 3514 ? 225.384 234.416 179.345 1.00 24.45  ? 3514 ILE A N     1 
ATOM   14084 C  CA    . ILE A 1 3514 ? 223.996 234.100 179.669 1.00 30.70  ? 3514 ILE A CA    1 
ATOM   14085 C  C     . ILE A 1 3514 ? 223.921 232.948 180.663 1.00 41.11  ? 3514 ILE A C     1 
ATOM   14086 O  O     . ILE A 1 3514 ? 223.118 232.974 181.603 1.00 36.12  ? 3514 ILE A O     1 
ATOM   14087 C  CB    . ILE A 1 3514 ? 223.196 233.791 178.391 1.00 34.53  ? 3514 ILE A CB    1 
ATOM   14088 C  CG1   . ILE A 1 3514 ? 223.197 234.992 177.450 1.00 40.69  ? 3514 ILE A CG1   1 
ATOM   14089 C  CG2   . ILE A 1 3514 ? 221.768 233.426 178.735 1.00 33.93  ? 3514 ILE A CG2   1 
ATOM   14090 C  CD1   . ILE A 1 3514 ? 222.555 234.702 176.117 1.00 44.04  ? 3514 ILE A CD1   1 
ATOM   14091 N  N     . ALA A 1 3515 ? 224.752 231.921 180.479 1.00 43.56  ? 3515 ALA A N     1 
ATOM   14092 C  CA    . ALA A 1 3515 ? 224.638 230.719 181.292 1.00 23.98  ? 3515 ALA A CA    1 
ATOM   14093 C  C     . ALA A 1 3515 ? 225.338 230.824 182.639 1.00 32.02  ? 3515 ALA A C     1 
ATOM   14094 O  O     . ALA A 1 3515 ? 224.967 230.095 183.565 1.00 39.69  ? 3515 ALA A O     1 
ATOM   14095 C  CB    . ALA A 1 3515 ? 225.198 229.521 180.531 1.00 28.41  ? 3515 ALA A CB    1 
ATOM   14096 N  N     . TYR A 1 3516 ? 226.327 231.698 182.780 1.00 36.56  ? 3516 TYR A N     1 
ATOM   14097 C  CA    . TYR A 1 3516 ? 227.166 231.689 183.972 1.00 25.70  ? 3516 TYR A CA    1 
ATOM   14098 C  C     . TYR A 1 3516 ? 227.076 232.956 184.804 1.00 35.98  ? 3516 TYR A C     1 
ATOM   14099 O  O     . TYR A 1 3516 ? 226.943 232.872 186.027 1.00 47.33  ? 3516 TYR A O     1 
ATOM   14100 C  CB    . TYR A 1 3516 ? 228.629 231.464 183.574 1.00 28.59  ? 3516 TYR A CB    1 
ATOM   14101 C  CG    . TYR A 1 3516 ? 228.941 230.057 183.128 1.00 36.33  ? 3516 TYR A CG    1 
ATOM   14102 C  CD1   . TYR A 1 3516 ? 228.800 228.984 183.994 1.00 37.50  ? 3516 TYR A CD1   1 
ATOM   14103 C  CD2   . TYR A 1 3516 ? 229.385 229.803 181.840 1.00 34.31  ? 3516 TYR A CD2   1 
ATOM   14104 C  CE1   . TYR A 1 3516 ? 229.092 227.702 183.591 1.00 34.36  ? 3516 TYR A CE1   1 
ATOM   14105 C  CE2   . TYR A 1 3516 ? 229.675 228.524 181.429 1.00 31.24  ? 3516 TYR A CE2   1 
ATOM   14106 C  CZ    . TYR A 1 3516 ? 229.526 227.478 182.308 1.00 33.75  ? 3516 TYR A CZ    1 
ATOM   14107 O  OH    . TYR A 1 3516 ? 229.817 226.201 181.899 1.00 49.39  ? 3516 TYR A OH    1 
ATOM   14108 N  N     . ALA A 1 3517 ? 227.143 234.130 184.180 1.00 31.02  ? 3517 ALA A N     1 
ATOM   14109 C  CA    . ALA A 1 3517 ? 227.329 235.386 184.893 1.00 33.94  ? 3517 ALA A CA    1 
ATOM   14110 C  C     . ALA A 1 3517 ? 226.031 235.973 185.432 1.00 32.65  ? 3517 ALA A C     1 
ATOM   14111 O  O     . ALA A 1 3517 ? 225.989 237.167 185.742 1.00 52.31  ? 3517 ALA A O     1 
ATOM   14112 C  CB    . ALA A 1 3517 ? 228.023 236.403 183.985 1.00 39.20  ? 3517 ALA A CB    1 
ATOM   14113 N  N     . GLY A 1 3518 ? 224.976 235.169 185.550 1.00 39.15  ? 3518 GLY A N     1 
ATOM   14114 C  CA    . GLY A 1 3518 ? 223.708 235.700 186.021 1.00 33.53  ? 3518 GLY A CA    1 
ATOM   14115 C  C     . GLY A 1 3518 ? 223.735 236.141 187.472 1.00 29.88  ? 3518 GLY A C     1 
ATOM   14116 O  O     . GLY A 1 3518 ? 223.213 237.205 187.815 1.00 38.34  ? 3518 GLY A O     1 
ATOM   14117 N  N     . TYR A 1 3519 ? 224.339 235.334 188.345 1.00 40.55  ? 3519 TYR A N     1 
ATOM   14118 C  CA    . TYR A 1 3519 ? 224.264 235.592 189.778 1.00 35.85  ? 3519 TYR A CA    1 
ATOM   14119 C  C     . TYR A 1 3519 ? 225.194 236.712 190.226 1.00 43.59  ? 3519 TYR A C     1 
ATOM   14120 O  O     . TYR A 1 3519 ? 224.912 237.379 191.226 1.00 45.62  ? 3519 TYR A O     1 
ATOM   14121 C  CB    . TYR A 1 3519 ? 224.581 234.313 190.554 1.00 30.98  ? 3519 TYR A CB    1 
ATOM   14122 C  CG    . TYR A 1 3519 ? 224.553 234.488 192.053 1.00 40.94  ? 3519 TYR A CG    1 
ATOM   14123 C  CD1   . TYR A 1 3519 ? 223.352 234.637 192.730 1.00 47.08  ? 3519 TYR A CD1   1 
ATOM   14124 C  CD2   . TYR A 1 3519 ? 225.727 234.511 192.791 1.00 47.71  ? 3519 TYR A CD2   1 
ATOM   14125 C  CE1   . TYR A 1 3519 ? 223.320 234.800 194.098 1.00 44.29  ? 3519 TYR A CE1   1 
ATOM   14126 C  CE2   . TYR A 1 3519 ? 225.705 234.675 194.160 1.00 48.19  ? 3519 TYR A CE2   1 
ATOM   14127 C  CZ    . TYR A 1 3519 ? 224.498 234.819 194.808 1.00 45.53  ? 3519 TYR A CZ    1 
ATOM   14128 O  OH    . TYR A 1 3519 ? 224.467 234.981 196.172 1.00 49.38  ? 3519 TYR A OH    1 
ATOM   14129 N  N     . PHE A 1 3520 ? 226.291 236.935 189.513 1.00 47.68  ? 3520 PHE A N     1 
ATOM   14130 C  CA    . PHE A 1 3520 ? 227.320 237.849 189.977 1.00 41.32  ? 3520 PHE A CA    1 
ATOM   14131 C  C     . PHE A 1 3520 ? 226.916 239.300 189.728 1.00 45.90  ? 3520 PHE A C     1 
ATOM   14132 O  O     . PHE A 1 3520 ? 225.950 239.599 189.023 1.00 48.57  ? 3520 PHE A O     1 
ATOM   14133 C  CB    . PHE A 1 3520 ? 228.647 237.534 189.294 1.00 44.13  ? 3520 PHE A CB    1 
ATOM   14134 C  CG    . PHE A 1 3520 ? 229.049 236.096 189.404 1.00 40.75  ? 3520 PHE A CG    1 
ATOM   14135 C  CD1   . PHE A 1 3520 ? 229.664 235.621 190.547 1.00 44.13  ? 3520 PHE A CD1   1 
ATOM   14136 C  CD2   . PHE A 1 3520 ? 228.794 235.215 188.373 1.00 43.69  ? 3520 PHE A CD2   1 
ATOM   14137 C  CE1   . PHE A 1 3520 ? 230.027 234.298 190.652 1.00 46.15  ? 3520 PHE A CE1   1 
ATOM   14138 C  CE2   . PHE A 1 3520 ? 229.152 233.890 188.475 1.00 44.78  ? 3520 PHE A CE2   1 
ATOM   14139 C  CZ    . PHE A 1 3520 ? 229.771 233.431 189.614 1.00 46.04  ? 3520 PHE A CZ    1 
ATOM   14140 N  N     . ASP A 1 3521 ? 227.677 240.211 190.330 1.00 44.47  ? 3521 ASP A N     1 
ATOM   14141 C  CA    . ASP A 1 3521 ? 227.454 241.637 190.165 1.00 42.46  ? 3521 ASP A CA    1 
ATOM   14142 C  C     . ASP A 1 3521 ? 228.237 242.155 188.959 1.00 45.38  ? 3521 ASP A C     1 
ATOM   14143 O  O     . ASP A 1 3521 ? 228.871 241.395 188.226 1.00 59.31  ? 3521 ASP A O     1 
ATOM   14144 C  CB    . ASP A 1 3521 ? 227.819 242.386 191.447 1.00 48.23  ? 3521 ASP A CB    1 
ATOM   14145 C  CG    . ASP A 1 3521 ? 229.288 242.256 191.814 1.00 59.88  ? 3521 ASP A CG    1 
ATOM   14146 O  OD1   . ASP A 1 3521 ? 230.037 241.552 191.105 1.00 59.16  ? 3521 ASP A OD1   1 
ATOM   14147 O  OD2   . ASP A 1 3521 ? 229.698 242.870 192.821 1.00 55.40  ? 3521 ASP A OD2   1 
ATOM   14148 N  N     . GLN A 1 3522 ? 228.197 243.474 188.757 1.00 43.13  ? 3522 GLN A N     1 
ATOM   14149 C  CA    . GLN A 1 3522 ? 228.784 244.060 187.555 1.00 48.33  ? 3522 GLN A CA    1 
ATOM   14150 C  C     . GLN A 1 3522 ? 230.287 243.825 187.488 1.00 53.78  ? 3522 GLN A C     1 
ATOM   14151 O  O     . GLN A 1 3522 ? 230.820 243.468 186.429 1.00 56.88  ? 3522 GLN A O     1 
ATOM   14152 C  CB    . GLN A 1 3522 ? 228.477 245.555 187.504 1.00 52.66  ? 3522 GLN A CB    1 
ATOM   14153 C  CG    . GLN A 1 3522 ? 229.157 246.285 186.364 1.00 52.35  ? 3522 GLN A CG    1 
ATOM   14154 C  CD    . GLN A 1 3522 ? 228.763 247.743 186.295 1.00 52.70  ? 3522 GLN A CD    1 
ATOM   14155 O  OE1   . GLN A 1 3522 ? 229.085 248.527 187.185 1.00 49.87  ? 3522 GLN A OE1   1 
ATOM   14156 N  NE2   . GLN A 1 3522 ? 228.055 248.114 185.236 1.00 53.11  ? 3522 GLN A NE2   1 
ATOM   14157 N  N     . GLN A 1 3523 ? 230.988 244.014 188.606 1.00 53.74  ? 3523 GLN A N     1 
ATOM   14158 C  CA    . GLN A 1 3523 ? 232.441 243.890 188.587 1.00 51.22  ? 3523 GLN A CA    1 
ATOM   14159 C  C     . GLN A 1 3523 ? 232.877 242.468 188.262 1.00 51.84  ? 3523 GLN A C     1 
ATOM   14160 O  O     . GLN A 1 3523 ? 233.784 242.263 187.448 1.00 55.80  ? 3523 GLN A O     1 
ATOM   14161 C  CB    . GLN A 1 3523 ? 233.029 244.339 189.922 1.00 54.72  ? 3523 GLN A CB    1 
ATOM   14162 C  CG    . GLN A 1 3523 ? 234.544 244.307 189.954 1.00 60.32  ? 3523 GLN A CG    1 
ATOM   14163 C  CD    . GLN A 1 3523 ? 235.164 245.247 188.937 1.00 65.14  ? 3523 GLN A CD    1 
ATOM   14164 O  OE1   . GLN A 1 3523 ? 235.666 244.813 187.900 1.00 59.01  ? 3523 GLN A OE1   1 
ATOM   14165 N  NE2   . GLN A 1 3523 ? 235.132 246.541 189.230 1.00 60.74  ? 3523 GLN A NE2   1 
ATOM   14166 N  N     . MET A 1 3524 ? 232.237 241.468 188.868 1.00 51.30  ? 3524 MET A N     1 
ATOM   14167 C  CA    . MET A 1 3524 ? 232.645 240.094 188.600 1.00 48.47  ? 3524 MET A CA    1 
ATOM   14168 C  C     . MET A 1 3524 ? 232.136 239.595 187.253 1.00 49.57  ? 3524 MET A C     1 
ATOM   14169 O  O     . MET A 1 3524 ? 232.800 238.772 186.615 1.00 57.12  ? 3524 MET A O     1 
ATOM   14170 C  CB    . MET A 1 3524 ? 232.196 239.175 189.734 1.00 42.51  ? 3524 MET A CB    1 
ATOM   14171 C  CG    . MET A 1 3524 ? 232.308 237.705 189.395 1.00 55.87  ? 3524 MET A CG    1 
ATOM   14172 S  SD    . MET A 1 3524 ? 233.947 237.055 189.763 1.00 70.14  ? 3524 MET A SD    1 
ATOM   14173 C  CE    . MET A 1 3524 ? 234.021 237.293 191.530 1.00 55.98  ? 3524 MET A CE    1 
ATOM   14174 N  N     . ARG A 1 3525 ? 230.987 240.088 186.790 1.00 40.46  ? 3525 ARG A N     1 
ATOM   14175 C  CA    . ARG A 1 3525 ? 230.581 239.805 185.418 1.00 36.80  ? 3525 ARG A CA    1 
ATOM   14176 C  C     . ARG A 1 3525 ? 231.628 240.310 184.435 1.00 47.10  ? 3525 ARG A C     1 
ATOM   14177 O  O     . ARG A 1 3525 ? 232.018 239.593 183.502 1.00 55.90  ? 3525 ARG A O     1 
ATOM   14178 C  CB    . ARG A 1 3525 ? 229.223 240.441 185.129 1.00 37.04  ? 3525 ARG A CB    1 
ATOM   14179 C  CG    . ARG A 1 3525 ? 228.040 239.682 185.696 1.00 33.48  ? 3525 ARG A CG    1 
ATOM   14180 C  CD    . ARG A 1 3525 ? 226.733 240.316 185.264 1.00 34.85  ? 3525 ARG A CD    1 
ATOM   14181 N  NE    . ARG A 1 3525 ? 225.606 239.840 186.057 1.00 34.84  ? 3525 ARG A NE    1 
ATOM   14182 C  CZ    . ARG A 1 3525 ? 224.335 240.048 185.747 1.00 32.29  ? 3525 ARG A CZ    1 
ATOM   14183 N  NH1   . ARG A 1 3525 ? 223.989 240.723 184.666 1.00 34.82  ? 3525 ARG A NH1   1 
ATOM   14184 N  NH2   . ARG A 1 3525 ? 223.386 239.568 186.544 1.00 34.66  ? 3525 ARG A NH2   1 
ATOM   14185 N  N     . GLN A 1 3526 ? 232.116 241.535 184.646 1.00 50.12  ? 3526 GLN A N     1 
ATOM   14186 C  CA    . GLN A 1 3526 ? 233.162 242.077 183.787 1.00 46.48  ? 3526 GLN A CA    1 
ATOM   14187 C  C     . GLN A 1 3526 ? 234.457 241.285 183.918 1.00 46.47  ? 3526 GLN A C     1 
ATOM   14188 O  O     . GLN A 1 3526 ? 235.155 241.064 182.923 1.00 51.90  ? 3526 GLN A O     1 
ATOM   14189 C  CB    . GLN A 1 3526 ? 233.399 243.550 184.112 1.00 46.09  ? 3526 GLN A CB    1 
ATOM   14190 C  CG    . GLN A 1 3526 ? 234.228 244.284 183.076 1.00 52.25  ? 3526 GLN A CG    1 
ATOM   14191 C  CD    . GLN A 1 3526 ? 233.797 243.969 181.659 1.00 57.93  ? 3526 GLN A CD    1 
ATOM   14192 O  OE1   . GLN A 1 3526 ? 232.655 244.219 181.276 1.00 55.77  ? 3526 GLN A OE1   1 
ATOM   14193 N  NE2   . GLN A 1 3526 ? 234.712 243.419 180.871 1.00 53.72  ? 3526 GLN A NE2   1 
ATOM   14194 N  N     . ASN A 1 3527 ? 234.803 240.861 185.136 1.00 39.80  ? 3527 ASN A N     1 
ATOM   14195 C  CA    . ASN A 1 3527 ? 236.012 240.066 185.329 1.00 39.02  ? 3527 ASN A CA    1 
ATOM   14196 C  C     . ASN A 1 3527 ? 235.938 238.754 184.562 1.00 49.68  ? 3527 ASN A C     1 
ATOM   14197 O  O     . ASN A 1 3527 ? 236.899 238.361 183.888 1.00 57.18  ? 3527 ASN A O     1 
ATOM   14198 C  CB    . ASN A 1 3527 ? 236.225 239.794 186.817 1.00 43.44  ? 3527 ASN A CB    1 
ATOM   14199 C  CG    . ASN A 1 3527 ? 236.774 240.993 187.557 1.00 58.13  ? 3527 ASN A CG    1 
ATOM   14200 O  OD1   . ASN A 1 3527 ? 237.070 242.026 186.957 1.00 59.52  ? 3527 ASN A OD1   1 
ATOM   14201 N  ND2   . ASN A 1 3527 ? 236.911 240.863 188.871 1.00 49.07  ? 3527 ASN A ND2   1 
ATOM   14202 N  N     . LEU A 1 3528 ? 234.800 238.062 184.652 1.00 49.01  ? 3528 LEU A N     1 
ATOM   14203 C  CA    . LEU A 1 3528 ? 234.630 236.805 183.933 1.00 39.48  ? 3528 LEU A CA    1 
ATOM   14204 C  C     . LEU A 1 3528 ? 234.683 237.018 182.428 1.00 40.09  ? 3528 LEU A C     1 
ATOM   14205 O  O     . LEU A 1 3528 ? 235.330 236.245 181.708 1.00 52.95  ? 3528 LEU A O     1 
ATOM   14206 C  CB    . LEU A 1 3528 ? 233.312 236.148 184.335 1.00 41.70  ? 3528 LEU A CB    1 
ATOM   14207 C  CG    . LEU A 1 3528 ? 233.271 235.454 185.695 1.00 42.81  ? 3528 LEU A CG    1 
ATOM   14208 C  CD1   . LEU A 1 3528 ? 231.862 234.989 186.012 1.00 44.43  ? 3528 LEU A CD1   1 
ATOM   14209 C  CD2   . LEU A 1 3528 ? 234.238 234.288 185.726 1.00 48.23  ? 3528 LEU A CD2   1 
ATOM   14210 N  N     . PHE A 1 3529 ? 234.005 238.056 181.930 1.00 33.32  ? 3529 PHE A N     1 
ATOM   14211 C  CA    . PHE A 1 3529 ? 234.031 238.312 180.494 1.00 40.69  ? 3529 PHE A CA    1 
ATOM   14212 C  C     . PHE A 1 3529 ? 235.438 238.646 180.019 1.00 47.76  ? 3529 PHE A C     1 
ATOM   14213 O  O     . PHE A 1 3529 ? 235.857 238.202 178.945 1.00 50.35  ? 3529 PHE A O     1 
ATOM   14214 C  CB    . PHE A 1 3529 ? 233.059 239.433 180.137 1.00 45.43  ? 3529 PHE A CB    1 
ATOM   14215 C  CG    . PHE A 1 3529 ? 232.543 239.354 178.731 1.00 44.94  ? 3529 PHE A CG    1 
ATOM   14216 C  CD1   . PHE A 1 3529 ? 231.482 238.525 178.416 1.00 45.09  ? 3529 PHE A CD1   1 
ATOM   14217 C  CD2   . PHE A 1 3529 ? 233.122 240.102 177.723 1.00 45.34  ? 3529 PHE A CD2   1 
ATOM   14218 C  CE1   . PHE A 1 3529 ? 231.007 238.448 177.124 1.00 42.84  ? 3529 PHE A CE1   1 
ATOM   14219 C  CE2   . PHE A 1 3529 ? 232.650 240.029 176.431 1.00 49.20  ? 3529 PHE A CE2   1 
ATOM   14220 C  CZ    . PHE A 1 3529 ? 231.591 239.202 176.131 1.00 44.07  ? 3529 PHE A CZ    1 
ATOM   14221 N  N     . THR A 1 3530 ? 236.185 239.422 180.808 1.00 49.99  ? 3530 THR A N     1 
ATOM   14222 C  CA    . THR A 1 3530 ? 237.558 239.752 180.445 1.00 44.12  ? 3530 THR A CA    1 
ATOM   14223 C  C     . THR A 1 3530 ? 238.439 238.511 180.429 1.00 49.41  ? 3530 THR A C     1 
ATOM   14224 O  O     . THR A 1 3530 ? 239.276 238.350 179.535 1.00 55.46  ? 3530 THR A O     1 
ATOM   14225 C  CB    . THR A 1 3530 ? 238.120 240.793 181.411 1.00 50.72  ? 3530 THR A CB    1 
ATOM   14226 O  OG1   . THR A 1 3530 ? 237.174 241.857 181.570 1.00 52.79  ? 3530 THR A OG1   1 
ATOM   14227 C  CG2   . THR A 1 3530 ? 239.424 241.361 180.879 1.00 52.66  ? 3530 THR A CG2   1 
ATOM   14228 N  N     . THR A 1 3531 ? 238.270 237.622 181.411 1.00 44.27  ? 3531 THR A N     1 
ATOM   14229 C  CA    . THR A 1 3531 ? 239.057 236.392 181.433 1.00 41.24  ? 3531 THR A CA    1 
ATOM   14230 C  C     . THR A 1 3531 ? 238.761 235.524 180.217 1.00 47.40  ? 3531 THR A C     1 
ATOM   14231 O  O     . THR A 1 3531 ? 239.683 235.005 179.570 1.00 54.71  ? 3531 THR A O     1 
ATOM   14232 C  CB    . THR A 1 3531 ? 238.782 235.616 182.719 1.00 44.36  ? 3531 THR A CB    1 
ATOM   14233 O  OG1   . THR A 1 3531 ? 238.860 236.503 183.841 1.00 52.60  ? 3531 THR A OG1   1 
ATOM   14234 C  CG2   . THR A 1 3531 ? 239.798 234.504 182.892 1.00 44.05  ? 3531 THR A CG2   1 
ATOM   14235 N  N     . TRP A 1 3532 ? 237.479 235.359 179.884 1.00 48.20  ? 3532 TRP A N     1 
ATOM   14236 C  CA    . TRP A 1 3532 ? 237.121 234.561 178.715 1.00 39.71  ? 3532 TRP A CA    1 
ATOM   14237 C  C     . TRP A 1 3532 ? 237.651 235.189 177.433 1.00 42.15  ? 3532 TRP A C     1 
ATOM   14238 O  O     . TRP A 1 3532 ? 238.144 234.480 176.548 1.00 53.24  ? 3532 TRP A O     1 
ATOM   14239 C  CB    . TRP A 1 3532 ? 235.606 234.385 178.636 1.00 37.85  ? 3532 TRP A CB    1 
ATOM   14240 C  CG    . TRP A 1 3532 ? 234.991 233.799 179.862 1.00 36.26  ? 3532 TRP A CG    1 
ATOM   14241 C  CD1   . TRP A 1 3532 ? 235.576 232.946 180.747 1.00 40.38  ? 3532 TRP A CD1   1 
ATOM   14242 C  CD2   . TRP A 1 3532 ? 233.660 234.018 180.336 1.00 35.28  ? 3532 TRP A CD2   1 
ATOM   14243 N  NE1   . TRP A 1 3532 ? 234.694 232.624 181.747 1.00 38.08  ? 3532 TRP A NE1   1 
ATOM   14244 C  CE2   . TRP A 1 3532 ? 233.509 233.270 181.517 1.00 39.15  ? 3532 TRP A CE2   1 
ATOM   14245 C  CE3   . TRP A 1 3532 ? 232.583 234.780 179.878 1.00 34.55  ? 3532 TRP A CE3   1 
ATOM   14246 C  CZ2   . TRP A 1 3532 ? 232.325 233.259 182.244 1.00 38.59  ? 3532 TRP A CZ2   1 
ATOM   14247 C  CZ3   . TRP A 1 3532 ? 231.411 234.769 180.602 1.00 38.15  ? 3532 TRP A CZ3   1 
ATOM   14248 C  CH2   . TRP A 1 3532 ? 231.290 234.013 181.771 1.00 36.88  ? 3532 TRP A CH2   1 
ATOM   14249 N  N     . SER A 1 3533 ? 237.556 236.516 177.312 1.00 45.98  ? 3533 SER A N     1 
ATOM   14250 C  CA    . SER A 1 3533 ? 238.058 237.190 176.120 1.00 47.61  ? 3533 SER A CA    1 
ATOM   14251 C  C     . SER A 1 3533 ? 239.569 237.043 176.000 1.00 46.93  ? 3533 SER A C     1 
ATOM   14252 O  O     . SER A 1 3533 ? 240.095 236.844 174.899 1.00 49.13  ? 3533 SER A O     1 
ATOM   14253 C  CB    . SER A 1 3533 ? 237.661 238.664 176.148 1.00 53.82  ? 3533 SER A CB    1 
ATOM   14254 O  OG    . SER A 1 3533 ? 236.295 238.816 176.493 1.00 56.36  ? 3533 SER A OG    1 
ATOM   14255 N  N     . HIS A 1 3534 ? 240.285 237.139 177.122 1.00 52.90  ? 3534 HIS A N     1 
ATOM   14256 C  CA    . HIS A 1 3534 ? 241.730 236.952 177.092 1.00 57.93  ? 3534 HIS A CA    1 
ATOM   14257 C  C     . HIS A 1 3534 ? 242.094 235.536 176.666 1.00 59.62  ? 3534 HIS A C     1 
ATOM   14258 O  O     . HIS A 1 3534 ? 243.034 235.337 175.887 1.00 64.48  ? 3534 HIS A O     1 
ATOM   14259 C  CB    . HIS A 1 3534 ? 242.333 237.272 178.458 1.00 55.92  ? 3534 HIS A CB    1 
ATOM   14260 C  CG    . HIS A 1 3534 ? 243.823 237.140 178.502 1.00 62.03  ? 3534 HIS A CG    1 
ATOM   14261 N  ND1   . HIS A 1 3534 ? 244.668 238.058 177.918 1.00 64.88  ? 3534 HIS A ND1   1 
ATOM   14262 C  CD2   . HIS A 1 3534 ? 244.619 236.198 179.060 1.00 60.85  ? 3534 HIS A CD2   1 
ATOM   14263 C  CE1   . HIS A 1 3534 ? 245.921 237.687 178.113 1.00 64.45  ? 3534 HIS A CE1   1 
ATOM   14264 N  NE2   . HIS A 1 3534 ? 245.919 236.562 178.804 1.00 63.33  ? 3534 HIS A NE2   1 
ATOM   14265 N  N     . HIS A 1 3535 ? 241.366 234.536 177.170 1.00 58.21  ? 3535 HIS A N     1 
ATOM   14266 C  CA    . HIS A 1 3535 ? 241.637 233.167 176.738 1.00 50.37  ? 3535 HIS A CA    1 
ATOM   14267 C  C     . HIS A 1 3535 ? 241.359 232.988 175.252 1.00 49.79  ? 3535 HIS A C     1 
ATOM   14268 O  O     . HIS A 1 3535 ? 242.132 232.328 174.548 1.00 60.18  ? 3535 HIS A O     1 
ATOM   14269 C  CB    . HIS A 1 3535 ? 240.817 232.169 177.547 1.00 48.56  ? 3535 HIS A CB    1 
ATOM   14270 C  CG    . HIS A 1 3535 ? 241.109 230.741 177.204 1.00 53.35  ? 3535 HIS A CG    1 
ATOM   14271 N  ND1   . HIS A 1 3535 ? 240.588 230.121 176.089 1.00 55.39  ? 3535 HIS A ND1   1 
ATOM   14272 C  CD2   . HIS A 1 3535 ? 241.883 229.816 177.820 1.00 54.09  ? 3535 HIS A CD2   1 
ATOM   14273 C  CE1   . HIS A 1 3535 ? 241.019 228.874 176.038 1.00 53.72  ? 3535 HIS A CE1   1 
ATOM   14274 N  NE2   . HIS A 1 3535 ? 241.807 228.663 177.077 1.00 55.98  ? 3535 HIS A NE2   1 
ATOM   14275 N  N     . LEU A 1 3536 ? 240.256 233.553 174.758 1.00 50.25  ? 3536 LEU A N     1 
ATOM   14276 C  CA    . LEU A 1 3536 ? 239.954 233.444 173.334 1.00 51.24  ? 3536 LEU A CA    1 
ATOM   14277 C  C     . LEU A 1 3536 ? 241.023 234.131 172.496 1.00 57.88  ? 3536 LEU A C     1 
ATOM   14278 O  O     . LEU A 1 3536 ? 241.342 233.682 171.390 1.00 62.11  ? 3536 LEU A O     1 
ATOM   14279 C  CB    . LEU A 1 3536 ? 238.577 234.033 173.035 1.00 55.43  ? 3536 LEU A CB    1 
ATOM   14280 C  CG    . LEU A 1 3536 ? 237.347 233.307 173.583 1.00 50.89  ? 3536 LEU A CG    1 
ATOM   14281 C  CD1   . LEU A 1 3536 ? 236.120 233.664 172.763 1.00 54.56  ? 3536 LEU A CD1   1 
ATOM   14282 C  CD2   . LEU A 1 3536 ? 237.561 231.809 173.599 1.00 50.66  ? 3536 LEU A CD2   1 
ATOM   14283 N  N     . GLN A 1 3537 ? 241.577 235.234 173.003 1.00 64.58  ? 3537 GLN A N     1 
ATOM   14284 C  CA    . GLN A 1 3537 ? 242.696 235.882 172.328 1.00 64.39  ? 3537 GLN A CA    1 
ATOM   14285 C  C     . GLN A 1 3537 ? 243.922 234.980 172.310 1.00 62.72  ? 3537 GLN A C     1 
ATOM   14286 O  O     . GLN A 1 3537 ? 244.633 234.906 171.301 1.00 66.47  ? 3537 GLN A O     1 
ATOM   14287 C  CB    . GLN A 1 3537 ? 243.020 237.209 173.011 1.00 63.27  ? 3537 GLN A CB    1 
ATOM   14288 C  CG    . GLN A 1 3537 ? 244.123 238.002 172.338 1.00 63.51  ? 3537 GLN A CG    1 
ATOM   14289 C  CD    . GLN A 1 3537 ? 244.119 239.458 172.750 1.00 67.54  ? 3537 GLN A CD    1 
ATOM   14290 O  OE1   . GLN A 1 3537 ? 243.249 239.898 173.500 1.00 67.21  ? 3537 GLN A OE1   1 
ATOM   14291 N  NE2   . GLN A 1 3537 ? 245.095 240.214 172.261 1.00 66.13  ? 3537 GLN A NE2   1 
ATOM   14292 N  N     . GLN A 1 3538 ? 244.188 234.290 173.421 1.00 60.70  ? 3538 GLN A N     1 
ATOM   14293 C  CA    . GLN A 1 3538 ? 245.346 233.404 173.485 1.00 60.68  ? 3538 GLN A CA    1 
ATOM   14294 C  C     . GLN A 1 3538 ? 245.240 232.257 172.488 1.00 67.73  ? 3538 GLN A C     1 
ATOM   14295 O  O     . GLN A 1 3538 ? 246.245 231.872 171.881 1.00 71.92  ? 3538 GLN A O     1 
ATOM   14296 C  CB    . GLN A 1 3538 ? 245.508 232.852 174.899 1.00 62.78  ? 3538 GLN A CB    1 
ATOM   14297 C  CG    . GLN A 1 3538 ? 246.012 233.857 175.914 1.00 66.89  ? 3538 GLN A CG    1 
ATOM   14298 C  CD    . GLN A 1 3538 ? 246.767 233.196 177.049 1.00 70.86  ? 3538 GLN A CD    1 
ATOM   14299 O  OE1   . GLN A 1 3538 ? 247.460 232.200 176.849 1.00 72.55  ? 3538 GLN A OE1   1 
ATOM   14300 N  NE2   . GLN A 1 3538 ? 246.633 233.745 178.249 1.00 68.72  ? 3538 GLN A NE2   1 
ATOM   14301 N  N     . ALA A 1 3539 ? 244.044 231.703 172.304 1.00 68.45  ? 3539 ALA A N     1 
ATOM   14302 C  CA    . ALA A 1 3539 ? 243.832 230.563 171.424 1.00 65.62  ? 3539 ALA A CA    1 
ATOM   14303 C  C     . ALA A 1 3539 ? 243.549 230.969 169.984 1.00 65.11  ? 3539 ALA A C     1 
ATOM   14304 O  O     . ALA A 1 3539 ? 243.146 230.118 169.185 1.00 69.33  ? 3539 ALA A O     1 
ATOM   14305 C  CB    . ALA A 1 3539 ? 242.687 229.697 171.951 1.00 67.75  ? 3539 ALA A CB    1 
ATOM   14306 N  N     . ASN A 1 3540 ? 243.749 232.242 169.640 1.00 64.56  ? 3540 ASN A N     1 
ATOM   14307 C  CA    . ASN A 1 3540 ? 243.555 232.741 168.277 1.00 68.55  ? 3540 ASN A CA    1 
ATOM   14308 C  C     . ASN A 1 3540 ? 242.149 232.446 167.760 1.00 73.24  ? 3540 ASN A C     1 
ATOM   14309 O  O     . ASN A 1 3540 ? 241.965 232.002 166.625 1.00 74.13  ? 3540 ASN A O     1 
ATOM   14310 C  CB    . ASN A 1 3540 ? 244.611 232.179 167.325 1.00 68.72  ? 3540 ASN A CB    1 
ATOM   14311 C  CG    . ASN A 1 3540 ? 245.885 232.995 167.327 1.00 76.78  ? 3540 ASN A CG    1 
ATOM   14312 O  OD1   . ASN A 1 3540 ? 245.925 234.103 167.862 1.00 75.35  ? 3540 ASN A OD1   1 
ATOM   14313 N  ND2   . ASN A 1 3540 ? 246.937 232.453 166.724 1.00 75.28  ? 3540 ASN A ND2   1 
ATOM   14314 N  N     . ILE A 1 3541 ? 241.148 232.693 168.599 1.00 65.52  ? 3541 ILE A N     1 
ATOM   14315 C  CA    . ILE A 1 3541 ? 239.747 232.598 168.211 1.00 65.58  ? 3541 ILE A CA    1 
ATOM   14316 C  C     . ILE A 1 3541 ? 239.218 234.017 168.066 1.00 67.98  ? 3541 ILE A C     1 
ATOM   14317 O  O     . ILE A 1 3541 ? 239.202 234.784 169.036 1.00 66.94  ? 3541 ILE A O     1 
ATOM   14318 C  CB    . ILE A 1 3541 ? 238.926 231.795 169.231 1.00 65.52  ? 3541 ILE A CB    1 
ATOM   14319 C  CG1   . ILE A 1 3541 ? 239.387 230.337 169.247 1.00 62.92  ? 3541 ILE A CG1   1 
ATOM   14320 C  CG2   . ILE A 1 3541 ? 237.445 231.878 168.908 1.00 61.71  ? 3541 ILE A CG2   1 
ATOM   14321 C  CD1   . ILE A 1 3541 ? 238.733 229.506 170.318 1.00 64.76  ? 3541 ILE A CD1   1 
ATOM   14322 N  N     . GLN A 1 3542 ? 238.794 234.367 166.856 1.00 71.43  ? 3542 GLN A N     1 
ATOM   14323 C  CA    . GLN A 1 3542 ? 238.415 235.738 166.549 1.00 67.56  ? 3542 GLN A CA    1 
ATOM   14324 C  C     . GLN A 1 3542 ? 237.083 236.099 167.191 1.00 68.05  ? 3542 GLN A C     1 
ATOM   14325 O  O     . GLN A 1 3542 ? 236.156 235.285 167.239 1.00 70.87  ? 3542 GLN A O     1 
ATOM   14326 C  CB    . GLN A 1 3542 ? 238.330 235.937 165.036 1.00 68.85  ? 3542 GLN A CB    1 
ATOM   14327 C  CG    . GLN A 1 3542 ? 239.641 235.713 164.302 1.00 70.70  ? 3542 GLN A CG    1 
ATOM   14328 C  CD    . GLN A 1 3542 ? 240.740 236.638 164.779 1.00 72.17  ? 3542 GLN A CD    1 
ATOM   14329 O  OE1   . GLN A 1 3542 ? 240.725 237.836 164.497 1.00 70.37  ? 3542 GLN A OE1   1 
ATOM   14330 N  NE2   . GLN A 1 3542 ? 241.705 236.085 165.503 1.00 68.79  ? 3542 GLN A NE2   1 
ATOM   14331 N  N     . PHE A 1 3543 ? 236.999 237.330 167.689 1.00 68.85  ? 3543 PHE A N     1 
ATOM   14332 C  CA    . PHE A 1 3543 ? 235.752 237.905 168.177 1.00 62.69  ? 3543 PHE A CA    1 
ATOM   14333 C  C     . PHE A 1 3543 ? 235.899 239.418 168.169 1.00 66.78  ? 3543 PHE A C     1 
ATOM   14334 O  O     . PHE A 1 3543 ? 237.013 239.949 168.173 1.00 70.58  ? 3543 PHE A O     1 
ATOM   14335 C  CB    . PHE A 1 3543 ? 235.392 237.393 169.576 1.00 59.80  ? 3543 PHE A CB    1 
ATOM   14336 C  CG    . PHE A 1 3543 ? 236.399 237.745 170.630 1.00 62.57  ? 3543 PHE A CG    1 
ATOM   14337 C  CD1   . PHE A 1 3543 ? 237.552 236.997 170.784 1.00 61.10  ? 3543 PHE A CD1   1 
ATOM   14338 C  CD2   . PHE A 1 3543 ? 236.187 238.819 171.474 1.00 64.30  ? 3543 PHE A CD2   1 
ATOM   14339 C  CE1   . PHE A 1 3543 ? 238.476 237.318 171.752 1.00 62.48  ? 3543 PHE A CE1   1 
ATOM   14340 C  CE2   . PHE A 1 3543 ? 237.110 239.144 172.446 1.00 62.74  ? 3543 PHE A CE2   1 
ATOM   14341 C  CZ    . PHE A 1 3543 ? 238.255 238.392 172.584 1.00 63.06  ? 3543 PHE A CZ    1 
ATOM   14342 N  N     . ARG A 1 3544 ? 234.763 240.110 168.154 1.00 73.98  ? 3544 ARG A N     1 
ATOM   14343 C  CA    . ARG A 1 3544 ? 234.750 241.567 168.062 1.00 73.57  ? 3544 ARG A CA    1 
ATOM   14344 C  C     . ARG A 1 3544 ? 234.775 242.158 169.466 1.00 78.50  ? 3544 ARG A C     1 
ATOM   14345 O  O     . ARG A 1 3544 ? 233.967 241.784 170.322 1.00 83.30  ? 3544 ARG A O     1 
ATOM   14346 C  CB    . ARG A 1 3544 ? 233.533 242.054 167.281 1.00 71.77  ? 3544 ARG A CB    1 
ATOM   14347 C  CG    . ARG A 1 3544 ? 233.553 241.656 165.818 1.00 77.88  ? 3544 ARG A CG    1 
ATOM   14348 C  CD    . ARG A 1 3544 ? 232.321 242.145 165.082 1.00 80.12  ? 3544 ARG A CD    1 
ATOM   14349 N  NE    . ARG A 1 3544 ? 232.297 243.600 165.003 1.00 84.03  ? 3544 ARG A NE    1 
ATOM   14350 C  CZ    . ARG A 1 3544 ? 231.271 244.313 164.559 1.00 82.11  ? 3544 ARG A CZ    1 
ATOM   14351 N  NH1   . ARG A 1 3544 ? 230.159 243.736 164.135 1.00 79.15  ? 3544 ARG A NH1   1 
ATOM   14352 N  NH2   . ARG A 1 3544 ? 231.366 245.640 164.532 1.00 78.71  ? 3544 ARG A NH2   1 
ATOM   14353 N  N     . THR A 1 3545 ? 235.699 243.092 169.697 1.00 87.19  ? 3545 THR A N     1 
ATOM   14354 C  CA    . THR A 1 3545 ? 235.840 243.705 171.013 1.00 89.77  ? 3545 THR A CA    1 
ATOM   14355 C  C     . THR A 1 3545 ? 234.980 244.954 171.160 1.00 86.58  ? 3545 THR A C     1 
ATOM   14356 O  O     . THR A 1 3545 ? 234.609 245.318 172.281 1.00 82.46  ? 3545 THR A O     1 
ATOM   14357 C  CB    . THR A 1 3545 ? 237.310 244.050 171.271 1.00 87.72  ? 3545 THR A CB    1 
ATOM   14358 O  OG1   . THR A 1 3545 ? 238.139 242.957 170.856 1.00 83.19  ? 3545 THR A OG1   1 
ATOM   14359 C  CG2   . THR A 1 3545 ? 237.551 244.317 172.749 1.00 84.53  ? 3545 THR A CG2   1 
ATOM   14360 N  N     . ASP A 1 3546 ? 234.652 245.616 170.048 1.00 87.42  ? 3546 ASP A N     1 
ATOM   14361 C  CA    . ASP A 1 3546 ? 233.932 246.884 170.122 1.00 87.34  ? 3546 ASP A CA    1 
ATOM   14362 C  C     . ASP A 1 3546 ? 232.512 246.702 170.646 1.00 89.46  ? 3546 ASP A C     1 
ATOM   14363 O  O     . ASP A 1 3546 ? 232.044 247.499 171.467 1.00 90.29  ? 3546 ASP A O     1 
ATOM   14364 C  CB    . ASP A 1 3546 ? 233.911 247.552 168.748 1.00 87.18  ? 3546 ASP A CB    1 
ATOM   14365 C  CG    . ASP A 1 3546 ? 233.407 246.627 167.658 1.00 88.05  ? 3546 ASP A CG    1 
ATOM   14366 O  OD1   . ASP A 1 3546 ? 233.215 245.426 167.938 1.00 89.49  ? 3546 ASP A OD1   1 
ATOM   14367 O  OD2   . ASP A 1 3546 ? 233.201 247.101 166.521 1.00 84.75  ? 3546 ASP A OD2   1 
ATOM   14368 N  N     . ILE A 1 3547 ? 231.811 245.664 170.184 1.00 79.68  ? 3547 ILE A N     1 
ATOM   14369 C  CA    . ILE A 1 3547 ? 230.390 245.537 170.477 1.00 79.46  ? 3547 ILE A CA    1 
ATOM   14370 C  C     . ILE A 1 3547 ? 230.177 245.236 171.957 1.00 79.63  ? 3547 ILE A C     1 
ATOM   14371 O  O     . ILE A 1 3547 ? 231.052 244.689 172.643 1.00 74.29  ? 3547 ILE A O     1 
ATOM   14372 C  CB    . ILE A 1 3547 ? 229.746 244.456 169.588 1.00 80.69  ? 3547 ILE A CB    1 
ATOM   14373 C  CG1   . ILE A 1 3547 ? 228.248 244.728 169.422 1.00 79.33  ? 3547 ILE A CG1   1 
ATOM   14374 C  CG2   . ILE A 1 3547 ? 229.986 243.067 170.163 1.00 76.24  ? 3547 ILE A CG2   1 
ATOM   14375 C  CD1   . ILE A 1 3547 ? 227.609 243.977 168.277 1.00 76.59  ? 3547 ILE A CD1   1 
ATOM   14376 N  N     . ALA A 1 3548 ? 229.005 245.614 172.457 1.00 71.94  ? 3548 ALA A N     1 
ATOM   14377 C  CA    . ALA A 1 3548 ? 228.604 245.366 173.831 1.00 69.13  ? 3548 ALA A CA    1 
ATOM   14378 C  C     . ALA A 1 3548 ? 227.675 244.161 173.901 1.00 64.86  ? 3548 ALA A C     1 
ATOM   14379 O  O     . ALA A 1 3548 ? 227.025 243.789 172.922 1.00 66.55  ? 3548 ALA A O     1 
ATOM   14380 C  CB    . ALA A 1 3548 ? 227.915 246.597 174.426 1.00 65.70  ? 3548 ALA A CB    1 
ATOM   14381 N  N     . ARG A 1 3549 ? 227.623 243.549 175.086 1.00 50.20  ? 3549 ARG A N     1 
ATOM   14382 C  CA    . ARG A 1 3549 ? 226.818 242.345 175.264 1.00 49.72  ? 3549 ARG A CA    1 
ATOM   14383 C  C     . ARG A 1 3549 ? 225.333 242.635 175.080 1.00 54.02  ? 3549 ARG A C     1 
ATOM   14384 O  O     . ARG A 1 3549 ? 224.618 241.862 174.432 1.00 58.61  ? 3549 ARG A O     1 
ATOM   14385 C  CB    . ARG A 1 3549 ? 227.078 241.747 176.645 1.00 48.04  ? 3549 ARG A CB    1 
ATOM   14386 C  CG    . ARG A 1 3549 ? 228.515 241.883 177.111 1.00 50.07  ? 3549 ARG A CG    1 
ATOM   14387 C  CD    . ARG A 1 3549 ? 228.768 241.052 178.350 1.00 52.68  ? 3549 ARG A CD    1 
ATOM   14388 N  NE    . ARG A 1 3549 ? 228.533 241.807 179.574 1.00 48.55  ? 3549 ARG A NE    1 
ATOM   14389 C  CZ    . ARG A 1 3549 ? 229.482 242.406 180.279 1.00 52.42  ? 3549 ARG A CZ    1 
ATOM   14390 N  NH1   . ARG A 1 3549 ? 230.749 242.369 179.902 1.00 54.67  ? 3549 ARG A NH1   1 
ATOM   14391 N  NH2   . ARG A 1 3549 ? 229.152 243.057 181.390 1.00 47.39  ? 3549 ARG A NH2   1 
ATOM   14392 N  N     . THR A 1 3550 ? 224.853 243.742 175.650 1.00 59.84  ? 3550 THR A N     1 
ATOM   14393 C  CA    . THR A 1 3550 ? 223.433 244.069 175.560 1.00 50.93  ? 3550 THR A CA    1 
ATOM   14394 C  C     . THR A 1 3550 ? 223.017 244.338 174.120 1.00 56.66  ? 3550 THR A C     1 
ATOM   14395 O  O     . THR A 1 3550 ? 221.940 243.913 173.687 1.00 59.20  ? 3550 THR A O     1 
ATOM   14396 C  CB    . THR A 1 3550 ? 223.120 245.278 176.439 1.00 55.00  ? 3550 THR A CB    1 
ATOM   14397 O  OG1   . THR A 1 3550 ? 223.965 246.372 176.064 1.00 62.39  ? 3550 THR A OG1   1 
ATOM   14398 C  CG2   . THR A 1 3550 ? 223.365 244.946 177.895 1.00 54.15  ? 3550 THR A CG2   1 
ATOM   14399 N  N     . GLU A 1 3551 ? 223.853 245.053 173.366 1.00 63.08  ? 3551 GLU A N     1 
ATOM   14400 C  CA    . GLU A 1 3551 ? 223.530 245.341 171.975 1.00 60.48  ? 3551 GLU A CA    1 
ATOM   14401 C  C     . GLU A 1 3551 ? 223.655 244.101 171.101 1.00 66.01  ? 3551 GLU A C     1 
ATOM   14402 O  O     . GLU A 1 3551 ? 222.927 243.966 170.111 1.00 70.52  ? 3551 GLU A O     1 
ATOM   14403 C  CB    . GLU A 1 3551 ? 224.432 246.461 171.453 1.00 63.73  ? 3551 GLU A CB    1 
ATOM   14404 C  CG    . GLU A 1 3551 ? 224.131 246.902 170.031 1.00 70.48  ? 3551 GLU A CG    1 
ATOM   14405 C  CD    . GLU A 1 3551 ? 225.015 248.047 169.577 1.00 74.53  ? 3551 GLU A CD    1 
ATOM   14406 O  OE1   . GLU A 1 3551 ? 225.878 248.483 170.367 1.00 71.80  ? 3551 GLU A OE1   1 
ATOM   14407 O  OE2   . GLU A 1 3551 ? 224.848 248.510 168.429 1.00 69.78  ? 3551 GLU A OE2   1 
ATOM   14408 N  N     . TYR A 1 3552 ? 224.566 243.189 171.443 1.00 59.92  ? 3552 TYR A N     1 
ATOM   14409 C  CA    . TYR A 1 3552 ? 224.752 241.988 170.637 1.00 55.47  ? 3552 TYR A CA    1 
ATOM   14410 C  C     . TYR A 1 3552 ? 223.647 240.965 170.870 1.00 51.01  ? 3552 TYR A C     1 
ATOM   14411 O  O     . TYR A 1 3552 ? 223.206 240.303 169.925 1.00 53.50  ? 3552 TYR A O     1 
ATOM   14412 C  CB    . TYR A 1 3552 ? 226.115 241.362 170.928 1.00 56.18  ? 3552 TYR A CB    1 
ATOM   14413 C  CG    . TYR A 1 3552 ? 226.463 240.233 169.990 1.00 54.42  ? 3552 TYR A CG    1 
ATOM   14414 C  CD1   . TYR A 1 3552 ? 226.577 240.452 168.627 1.00 57.71  ? 3552 TYR A CD1   1 
ATOM   14415 C  CD2   . TYR A 1 3552 ? 226.668 238.947 170.466 1.00 54.27  ? 3552 TYR A CD2   1 
ATOM   14416 C  CE1   . TYR A 1 3552 ? 226.890 239.424 167.764 1.00 57.68  ? 3552 TYR A CE1   1 
ATOM   14417 C  CE2   . TYR A 1 3552 ? 226.980 237.913 169.611 1.00 56.27  ? 3552 TYR A CE2   1 
ATOM   14418 C  CZ    . TYR A 1 3552 ? 227.090 238.157 168.261 1.00 59.89  ? 3552 TYR A CZ    1 
ATOM   14419 O  OH    . TYR A 1 3552 ? 227.403 237.132 167.402 1.00 62.67  ? 3552 TYR A OH    1 
ATOM   14420 N  N     . LEU A 1 3553 ? 223.188 240.821 172.109 1.00 51.38  ? 3553 LEU A N     1 
ATOM   14421 C  CA    . LEU A 1 3553 ? 222.208 239.799 172.449 1.00 50.55  ? 3553 LEU A CA    1 
ATOM   14422 C  C     . LEU A 1 3553 ? 220.769 240.287 172.368 1.00 53.77  ? 3553 LEU A C     1 
ATOM   14423 O  O     . LEU A 1 3553 ? 219.857 239.527 172.706 1.00 54.52  ? 3553 LEU A O     1 
ATOM   14424 C  CB    . LEU A 1 3553 ? 222.483 239.253 173.851 1.00 53.64  ? 3553 LEU A CB    1 
ATOM   14425 C  CG    . LEU A 1 3553 ? 223.669 238.298 173.955 1.00 52.25  ? 3553 LEU A CG    1 
ATOM   14426 C  CD1   . LEU A 1 3553 ? 224.046 238.060 175.406 1.00 47.96  ? 3553 LEU A CD1   1 
ATOM   14427 C  CD2   . LEU A 1 3553 ? 223.335 236.993 173.259 1.00 48.20  ? 3553 LEU A CD2   1 
ATOM   14428 N  N     . SER A 1 3554 ? 220.539 241.522 171.932 1.00 55.55  ? 3554 SER A N     1 
ATOM   14429 C  CA    . SER A 1 3554 ? 219.186 242.044 171.830 1.00 53.31  ? 3554 SER A CA    1 
ATOM   14430 C  C     . SER A 1 3554 ? 219.142 243.109 170.745 1.00 60.83  ? 3554 SER A C     1 
ATOM   14431 O  O     . SER A 1 3554 ? 220.166 243.683 170.370 1.00 63.23  ? 3554 SER A O     1 
ATOM   14432 C  CB    . SER A 1 3554 ? 218.710 242.622 173.167 1.00 53.76  ? 3554 SER A CB    1 
ATOM   14433 O  OG    . SER A 1 3554 ? 219.563 243.666 173.597 1.00 59.11  ? 3554 SER A OG    1 
ATOM   14434 N  N     . ASN A 1 3555 ? 217.940 243.367 170.244 1.00 67.92  ? 3555 ASN A N     1 
ATOM   14435 C  CA    . ASN A 1 3555 ? 217.702 244.460 169.313 1.00 63.16  ? 3555 ASN A CA    1 
ATOM   14436 C  C     . ASN A 1 3555 ? 216.952 245.577 170.026 1.00 67.48  ? 3555 ASN A C     1 
ATOM   14437 O  O     . ASN A 1 3555 ? 216.339 245.377 171.077 1.00 65.32  ? 3555 ASN A O     1 
ATOM   14438 C  CB    . ASN A 1 3555 ? 216.930 243.979 168.077 1.00 61.62  ? 3555 ASN A CB    1 
ATOM   14439 C  CG    . ASN A 1 3555 ? 215.639 243.270 168.430 1.00 62.97  ? 3555 ASN A CG    1 
ATOM   14440 O  OD1   . ASN A 1 3555 ? 215.290 243.134 169.598 1.00 64.81  ? 3555 ASN A OD1   1 
ATOM   14441 N  ND2   . ASN A 1 3555 ? 214.926 242.805 167.413 1.00 61.79  ? 3555 ASN A ND2   1 
ATOM   14442 N  N     . ALA A 1 3556 ? 217.007 246.772 169.437 1.00 69.08  ? 3556 ALA A N     1 
ATOM   14443 C  CA    . ALA A 1 3556 ? 216.512 247.953 170.135 1.00 64.75  ? 3556 ALA A CA    1 
ATOM   14444 C  C     . ALA A 1 3556 ? 214.988 247.991 170.194 1.00 63.08  ? 3556 ALA A C     1 
ATOM   14445 O  O     . ALA A 1 3556 ? 214.426 248.714 171.022 1.00 67.48  ? 3556 ALA A O     1 
ATOM   14446 C  CB    . ALA A 1 3556 ? 217.068 249.217 169.481 1.00 64.15  ? 3556 ALA A CB    1 
ATOM   14447 N  N     . ASP A 1 3557 ? 214.304 247.230 169.337 1.00 63.78  ? 3557 ASP A N     1 
ATOM   14448 C  CA    . ASP A 1 3557 ? 212.847 247.161 169.422 1.00 68.20  ? 3557 ASP A CA    1 
ATOM   14449 C  C     . ASP A 1 3557 ? 212.399 246.522 170.732 1.00 71.91  ? 3557 ASP A C     1 
ATOM   14450 O  O     . ASP A 1 3557 ? 211.562 247.078 171.454 1.00 74.69  ? 3557 ASP A O     1 
ATOM   14451 C  CB    . ASP A 1 3557 ? 212.289 246.389 168.228 1.00 70.64  ? 3557 ASP A CB    1 
ATOM   14452 C  CG    . ASP A 1 3557 ? 212.773 246.937 166.899 1.00 75.58  ? 3557 ASP A CG    1 
ATOM   14453 O  OD1   . ASP A 1 3557 ? 212.912 248.172 166.777 1.00 75.82  ? 3557 ASP A OD1   1 
ATOM   14454 O  OD2   . ASP A 1 3557 ? 213.022 246.130 165.979 1.00 71.69  ? 3557 ASP A OD2   1 
ATOM   14455 N  N     . GLU A 1 3558 ? 212.964 245.364 171.072 1.00 68.95  ? 3558 GLU A N     1 
ATOM   14456 C  CA    . GLU A 1 3558 ? 212.635 244.732 172.342 1.00 64.29  ? 3558 GLU A CA    1 
ATOM   14457 C  C     . GLU A 1 3558 ? 213.275 245.439 173.528 1.00 60.59  ? 3558 GLU A C     1 
ATOM   14458 O  O     . GLU A 1 3558 ? 212.751 245.344 174.641 1.00 65.98  ? 3558 GLU A O     1 
ATOM   14459 C  CB    . GLU A 1 3558 ? 213.033 243.255 172.313 1.00 64.81  ? 3558 GLU A CB    1 
ATOM   14460 C  CG    . GLU A 1 3558 ? 214.490 242.972 172.608 1.00 64.90  ? 3558 GLU A CG    1 
ATOM   14461 C  CD    . GLU A 1 3558 ? 214.846 241.520 172.370 1.00 69.91  ? 3558 GLU A CD    1 
ATOM   14462 O  OE1   . GLU A 1 3558 ? 213.938 240.668 172.434 1.00 71.81  ? 3558 GLU A OE1   1 
ATOM   14463 O  OE2   . GLU A 1 3558 ? 216.028 241.230 172.098 1.00 68.71  ? 3558 GLU A OE2   1 
ATOM   14464 N  N     . ARG A 1 3559 ? 214.383 246.154 173.318 1.00 61.76  ? 3559 ARG A N     1 
ATOM   14465 C  CA    . ARG A 1 3559 ? 214.916 247.007 174.375 1.00 59.91  ? 3559 ARG A CA    1 
ATOM   14466 C  C     . ARG A 1 3559 ? 213.936 248.121 174.719 1.00 61.48  ? 3559 ARG A C     1 
ATOM   14467 O  O     . ARG A 1 3559 ? 213.716 248.425 175.897 1.00 65.30  ? 3559 ARG A O     1 
ATOM   14468 C  CB    . ARG A 1 3559 ? 216.263 247.590 173.951 1.00 59.96  ? 3559 ARG A CB    1 
ATOM   14469 C  CG    . ARG A 1 3559 ? 217.462 246.794 174.428 1.00 60.75  ? 3559 ARG A CG    1 
ATOM   14470 C  CD    . ARG A 1 3559 ? 218.760 247.527 174.144 1.00 59.50  ? 3559 ARG A CD    1 
ATOM   14471 N  NE    . ARG A 1 3559 ? 219.463 246.962 172.999 1.00 63.16  ? 3559 ARG A NE    1 
ATOM   14472 C  CZ    . ARG A 1 3559 ? 219.906 247.669 171.969 1.00 68.49  ? 3559 ARG A CZ    1 
ATOM   14473 N  NH1   . ARG A 1 3559 ? 219.744 248.980 171.911 1.00 68.50  ? 3559 ARG A NH1   1 
ATOM   14474 N  NH2   . ARG A 1 3559 ? 220.530 247.046 170.974 1.00 64.26  ? 3559 ARG A NH2   1 
ATOM   14475 N  N     . LEU A 1 3560 ? 213.339 248.742 173.699 1.00 65.98  ? 3560 LEU A N     1 
ATOM   14476 C  CA    . LEU A 1 3560 ? 212.316 249.754 173.934 1.00 65.84  ? 3560 LEU A CA    1 
ATOM   14477 C  C     . LEU A 1 3560 ? 211.070 249.140 174.556 1.00 66.40  ? 3560 LEU A C     1 
ATOM   14478 O  O     . LEU A 1 3560 ? 210.419 249.761 175.404 1.00 69.52  ? 3560 LEU A O     1 
ATOM   14479 C  CB    . LEU A 1 3560 ? 211.970 250.457 172.622 1.00 70.40  ? 3560 LEU A CB    1 
ATOM   14480 C  CG    . LEU A 1 3560 ? 210.953 251.598 172.691 1.00 75.87  ? 3560 LEU A CG    1 
ATOM   14481 C  CD1   . LEU A 1 3560 ? 211.474 252.738 173.554 1.00 73.50  ? 3560 LEU A CD1   1 
ATOM   14482 C  CD2   . LEU A 1 3560 ? 210.604 252.086 171.295 1.00 70.48  ? 3560 LEU A CD2   1 
ATOM   14483 N  N     . ARG A 1 3561 ? 210.714 247.924 174.135 1.00 63.10  ? 3561 ARG A N     1 
ATOM   14484 C  CA    . ARG A 1 3561 ? 209.571 247.241 174.734 1.00 63.28  ? 3561 ARG A CA    1 
ATOM   14485 C  C     . ARG A 1 3561 ? 209.790 246.983 176.219 1.00 70.81  ? 3561 ARG A C     1 
ATOM   14486 O  O     . ARG A 1 3561 ? 208.874 247.164 177.029 1.00 68.81  ? 3561 ARG A O     1 
ATOM   14487 C  CB    . ARG A 1 3561 ? 209.301 245.927 174.005 1.00 65.40  ? 3561 ARG A CB    1 
ATOM   14488 C  CG    . ARG A 1 3561 ? 208.060 245.206 174.497 1.00 69.11  ? 3561 ARG A CG    1 
ATOM   14489 C  CD    . ARG A 1 3561 ? 207.835 243.920 173.732 1.00 70.48  ? 3561 ARG A CD    1 
ATOM   14490 N  NE    . ARG A 1 3561 ? 208.881 242.944 174.008 1.00 70.13  ? 3561 ARG A NE    1 
ATOM   14491 C  CZ    . ARG A 1 3561 ? 209.031 241.803 173.351 1.00 75.80  ? 3561 ARG A CZ    1 
ATOM   14492 N  NH1   . ARG A 1 3561 ? 208.199 241.448 172.385 1.00 75.84  ? 3561 ARG A NH1   1 
ATOM   14493 N  NH2   . ARG A 1 3561 ? 210.039 240.996 173.672 1.00 73.94  ? 3561 ARG A NH2   1 
ATOM   14494 N  N     . TRP A 1 3562 ? 210.997 246.549 176.595 1.00 67.06  ? 3562 TRP A N     1 
ATOM   14495 C  CA    . TRP A 1 3562 ? 211.297 246.314 178.004 1.00 57.51  ? 3562 TRP A CA    1 
ATOM   14496 C  C     . TRP A 1 3562 ? 211.200 247.602 178.808 1.00 61.50  ? 3562 TRP A C     1 
ATOM   14497 O  O     . TRP A 1 3562 ? 210.711 247.598 179.943 1.00 62.21  ? 3562 TRP A O     1 
ATOM   14498 C  CB    . TRP A 1 3562 ? 212.688 245.701 178.155 1.00 54.27  ? 3562 TRP A CB    1 
ATOM   14499 C  CG    . TRP A 1 3562 ? 212.835 244.349 177.540 1.00 56.97  ? 3562 TRP A CG    1 
ATOM   14500 C  CD1   . TRP A 1 3562 ? 211.847 243.440 177.312 1.00 58.94  ? 3562 TRP A CD1   1 
ATOM   14501 C  CD2   . TRP A 1 3562 ? 214.048 243.751 177.072 1.00 58.60  ? 3562 TRP A CD2   1 
ATOM   14502 N  NE1   . TRP A 1 3562 ? 212.369 242.311 176.731 1.00 60.52  ? 3562 TRP A NE1   1 
ATOM   14503 C  CE2   . TRP A 1 3562 ? 213.720 242.478 176.571 1.00 56.37  ? 3562 TRP A CE2   1 
ATOM   14504 C  CE3   . TRP A 1 3562 ? 215.381 244.169 177.026 1.00 57.38  ? 3562 TRP A CE3   1 
ATOM   14505 C  CZ2   . TRP A 1 3562 ? 214.673 241.621 176.031 1.00 55.29  ? 3562 TRP A CZ2   1 
ATOM   14506 C  CZ3   . TRP A 1 3562 ? 216.325 243.317 176.490 1.00 53.52  ? 3562 TRP A CZ3   1 
ATOM   14507 C  CH2   . TRP A 1 3562 ? 215.966 242.058 176.000 1.00 56.92  ? 3562 TRP A CH2   1 
ATOM   14508 N  N     . GLN A 1 3563 ? 211.671 248.714 178.239 1.00 61.44  ? 3563 GLN A N     1 
ATOM   14509 C  CA    . GLN A 1 3563 ? 211.583 249.995 178.931 1.00 62.74  ? 3563 GLN A CA    1 
ATOM   14510 C  C     . GLN A 1 3563 ? 210.133 250.368 179.209 1.00 65.58  ? 3563 GLN A C     1 
ATOM   14511 O  O     . GLN A 1 3563 ? 209.821 250.944 180.258 1.00 65.79  ? 3563 GLN A O     1 
ATOM   14512 C  CB    . GLN A 1 3563 ? 212.267 251.085 178.108 1.00 62.20  ? 3563 GLN A CB    1 
ATOM   14513 C  CG    . GLN A 1 3563 ? 213.764 250.894 177.945 1.00 63.95  ? 3563 GLN A CG    1 
ATOM   14514 C  CD    . GLN A 1 3563 ? 214.506 250.935 179.262 1.00 68.19  ? 3563 GLN A CD    1 
ATOM   14515 O  OE1   . GLN A 1 3563 ? 215.002 249.915 179.740 1.00 68.42  ? 3563 GLN A OE1   1 
ATOM   14516 N  NE2   . GLN A 1 3563 ? 214.588 252.117 179.858 1.00 68.54  ? 3563 GLN A NE2   1 
ATOM   14517 N  N     . ALA A 1 3564 ? 209.231 250.050 178.278 1.00 63.40  ? 3564 ALA A N     1 
ATOM   14518 C  CA    . ALA A 1 3564 ? 207.812 250.297 178.499 1.00 61.49  ? 3564 ALA A CA    1 
ATOM   14519 C  C     . ALA A 1 3564 ? 207.241 249.424 179.607 1.00 65.18  ? 3564 ALA A C     1 
ATOM   14520 O  O     . ALA A 1 3564 ? 206.216 249.782 180.196 1.00 66.09  ? 3564 ALA A O     1 
ATOM   14521 C  CB    . ALA A 1 3564 ? 207.031 250.072 177.204 1.00 59.87  ? 3564 ALA A CB    1 
ATOM   14522 N  N     . SER A 1 3565 ? 207.881 248.291 179.905 1.00 65.10  ? 3565 SER A N     1 
ATOM   14523 C  CA    . SER A 1 3565 ? 207.430 247.378 180.947 1.00 59.17  ? 3565 SER A CA    1 
ATOM   14524 C  C     . SER A 1 3565 ? 208.069 247.670 182.299 1.00 60.74  ? 3565 SER A C     1 
ATOM   14525 O  O     . SER A 1 3565 ? 208.186 246.761 183.131 1.00 64.83  ? 3565 SER A O     1 
ATOM   14526 C  CB    . SER A 1 3565 ? 207.704 245.933 180.532 1.00 61.37  ? 3565 SER A CB    1 
ATOM   14527 O  OG    . SER A 1 3565 ? 207.080 245.629 179.298 1.00 63.83  ? 3565 SER A OG    1 
ATOM   14528 N  N     . SER A 1 3566 ? 208.492 248.913 182.531 1.00 61.43  ? 3566 SER A N     1 
ATOM   14529 C  CA    . SER A 1 3566 ? 209.092 249.341 183.794 1.00 61.85  ? 3566 SER A CA    1 
ATOM   14530 C  C     . SER A 1 3566 ? 210.383 248.573 184.085 1.00 60.91  ? 3566 SER A C     1 
ATOM   14531 O  O     . SER A 1 3566 ? 210.537 247.922 185.119 1.00 64.36  ? 3566 SER A O     1 
ATOM   14532 C  CB    . SER A 1 3566 ? 208.097 249.205 184.952 1.00 65.82  ? 3566 SER A CB    1 
ATOM   14533 O  OG    . SER A 1 3566 ? 208.692 249.589 186.178 1.00 70.20  ? 3566 SER A OG    1 
ATOM   14534 N  N     . LEU A 1 3567 ? 211.318 248.663 183.143 1.00 57.73  ? 3567 LEU A N     1 
ATOM   14535 C  CA    . LEU A 1 3567 ? 212.647 248.109 183.335 1.00 58.67  ? 3567 LEU A CA    1 
ATOM   14536 C  C     . LEU A 1 3567 ? 213.665 249.233 183.403 1.00 61.31  ? 3567 LEU A C     1 
ATOM   14537 O  O     . LEU A 1 3567 ? 213.720 250.064 182.487 1.00 63.48  ? 3567 LEU A O     1 
ATOM   14538 C  CB    . LEU A 1 3567 ? 213.013 247.146 182.201 1.00 61.13  ? 3567 LEU A CB    1 
ATOM   14539 C  CG    . LEU A 1 3567 ? 214.396 246.498 182.317 1.00 57.44  ? 3567 LEU A CG    1 
ATOM   14540 C  CD1   . LEU A 1 3567 ? 214.375 245.355 183.317 1.00 52.88  ? 3567 LEU A CD1   1 
ATOM   14541 C  CD2   . LEU A 1 3567 ? 214.893 246.017 180.969 1.00 58.06  ? 3567 LEU A CD2   1 
ATOM   14542 N  N     . PRO A 1 3568 ? 214.467 249.305 184.464 1.00 63.58  ? 3568 PRO A N     1 
ATOM   14543 C  CA    . PRO A 1 3568 ? 215.502 250.343 184.536 1.00 62.48  ? 3568 PRO A CA    1 
ATOM   14544 C  C     . PRO A 1 3568 ? 216.480 250.236 183.376 1.00 64.22  ? 3568 PRO A C     1 
ATOM   14545 O  O     . PRO A 1 3568 ? 216.778 249.148 182.880 1.00 65.33  ? 3568 PRO A O     1 
ATOM   14546 C  CB    . PRO A 1 3568 ? 216.192 250.072 185.880 1.00 60.96  ? 3568 PRO A CB    1 
ATOM   14547 C  CG    . PRO A 1 3568 ? 215.686 248.739 186.340 1.00 58.89  ? 3568 PRO A CG    1 
ATOM   14548 C  CD    . PRO A 1 3568 ? 214.355 248.540 185.714 1.00 62.58  ? 3568 PRO A CD    1 
ATOM   14549 N  N     . ALA A 1 3569 ? 216.975 251.393 182.942 1.00 62.61  ? 3569 ALA A N     1 
ATOM   14550 C  CA    . ALA A 1 3569 ? 217.811 251.492 181.753 1.00 66.71  ? 3569 ALA A CA    1 
ATOM   14551 C  C     . ALA A 1 3569 ? 219.271 251.139 182.008 1.00 69.98  ? 3569 ALA A C     1 
ATOM   14552 O  O     . ALA A 1 3569 ? 220.125 251.478 181.182 1.00 68.75  ? 3569 ALA A O     1 
ATOM   14553 C  CB    . ALA A 1 3569 ? 217.717 252.903 181.165 1.00 63.06  ? 3569 ALA A CB    1 
ATOM   14554 N  N     . ASP A 1 3570 ? 219.579 250.476 183.119 1.00 60.41  ? 3570 ASP A N     1 
ATOM   14555 C  CA    . ASP A 1 3570 ? 220.946 250.061 183.391 1.00 56.49  ? 3570 ASP A CA    1 
ATOM   14556 C  C     . ASP A 1 3570 ? 221.379 248.960 182.429 1.00 55.07  ? 3570 ASP A C     1 
ATOM   14557 O  O     . ASP A 1 3570 ? 220.564 248.176 181.938 1.00 58.16  ? 3570 ASP A O     1 
ATOM   14558 C  CB    . ASP A 1 3570 ? 221.077 249.575 184.834 1.00 50.91  ? 3570 ASP A CB    1 
ATOM   14559 C  CG    . ASP A 1 3570 ? 222.519 249.395 185.261 1.00 57.83  ? 3570 ASP A CG    1 
ATOM   14560 O  OD1   . ASP A 1 3570 ? 223.410 249.996 184.626 1.00 58.67  ? 3570 ASP A OD1   1 
ATOM   14561 O  OD2   . ASP A 1 3570 ? 222.764 248.652 186.234 1.00 57.62  ? 3570 ASP A OD2   1 
ATOM   14562 N  N     . ASP A 1 3571 ? 222.685 248.917 182.152 1.00 49.47  ? 3571 ASP A N     1 
ATOM   14563 C  CA    . ASP A 1 3571 ? 223.230 247.842 181.329 1.00 44.82  ? 3571 ASP A CA    1 
ATOM   14564 C  C     . ASP A 1 3571 ? 223.088 246.493 182.020 1.00 46.35  ? 3571 ASP A C     1 
ATOM   14565 O  O     . ASP A 1 3571 ? 222.800 245.483 181.368 1.00 52.06  ? 3571 ASP A O     1 
ATOM   14566 C  CB    . ASP A 1 3571 ? 224.694 248.123 180.998 1.00 50.58  ? 3571 ASP A CB    1 
ATOM   14567 C  CG    . ASP A 1 3571 ? 224.864 248.843 179.676 1.00 61.07  ? 3571 ASP A CG    1 
ATOM   14568 O  OD1   . ASP A 1 3571 ? 223.863 249.381 179.160 1.00 59.77  ? 3571 ASP A OD1   1 
ATOM   14569 O  OD2   . ASP A 1 3571 ? 225.998 248.871 179.154 1.00 61.54  ? 3571 ASP A OD2   1 
ATOM   14570 N  N     . LEU A 1 3572 ? 223.291 246.457 183.338 1.00 45.81  ? 3572 LEU A N     1 
ATOM   14571 C  CA    . LEU A 1 3572 ? 223.106 245.217 184.083 1.00 42.92  ? 3572 LEU A CA    1 
ATOM   14572 C  C     . LEU A 1 3572 ? 221.660 244.747 184.018 1.00 44.14  ? 3572 LEU A C     1 
ATOM   14573 O  O     . LEU A 1 3572 ? 221.393 243.547 183.891 1.00 55.47  ? 3572 LEU A O     1 
ATOM   14574 C  CB    . LEU A 1 3572 ? 223.550 245.407 185.534 1.00 47.92  ? 3572 LEU A CB    1 
ATOM   14575 C  CG    . LEU A 1 3572 ? 223.514 244.197 186.468 1.00 43.41  ? 3572 LEU A CG    1 
ATOM   14576 C  CD1   . LEU A 1 3572 ? 224.733 244.194 187.368 1.00 42.37  ? 3572 LEU A CD1   1 
ATOM   14577 C  CD2   . LEU A 1 3572 ? 222.246 244.197 187.306 1.00 42.65  ? 3572 LEU A CD2   1 
ATOM   14578 N  N     . CYS A 1 3573 ? 220.709 245.677 184.105 1.00 44.54  ? 3573 CYS A N     1 
ATOM   14579 C  CA    . CYS A 1 3573 ? 219.305 245.295 184.016 1.00 39.77  ? 3573 CYS A CA    1 
ATOM   14580 C  C     . CYS A 1 3573 ? 218.938 244.830 182.613 1.00 42.90  ? 3573 CYS A C     1 
ATOM   14581 O  O     . CYS A 1 3573 ? 218.108 243.929 182.461 1.00 54.07  ? 3573 CYS A O     1 
ATOM   14582 C  CB    . CYS A 1 3573 ? 218.420 246.458 184.454 1.00 46.10  ? 3573 CYS A CB    1 
ATOM   14583 S  SG    . CYS A 1 3573 ? 218.650 246.908 186.185 1.00 68.22  ? 3573 CYS A SG    1 
ATOM   14584 N  N     . THR A 1 3574 ? 219.548 245.414 181.581 1.00 39.92  ? 3574 THR A N     1 
ATOM   14585 C  CA    . THR A 1 3574 ? 219.342 244.908 180.228 1.00 37.95  ? 3574 THR A CA    1 
ATOM   14586 C  C     . THR A 1 3574 ? 219.907 243.501 180.075 1.00 45.98  ? 3574 THR A C     1 
ATOM   14587 O  O     . THR A 1 3574 ? 219.288 242.644 179.435 1.00 56.89  ? 3574 THR A O     1 
ATOM   14588 C  CB    . THR A 1 3574 ? 219.973 245.854 179.209 1.00 43.14  ? 3574 THR A CB    1 
ATOM   14589 O  OG1   . THR A 1 3574 ? 219.440 247.172 179.387 1.00 53.25  ? 3574 THR A OG1   1 
ATOM   14590 C  CG2   . THR A 1 3574 ? 219.673 245.386 177.797 1.00 45.15  ? 3574 THR A CG2   1 
ATOM   14591 N  N     . GLU A 1 3575 ? 221.080 243.242 180.659 1.00 39.25  ? 3575 GLU A N     1 
ATOM   14592 C  CA    . GLU A 1 3575 ? 221.628 241.889 180.651 1.00 31.28  ? 3575 GLU A CA    1 
ATOM   14593 C  C     . GLU A 1 3575 ? 220.699 240.917 181.365 1.00 38.58  ? 3575 GLU A C     1 
ATOM   14594 O  O     . GLU A 1 3575 ? 220.492 239.788 180.906 1.00 51.47  ? 3575 GLU A O     1 
ATOM   14595 C  CB    . GLU A 1 3575 ? 223.008 241.878 181.305 1.00 36.51  ? 3575 GLU A CB    1 
ATOM   14596 C  CG    . GLU A 1 3575 ? 224.081 242.604 180.520 1.00 46.78  ? 3575 GLU A CG    1 
ATOM   14597 C  CD    . GLU A 1 3575 ? 225.324 242.873 181.344 1.00 52.20  ? 3575 GLU A CD    1 
ATOM   14598 O  OE1   . GLU A 1 3575 ? 225.321 242.554 182.551 1.00 46.61  ? 3575 GLU A OE1   1 
ATOM   14599 O  OE2   . GLU A 1 3575 ? 226.305 243.404 180.784 1.00 52.15  ? 3575 GLU A OE2   1 
ATOM   14600 N  N     . ASN A 1 3576 ? 220.134 241.340 182.495 1.00 41.01  ? 3576 ASN A N     1 
ATOM   14601 C  CA    . ASN A 1 3576 ? 219.207 240.488 183.230 1.00 33.37  ? 3576 ASN A CA    1 
ATOM   14602 C  C     . ASN A 1 3576 ? 217.941 240.221 182.427 1.00 37.77  ? 3576 ASN A C     1 
ATOM   14603 O  O     . ASN A 1 3576 ? 217.392 239.117 182.472 1.00 47.65  ? 3576 ASN A O     1 
ATOM   14604 C  CB    . ASN A 1 3576 ? 218.871 241.123 184.576 1.00 34.35  ? 3576 ASN A CB    1 
ATOM   14605 C  CG    . ASN A 1 3576 ? 220.051 241.138 185.518 1.00 39.20  ? 3576 ASN A CG    1 
ATOM   14606 O  OD1   . ASN A 1 3576 ? 221.123 240.632 185.193 1.00 42.28  ? 3576 ASN A OD1   1 
ATOM   14607 N  ND2   . ASN A 1 3576 ? 219.864 241.724 186.691 1.00 43.87  ? 3576 ASN A ND2   1 
ATOM   14608 N  N     . ALA A 1 3577 ? 217.454 241.223 181.695 1.00 33.27  ? 3577 ALA A N     1 
ATOM   14609 C  CA    . ALA A 1 3577 ? 216.299 241.011 180.827 1.00 29.38  ? 3577 ALA A CA    1 
ATOM   14610 C  C     . ALA A 1 3577 ? 216.625 240.036 179.702 1.00 38.93  ? 3577 ALA A C     1 
ATOM   14611 O  O     . ALA A 1 3577 ? 215.798 239.187 179.346 1.00 48.63  ? 3577 ALA A O     1 
ATOM   14612 C  CB    . ALA A 1 3577 ? 215.815 242.344 180.263 1.00 41.57  ? 3577 ALA A CB    1 
ATOM   14613 N  N     . ILE A 1 3578 ? 217.826 240.144 179.131 1.00 41.70  ? 3578 ILE A N     1 
ATOM   14614 C  CA    . ILE A 1 3578 ? 218.262 239.192 178.112 1.00 39.37  ? 3578 ILE A CA    1 
ATOM   14615 C  C     . ILE A 1 3578 ? 218.287 237.781 178.682 1.00 43.13  ? 3578 ILE A C     1 
ATOM   14616 O  O     . ILE A 1 3578 ? 217.859 236.821 178.031 1.00 58.40  ? 3578 ILE A O     1 
ATOM   14617 C  CB    . ILE A 1 3578 ? 219.639 239.599 177.557 1.00 37.27  ? 3578 ILE A CB    1 
ATOM   14618 C  CG1   . ILE A 1 3578 ? 219.541 240.920 176.796 1.00 41.14  ? 3578 ILE A CG1   1 
ATOM   14619 C  CG2   . ILE A 1 3578 ? 220.203 238.504 176.671 1.00 41.16  ? 3578 ILE A CG2   1 
ATOM   14620 C  CD1   . ILE A 1 3578 ? 220.874 241.454 176.342 1.00 40.67  ? 3578 ILE A CD1   1 
ATOM   14621 N  N     . MET A 1 3579 ? 218.797 237.635 179.905 1.00 33.06  ? 3579 MET A N     1 
ATOM   14622 C  CA    . MET A 1 3579 ? 218.809 236.332 180.562 1.00 27.18  ? 3579 MET A CA    1 
ATOM   14623 C  C     . MET A 1 3579 ? 217.394 235.818 180.793 1.00 32.25  ? 3579 MET A C     1 
ATOM   14624 O  O     . MET A 1 3579 ? 217.115 234.632 180.587 1.00 38.84  ? 3579 MET A O     1 
ATOM   14625 C  CB    . MET A 1 3579 ? 219.564 236.435 181.883 1.00 29.05  ? 3579 MET A CB    1 
ATOM   14626 C  CG    . MET A 1 3579 ? 221.040 236.709 181.711 1.00 34.18  ? 3579 MET A CG    1 
ATOM   14627 S  SD    . MET A 1 3579 ? 221.907 236.841 183.275 1.00 47.00  ? 3579 MET A SD    1 
ATOM   14628 C  CE    . MET A 1 3579 ? 223.548 237.254 182.698 1.00 42.53  ? 3579 MET A CE    1 
ATOM   14629 N  N     . LEU A 1 3580 ? 216.490 236.698 181.224 1.00 42.01  ? 3580 LEU A N     1 
ATOM   14630 C  CA    . LEU A 1 3580 ? 215.092 236.351 181.437 1.00 36.38  ? 3580 LEU A CA    1 
ATOM   14631 C  C     . LEU A 1 3580 ? 214.355 236.055 180.141 1.00 38.59  ? 3580 LEU A C     1 
ATOM   14632 O  O     . LEU A 1 3580 ? 213.243 235.521 180.191 1.00 44.42  ? 3580 LEU A O     1 
ATOM   14633 C  CB    . LEU A 1 3580 ? 214.383 237.483 182.179 1.00 32.67  ? 3580 LEU A CB    1 
ATOM   14634 C  CG    . LEU A 1 3580 ? 214.694 237.622 183.667 1.00 37.35  ? 3580 LEU A CG    1 
ATOM   14635 C  CD1   . LEU A 1 3580 ? 214.075 238.890 184.220 1.00 40.50  ? 3580 LEU A CD1   1 
ATOM   14636 C  CD2   . LEU A 1 3580 ? 214.181 236.413 184.415 1.00 43.39  ? 3580 LEU A CD2   1 
ATOM   14637 N  N     . LYS A 1 3581 ? 214.927 236.409 178.993 1.00 39.61  ? 3581 LYS A N     1 
ATOM   14638 C  CA    . LYS A 1 3581 ? 214.352 236.045 177.704 1.00 43.68  ? 3581 LYS A CA    1 
ATOM   14639 C  C     . LYS A 1 3581 ? 214.923 234.739 177.164 1.00 46.42  ? 3581 LYS A C     1 
ATOM   14640 O  O     . LYS A 1 3581 ? 214.166 233.826 176.826 1.00 51.35  ? 3581 LYS A O     1 
ATOM   14641 C  CB    . LYS A 1 3581 ? 214.573 237.170 176.688 1.00 39.69  ? 3581 LYS A CB    1 
ATOM   14642 C  CG    . LYS A 1 3581 ? 213.972 236.888 175.324 1.00 41.73  ? 3581 LYS A CG    1 
ATOM   14643 C  CD    . LYS A 1 3581 ? 214.098 238.089 174.409 1.00 52.42  ? 3581 LYS A CD    1 
ATOM   14644 C  CE    . LYS A 1 3581 ? 215.535 238.294 173.965 1.00 53.04  ? 3581 LYS A CE    1 
ATOM   14645 N  NZ    . LYS A 1 3581 ? 215.968 237.224 173.029 1.00 52.48  ? 3581 LYS A NZ    1 
ATOM   14646 N  N     . ARG A 1 3582 ? 216.249 234.632 177.078 1.00 44.30  ? 3582 ARG A N     1 
ATOM   14647 C  CA    . ARG A 1 3582 ? 216.909 233.424 176.586 1.00 38.03  ? 3582 ARG A CA    1 
ATOM   14648 C  C     . ARG A 1 3582 ? 217.397 232.612 177.782 1.00 45.78  ? 3582 ARG A C     1 
ATOM   14649 O  O     . ARG A 1 3582 ? 218.575 232.623 178.136 1.00 57.19  ? 3582 ARG A O     1 
ATOM   14650 C  CB    . ARG A 1 3582 ? 218.063 233.782 175.658 1.00 39.83  ? 3582 ARG A CB    1 
ATOM   14651 C  CG    . ARG A 1 3582 ? 217.824 234.989 174.782 1.00 41.04  ? 3582 ARG A CG    1 
ATOM   14652 C  CD    . ARG A 1 3582 ? 219.081 235.334 174.006 1.00 46.58  ? 3582 ARG A CD    1 
ATOM   14653 N  NE    . ARG A 1 3582 ? 218.900 236.499 173.151 1.00 54.63  ? 3582 ARG A NE    1 
ATOM   14654 C  CZ    . ARG A 1 3582 ? 219.029 236.488 171.832 1.00 52.67  ? 3582 ARG A CZ    1 
ATOM   14655 N  NH1   . ARG A 1 3582 ? 219.332 235.379 171.178 1.00 45.52  ? 3582 ARG A NH1   1 
ATOM   14656 N  NH2   . ARG A 1 3582 ? 218.850 237.616 171.153 1.00 51.60  ? 3582 ARG A NH2   1 
ATOM   14657 N  N     . PHE A 1 3583 ? 216.475 231.891 178.410 1.00 38.33  ? 3583 PHE A N     1 
ATOM   14658 C  CA    . PHE A 1 3583 ? 216.809 231.028 179.534 1.00 40.52  ? 3583 PHE A CA    1 
ATOM   14659 C  C     . PHE A 1 3583 ? 216.472 229.588 179.182 1.00 45.12  ? 3583 PHE A C     1 
ATOM   14660 O  O     . PHE A 1 3583 ? 215.403 229.311 178.629 1.00 48.20  ? 3583 PHE A O     1 
ATOM   14661 C  CB    . PHE A 1 3583 ? 216.085 231.467 180.815 1.00 39.48  ? 3583 PHE A CB    1 
ATOM   14662 C  CG    . PHE A 1 3583 ? 214.585 231.393 180.736 1.00 43.22  ? 3583 PHE A CG    1 
ATOM   14663 C  CD1   . PHE A 1 3583 ? 213.912 230.213 181.007 1.00 45.95  ? 3583 PHE A CD1   1 
ATOM   14664 C  CD2   . PHE A 1 3583 ? 213.847 232.510 180.401 1.00 46.80  ? 3583 PHE A CD2   1 
ATOM   14665 C  CE1   . PHE A 1 3583 ? 212.542 230.151 180.932 1.00 44.75  ? 3583 PHE A CE1   1 
ATOM   14666 C  CE2   . PHE A 1 3583 ? 212.476 232.453 180.328 1.00 44.36  ? 3583 PHE A CE2   1 
ATOM   14667 C  CZ    . PHE A 1 3583 ? 211.824 231.273 180.592 1.00 46.27  ? 3583 PHE A CZ    1 
ATOM   14668 N  N     . ASN A 1 3584 ? 217.406 228.680 179.465 1.00 46.59  ? 3584 ASN A N     1 
ATOM   14669 C  CA    . ASN A 1 3584 ? 217.123 227.257 179.332 1.00 41.04  ? 3584 ASN A CA    1 
ATOM   14670 C  C     . ASN A 1 3584 ? 216.442 226.726 180.587 1.00 47.33  ? 3584 ASN A C     1 
ATOM   14671 O  O     . ASN A 1 3584 ? 215.312 226.232 180.533 1.00 57.68  ? 3584 ASN A O     1 
ATOM   14672 C  CB    . ASN A 1 3584 ? 218.412 226.488 179.045 1.00 36.84  ? 3584 ASN A CB    1 
ATOM   14673 C  CG    . ASN A 1 3584 ? 218.760 226.475 177.576 1.00 49.71  ? 3584 ASN A CG    1 
ATOM   14674 O  OD1   . ASN A 1 3584 ? 218.011 226.987 176.745 1.00 54.98  ? 3584 ASN A OD1   1 
ATOM   14675 N  ND2   . ASN A 1 3584 ? 219.901 225.888 177.244 1.00 49.80  ? 3584 ASN A ND2   1 
ATOM   14676 N  N     . ARG A 1 3585 ? 217.116 226.826 181.727 1.00 43.42  ? 3585 ARG A N     1 
ATOM   14677 C  CA    . ARG A 1 3585 ? 216.490 226.509 182.997 1.00 38.35  ? 3585 ARG A CA    1 
ATOM   14678 C  C     . ARG A 1 3585 ? 215.648 227.686 183.468 1.00 36.01  ? 3585 ARG A C     1 
ATOM   14679 O  O     . ARG A 1 3585 ? 215.945 228.846 183.170 1.00 42.72  ? 3585 ARG A O     1 
ATOM   14680 C  CB    . ARG A 1 3585 ? 217.544 226.159 184.046 1.00 37.23  ? 3585 ARG A CB    1 
ATOM   14681 C  CG    . ARG A 1 3585 ? 218.273 224.858 183.777 1.00 36.83  ? 3585 ARG A CG    1 
ATOM   14682 C  CD    . ARG A 1 3585 ? 219.452 224.685 184.710 1.00 35.58  ? 3585 ARG A CD    1 
ATOM   14683 N  NE    . ARG A 1 3585 ? 220.412 225.770 184.560 1.00 35.63  ? 3585 ARG A NE    1 
ATOM   14684 C  CZ    . ARG A 1 3585 ? 221.397 226.024 185.410 1.00 36.80  ? 3585 ARG A CZ    1 
ATOM   14685 N  NH1   . ARG A 1 3585 ? 221.592 225.279 186.484 1.00 38.52  ? 3585 ARG A NH1   1 
ATOM   14686 N  NH2   . ARG A 1 3585 ? 222.208 227.050 185.173 1.00 33.51  ? 3585 ARG A NH2   1 
ATOM   14687 N  N     . TYR A 1 3586 ? 214.588 227.377 184.201 1.00 42.62  ? 3586 TYR A N     1 
ATOM   14688 C  CA    . TYR A 1 3586 ? 213.666 228.410 184.645 1.00 43.07  ? 3586 TYR A CA    1 
ATOM   14689 C  C     . TYR A 1 3586 ? 214.391 229.389 185.562 1.00 44.00  ? 3586 TYR A C     1 
ATOM   14690 O  O     . TYR A 1 3586 ? 215.080 228.961 186.496 1.00 50.29  ? 3586 TYR A O     1 
ATOM   14691 C  CB    . TYR A 1 3586 ? 212.475 227.784 185.363 1.00 40.14  ? 3586 TYR A CB    1 
ATOM   14692 C  CG    . TYR A 1 3586 ? 211.601 226.965 184.445 1.00 48.24  ? 3586 TYR A CG    1 
ATOM   14693 C  CD1   . TYR A 1 3586 ? 211.042 227.528 183.308 1.00 49.67  ? 3586 TYR A CD1   1 
ATOM   14694 C  CD2   . TYR A 1 3586 ? 211.346 225.629 184.707 1.00 47.10  ? 3586 TYR A CD2   1 
ATOM   14695 C  CE1   . TYR A 1 3586 ? 210.248 226.785 182.462 1.00 47.88  ? 3586 TYR A CE1   1 
ATOM   14696 C  CE2   . TYR A 1 3586 ? 210.552 224.878 183.868 1.00 46.43  ? 3586 TYR A CE2   1 
ATOM   14697 C  CZ    . TYR A 1 3586 ? 210.006 225.462 182.747 1.00 51.08  ? 3586 TYR A CZ    1 
ATOM   14698 O  OH    . TYR A 1 3586 ? 209.213 224.717 181.905 1.00 54.47  ? 3586 TYR A OH    1 
ATOM   14699 N  N     . PRO A 1 3587 ? 214.273 230.692 185.329 1.00 38.60  ? 3587 PRO A N     1 
ATOM   14700 C  CA    . PRO A 1 3587 ? 215.101 231.647 186.070 1.00 34.45  ? 3587 PRO A CA    1 
ATOM   14701 C  C     . PRO A 1 3587 ? 214.692 231.756 187.527 1.00 34.59  ? 3587 PRO A C     1 
ATOM   14702 O  O     . PRO A 1 3587 ? 213.541 231.516 187.899 1.00 48.26  ? 3587 PRO A O     1 
ATOM   14703 C  CB    . PRO A 1 3587 ? 214.870 232.972 185.332 1.00 32.20  ? 3587 PRO A CB    1 
ATOM   14704 C  CG    . PRO A 1 3587 ? 214.103 232.624 184.087 1.00 42.63  ? 3587 PRO A CG    1 
ATOM   14705 C  CD    . PRO A 1 3587 ? 213.369 231.366 184.388 1.00 41.51  ? 3587 PRO A CD    1 
ATOM   14706 N  N     . LEU A 1 3588 ? 215.665 232.119 188.357 1.00 34.30  ? 3588 LEU A N     1 
ATOM   14707 C  CA    . LEU A 1 3588 ? 215.434 232.485 189.749 1.00 34.51  ? 3588 LEU A CA    1 
ATOM   14708 C  C     . LEU A 1 3588 ? 215.839 233.945 189.891 1.00 47.15  ? 3588 LEU A C     1 
ATOM   14709 O  O     . LEU A 1 3588 ? 217.029 234.271 189.841 1.00 52.97  ? 3588 LEU A O     1 
ATOM   14710 C  CB    . LEU A 1 3588 ? 216.222 231.588 190.702 1.00 40.36  ? 3588 LEU A CB    1 
ATOM   14711 C  CG    . LEU A 1 3588 ? 215.770 231.558 192.164 1.00 36.17  ? 3588 LEU A CG    1 
ATOM   14712 C  CD1   . LEU A 1 3588 ? 216.104 230.218 192.791 1.00 41.09  ? 3588 LEU A CD1   1 
ATOM   14713 C  CD2   . LEU A 1 3588 ? 216.405 232.681 192.962 1.00 38.72  ? 3588 LEU A CD2   1 
ATOM   14714 N  N     . ILE A 1 3589 ? 214.855 234.817 190.060 1.00 42.64  ? 3589 ILE A N     1 
ATOM   14715 C  CA    . ILE A 1 3589 ? 215.082 236.255 190.062 1.00 37.62  ? 3589 ILE A CA    1 
ATOM   14716 C  C     . ILE A 1 3589 ? 215.343 236.717 191.488 1.00 43.10  ? 3589 ILE A C     1 
ATOM   14717 O  O     . ILE A 1 3589 ? 214.577 236.402 192.404 1.00 49.94  ? 3589 ILE A O     1 
ATOM   14718 C  CB    . ILE A 1 3589 ? 213.882 236.997 189.455 1.00 37.97  ? 3589 ILE A CB    1 
ATOM   14719 C  CG1   . ILE A 1 3589 ? 213.542 236.423 188.081 1.00 40.50  ? 3589 ILE A CG1   1 
ATOM   14720 C  CG2   . ILE A 1 3589 ? 214.181 238.470 189.339 1.00 45.04  ? 3589 ILE A CG2   1 
ATOM   14721 C  CD1   . ILE A 1 3589 ? 212.145 236.755 187.616 1.00 42.91  ? 3589 ILE A CD1   1 
ATOM   14722 N  N     . ILE A 1 3590 ? 216.426 237.459 191.678 1.00 46.69  ? 3590 ILE A N     1 
ATOM   14723 C  CA    . ILE A 1 3590 ? 216.774 238.038 192.969 1.00 42.59  ? 3590 ILE A CA    1 
ATOM   14724 C  C     . ILE A 1 3590 ? 216.656 239.549 192.822 1.00 43.55  ? 3590 ILE A C     1 
ATOM   14725 O  O     . ILE A 1 3590 ? 217.519 240.195 192.218 1.00 52.27  ? 3590 ILE A O     1 
ATOM   14726 C  CB    . ILE A 1 3590 ? 218.177 237.627 193.426 1.00 43.87  ? 3590 ILE A CB    1 
ATOM   14727 C  CG1   . ILE A 1 3590 ? 218.371 236.119 193.275 1.00 44.81  ? 3590 ILE A CG1   1 
ATOM   14728 C  CG2   . ILE A 1 3590 ? 218.409 238.053 194.864 1.00 41.82  ? 3590 ILE A CG2   1 
ATOM   14729 C  CD1   . ILE A 1 3590 ? 219.758 235.647 193.634 1.00 42.68  ? 3590 ILE A CD1   1 
ATOM   14730 N  N     . ASP A 1 3591 ? 215.585 240.120 193.368 1.00 48.55  ? 3591 ASP A N     1 
ATOM   14731 C  CA    . ASP A 1 3591 ? 215.375 241.564 193.349 1.00 55.18  ? 3591 ASP A CA    1 
ATOM   14732 C  C     . ASP A 1 3591 ? 214.874 241.997 194.719 1.00 59.32  ? 3591 ASP A C     1 
ATOM   14733 O  O     . ASP A 1 3591 ? 213.765 241.598 195.127 1.00 64.15  ? 3591 ASP A O     1 
ATOM   14734 C  CB    . ASP A 1 3591 ? 214.400 241.970 192.239 1.00 53.92  ? 3591 ASP A CB    1 
ATOM   14735 C  CG    . ASP A 1 3591 ? 213.074 241.237 192.320 1.00 63.18  ? 3591 ASP A CG    1 
ATOM   14736 O  OD1   . ASP A 1 3591 ? 212.158 241.721 193.014 1.00 61.86  ? 3591 ASP A OD1   1 
ATOM   14737 O  OD2   . ASP A 1 3591 ? 212.948 240.166 191.693 1.00 68.93  ? 3591 ASP A OD2   1 
ATOM   14738 N  N     . PRO A 1 3592 ? 215.642 242.775 195.471 1.00 58.67  ? 3592 PRO A N     1 
ATOM   14739 C  CA    . PRO A 1 3592 ? 215.140 243.267 196.759 1.00 59.98  ? 3592 PRO A CA    1 
ATOM   14740 C  C     . PRO A 1 3592 ? 214.179 244.432 196.590 1.00 62.68  ? 3592 PRO A C     1 
ATOM   14741 O  O     . PRO A 1 3592 ? 213.284 244.637 197.414 1.00 65.05  ? 3592 PRO A O     1 
ATOM   14742 C  CB    . PRO A 1 3592 ? 216.417 243.688 197.493 1.00 57.20  ? 3592 PRO A CB    1 
ATOM   14743 C  CG    . PRO A 1 3592 ? 217.377 244.018 196.409 1.00 57.50  ? 3592 PRO A CG    1 
ATOM   14744 C  CD    . PRO A 1 3592 ? 217.058 243.113 195.255 1.00 51.92  ? 3592 PRO A CD    1 
ATOM   14745 N  N     . SER A 1 3593 ? 214.358 245.200 195.515 1.00 69.14  ? 3593 SER A N     1 
ATOM   14746 C  CA    . SER A 1 3593 ? 213.522 246.371 195.279 1.00 66.96  ? 3593 SER A CA    1 
ATOM   14747 C  C     . SER A 1 3593 ? 212.131 245.990 194.787 1.00 70.22  ? 3593 SER A C     1 
ATOM   14748 O  O     . SER A 1 3593 ? 211.137 246.597 195.201 1.00 74.70  ? 3593 SER A O     1 
ATOM   14749 C  CB    . SER A 1 3593 ? 214.202 247.302 194.277 1.00 64.33  ? 3593 SER A CB    1 
ATOM   14750 O  OG    . SER A 1 3593 ? 215.425 247.795 194.794 1.00 72.29  ? 3593 SER A OG    1 
ATOM   14751 N  N     . GLY A 1 3594 ? 212.039 244.996 193.908 1.00 69.39  ? 3594 GLY A N     1 
ATOM   14752 C  CA    . GLY A 1 3594 ? 210.769 244.575 193.356 1.00 68.29  ? 3594 GLY A CA    1 
ATOM   14753 C  C     . GLY A 1 3594 ? 210.478 245.047 191.949 1.00 67.82  ? 3594 GLY A C     1 
ATOM   14754 O  O     . GLY A 1 3594 ? 209.392 244.758 191.434 1.00 65.82  ? 3594 GLY A O     1 
ATOM   14755 N  N     . GLN A 1 3595 ? 211.406 245.762 191.308 1.00 67.56  ? 3595 GLN A N     1 
ATOM   14756 C  CA    . GLN A 1 3595 ? 211.175 246.199 189.935 1.00 67.22  ? 3595 GLN A CA    1 
ATOM   14757 C  C     . GLN A 1 3595 ? 211.170 245.021 188.970 1.00 70.68  ? 3595 GLN A C     1 
ATOM   14758 O  O     . GLN A 1 3595 ? 210.465 245.049 187.955 1.00 71.58  ? 3595 GLN A O     1 
ATOM   14759 C  CB    . GLN A 1 3595 ? 212.229 247.221 189.511 1.00 67.11  ? 3595 GLN A CB    1 
ATOM   14760 C  CG    . GLN A 1 3595 ? 212.128 248.564 190.208 1.00 73.03  ? 3595 GLN A CG    1 
ATOM   14761 C  CD    . GLN A 1 3595 ? 213.487 249.174 190.484 1.00 75.20  ? 3595 GLN A CD    1 
ATOM   14762 O  OE1   . GLN A 1 3595 ? 214.079 248.949 191.537 1.00 70.41  ? 3595 GLN A OE1   1 
ATOM   14763 N  NE2   . GLN A 1 3595 ? 213.989 249.952 189.532 1.00 74.86  ? 3595 GLN A NE2   1 
ATOM   14764 N  N     . ALA A 1 3596 ? 211.963 243.987 189.257 1.00 62.92  ? 3596 ALA A N     1 
ATOM   14765 C  CA    . ALA A 1 3596 ? 212.030 242.835 188.364 1.00 56.58  ? 3596 ALA A CA    1 
ATOM   14766 C  C     . ALA A 1 3596 ? 210.700 242.098 188.304 1.00 55.36  ? 3596 ALA A C     1 
ATOM   14767 O  O     . ALA A 1 3596 ? 210.281 241.644 187.234 1.00 58.80  ? 3596 ALA A O     1 
ATOM   14768 C  CB    . ALA A 1 3596 ? 213.145 241.893 188.808 1.00 58.90  ? 3596 ALA A CB    1 
ATOM   14769 N  N     . THR A 1 3597 ? 210.026 241.960 189.447 1.00 59.93  ? 3597 THR A N     1 
ATOM   14770 C  CA    . THR A 1 3597 ? 208.717 241.315 189.466 1.00 63.72  ? 3597 THR A CA    1 
ATOM   14771 C  C     . THR A 1 3597 ? 207.702 242.100 188.642 1.00 66.83  ? 3597 THR A C     1 
ATOM   14772 O  O     . THR A 1 3597 ? 206.938 241.517 187.861 1.00 66.50  ? 3597 THR A O     1 
ATOM   14773 C  CB    . THR A 1 3597 ? 208.239 241.161 190.909 1.00 66.93  ? 3597 THR A CB    1 
ATOM   14774 O  OG1   . THR A 1 3597 ? 209.059 240.199 191.584 1.00 64.15  ? 3597 THR A OG1   1 
ATOM   14775 C  CG2   . THR A 1 3597 ? 206.789 240.713 190.954 1.00 65.61  ? 3597 THR A CG2   1 
ATOM   14776 N  N     . GLU A 1 3598 ? 207.690 243.426 188.795 1.00 65.59  ? 3598 GLU A N     1 
ATOM   14777 C  CA    . GLU A 1 3598 ? 206.787 244.256 188.004 1.00 63.11  ? 3598 GLU A CA    1 
ATOM   14778 C  C     . GLU A 1 3598 ? 207.105 244.155 186.519 1.00 66.99  ? 3598 GLU A C     1 
ATOM   14779 O  O     . GLU A 1 3598 ? 206.193 244.111 185.687 1.00 71.61  ? 3598 GLU A O     1 
ATOM   14780 C  CB    . GLU A 1 3598 ? 206.864 245.709 188.470 1.00 63.19  ? 3598 GLU A CB    1 
ATOM   14781 C  CG    . GLU A 1 3598 ? 206.714 245.894 189.972 1.00 68.93  ? 3598 GLU A CG    1 
ATOM   14782 C  CD    . GLU A 1 3598 ? 207.031 247.309 190.421 1.00 74.27  ? 3598 GLU A CD    1 
ATOM   14783 O  OE1   . GLU A 1 3598 ? 207.154 248.198 189.552 1.00 72.88  ? 3598 GLU A OE1   1 
ATOM   14784 O  OE2   . GLU A 1 3598 ? 207.161 247.532 191.643 1.00 70.51  ? 3598 GLU A OE2   1 
ATOM   14785 N  N     . PHE A 1 3599 ? 208.392 244.124 186.168 1.00 60.49  ? 3599 PHE A N     1 
ATOM   14786 C  CA    . PHE A 1 3599 ? 208.779 243.994 184.768 1.00 52.25  ? 3599 PHE A CA    1 
ATOM   14787 C  C     . PHE A 1 3599 ? 208.324 242.660 184.190 1.00 57.44  ? 3599 PHE A C     1 
ATOM   14788 O  O     . PHE A 1 3599 ? 207.817 242.604 183.063 1.00 63.36  ? 3599 PHE A O     1 
ATOM   14789 C  CB    . PHE A 1 3599 ? 210.292 244.157 184.634 1.00 55.87  ? 3599 PHE A CB    1 
ATOM   14790 C  CG    . PHE A 1 3599 ? 210.859 243.579 183.372 1.00 56.26  ? 3599 PHE A CG    1 
ATOM   14791 C  CD1   . PHE A 1 3599 ? 210.661 244.209 182.159 1.00 58.22  ? 3599 PHE A CD1   1 
ATOM   14792 C  CD2   . PHE A 1 3599 ? 211.602 242.412 183.401 1.00 58.84  ? 3599 PHE A CD2   1 
ATOM   14793 C  CE1   . PHE A 1 3599 ? 211.188 243.685 180.999 1.00 61.01  ? 3599 PHE A CE1   1 
ATOM   14794 C  CE2   . PHE A 1 3599 ? 212.127 241.882 182.242 1.00 57.70  ? 3599 PHE A CE2   1 
ATOM   14795 C  CZ    . PHE A 1 3599 ? 211.919 242.519 181.040 1.00 56.99  ? 3599 PHE A CZ    1 
ATOM   14796 N  N     . ILE A 1 3600 ? 208.492 241.575 184.949 1.00 64.90  ? 3600 ILE A N     1 
ATOM   14797 C  CA    . ILE A 1 3600 ? 208.045 240.264 184.485 1.00 61.99  ? 3600 ILE A CA    1 
ATOM   14798 C  C     . ILE A 1 3600 ? 206.535 240.252 184.293 1.00 64.50  ? 3600 ILE A C     1 
ATOM   14799 O  O     . ILE A 1 3600 ? 206.026 239.727 183.295 1.00 67.31  ? 3600 ILE A O     1 
ATOM   14800 C  CB    . ILE A 1 3600 ? 208.501 239.163 185.460 1.00 58.39  ? 3600 ILE A CB    1 
ATOM   14801 C  CG1   . ILE A 1 3600 ? 210.010 238.952 185.358 1.00 62.48  ? 3600 ILE A CG1   1 
ATOM   14802 C  CG2   . ILE A 1 3600 ? 207.769 237.864 185.183 1.00 60.68  ? 3600 ILE A CG2   1 
ATOM   14803 C  CD1   . ILE A 1 3600 ? 210.455 238.458 184.003 1.00 59.15  ? 3600 ILE A CD1   1 
ATOM   14804 N  N     . MET A 1 3601 ? 205.795 240.829 185.242 1.00 65.90  ? 3601 MET A N     1 
ATOM   14805 C  CA    . MET A 1 3601 ? 204.341 240.857 185.118 1.00 59.64  ? 3601 MET A CA    1 
ATOM   14806 C  C     . MET A 1 3601 ? 203.890 241.690 183.927 1.00 65.46  ? 3601 MET A C     1 
ATOM   14807 O  O     . MET A 1 3601 ? 202.953 241.311 183.216 1.00 69.94  ? 3601 MET A O     1 
ATOM   14808 C  CB    . MET A 1 3601 ? 203.713 241.374 186.406 1.00 61.94  ? 3601 MET A CB    1 
ATOM   14809 C  CG    . MET A 1 3601 ? 203.852 240.396 187.531 1.00 65.51  ? 3601 MET A CG    1 
ATOM   14810 S  SD    . MET A 1 3601 ? 202.472 239.251 187.454 1.00 77.02  ? 3601 MET A SD    1 
ATOM   14811 C  CE    . MET A 1 3601 ? 202.705 238.389 188.986 1.00 69.01  ? 3601 MET A CE    1 
ATOM   14812 N  N     . ASN A 1 3602 ? 204.536 242.832 183.695 1.00 65.51  ? 3602 ASN A N     1 
ATOM   14813 C  CA    . ASN A 1 3602 ? 204.173 243.654 182.548 1.00 63.56  ? 3602 ASN A CA    1 
ATOM   14814 C  C     . ASN A 1 3602 ? 204.543 242.979 181.234 1.00 65.06  ? 3602 ASN A C     1 
ATOM   14815 O  O     . ASN A 1 3602 ? 203.871 243.194 180.220 1.00 68.61  ? 3602 ASN A O     1 
ATOM   14816 C  CB    . ASN A 1 3602 ? 204.836 245.026 182.655 1.00 63.41  ? 3602 ASN A CB    1 
ATOM   14817 C  CG    . ASN A 1 3602 ? 204.338 245.819 183.845 1.00 64.78  ? 3602 ASN A CG    1 
ATOM   14818 O  OD1   . ASN A 1 3602 ? 203.175 245.714 184.230 1.00 63.33  ? 3602 ASN A OD1   1 
ATOM   14819 N  ND2   . ASN A 1 3602 ? 205.216 246.620 184.433 1.00 65.97  ? 3602 ASN A ND2   1 
ATOM   14820 N  N     . GLU A 1 3603 ? 205.602 242.166 181.229 1.00 61.79  ? 3603 GLU A N     1 
ATOM   14821 C  CA    . GLU A 1 3603 ? 206.004 241.491 180.000 1.00 63.23  ? 3603 GLU A CA    1 
ATOM   14822 C  C     . GLU A 1 3603 ? 205.020 240.395 179.612 1.00 66.31  ? 3603 GLU A C     1 
ATOM   14823 O  O     . GLU A 1 3603 ? 204.705 240.227 178.429 1.00 65.67  ? 3603 GLU A O     1 
ATOM   14824 C  CB    . GLU A 1 3603 ? 207.408 240.914 180.151 1.00 62.66  ? 3603 GLU A CB    1 
ATOM   14825 C  CG    . GLU A 1 3603 ? 208.503 241.901 179.829 1.00 64.53  ? 3603 GLU A CG    1 
ATOM   14826 C  CD    . GLU A 1 3603 ? 208.498 242.315 178.375 1.00 70.06  ? 3603 GLU A CD    1 
ATOM   14827 O  OE1   . GLU A 1 3603 ? 208.719 241.445 177.507 1.00 66.31  ? 3603 GLU A OE1   1 
ATOM   14828 O  OE2   . GLU A 1 3603 ? 208.275 243.511 178.098 1.00 72.02  ? 3603 GLU A OE2   1 
ATOM   14829 N  N     . TYR A 1 3604 ? 204.529 239.635 180.590 1.00 70.18  ? 3604 TYR A N     1 
ATOM   14830 C  CA    . TYR A 1 3604 ? 203.638 238.512 180.337 1.00 71.25  ? 3604 TYR A CA    1 
ATOM   14831 C  C     . TYR A 1 3604 ? 202.187 238.830 180.675 1.00 71.67  ? 3604 TYR A C     1 
ATOM   14832 O  O     . TYR A 1 3604 ? 201.411 237.914 180.968 1.00 68.89  ? 3604 TYR A O     1 
ATOM   14833 C  CB    . TYR A 1 3604 ? 204.103 237.282 181.117 1.00 69.02  ? 3604 TYR A CB    1 
ATOM   14834 C  CG    . TYR A 1 3604 ? 205.396 236.685 180.613 1.00 66.72  ? 3604 TYR A CG    1 
ATOM   14835 C  CD1   . TYR A 1 3604 ? 206.621 237.206 181.002 1.00 67.54  ? 3604 TYR A CD1   1 
ATOM   14836 C  CD2   . TYR A 1 3604 ? 205.390 235.601 179.749 1.00 66.41  ? 3604 TYR A CD2   1 
ATOM   14837 C  CE1   . TYR A 1 3604 ? 207.804 236.664 180.544 1.00 66.40  ? 3604 TYR A CE1   1 
ATOM   14838 C  CE2   . TYR A 1 3604 ? 206.567 235.052 179.286 1.00 69.55  ? 3604 TYR A CE2   1 
ATOM   14839 C  CZ    . TYR A 1 3604 ? 207.771 235.587 179.686 1.00 70.76  ? 3604 TYR A CZ    1 
ATOM   14840 O  OH    . TYR A 1 3604 ? 208.946 235.041 179.226 1.00 69.85  ? 3604 TYR A OH    1 
ATOM   14841 N  N     . LYS A 1 3605 ? 201.806 240.109 180.645 1.00 75.78  ? 3605 LYS A N     1 
ATOM   14842 C  CA    . LYS A 1 3605 ? 200.427 240.477 180.947 1.00 76.03  ? 3605 LYS A CA    1 
ATOM   14843 C  C     . LYS A 1 3605 ? 199.470 239.943 179.889 1.00 75.75  ? 3605 LYS A C     1 
ATOM   14844 O  O     . LYS A 1 3605 ? 198.350 239.525 180.207 1.00 74.58  ? 3605 LYS A O     1 
ATOM   14845 C  CB    . LYS A 1 3605 ? 200.304 241.995 181.069 1.00 75.46  ? 3605 LYS A CB    1 
ATOM   14846 C  CG    . LYS A 1 3605 ? 198.895 242.486 181.357 1.00 75.61  ? 3605 LYS A CG    1 
ATOM   14847 C  CD    . LYS A 1 3605 ? 198.911 243.848 182.028 1.00 74.18  ? 3605 LYS A CD    1 
ATOM   14848 C  CE    . LYS A 1 3605 ? 199.436 243.754 183.450 1.00 76.09  ? 3605 LYS A CE    1 
ATOM   14849 N  NZ    . LYS A 1 3605 ? 200.120 245.007 183.870 1.00 77.81  ? 3605 LYS A NZ    1 
ATOM   14850 N  N     . ASP A 1 3606 ? 199.891 239.952 178.622 1.00 78.37  ? 3606 ASP A N     1 
ATOM   14851 C  CA    . ASP A 1 3606 ? 199.034 239.445 177.555 1.00 81.17  ? 3606 ASP A CA    1 
ATOM   14852 C  C     . ASP A 1 3606 ? 198.798 237.946 177.699 1.00 82.08  ? 3606 ASP A C     1 
ATOM   14853 O  O     . ASP A 1 3606 ? 197.765 237.427 177.258 1.00 81.21  ? 3606 ASP A O     1 
ATOM   14854 C  CB    . ASP A 1 3606 ? 199.644 239.766 176.190 1.00 82.17  ? 3606 ASP A CB    1 
ATOM   14855 C  CG    . ASP A 1 3606 ? 201.112 239.396 176.103 1.00 83.51  ? 3606 ASP A CG    1 
ATOM   14856 O  OD1   . ASP A 1 3606 ? 201.676 238.947 177.122 1.00 84.27  ? 3606 ASP A OD1   1 
ATOM   14857 O  OD2   . ASP A 1 3606 ? 201.702 239.556 175.014 1.00 78.40  ? 3606 ASP A OD2   1 
ATOM   14858 N  N     . ARG A 1 3607 ? 199.740 237.235 178.312 1.00 78.27  ? 3607 ARG A N     1 
ATOM   14859 C  CA    . ARG A 1 3607 ? 199.619 235.801 178.535 1.00 76.36  ? 3607 ARG A CA    1 
ATOM   14860 C  C     . ARG A 1 3607 ? 198.990 235.464 179.882 1.00 73.63  ? 3607 ARG A C     1 
ATOM   14861 O  O     . ARG A 1 3607 ? 198.932 234.285 180.246 1.00 76.05  ? 3607 ARG A O     1 
ATOM   14862 C  CB    . ARG A 1 3607 ? 200.990 235.133 178.407 1.00 77.94  ? 3607 ARG A CB    1 
ATOM   14863 C  CG    . ARG A 1 3607 ? 201.829 235.671 177.257 1.00 76.19  ? 3607 ARG A CG    1 
ATOM   14864 C  CD    . ARG A 1 3607 ? 203.023 234.779 176.972 1.00 75.97  ? 3607 ARG A CD    1 
ATOM   14865 N  NE    . ARG A 1 3607 ? 202.695 233.367 177.129 1.00 84.08  ? 3607 ARG A NE    1 
ATOM   14866 C  CZ    . ARG A 1 3607 ? 203.587 232.386 177.137 1.00 82.08  ? 3607 ARG A CZ    1 
ATOM   14867 N  NH1   . ARG A 1 3607 ? 204.880 232.624 176.985 1.00 76.10  ? 3607 ARG A NH1   1 
ATOM   14868 N  NH2   . ARG A 1 3607 ? 203.172 231.133 177.303 1.00 78.65  ? 3607 ARG A NH2   1 
ATOM   14869 N  N     . LYS A 1 3608 ? 198.529 236.471 180.627 1.00 77.40  ? 3608 LYS A N     1 
ATOM   14870 C  CA    . LYS A 1 3608 ? 197.814 236.277 181.892 1.00 80.99  ? 3608 LYS A CA    1 
ATOM   14871 C  C     . LYS A 1 3608 ? 198.685 235.568 182.929 1.00 81.83  ? 3608 LYS A C     1 
ATOM   14872 O  O     . LYS A 1 3608 ? 198.330 234.514 183.461 1.00 80.97  ? 3608 LYS A O     1 
ATOM   14873 C  CB    . LYS A 1 3608 ? 196.497 235.524 181.675 1.00 82.13  ? 3608 LYS A CB    1 
ATOM   14874 C  CG    . LYS A 1 3608 ? 195.643 236.050 180.528 1.00 83.58  ? 3608 LYS A CG    1 
ATOM   14875 C  CD    . LYS A 1 3608 ? 195.397 237.549 180.641 1.00 85.19  ? 3608 LYS A CD    1 
ATOM   14876 C  CE    . LYS A 1 3608 ? 194.591 237.893 181.885 1.00 85.32  ? 3608 LYS A CE    1 
ATOM   14877 N  NZ    . LYS A 1 3608 ? 194.413 239.364 182.038 1.00 83.35  ? 3608 LYS A NZ    1 
ATOM   14878 N  N     . ILE A 1 3609 ? 199.842 236.166 183.221 1.00 78.65  ? 3609 ILE A N     1 
ATOM   14879 C  CA    . ILE A 1 3609 ? 200.711 235.632 184.261 1.00 72.60  ? 3609 ILE A CA    1 
ATOM   14880 C  C     . ILE A 1 3609 ? 200.109 235.929 185.628 1.00 72.43  ? 3609 ILE A C     1 
ATOM   14881 O  O     . ILE A 1 3609 ? 199.594 237.026 185.880 1.00 74.82  ? 3609 ILE A O     1 
ATOM   14882 C  CB    . ILE A 1 3609 ? 202.129 236.214 184.121 1.00 71.95  ? 3609 ILE A CB    1 
ATOM   14883 C  CG1   . ILE A 1 3609 ? 203.049 235.675 185.217 1.00 73.38  ? 3609 ILE A CG1   1 
ATOM   14884 C  CG2   . ILE A 1 3609 ? 202.095 237.734 184.138 1.00 70.82  ? 3609 ILE A CG2   1 
ATOM   14885 C  CD1   . ILE A 1 3609 ? 204.490 236.096 185.062 1.00 72.25  ? 3609 ILE A CD1   1 
ATOM   14886 N  N     . THR A 1 3610 ? 200.156 234.939 186.516 1.00 75.10  ? 3610 THR A N     1 
ATOM   14887 C  CA    . THR A 1 3610 ? 199.568 235.043 187.844 1.00 79.32  ? 3610 THR A CA    1 
ATOM   14888 C  C     . THR A 1 3610 ? 200.656 234.958 188.904 1.00 76.60  ? 3610 THR A C     1 
ATOM   14889 O  O     . THR A 1 3610 ? 201.665 234.271 188.716 1.00 80.12  ? 3610 THR A O     1 
ATOM   14890 C  CB    . THR A 1 3610 ? 198.533 233.939 188.083 1.00 78.40  ? 3610 THR A CB    1 
ATOM   14891 O  OG1   . THR A 1 3610 ? 199.038 232.695 187.585 1.00 76.49  ? 3610 THR A OG1   1 
ATOM   14892 C  CG2   . THR A 1 3610 ? 197.226 234.270 187.379 1.00 76.09  ? 3610 THR A CG2   1 
ATOM   14893 N  N     . ARG A 1 3611 ? 200.448 235.657 190.015 1.00 72.26  ? 3611 ARG A N     1 
ATOM   14894 C  CA    . ARG A 1 3611 ? 201.387 235.619 191.124 1.00 72.28  ? 3611 ARG A CA    1 
ATOM   14895 C  C     . ARG A 1 3611 ? 200.965 234.579 192.150 1.00 73.31  ? 3611 ARG A C     1 
ATOM   14896 O  O     . ARG A 1 3611 ? 199.780 234.411 192.450 1.00 77.02  ? 3611 ARG A O     1 
ATOM   14897 C  CB    . ARG A 1 3611 ? 201.510 236.985 191.800 1.00 75.70  ? 3611 ARG A CB    1 
ATOM   14898 C  CG    . ARG A 1 3611 ? 202.564 237.032 192.896 1.00 77.10  ? 3611 ARG A CG    1 
ATOM   14899 C  CD    . ARG A 1 3611 ? 202.681 238.413 193.511 1.00 75.74  ? 3611 ARG A CD    1 
ATOM   14900 N  NE    . ARG A 1 3611 ? 203.151 239.395 192.542 1.00 77.79  ? 3611 ARG A NE    1 
ATOM   14901 C  CZ    . ARG A 1 3611 ? 202.422 240.400 192.076 1.00 81.82  ? 3611 ARG A CZ    1 
ATOM   14902 N  NH1   . ARG A 1 3611 ? 201.175 240.591 192.473 1.00 81.02  ? 3611 ARG A NH1   1 
ATOM   14903 N  NH2   . ARG A 1 3611 ? 202.960 241.235 191.192 1.00 78.14  ? 3611 ARG A NH2   1 
ATOM   14904 N  N     . THR A 1 3612 ? 201.958 233.879 192.687 1.00 69.27  ? 3612 THR A N     1 
ATOM   14905 C  CA    . THR A 1 3612 ? 201.745 232.861 193.699 1.00 66.92  ? 3612 THR A CA    1 
ATOM   14906 C  C     . THR A 1 3612 ? 202.967 232.892 194.607 1.00 66.07  ? 3612 THR A C     1 
ATOM   14907 O  O     . THR A 1 3612 ? 203.987 233.499 194.277 1.00 73.56  ? 3612 THR A O     1 
ATOM   14908 C  CB    . THR A 1 3612 ? 201.521 231.486 193.046 1.00 71.13  ? 3612 THR A CB    1 
ATOM   14909 O  OG1   . THR A 1 3612 ? 200.393 231.561 192.166 1.00 76.91  ? 3612 THR A OG1   1 
ATOM   14910 C  CG2   . THR A 1 3612 ? 201.222 230.414 194.078 1.00 71.52  ? 3612 THR A CG2   1 
ATOM   14911 N  N     . SER A 1 3613 ? 202.852 232.271 195.774 1.00 62.70  ? 3613 SER A N     1 
ATOM   14912 C  CA    . SER A 1 3613 ? 203.982 232.112 196.672 1.00 64.93  ? 3613 SER A CA    1 
ATOM   14913 C  C     . SER A 1 3613 ? 204.064 230.661 197.116 1.00 66.67  ? 3613 SER A C     1 
ATOM   14914 O  O     . SER A 1 3613 ? 203.057 229.950 197.158 1.00 72.18  ? 3613 SER A O     1 
ATOM   14915 C  CB    . SER A 1 3613 ? 203.872 233.027 197.894 1.00 66.69  ? 3613 SER A CB    1 
ATOM   14916 O  OG    . SER A 1 3613 ? 204.817 232.660 198.883 1.00 65.59  ? 3613 SER A OG    1 
ATOM   14917 N  N     . PHE A 1 3614 ? 205.283 230.222 197.437 1.00 65.95  ? 3614 PHE A N     1 
ATOM   14918 C  CA    . PHE A 1 3614 ? 205.455 228.875 197.967 1.00 68.51  ? 3614 PHE A CA    1 
ATOM   14919 C  C     . PHE A 1 3614 ? 204.747 228.724 199.306 1.00 68.31  ? 3614 PHE A C     1 
ATOM   14920 O  O     . PHE A 1 3614 ? 204.333 227.620 199.677 1.00 70.57  ? 3614 PHE A O     1 
ATOM   14921 C  CB    . PHE A 1 3614 ? 206.941 228.544 198.101 1.00 65.95  ? 3614 PHE A CB    1 
ATOM   14922 C  CG    . PHE A 1 3614 ? 207.598 228.146 196.808 1.00 65.24  ? 3614 PHE A CG    1 
ATOM   14923 C  CD1   . PHE A 1 3614 ? 207.148 227.054 196.093 1.00 69.77  ? 3614 PHE A CD1   1 
ATOM   14924 C  CD2   . PHE A 1 3614 ? 208.675 228.858 196.316 1.00 63.71  ? 3614 PHE A CD2   1 
ATOM   14925 C  CE1   . PHE A 1 3614 ? 207.757 226.691 194.912 1.00 70.33  ? 3614 PHE A CE1   1 
ATOM   14926 C  CE2   . PHE A 1 3614 ? 209.284 228.499 195.136 1.00 64.31  ? 3614 PHE A CE2   1 
ATOM   14927 C  CZ    . PHE A 1 3614 ? 208.824 227.416 194.433 1.00 68.28  ? 3614 PHE A CZ    1 
ATOM   14928 N  N     . LEU A 1 3615 ? 204.590 229.827 200.042 1.00 71.81  ? 3615 LEU A N     1 
ATOM   14929 C  CA    . LEU A 1 3615 ? 203.898 229.771 201.326 1.00 72.83  ? 3615 LEU A CA    1 
ATOM   14930 C  C     . LEU A 1 3615 ? 202.394 229.620 201.139 1.00 74.10  ? 3615 LEU A C     1 
ATOM   14931 O  O     . LEU A 1 3615 ? 201.718 229.004 201.971 1.00 72.46  ? 3615 LEU A O     1 
ATOM   14932 C  CB    . LEU A 1 3615 ? 204.202 231.023 202.150 1.00 69.25  ? 3615 LEU A CB    1 
ATOM   14933 C  CG    . LEU A 1 3615 ? 205.495 231.087 202.969 1.00 72.72  ? 3615 LEU A CG    1 
ATOM   14934 C  CD1   . LEU A 1 3615 ? 205.500 230.022 204.058 1.00 74.07  ? 3615 LEU A CD1   1 
ATOM   14935 C  CD2   . LEU A 1 3615 ? 206.735 230.992 202.097 1.00 72.01  ? 3615 LEU A CD2   1 
ATOM   14936 N  N     . ASP A 1 3616 ? 201.852 230.186 200.061 1.00 73.94  ? 3616 ASP A N     1 
ATOM   14937 C  CA    . ASP A 1 3616 ? 200.415 230.150 199.821 1.00 72.37  ? 3616 ASP A CA    1 
ATOM   14938 C  C     . ASP A 1 3616 ? 199.923 228.716 199.683 1.00 78.71  ? 3616 ASP A C     1 
ATOM   14939 O  O     . ASP A 1 3616 ? 200.546 227.893 199.009 1.00 80.42  ? 3616 ASP A O     1 
ATOM   14940 C  CB    . ASP A 1 3616 ? 200.077 230.947 198.561 1.00 72.08  ? 3616 ASP A CB    1 
ATOM   14941 C  CG    . ASP A 1 3616 ? 200.427 232.415 198.689 1.00 76.84  ? 3616 ASP A CG    1 
ATOM   14942 O  OD1   . ASP A 1 3616 ? 200.976 232.806 199.740 1.00 77.27  ? 3616 ASP A OD1   1 
ATOM   14943 O  OD2   . ASP A 1 3616 ? 200.155 233.179 197.740 1.00 73.46  ? 3616 ASP A OD2   1 
ATOM   14944 N  N     . ASP A 1 3617 ? 198.795 228.422 200.335 1.00 83.12  ? 3617 ASP A N     1 
ATOM   14945 C  CA    . ASP A 1 3617 ? 198.221 227.083 200.254 1.00 83.88  ? 3617 ASP A CA    1 
ATOM   14946 C  C     . ASP A 1 3617 ? 197.749 226.762 198.842 1.00 84.29  ? 3617 ASP A C     1 
ATOM   14947 O  O     . ASP A 1 3617 ? 197.844 225.609 198.405 1.00 81.10  ? 3617 ASP A O     1 
ATOM   14948 C  CB    . ASP A 1 3617 ? 197.066 226.943 201.244 1.00 82.94  ? 3617 ASP A CB    1 
ATOM   14949 C  CG    . ASP A 1 3617 ? 196.520 225.530 201.307 1.00 88.90  ? 3617 ASP A CG    1 
ATOM   14950 O  OD1   . ASP A 1 3617 ? 197.193 224.658 201.896 1.00 84.23  ? 3617 ASP A OD1   1 
ATOM   14951 O  OD2   . ASP A 1 3617 ? 195.420 225.289 200.767 1.00 89.61  ? 3617 ASP A OD2   1 
ATOM   14952 N  N     . ALA A 1 3618 ? 197.249 227.761 198.116 1.00 80.16  ? 3618 ALA A N     1 
ATOM   14953 C  CA    . ALA A 1 3618 ? 196.774 227.559 196.754 1.00 80.94  ? 3618 ALA A CA    1 
ATOM   14954 C  C     . ALA A 1 3618 ? 197.901 227.418 195.742 1.00 82.69  ? 3618 ALA A C     1 
ATOM   14955 O  O     . ALA A 1 3618 ? 197.629 227.476 194.538 1.00 85.43  ? 3618 ALA A O     1 
ATOM   14956 C  CB    . ALA A 1 3618 ? 195.858 228.714 196.344 1.00 78.78  ? 3618 ALA A CB    1 
ATOM   14957 N  N     . PHE A 1 3619 ? 199.148 227.245 196.187 1.00 73.37  ? 3619 PHE A N     1 
ATOM   14958 C  CA    . PHE A 1 3619 ? 200.257 227.117 195.248 1.00 72.57  ? 3619 PHE A CA    1 
ATOM   14959 C  C     . PHE A 1 3619 ? 200.107 225.876 194.378 1.00 76.91  ? 3619 PHE A C     1 
ATOM   14960 O  O     . PHE A 1 3619 ? 200.393 225.910 193.177 1.00 79.21  ? 3619 PHE A O     1 
ATOM   14961 C  CB    . PHE A 1 3619 ? 201.589 227.082 195.998 1.00 71.84  ? 3619 PHE A CB    1 
ATOM   14962 C  CG    . PHE A 1 3619 ? 202.743 226.643 195.145 1.00 74.48  ? 3619 PHE A CG    1 
ATOM   14963 C  CD1   . PHE A 1 3619 ? 203.112 227.374 194.029 1.00 73.15  ? 3619 PHE A CD1   1 
ATOM   14964 C  CD2   . PHE A 1 3619 ? 203.447 225.492 195.448 1.00 72.09  ? 3619 PHE A CD2   1 
ATOM   14965 C  CE1   . PHE A 1 3619 ? 204.164 226.970 193.238 1.00 72.17  ? 3619 PHE A CE1   1 
ATOM   14966 C  CE2   . PHE A 1 3619 ? 204.501 225.084 194.659 1.00 73.61  ? 3619 PHE A CE2   1 
ATOM   14967 C  CZ    . PHE A 1 3619 ? 204.858 225.823 193.551 1.00 73.67  ? 3619 PHE A CZ    1 
ATOM   14968 N  N     . ARG A 1 3620 ? 199.667 224.765 194.972 1.00 77.95  ? 3620 ARG A N     1 
ATOM   14969 C  CA    . ARG A 1 3620 ? 199.529 223.525 194.214 1.00 74.25  ? 3620 ARG A CA    1 
ATOM   14970 C  C     . ARG A 1 3620 ? 198.508 223.677 193.096 1.00 76.35  ? 3620 ARG A C     1 
ATOM   14971 O  O     . ARG A 1 3620 ? 198.753 223.269 191.954 1.00 79.92  ? 3620 ARG A O     1 
ATOM   14972 C  CB    . ARG A 1 3620 ? 199.126 222.386 195.147 1.00 75.47  ? 3620 ARG A CB    1 
ATOM   14973 C  CG    . ARG A 1 3620 ? 200.123 222.103 196.244 1.00 76.92  ? 3620 ARG A CG    1 
ATOM   14974 C  CD    . ARG A 1 3620 ? 201.406 221.526 195.691 1.00 78.47  ? 3620 ARG A CD    1 
ATOM   14975 N  NE    . ARG A 1 3620 ? 202.362 221.272 196.760 1.00 82.35  ? 3620 ARG A NE    1 
ATOM   14976 C  CZ    . ARG A 1 3620 ? 202.448 220.130 197.427 1.00 81.01  ? 3620 ARG A CZ    1 
ATOM   14977 N  NH1   . ARG A 1 3620 ? 201.672 219.100 197.137 1.00 76.24  ? 3620 ARG A NH1   1 
ATOM   14978 N  NH2   . ARG A 1 3620 ? 203.333 220.022 198.411 1.00 79.06  ? 3620 ARG A NH2   1 
ATOM   14979 N  N     . LYS A 1 3621 ? 197.352 224.267 193.408 1.00 77.42  ? 3621 LYS A N     1 
ATOM   14980 C  CA    . LYS A 1 3621 ? 196.305 224.421 192.405 1.00 77.11  ? 3621 LYS A CA    1 
ATOM   14981 C  C     . LYS A 1 3621 ? 196.744 225.359 191.290 1.00 74.30  ? 3621 LYS A C     1 
ATOM   14982 O  O     . LYS A 1 3621 ? 196.508 225.082 190.109 1.00 74.39  ? 3621 LYS A O     1 
ATOM   14983 C  CB    . LYS A 1 3621 ? 195.023 224.929 193.063 1.00 76.13  ? 3621 LYS A CB    1 
ATOM   14984 C  CG    . LYS A 1 3621 ? 194.594 224.121 194.274 1.00 75.57  ? 3621 LYS A CG    1 
ATOM   14985 C  CD    . LYS A 1 3621 ? 194.392 222.658 193.917 1.00 78.05  ? 3621 LYS A CD    1 
ATOM   14986 C  CE    . LYS A 1 3621 ? 193.185 222.466 193.016 1.00 78.27  ? 3621 LYS A CE    1 
ATOM   14987 N  NZ    . LYS A 1 3621 ? 192.986 221.035 192.661 1.00 74.96  ? 3621 LYS A NZ    1 
ATOM   14988 N  N     . ASN A 1 3622 ? 197.384 226.475 191.646 1.00 70.38  ? 3622 ASN A N     1 
ATOM   14989 C  CA    . ASN A 1 3622 ? 197.849 227.419 190.635 1.00 72.49  ? 3622 ASN A CA    1 
ATOM   14990 C  C     . ASN A 1 3622 ? 198.915 226.789 189.749 1.00 73.35  ? 3622 ASN A C     1 
ATOM   14991 O  O     . ASN A 1 3622 ? 198.913 226.972 188.527 1.00 75.83  ? 3622 ASN A O     1 
ATOM   14992 C  CB    . ASN A 1 3622 ? 198.378 228.685 191.306 1.00 74.59  ? 3622 ASN A CB    1 
ATOM   14993 C  CG    . ASN A 1 3622 ? 197.335 229.364 192.172 1.00 76.00  ? 3622 ASN A CG    1 
ATOM   14994 O  OD1   . ASN A 1 3622 ? 196.152 229.028 192.118 1.00 75.53  ? 3622 ASN A OD1   1 
ATOM   14995 N  ND2   . ASN A 1 3622 ? 197.770 230.321 192.982 1.00 71.82  ? 3622 ASN A ND2   1 
ATOM   14996 N  N     . LEU A 1 3623 ? 199.835 226.033 190.352 1.00 70.72  ? 3623 LEU A N     1 
ATOM   14997 C  CA    . LEU A 1 3623 ? 200.871 225.359 189.578 1.00 70.61  ? 3623 LEU A CA    1 
ATOM   14998 C  C     . LEU A 1 3623 ? 200.267 224.336 188.624 1.00 73.77  ? 3623 LEU A C     1 
ATOM   14999 O  O     . LEU A 1 3623 ? 200.655 224.257 187.453 1.00 74.58  ? 3623 LEU A O     1 
ATOM   15000 C  CB    . LEU A 1 3623 ? 201.872 224.692 190.523 1.00 67.21  ? 3623 LEU A CB    1 
ATOM   15001 C  CG    . LEU A 1 3623 ? 202.934 223.803 189.879 1.00 69.58  ? 3623 LEU A CG    1 
ATOM   15002 C  CD1   . LEU A 1 3623 ? 203.805 224.607 188.929 1.00 71.91  ? 3623 LEU A CD1   1 
ATOM   15003 C  CD2   . LEU A 1 3623 ? 203.778 223.131 190.947 1.00 69.58  ? 3623 LEU A CD2   1 
ATOM   15004 N  N     . GLU A 1 3624 ? 199.308 223.545 189.109 1.00 73.54  ? 3624 GLU A N     1 
ATOM   15005 C  CA    . GLU A 1 3624 ? 198.674 222.540 188.262 1.00 70.39  ? 3624 GLU A CA    1 
ATOM   15006 C  C     . GLU A 1 3624 ? 197.903 223.192 187.121 1.00 72.88  ? 3624 GLU A C     1 
ATOM   15007 O  O     . GLU A 1 3624 ? 197.940 222.719 185.978 1.00 72.85  ? 3624 GLU A O     1 
ATOM   15008 C  CB    . GLU A 1 3624 ? 197.756 221.659 189.108 1.00 70.86  ? 3624 GLU A CB    1 
ATOM   15009 C  CG    . GLU A 1 3624 ? 197.099 220.526 188.349 1.00 76.39  ? 3624 GLU A CG    1 
ATOM   15010 C  CD    . GLU A 1 3624 ? 196.242 219.654 189.243 1.00 79.79  ? 3624 GLU A CD    1 
ATOM   15011 O  OE1   . GLU A 1 3624 ? 196.149 219.953 190.453 1.00 77.40  ? 3624 GLU A OE1   1 
ATOM   15012 O  OE2   . GLU A 1 3624 ? 195.664 218.669 188.739 1.00 76.84  ? 3624 GLU A OE2   1 
ATOM   15013 N  N     . SER A 1 3625 ? 197.199 224.288 187.413 1.00 73.16  ? 3625 SER A N     1 
ATOM   15014 C  CA    . SER A 1 3625 ? 196.457 224.996 186.377 1.00 71.64  ? 3625 SER A CA    1 
ATOM   15015 C  C     . SER A 1 3625 ? 197.398 225.586 185.336 1.00 73.47  ? 3625 SER A C     1 
ATOM   15016 O  O     . SER A 1 3625 ? 197.110 225.554 184.134 1.00 75.61  ? 3625 SER A O     1 
ATOM   15017 C  CB    . SER A 1 3625 ? 195.594 226.088 187.008 1.00 70.77  ? 3625 SER A CB    1 
ATOM   15018 O  OG    . SER A 1 3625 ? 194.872 226.801 186.021 1.00 74.17  ? 3625 SER A OG    1 
ATOM   15019 N  N     . ALA A 1 3626 ? 198.529 226.138 185.781 1.00 70.84  ? 3626 ALA A N     1 
ATOM   15020 C  CA    . ALA A 1 3626 ? 199.506 226.680 184.844 1.00 68.36  ? 3626 ALA A CA    1 
ATOM   15021 C  C     . ALA A 1 3626 ? 200.098 225.585 183.968 1.00 70.54  ? 3626 ALA A C     1 
ATOM   15022 O  O     . ALA A 1 3626 ? 200.287 225.778 182.762 1.00 67.91  ? 3626 ALA A O     1 
ATOM   15023 C  CB    . ALA A 1 3626 ? 200.608 227.417 185.602 1.00 64.09  ? 3626 ALA A CB    1 
ATOM   15024 N  N     . LEU A 1 3627 ? 200.403 224.427 184.559 1.00 69.54  ? 3627 LEU A N     1 
ATOM   15025 C  CA    . LEU A 1 3627 ? 200.954 223.324 183.778 1.00 67.06  ? 3627 LEU A CA    1 
ATOM   15026 C  C     . LEU A 1 3627 ? 199.952 222.818 182.747 1.00 71.16  ? 3627 LEU A C     1 
ATOM   15027 O  O     . LEU A 1 3627 ? 200.311 222.576 181.589 1.00 73.10  ? 3627 LEU A O     1 
ATOM   15028 C  CB    . LEU A 1 3627 ? 201.390 222.188 184.701 1.00 68.45  ? 3627 LEU A CB    1 
ATOM   15029 C  CG    . LEU A 1 3627 ? 202.566 222.462 185.638 1.00 68.08  ? 3627 LEU A CG    1 
ATOM   15030 C  CD1   . LEU A 1 3627 ? 202.474 221.583 186.861 1.00 66.49  ? 3627 LEU A CD1   1 
ATOM   15031 C  CD2   . LEU A 1 3627 ? 203.883 222.238 184.931 1.00 70.80  ? 3627 LEU A CD2   1 
ATOM   15032 N  N     . ARG A 1 3628 ? 198.690 222.645 183.148 1.00 74.77  ? 3628 ARG A N     1 
ATOM   15033 C  CA    . ARG A 1 3628 ? 197.685 222.151 182.211 1.00 75.07  ? 3628 ARG A CA    1 
ATOM   15034 C  C     . ARG A 1 3628 ? 197.407 223.162 181.106 1.00 78.04  ? 3628 ARG A C     1 
ATOM   15035 O  O     . ARG A 1 3628 ? 197.436 222.822 179.918 1.00 74.76  ? 3628 ARG A O     1 
ATOM   15036 C  CB    . ARG A 1 3628 ? 196.392 221.806 182.950 1.00 73.94  ? 3628 ARG A CB    1 
ATOM   15037 C  CG    . ARG A 1 3628 ? 196.497 220.628 183.895 1.00 76.85  ? 3628 ARG A CG    1 
ATOM   15038 C  CD    . ARG A 1 3628 ? 195.157 220.347 184.550 1.00 75.41  ? 3628 ARG A CD    1 
ATOM   15039 N  NE    . ARG A 1 3628 ? 195.239 219.274 185.532 1.00 78.02  ? 3628 ARG A NE    1 
ATOM   15040 C  CZ    . ARG A 1 3628 ? 195.075 217.989 185.249 1.00 80.71  ? 3628 ARG A CZ    1 
ATOM   15041 N  NH1   . ARG A 1 3628 ? 194.826 217.579 184.016 1.00 77.91  ? 3628 ARG A NH1   1 
ATOM   15042 N  NH2   . ARG A 1 3628 ? 195.164 217.093 186.228 1.00 78.33  ? 3628 ARG A NH2   1 
ATOM   15043 N  N     . PHE A 1 3629 ? 197.141 224.412 181.477 1.00 77.85  ? 3629 PHE A N     1 
ATOM   15044 C  CA    . PHE A 1 3629 ? 196.679 225.420 180.533 1.00 73.79  ? 3629 PHE A CA    1 
ATOM   15045 C  C     . PHE A 1 3629 ? 197.813 226.187 179.868 1.00 72.15  ? 3629 PHE A C     1 
ATOM   15046 O  O     . PHE A 1 3629 ? 197.548 226.998 178.975 1.00 74.84  ? 3629 PHE A O     1 
ATOM   15047 C  CB    . PHE A 1 3629 ? 195.740 226.404 181.240 1.00 70.33  ? 3629 PHE A CB    1 
ATOM   15048 C  CG    . PHE A 1 3629 ? 194.547 225.751 181.883 1.00 75.91  ? 3629 PHE A CG    1 
ATOM   15049 C  CD1   . PHE A 1 3629 ? 194.081 224.525 181.435 1.00 73.60  ? 3629 PHE A CD1   1 
ATOM   15050 C  CD2   . PHE A 1 3629 ? 193.899 226.357 182.946 1.00 78.99  ? 3629 PHE A CD2   1 
ATOM   15051 C  CE1   . PHE A 1 3629 ? 192.991 223.922 182.029 1.00 74.45  ? 3629 PHE A CE1   1 
ATOM   15052 C  CE2   . PHE A 1 3629 ? 192.807 225.758 183.544 1.00 76.44  ? 3629 PHE A CE2   1 
ATOM   15053 C  CZ    . PHE A 1 3629 ? 192.353 224.539 183.084 1.00 76.74  ? 3629 PHE A CZ    1 
ATOM   15054 N  N     . GLY A 1 3630 ? 199.057 225.951 180.269 1.00 69.89  ? 3630 GLY A N     1 
ATOM   15055 C  CA    . GLY A 1 3630 ? 200.178 226.665 179.686 1.00 70.91  ? 3630 GLY A CA    1 
ATOM   15056 C  C     . GLY A 1 3630 ? 200.205 228.145 179.996 1.00 69.62  ? 3630 GLY A C     1 
ATOM   15057 O  O     . GLY A 1 3630 ? 200.506 228.955 179.110 1.00 71.54  ? 3630 GLY A O     1 
ATOM   15058 N  N     . ASN A 1 3631 ? 199.896 228.519 181.225 1.00 68.06  ? 3631 ASN A N     1 
ATOM   15059 C  CA    . ASN A 1 3631 ? 199.964 229.921 181.593 1.00 70.06  ? 3631 ASN A CA    1 
ATOM   15060 C  C     . ASN A 1 3631 ? 201.264 230.217 182.327 1.00 71.76  ? 3631 ASN A C     1 
ATOM   15061 O  O     . ASN A 1 3631 ? 201.766 229.376 183.078 1.00 76.63  ? 3631 ASN A O     1 
ATOM   15062 C  CB    . ASN A 1 3631 ? 198.784 230.309 182.489 1.00 68.57  ? 3631 ASN A CB    1 
ATOM   15063 C  CG    . ASN A 1 3631 ? 197.454 230.212 181.775 1.00 71.28  ? 3631 ASN A CG    1 
ATOM   15064 O  OD1   . ASN A 1 3631 ? 197.356 230.485 180.580 1.00 72.01  ? 3631 ASN A OD1   1 
ATOM   15065 N  ND2   . ASN A 1 3631 ? 196.419 229.821 182.507 1.00 69.91  ? 3631 ASN A ND2   1 
ATOM   15066 N  N     . PRO A 1 3632 ? 201.840 231.399 182.118 1.00 64.94  ? 3632 PRO A N     1 
ATOM   15067 C  CA    . PRO A 1 3632 ? 203.028 231.778 182.886 1.00 61.65  ? 3632 PRO A CA    1 
ATOM   15068 C  C     . PRO A 1 3632 ? 202.717 231.874 184.372 1.00 63.22  ? 3632 PRO A C     1 
ATOM   15069 O  O     . PRO A 1 3632 ? 201.612 232.240 184.777 1.00 66.54  ? 3632 PRO A O     1 
ATOM   15070 C  CB    . PRO A 1 3632 ? 203.415 233.142 182.302 1.00 63.74  ? 3632 PRO A CB    1 
ATOM   15071 C  CG    . PRO A 1 3632 ? 202.206 233.614 181.566 1.00 66.26  ? 3632 PRO A CG    1 
ATOM   15072 C  CD    . PRO A 1 3632 ? 201.506 232.391 181.086 1.00 67.85  ? 3632 PRO A CD    1 
ATOM   15073 N  N     . LEU A 1 3633 ? 203.710 231.529 185.187 1.00 58.05  ? 3633 LEU A N     1 
ATOM   15074 C  CA    . LEU A 1 3633 ? 203.578 231.559 186.634 1.00 55.13  ? 3633 LEU A CA    1 
ATOM   15075 C  C     . LEU A 1 3633 ? 204.769 232.283 187.243 1.00 57.23  ? 3633 LEU A C     1 
ATOM   15076 O  O     . LEU A 1 3633 ? 205.880 232.242 186.710 1.00 63.16  ? 3633 LEU A O     1 
ATOM   15077 C  CB    . LEU A 1 3633 ? 203.473 230.145 187.216 1.00 53.50  ? 3633 LEU A CB    1 
ATOM   15078 C  CG    . LEU A 1 3633 ? 202.957 230.035 188.651 1.00 61.30  ? 3633 LEU A CG    1 
ATOM   15079 C  CD1   . LEU A 1 3633 ? 201.454 230.241 188.696 1.00 62.34  ? 3633 LEU A CD1   1 
ATOM   15080 C  CD2   . LEU A 1 3633 ? 203.334 228.695 189.253 1.00 62.67  ? 3633 LEU A CD2   1 
ATOM   15081 N  N     . LEU A 1 3634 ? 204.524 232.955 188.366 1.00 56.94  ? 3634 LEU A N     1 
ATOM   15082 C  CA    . LEU A 1 3634 ? 205.579 233.611 189.127 1.00 56.64  ? 3634 LEU A CA    1 
ATOM   15083 C  C     . LEU A 1 3634 ? 205.387 233.282 190.597 1.00 60.17  ? 3634 LEU A C     1 
ATOM   15084 O  O     . LEU A 1 3634 ? 204.306 233.512 191.147 1.00 64.43  ? 3634 LEU A O     1 
ATOM   15085 C  CB    . LEU A 1 3634 ? 205.569 235.126 188.911 1.00 58.90  ? 3634 LEU A CB    1 
ATOM   15086 C  CG    . LEU A 1 3634 ? 206.485 235.917 189.846 1.00 60.46  ? 3634 LEU A CG    1 
ATOM   15087 C  CD1   . LEU A 1 3634 ? 207.907 235.952 189.314 1.00 61.31  ? 3634 LEU A CD1   1 
ATOM   15088 C  CD2   . LEU A 1 3634 ? 205.961 237.319 190.049 1.00 61.77  ? 3634 LEU A CD2   1 
ATOM   15089 N  N     . VAL A 1 3635 ? 206.428 232.748 191.231 1.00 56.49  ? 3635 VAL A N     1 
ATOM   15090 C  CA    . VAL A 1 3635 ? 206.401 232.390 192.643 1.00 56.41  ? 3635 VAL A CA    1 
ATOM   15091 C  C     . VAL A 1 3635 ? 207.365 233.310 193.378 1.00 59.25  ? 3635 VAL A C     1 
ATOM   15092 O  O     . VAL A 1 3635 ? 208.540 233.412 193.004 1.00 64.46  ? 3635 VAL A O     1 
ATOM   15093 C  CB    . VAL A 1 3635 ? 206.764 230.913 192.857 1.00 60.07  ? 3635 VAL A CB    1 
ATOM   15094 C  CG1   . VAL A 1 3635 ? 206.465 230.507 194.282 1.00 63.20  ? 3635 VAL A CG1   1 
ATOM   15095 C  CG2   . VAL A 1 3635 ? 206.007 230.038 191.877 1.00 60.10  ? 3635 VAL A CG2   1 
ATOM   15096 N  N     . GLN A 1 3636 ? 206.875 233.971 194.427 1.00 65.95  ? 3636 GLN A N     1 
ATOM   15097 C  CA    . GLN A 1 3636 ? 207.559 235.133 194.979 1.00 71.36  ? 3636 GLN A CA    1 
ATOM   15098 C  C     . GLN A 1 3636 ? 208.334 234.863 196.263 1.00 69.92  ? 3636 GLN A C     1 
ATOM   15099 O  O     . GLN A 1 3636 ? 209.029 235.767 196.738 1.00 76.76  ? 3636 GLN A O     1 
ATOM   15100 C  CB    . GLN A 1 3636 ? 206.555 236.265 195.229 1.00 70.02  ? 3636 GLN A CB    1 
ATOM   15101 C  CG    . GLN A 1 3636 ? 205.505 235.950 196.275 1.00 73.13  ? 3636 GLN A CG    1 
ATOM   15102 C  CD    . GLN A 1 3636 ? 204.631 237.145 196.594 1.00 76.05  ? 3636 GLN A CD    1 
ATOM   15103 O  OE1   . GLN A 1 3636 ? 204.892 238.257 196.137 1.00 76.32  ? 3636 GLN A OE1   1 
ATOM   15104 N  NE2   . GLN A 1 3636 ? 203.586 236.922 197.382 1.00 76.71  ? 3636 GLN A NE2   1 
ATOM   15105 N  N     . ASP A 1 3637 ? 208.246 233.664 196.840 1.00 57.07  ? 3637 ASP A N     1 
ATOM   15106 C  CA    . ASP A 1 3637 ? 208.988 233.331 198.061 1.00 65.06  ? 3637 ASP A CA    1 
ATOM   15107 C  C     . ASP A 1 3637 ? 209.696 231.996 197.844 1.00 70.64  ? 3637 ASP A C     1 
ATOM   15108 O  O     . ASP A 1 3637 ? 209.204 230.953 198.274 1.00 80.61  ? 3637 ASP A O     1 
ATOM   15109 C  CB    . ASP A 1 3637 ? 208.053 233.283 199.274 1.00 67.57  ? 3637 ASP A CB    1 
ATOM   15110 C  CG    . ASP A 1 3637 ? 207.517 234.650 199.658 1.00 75.19  ? 3637 ASP A CG    1 
ATOM   15111 O  OD1   . ASP A 1 3637 ? 208.213 235.657 199.416 1.00 77.56  ? 3637 ASP A OD1   1 
ATOM   15112 O  OD2   . ASP A 1 3637 ? 206.395 234.718 200.201 1.00 74.76  ? 3637 ASP A OD2   1 
ATOM   15113 N  N     . VAL A 1 3638 ? 210.878 232.038 197.219 1.00 61.44  ? 3638 VAL A N     1 
ATOM   15114 C  CA    . VAL A 1 3638 ? 211.582 230.809 196.853 1.00 59.30  ? 3638 VAL A CA    1 
ATOM   15115 C  C     . VAL A 1 3638 ? 212.471 230.292 197.976 1.00 63.51  ? 3638 VAL A C     1 
ATOM   15116 O  O     . VAL A 1 3638 ? 212.936 229.143 197.910 1.00 65.85  ? 3638 VAL A O     1 
ATOM   15117 C  CB    . VAL A 1 3638 ? 212.411 231.026 195.569 1.00 61.02  ? 3638 VAL A CB    1 
ATOM   15118 C  CG1   . VAL A 1 3638 ? 213.604 231.913 195.846 1.00 66.20  ? 3638 VAL A CG1   1 
ATOM   15119 C  CG2   . VAL A 1 3638 ? 212.832 229.701 194.942 1.00 62.04  ? 3638 VAL A CG2   1 
ATOM   15120 N  N     . GLU A 1 3639 ? 212.709 231.090 199.017 1.00 72.01  ? 3639 GLU A N     1 
ATOM   15121 C  CA    . GLU A 1 3639 ? 213.432 230.620 200.192 1.00 70.51  ? 3639 GLU A CA    1 
ATOM   15122 C  C     . GLU A 1 3639 ? 212.698 229.506 200.926 1.00 70.63  ? 3639 GLU A C     1 
ATOM   15123 O  O     . GLU A 1 3639 ? 213.314 228.813 201.742 1.00 70.53  ? 3639 GLU A O     1 
ATOM   15124 C  CB    . GLU A 1 3639 ? 213.692 231.791 201.138 1.00 69.04  ? 3639 GLU A CB    1 
ATOM   15125 C  CG    . GLU A 1 3639 ? 212.433 232.344 201.771 1.00 72.21  ? 3639 GLU A CG    1 
ATOM   15126 C  CD    . GLU A 1 3639 ? 211.732 233.346 200.875 1.00 75.86  ? 3639 GLU A CD    1 
ATOM   15127 O  OE1   . GLU A 1 3639 ? 212.052 233.403 199.669 1.00 75.49  ? 3639 GLU A OE1   1 
ATOM   15128 O  OE2   . GLU A 1 3639 ? 210.847 234.067 201.368 1.00 75.73  ? 3639 GLU A OE2   1 
ATOM   15129 N  N     . SER A 1 3640 ? 211.406 229.322 200.658 1.00 67.73  ? 3640 SER A N     1 
ATOM   15130 C  CA    . SER A 1 3640 ? 210.644 228.202 201.192 1.00 69.60  ? 3640 SER A CA    1 
ATOM   15131 C  C     . SER A 1 3640 ? 210.231 227.299 200.039 1.00 70.37  ? 3640 SER A C     1 
ATOM   15132 O  O     . SER A 1 3640 ? 209.072 226.886 199.943 1.00 72.06  ? 3640 SER A O     1 
ATOM   15133 C  CB    . SER A 1 3640 ? 209.421 228.690 201.966 1.00 73.14  ? 3640 SER A CB    1 
ATOM   15134 O  OG    . SER A 1 3640 ? 209.795 229.575 203.006 1.00 78.41  ? 3640 SER A OG    1 
ATOM   15135 N  N     . TYR A 1 3641 ? 211.184 227.015 199.153 1.00 66.01  ? 3641 TYR A N     1 
ATOM   15136 C  CA    . TYR A 1 3641 ? 210.914 226.278 197.926 1.00 61.45  ? 3641 TYR A CA    1 
ATOM   15137 C  C     . TYR A 1 3641 ? 210.255 224.936 198.221 1.00 67.71  ? 3641 TYR A C     1 
ATOM   15138 O  O     . TYR A 1 3641 ? 210.710 224.179 199.083 1.00 68.96  ? 3641 TYR A O     1 
ATOM   15139 C  CB    . TYR A 1 3641 ? 212.224 226.080 197.163 1.00 58.13  ? 3641 TYR A CB    1 
ATOM   15140 C  CG    . TYR A 1 3641 ? 212.189 225.039 196.072 1.00 60.83  ? 3641 TYR A CG    1 
ATOM   15141 C  CD1   . TYR A 1 3641 ? 211.590 225.305 194.852 1.00 63.15  ? 3641 TYR A CD1   1 
ATOM   15142 C  CD2   . TYR A 1 3641 ? 212.781 223.798 196.254 1.00 61.64  ? 3641 TYR A CD2   1 
ATOM   15143 C  CE1   . TYR A 1 3641 ? 211.565 224.360 193.850 1.00 66.79  ? 3641 TYR A CE1   1 
ATOM   15144 C  CE2   . TYR A 1 3641 ? 212.762 222.847 195.259 1.00 60.58  ? 3641 TYR A CE2   1 
ATOM   15145 C  CZ    . TYR A 1 3641 ? 212.152 223.133 194.059 1.00 64.84  ? 3641 TYR A CZ    1 
ATOM   15146 O  OH    . TYR A 1 3641 ? 212.132 222.186 193.063 1.00 64.61  ? 3641 TYR A OH    1 
ATOM   15147 N  N     . ASP A 1 3642 ? 209.170 224.650 197.500 1.00 67.15  ? 3642 ASP A N     1 
ATOM   15148 C  CA    . ASP A 1 3642 ? 208.434 223.408 197.666 1.00 66.06  ? 3642 ASP A CA    1 
ATOM   15149 C  C     . ASP A 1 3642 ? 209.004 222.365 196.721 1.00 67.05  ? 3642 ASP A C     1 
ATOM   15150 O  O     . ASP A 1 3642 ? 209.015 222.594 195.501 1.00 68.90  ? 3642 ASP A O     1 
ATOM   15151 C  CB    . ASP A 1 3642 ? 206.952 223.624 197.386 1.00 69.09  ? 3642 ASP A CB    1 
ATOM   15152 C  CG    . ASP A 1 3642 ? 206.074 222.605 198.081 1.00 75.04  ? 3642 ASP A CG    1 
ATOM   15153 O  OD1   . ASP A 1 3642 ? 205.947 221.479 197.564 1.00 74.70  ? 3642 ASP A OD1   1 
ATOM   15154 O  OD2   . ASP A 1 3642 ? 205.509 222.931 199.145 1.00 70.72  ? 3642 ASP A OD2   1 
ATOM   15155 N  N     . PRO A 1 3643 ? 209.478 221.219 197.217 1.00 63.79  ? 3643 PRO A N     1 
ATOM   15156 C  CA    . PRO A 1 3643 ? 210.194 220.269 196.351 1.00 61.57  ? 3643 PRO A CA    1 
ATOM   15157 C  C     . PRO A 1 3643 ? 209.326 219.575 195.314 1.00 65.10  ? 3643 PRO A C     1 
ATOM   15158 O  O     . PRO A 1 3643 ? 209.841 218.726 194.580 1.00 64.85  ? 3643 PRO A O     1 
ATOM   15159 C  CB    . PRO A 1 3643 ? 210.766 219.249 197.349 1.00 61.05  ? 3643 PRO A CB    1 
ATOM   15160 C  CG    . PRO A 1 3643 ? 210.706 219.923 198.682 1.00 64.76  ? 3643 PRO A CG    1 
ATOM   15161 C  CD    . PRO A 1 3643 ? 209.504 220.803 198.627 1.00 64.32  ? 3643 PRO A CD    1 
ATOM   15162 N  N     . VAL A 1 3644 ? 208.032 219.893 195.220 1.00 67.03  ? 3644 VAL A N     1 
ATOM   15163 C  CA    . VAL A 1 3644 ? 207.205 219.281 194.187 1.00 65.24  ? 3644 VAL A CA    1 
ATOM   15164 C  C     . VAL A 1 3644 ? 207.551 219.810 192.805 1.00 65.97  ? 3644 VAL A C     1 
ATOM   15165 O  O     . VAL A 1 3644 ? 207.163 219.206 191.799 1.00 65.44  ? 3644 VAL A O     1 
ATOM   15166 C  CB    . VAL A 1 3644 ? 205.711 219.495 194.485 1.00 64.30  ? 3644 VAL A CB    1 
ATOM   15167 C  CG1   . VAL A 1 3644 ? 205.352 218.901 195.836 1.00 66.29  ? 3644 VAL A CG1   1 
ATOM   15168 C  CG2   . VAL A 1 3644 ? 205.365 220.974 194.432 1.00 58.39  ? 3644 VAL A CG2   1 
ATOM   15169 N  N     . LEU A 1 3645 ? 208.275 220.924 192.725 1.00 65.06  ? 3645 LEU A N     1 
ATOM   15170 C  CA    . LEU A 1 3645 ? 208.666 221.507 191.450 1.00 57.66  ? 3645 LEU A CA    1 
ATOM   15171 C  C     . LEU A 1 3645 ? 209.868 220.814 190.828 1.00 56.84  ? 3645 LEU A C     1 
ATOM   15172 O  O     . LEU A 1 3645 ? 210.238 221.157 189.700 1.00 60.22  ? 3645 LEU A O     1 
ATOM   15173 C  CB    . LEU A 1 3645 ? 208.972 222.996 191.626 1.00 57.56  ? 3645 LEU A CB    1 
ATOM   15174 C  CG    . LEU A 1 3645 ? 207.838 223.979 191.339 1.00 59.23  ? 3645 LEU A CG    1 
ATOM   15175 C  CD1   . LEU A 1 3645 ? 208.286 225.391 191.646 1.00 58.33  ? 3645 LEU A CD1   1 
ATOM   15176 C  CD2   . LEU A 1 3645 ? 207.376 223.868 189.899 1.00 60.86  ? 3645 LEU A CD2   1 
ATOM   15177 N  N     . ASN A 1 3646 ? 210.480 219.861 191.530 1.00 58.16  ? 3646 ASN A N     1 
ATOM   15178 C  CA    . ASN A 1 3646 ? 211.685 219.210 191.020 1.00 55.90  ? 3646 ASN A CA    1 
ATOM   15179 C  C     . ASN A 1 3646 ? 211.482 218.564 189.655 1.00 60.08  ? 3646 ASN A C     1 
ATOM   15180 O  O     . ASN A 1 3646 ? 212.335 218.765 188.774 1.00 62.33  ? 3646 ASN A O     1 
ATOM   15181 C  CB    . ASN A 1 3646 ? 212.194 218.197 192.051 1.00 52.83  ? 3646 ASN A CB    1 
ATOM   15182 C  CG    . ASN A 1 3646 ? 212.838 218.860 193.249 1.00 56.64  ? 3646 ASN A CG    1 
ATOM   15183 O  OD1   . ASN A 1 3646 ? 212.930 220.084 193.318 1.00 63.68  ? 3646 ASN A OD1   1 
ATOM   15184 N  ND2   . ASN A 1 3646 ? 213.289 218.054 194.201 1.00 54.78  ? 3646 ASN A ND2   1 
ATOM   15185 N  N     . PRO A 1 3647 ? 210.424 217.783 189.404 1.00 57.64  ? 3647 PRO A N     1 
ATOM   15186 C  CA    . PRO A 1 3647 ? 210.204 217.303 188.030 1.00 60.14  ? 3647 PRO A CA    1 
ATOM   15187 C  C     . PRO A 1 3647 ? 209.986 218.422 187.029 1.00 64.31  ? 3647 PRO A C     1 
ATOM   15188 O  O     . PRO A 1 3647 ? 210.414 218.299 185.874 1.00 63.47  ? 3647 PRO A O     1 
ATOM   15189 C  CB    . PRO A 1 3647 ? 208.959 216.414 188.163 1.00 58.55  ? 3647 PRO A CB    1 
ATOM   15190 C  CG    . PRO A 1 3647 ? 208.309 216.851 189.420 1.00 57.99  ? 3647 PRO A CG    1 
ATOM   15191 C  CD    . PRO A 1 3647 ? 209.426 217.218 190.329 1.00 57.07  ? 3647 PRO A CD    1 
ATOM   15192 N  N     . VAL A 1 3648 ? 209.333 219.512 187.436 1.00 60.11  ? 3648 VAL A N     1 
ATOM   15193 C  CA    . VAL A 1 3648 ? 209.076 220.615 186.515 1.00 53.11  ? 3648 VAL A CA    1 
ATOM   15194 C  C     . VAL A 1 3648 ? 210.371 221.330 186.157 1.00 58.37  ? 3648 VAL A C     1 
ATOM   15195 O  O     . VAL A 1 3648 ? 210.618 221.648 184.988 1.00 61.19  ? 3648 VAL A O     1 
ATOM   15196 C  CB    . VAL A 1 3648 ? 208.047 221.584 187.120 1.00 52.37  ? 3648 VAL A CB    1 
ATOM   15197 C  CG1   . VAL A 1 3648 ? 207.718 222.686 186.133 1.00 53.98  ? 3648 VAL A CG1   1 
ATOM   15198 C  CG2   . VAL A 1 3648 ? 206.793 220.836 187.532 1.00 62.23  ? 3648 VAL A CG2   1 
ATOM   15199 N  N     . LEU A 1 3649 ? 211.215 221.600 187.155 1.00 57.35  ? 3649 LEU A N     1 
ATOM   15200 C  CA    . LEU A 1 3649 ? 212.466 222.304 186.894 1.00 50.66  ? 3649 LEU A CA    1 
ATOM   15201 C  C     . LEU A 1 3649 ? 213.429 221.442 186.087 1.00 54.26  ? 3649 LEU A C     1 
ATOM   15202 O  O     . LEU A 1 3649 ? 214.176 221.958 185.248 1.00 58.76  ? 3649 LEU A O     1 
ATOM   15203 C  CB    . LEU A 1 3649 ? 213.103 222.742 188.212 1.00 51.36  ? 3649 LEU A CB    1 
ATOM   15204 C  CG    . LEU A 1 3649 ? 212.266 223.675 189.089 1.00 39.60  ? 3649 LEU A CG    1 
ATOM   15205 C  CD1   . LEU A 1 3649 ? 213.092 224.219 190.237 1.00 44.10  ? 3649 LEU A CD1   1 
ATOM   15206 C  CD2   . LEU A 1 3649 ? 211.685 224.808 188.268 1.00 45.83  ? 3649 LEU A CD2   1 
ATOM   15207 N  N     . ASN A 1 3650 ? 213.431 220.131 186.326 1.00 49.02  ? 3650 ASN A N     1 
ATOM   15208 C  CA    . ASN A 1 3650 ? 214.263 219.220 185.551 1.00 50.76  ? 3650 ASN A CA    1 
ATOM   15209 C  C     . ASN A 1 3650 ? 213.671 218.887 184.189 1.00 56.46  ? 3650 ASN A C     1 
ATOM   15210 O  O     . ASN A 1 3650 ? 214.359 218.262 183.375 1.00 60.11  ? 3650 ASN A O     1 
ATOM   15211 C  CB    . ASN A 1 3650 ? 214.495 217.919 186.321 1.00 53.67  ? 3650 ASN A CB    1 
ATOM   15212 C  CG    . ASN A 1 3650 ? 215.469 218.082 187.464 1.00 58.56  ? 3650 ASN A CG    1 
ATOM   15213 O  OD1   . ASN A 1 3650 ? 216.554 218.634 187.298 1.00 58.79  ? 3650 ASN A OD1   1 
ATOM   15214 N  ND2   . ASN A 1 3650 ? 215.091 217.586 188.633 1.00 58.58  ? 3650 ASN A ND2   1 
ATOM   15215 N  N     . ARG A 1 3651 ? 212.425 219.288 183.927 1.00 56.63  ? 3651 ARG A N     1 
ATOM   15216 C  CA    . ARG A 1 3651 ? 211.721 218.947 182.690 1.00 57.33  ? 3651 ARG A CA    1 
ATOM   15217 C  C     . ARG A 1 3651 ? 211.662 217.436 182.485 1.00 61.52  ? 3651 ARG A C     1 
ATOM   15218 O  O     . ARG A 1 3651 ? 211.931 216.926 181.396 1.00 60.90  ? 3651 ARG A O     1 
ATOM   15219 C  CB    . ARG A 1 3651 ? 212.351 219.638 181.480 1.00 57.51  ? 3651 ARG A CB    1 
ATOM   15220 C  CG    . ARG A 1 3651 ? 212.099 221.130 181.429 1.00 59.26  ? 3651 ARG A CG    1 
ATOM   15221 C  CD    . ARG A 1 3651 ? 212.724 221.749 180.196 1.00 61.99  ? 3651 ARG A CD    1 
ATOM   15222 N  NE    . ARG A 1 3651 ? 212.457 223.179 180.119 1.00 62.79  ? 3651 ARG A NE    1 
ATOM   15223 C  CZ    . ARG A 1 3651 ? 213.216 224.110 180.680 1.00 62.45  ? 3651 ARG A CZ    1 
ATOM   15224 N  NH1   . ARG A 1 3651 ? 214.296 223.793 181.374 1.00 60.67  ? 3651 ARG A NH1   1 
ATOM   15225 N  NH2   . ARG A 1 3651 ? 212.883 225.389 180.541 1.00 59.08  ? 3651 ARG A NH2   1 
ATOM   15226 N  N     . GLU A 1 3652 ? 211.306 216.715 183.547 1.00 70.66  ? 3652 GLU A N     1 
ATOM   15227 C  CA    . GLU A 1 3652 ? 211.186 215.258 183.506 1.00 67.85  ? 3652 GLU A CA    1 
ATOM   15228 C  C     . GLU A 1 3652 ? 209.796 214.903 182.988 1.00 70.03  ? 3652 GLU A C     1 
ATOM   15229 O  O     . GLU A 1 3652 ? 208.870 214.592 183.741 1.00 74.20  ? 3652 GLU A O     1 
ATOM   15230 C  CB    . GLU A 1 3652 ? 211.441 214.662 184.882 1.00 66.48  ? 3652 GLU A CB    1 
ATOM   15231 C  CG    . GLU A 1 3652 ? 212.865 214.822 185.367 1.00 70.92  ? 3652 GLU A CG    1 
ATOM   15232 C  CD    . GLU A 1 3652 ? 213.077 214.238 186.745 1.00 75.06  ? 3652 GLU A CD    1 
ATOM   15233 O  OE1   . GLU A 1 3652 ? 212.081 213.821 187.372 1.00 73.60  ? 3652 GLU A OE1   1 
ATOM   15234 O  OE2   . GLU A 1 3652 ? 214.238 214.194 187.201 1.00 75.33  ? 3652 GLU A OE2   1 
ATOM   15235 N  N     . VAL A 1 3653 ? 209.654 214.948 181.667 1.00 73.39  ? 3653 VAL A N     1 
ATOM   15236 C  CA    . VAL A 1 3653 ? 208.382 214.699 181.001 1.00 73.20  ? 3653 VAL A CA    1 
ATOM   15237 C  C     . VAL A 1 3653 ? 208.492 213.412 180.197 1.00 74.59  ? 3653 VAL A C     1 
ATOM   15238 O  O     . VAL A 1 3653 ? 209.515 213.160 179.548 1.00 76.55  ? 3653 VAL A O     1 
ATOM   15239 C  CB    . VAL A 1 3653 ? 207.964 215.880 180.105 1.00 74.47  ? 3653 VAL A CB    1 
ATOM   15240 C  CG1   . VAL A 1 3653 ? 207.767 217.130 180.944 1.00 76.10  ? 3653 VAL A CG1   1 
ATOM   15241 C  CG2   . VAL A 1 3653 ? 208.998 216.134 179.026 1.00 70.37  ? 3653 VAL A CG2   1 
ATOM   15242 N  N     . ARG A 1 3654 ? 207.452 212.589 180.267 1.00 79.30  ? 3654 ARG A N     1 
ATOM   15243 C  CA    . ARG A 1 3654 ? 207.331 211.384 179.458 1.00 78.28  ? 3654 ARG A CA    1 
ATOM   15244 C  C     . ARG A 1 3654 ? 206.295 211.641 178.371 1.00 77.87  ? 3654 ARG A C     1 
ATOM   15245 O  O     . ARG A 1 3654 ? 205.183 212.096 178.659 1.00 79.48  ? 3654 ARG A O     1 
ATOM   15246 C  CB    . ARG A 1 3654 ? 206.957 210.178 180.325 1.00 76.72  ? 3654 ARG A CB    1 
ATOM   15247 C  CG    . ARG A 1 3654 ? 205.604 210.275 181.011 1.00 77.03  ? 3654 ARG A CG    1 
ATOM   15248 C  CD    . ARG A 1 3654 ? 205.311 209.058 181.871 1.00 78.06  ? 3654 ARG A CD    1 
ATOM   15249 N  NE    . ARG A 1 3654 ? 205.132 207.848 181.079 1.00 80.52  ? 3654 ARG A NE    1 
ATOM   15250 C  CZ    . ARG A 1 3654 ? 205.144 206.620 181.580 1.00 82.00  ? 3654 ARG A CZ    1 
ATOM   15251 N  NH1   . ARG A 1 3654 ? 205.310 206.404 182.874 1.00 79.31  ? 3654 ARG A NH1   1 
ATOM   15252 N  NH2   . ARG A 1 3654 ? 204.980 205.584 180.762 1.00 80.68  ? 3654 ARG A NH2   1 
ATOM   15253 N  N     . ARG A 1 3655 ? 206.672 211.383 177.122 1.00 75.64  ? 3655 ARG A N     1 
ATOM   15254 C  CA    . ARG A 1 3655 ? 205.812 211.656 175.972 1.00 79.03  ? 3655 ARG A CA    1 
ATOM   15255 C  C     . ARG A 1 3655 ? 205.166 210.345 175.537 1.00 78.60  ? 3655 ARG A C     1 
ATOM   15256 O  O     . ARG A 1 3655 ? 205.618 209.687 174.600 1.00 79.60  ? 3655 ARG A O     1 
ATOM   15257 C  CB    . ARG A 1 3655 ? 206.610 212.300 174.844 1.00 76.70  ? 3655 ARG A CB    1 
ATOM   15258 C  CG    . ARG A 1 3655 ? 207.200 213.652 175.208 1.00 77.23  ? 3655 ARG A CG    1 
ATOM   15259 C  CD    . ARG A 1 3655 ? 208.165 214.145 174.145 1.00 75.25  ? 3655 ARG A CD    1 
ATOM   15260 N  NE    . ARG A 1 3655 ? 208.152 215.598 174.025 1.00 72.98  ? 3655 ARG A NE    1 
ATOM   15261 C  CZ    . ARG A 1 3655 ? 208.864 216.419 174.784 1.00 74.53  ? 3655 ARG A CZ    1 
ATOM   15262 N  NH1   . ARG A 1 3655 ? 209.654 215.963 175.742 1.00 77.89  ? 3655 ARG A NH1   1 
ATOM   15263 N  NH2   . ARG A 1 3655 ? 208.782 217.729 174.577 1.00 74.93  ? 3655 ARG A NH2   1 
ATOM   15264 N  N     . THR A 1 3656 ? 204.093 209.969 176.225 1.00 83.02  ? 3656 THR A N     1 
ATOM   15265 C  CA    . THR A 1 3656 ? 203.353 208.750 175.923 1.00 86.15  ? 3656 THR A CA    1 
ATOM   15266 C  C     . THR A 1 3656 ? 202.247 209.082 174.930 1.00 87.28  ? 3656 THR A C     1 
ATOM   15267 O  O     . THR A 1 3656 ? 201.335 209.854 175.245 1.00 83.05  ? 3656 THR A O     1 
ATOM   15268 C  CB    . THR A 1 3656 ? 202.770 208.132 177.193 1.00 85.36  ? 3656 THR A CB    1 
ATOM   15269 O  OG1   . THR A 1 3656 ? 203.827 207.575 177.985 1.00 83.08  ? 3656 THR A OG1   1 
ATOM   15270 C  CG2   . THR A 1 3656 ? 201.778 207.034 176.843 1.00 82.15  ? 3656 THR A CG2   1 
ATOM   15271 N  N     . GLY A 1 3657 ? 202.324 208.490 173.741 1.00 87.15  ? 3657 GLY A N     1 
ATOM   15272 C  CA    . GLY A 1 3657 ? 201.367 208.818 172.698 1.00 84.86  ? 3657 GLY A CA    1 
ATOM   15273 C  C     . GLY A 1 3657 ? 201.486 210.275 172.303 1.00 87.63  ? 3657 GLY A C     1 
ATOM   15274 O  O     . GLY A 1 3657 ? 202.581 210.787 172.048 1.00 86.44  ? 3657 GLY A O     1 
ATOM   15275 N  N     . GLY A 1 3658 ? 200.348 210.957 172.244 1.00 88.98  ? 3658 GLY A N     1 
ATOM   15276 C  CA    . GLY A 1 3658 ? 200.308 212.373 171.955 1.00 88.47  ? 3658 GLY A CA    1 
ATOM   15277 C  C     . GLY A 1 3658 ? 200.332 213.273 173.170 1.00 88.78  ? 3658 GLY A C     1 
ATOM   15278 O  O     . GLY A 1 3658 ? 200.166 214.489 173.028 1.00 88.20  ? 3658 GLY A O     1 
ATOM   15279 N  N     . ARG A 1 3659 ? 200.538 212.718 174.360 1.00 83.82  ? 3659 ARG A N     1 
ATOM   15280 C  CA    . ARG A 1 3659 ? 200.474 213.469 175.605 1.00 83.57  ? 3659 ARG A CA    1 
ATOM   15281 C  C     . ARG A 1 3659 ? 201.866 213.593 176.206 1.00 85.53  ? 3659 ARG A C     1 
ATOM   15282 O  O     . ARG A 1 3659 ? 202.542 212.584 176.430 1.00 86.49  ? 3659 ARG A O     1 
ATOM   15283 C  CB    . ARG A 1 3659 ? 199.538 212.788 176.606 1.00 84.92  ? 3659 ARG A CB    1 
ATOM   15284 C  CG    . ARG A 1 3659 ? 198.068 212.829 176.230 1.00 83.71  ? 3659 ARG A CG    1 
ATOM   15285 C  CD    . ARG A 1 3659 ? 197.285 211.770 176.989 1.00 83.79  ? 3659 ARG A CD    1 
ATOM   15286 N  NE    . ARG A 1 3659 ? 197.459 211.898 178.431 1.00 83.84  ? 3659 ARG A NE    1 
ATOM   15287 C  CZ    . ARG A 1 3659 ? 196.464 211.914 179.309 1.00 86.46  ? 3659 ARG A CZ    1 
ATOM   15288 N  NH1   . ARG A 1 3659 ? 195.203 211.802 178.927 1.00 86.00  ? 3659 ARG A NH1   1 
ATOM   15289 N  NH2   . ARG A 1 3659 ? 196.743 212.045 180.603 1.00 85.41  ? 3659 ARG A NH2   1 
ATOM   15290 N  N     . VAL A 1 3660 ? 202.286 214.827 176.469 1.00 79.74  ? 3660 VAL A N     1 
ATOM   15291 C  CA    . VAL A 1 3660 ? 203.513 215.094 177.210 1.00 74.27  ? 3660 VAL A CA    1 
ATOM   15292 C  C     . VAL A 1 3660 ? 203.138 215.145 178.686 1.00 74.14  ? 3660 VAL A C     1 
ATOM   15293 O  O     . VAL A 1 3660 ? 202.526 216.110 179.147 1.00 76.61  ? 3660 VAL A O     1 
ATOM   15294 C  CB    . VAL A 1 3660 ? 204.176 216.398 176.754 1.00 75.88  ? 3660 VAL A CB    1 
ATOM   15295 C  CG1   . VAL A 1 3660 ? 205.449 216.646 177.539 1.00 76.81  ? 3660 VAL A CG1   1 
ATOM   15296 C  CG2   . VAL A 1 3660 ? 204.465 216.352 175.263 1.00 74.02  ? 3660 VAL A CG2   1 
ATOM   15297 N  N     . LEU A 1 3661 ? 203.505 214.106 179.428 1.00 76.00  ? 3661 LEU A N     1 
ATOM   15298 C  CA    . LEU A 1 3661 ? 203.030 213.908 180.789 1.00 76.50  ? 3661 LEU A CA    1 
ATOM   15299 C  C     . LEU A 1 3661 ? 204.101 214.303 181.795 1.00 75.24  ? 3661 LEU A C     1 
ATOM   15300 O  O     . LEU A 1 3661 ? 205.282 213.997 181.615 1.00 77.95  ? 3661 LEU A O     1 
ATOM   15301 C  CB    . LEU A 1 3661 ? 202.621 212.451 181.014 1.00 78.69  ? 3661 LEU A CB    1 
ATOM   15302 C  CG    . LEU A 1 3661 ? 201.390 211.969 180.246 1.00 79.46  ? 3661 LEU A CG    1 
ATOM   15303 C  CD1   . LEU A 1 3661 ? 201.114 210.506 180.544 1.00 78.30  ? 3661 LEU A CD1   1 
ATOM   15304 C  CD2   . LEU A 1 3661 ? 200.179 212.826 180.573 1.00 77.01  ? 3661 LEU A CD2   1 
ATOM   15305 N  N     . ILE A 1 3662 ? 203.676 214.984 182.856 1.00 76.99  ? 3662 ILE A N     1 
ATOM   15306 C  CA    . ILE A 1 3662 ? 204.544 215.356 183.966 1.00 76.45  ? 3662 ILE A CA    1 
ATOM   15307 C  C     . ILE A 1 3662 ? 203.848 214.964 185.261 1.00 75.28  ? 3662 ILE A C     1 
ATOM   15308 O  O     . ILE A 1 3662 ? 202.618 215.034 185.362 1.00 77.69  ? 3662 ILE A O     1 
ATOM   15309 C  CB    . ILE A 1 3662 ? 204.890 216.861 183.947 1.00 76.74  ? 3662 ILE A CB    1 
ATOM   15310 C  CG1   . ILE A 1 3662 ? 206.033 217.161 184.918 1.00 74.92  ? 3662 ILE A CG1   1 
ATOM   15311 C  CG2   . ILE A 1 3662 ? 203.670 217.712 184.265 1.00 73.96  ? 3662 ILE A CG2   1 
ATOM   15312 C  CD1   . ILE A 1 3662 ? 206.671 218.505 184.696 1.00 74.19  ? 3662 ILE A CD1   1 
ATOM   15313 N  N     . THR A 1 3663 ? 204.630 214.524 186.241 1.00 77.43  ? 3663 THR A N     1 
ATOM   15314 C  CA    . THR A 1 3663 ? 204.099 213.987 187.487 1.00 79.07  ? 3663 THR A CA    1 
ATOM   15315 C  C     . THR A 1 3663 ? 204.379 214.955 188.628 1.00 78.93  ? 3663 THR A C     1 
ATOM   15316 O  O     . THR A 1 3663 ? 205.532 215.333 188.856 1.00 81.41  ? 3663 THR A O     1 
ATOM   15317 C  CB    . THR A 1 3663 ? 204.705 212.618 187.795 1.00 81.72  ? 3663 THR A CB    1 
ATOM   15318 O  OG1   . THR A 1 3663 ? 206.094 212.772 188.114 1.00 78.60  ? 3663 THR A OG1   1 
ATOM   15319 C  CG2   . THR A 1 3663 ? 204.561 211.691 186.598 1.00 79.07  ? 3663 THR A CG2   1 
ATOM   15320 N  N     . LEU A 1 3664 ? 203.326 215.346 189.341 1.00 82.50  ? 3664 LEU A N     1 
ATOM   15321 C  CA    . LEU A 1 3664 ? 203.437 216.121 190.572 1.00 82.78  ? 3664 LEU A CA    1 
ATOM   15322 C  C     . LEU A 1 3664 ? 202.981 215.236 191.723 1.00 82.14  ? 3664 LEU A C     1 
ATOM   15323 O  O     . LEU A 1 3664 ? 201.797 214.894 191.817 1.00 84.67  ? 3664 LEU A O     1 
ATOM   15324 C  CB    . LEU A 1 3664 ? 202.602 217.397 190.512 1.00 81.08  ? 3664 LEU A CB    1 
ATOM   15325 C  CG    . LEU A 1 3664 ? 203.081 218.544 189.629 1.00 81.94  ? 3664 LEU A CG    1 
ATOM   15326 C  CD1   . LEU A 1 3664 ? 202.231 219.769 189.905 1.00 80.56  ? 3664 LEU A CD1   1 
ATOM   15327 C  CD2   . LEU A 1 3664 ? 204.552 218.837 189.865 1.00 81.24  ? 3664 LEU A CD2   1 
ATOM   15328 N  N     . GLY A 1 3665 ? 203.913 214.874 192.598 1.00 82.77  ? 3665 GLY A N     1 
ATOM   15329 C  CA    . GLY A 1 3665 ? 203.598 213.985 193.696 1.00 84.73  ? 3665 GLY A CA    1 
ATOM   15330 C  C     . GLY A 1 3665 ? 203.135 212.628 193.212 1.00 86.51  ? 3665 GLY A C     1 
ATOM   15331 O  O     . GLY A 1 3665 ? 203.923 211.856 192.657 1.00 87.55  ? 3665 GLY A O     1 
ATOM   15332 N  N     . ASP A 1 3666 ? 201.854 212.326 193.413 1.00 90.73  ? 3666 ASP A N     1 
ATOM   15333 C  CA    . ASP A 1 3666 ? 201.259 211.081 192.947 1.00 94.11  ? 3666 ASP A CA    1 
ATOM   15334 C  C     . ASP A 1 3666 ? 200.283 211.296 191.799 1.00 93.16  ? 3666 ASP A C     1 
ATOM   15335 O  O     . ASP A 1 3666 ? 199.501 210.393 191.484 1.00 93.81  ? 3666 ASP A O     1 
ATOM   15336 C  CB    . ASP A 1 3666 ? 200.559 210.367 194.105 1.00 93.66  ? 3666 ASP A CB    1 
ATOM   15337 C  CG    . ASP A 1 3666 ? 199.457 211.202 194.723 1.00 94.14  ? 3666 ASP A CG    1 
ATOM   15338 O  OD1   . ASP A 1 3666 ? 199.471 212.438 194.541 1.00 91.56  ? 3666 ASP A OD1   1 
ATOM   15339 O  OD2   . ASP A 1 3666 ? 198.574 210.623 195.389 1.00 92.35  ? 3666 ASP A OD2   1 
ATOM   15340 N  N     . GLN A 1 3667 ? 200.310 212.464 191.163 1.00 85.75  ? 3667 GLN A N     1 
ATOM   15341 C  CA    . GLN A 1 3667 ? 199.358 212.820 190.124 1.00 86.16  ? 3667 GLN A CA    1 
ATOM   15342 C  C     . GLN A 1 3667 ? 200.079 213.012 188.797 1.00 86.03  ? 3667 GLN A C     1 
ATOM   15343 O  O     . GLN A 1 3667 ? 201.219 213.483 188.753 1.00 87.50  ? 3667 GLN A O     1 
ATOM   15344 C  CB    . GLN A 1 3667 ? 198.594 214.097 190.498 1.00 85.22  ? 3667 GLN A CB    1 
ATOM   15345 C  CG    . GLN A 1 3667 ? 197.512 214.500 189.515 1.00 85.24  ? 3667 GLN A CG    1 
ATOM   15346 C  CD    . GLN A 1 3667 ? 196.755 215.731 189.963 1.00 87.78  ? 3667 GLN A CD    1 
ATOM   15347 O  OE1   . GLN A 1 3667 ? 197.060 216.317 191.001 1.00 85.52  ? 3667 GLN A OE1   1 
ATOM   15348 N  NE2   . GLN A 1 3667 ? 195.761 216.132 189.180 1.00 87.75  ? 3667 GLN A NE2   1 
ATOM   15349 N  N     . ASP A 1 3668 ? 199.403 212.642 187.714 1.00 81.87  ? 3668 ASP A N     1 
ATOM   15350 C  CA    . ASP A 1 3668 ? 199.926 212.778 186.362 1.00 78.75  ? 3668 ASP A CA    1 
ATOM   15351 C  C     . ASP A 1 3668 ? 199.210 213.934 185.677 1.00 85.69  ? 3668 ASP A C     1 
ATOM   15352 O  O     . ASP A 1 3668 ? 197.978 214.013 185.709 1.00 88.10  ? 3668 ASP A O     1 
ATOM   15353 C  CB    . ASP A 1 3668 ? 199.738 211.479 185.575 1.00 79.33  ? 3668 ASP A CB    1 
ATOM   15354 C  CG    . ASP A 1 3668 ? 200.511 211.462 184.270 1.00 85.86  ? 3668 ASP A CG    1 
ATOM   15355 O  OD1   . ASP A 1 3668 ? 200.841 212.545 183.744 1.00 86.44  ? 3668 ASP A OD1   1 
ATOM   15356 O  OD2   . ASP A 1 3668 ? 200.797 210.354 183.772 1.00 83.36  ? 3668 ASP A OD2   1 
ATOM   15357 N  N     . ILE A 1 3669 ? 199.984 214.827 185.062 1.00 83.35  ? 3669 ILE A N     1 
ATOM   15358 C  CA    . ILE A 1 3669 ? 199.471 216.073 184.508 1.00 79.29  ? 3669 ILE A CA    1 
ATOM   15359 C  C     . ILE A 1 3669 ? 199.997 216.238 183.089 1.00 77.27  ? 3669 ILE A C     1 
ATOM   15360 O  O     . ILE A 1 3669 ? 201.172 215.971 182.818 1.00 80.00  ? 3669 ILE A O     1 
ATOM   15361 C  CB    . ILE A 1 3669 ? 199.869 217.281 185.383 1.00 80.19  ? 3669 ILE A CB    1 
ATOM   15362 C  CG1   . ILE A 1 3669 ? 199.246 217.159 186.773 1.00 79.39  ? 3669 ILE A CG1   1 
ATOM   15363 C  CG2   . ILE A 1 3669 ? 199.444 218.587 184.734 1.00 76.78  ? 3669 ILE A CG2   1 
ATOM   15364 C  CD1   . ILE A 1 3669 ? 199.788 218.153 187.767 1.00 79.69  ? 3669 ILE A CD1   1 
ATOM   15365 N  N     . ASP A 1 3670 ? 199.122 216.671 182.184 1.00 77.04  ? 3670 ASP A N     1 
ATOM   15366 C  CA    . ASP A 1 3670 ? 199.494 216.910 180.793 1.00 77.22  ? 3670 ASP A CA    1 
ATOM   15367 C  C     . ASP A 1 3670 ? 200.152 218.280 180.680 1.00 78.31  ? 3670 ASP A C     1 
ATOM   15368 O  O     . ASP A 1 3670 ? 199.480 219.311 180.784 1.00 78.81  ? 3670 ASP A O     1 
ATOM   15369 C  CB    . ASP A 1 3670 ? 198.268 216.818 179.892 1.00 76.69  ? 3670 ASP A CB    1 
ATOM   15370 C  CG    . ASP A 1 3670 ? 198.605 216.336 178.498 1.00 81.00  ? 3670 ASP A CG    1 
ATOM   15371 O  OD1   . ASP A 1 3670 ? 199.579 216.850 177.907 1.00 79.89  ? 3670 ASP A OD1   1 
ATOM   15372 O  OD2   . ASP A 1 3670 ? 197.892 215.447 177.990 1.00 80.29  ? 3670 ASP A OD2   1 
ATOM   15373 N  N     . LEU A 1 3671 ? 201.464 218.295 180.465 1.00 75.55  ? 3671 LEU A N     1 
ATOM   15374 C  CA    . LEU A 1 3671 ? 202.191 219.550 180.339 1.00 70.12  ? 3671 LEU A CA    1 
ATOM   15375 C  C     . LEU A 1 3671 ? 201.862 220.239 179.020 1.00 72.27  ? 3671 LEU A C     1 
ATOM   15376 O  O     . LEU A 1 3671 ? 201.753 219.595 177.973 1.00 73.94  ? 3671 LEU A O     1 
ATOM   15377 C  CB    . LEU A 1 3671 ? 203.695 219.299 180.435 1.00 71.09  ? 3671 LEU A CB    1 
ATOM   15378 C  CG    . LEU A 1 3671 ? 204.602 220.522 180.298 1.00 73.02  ? 3671 LEU A CG    1 
ATOM   15379 C  CD1   . LEU A 1 3671 ? 204.719 221.247 181.622 1.00 71.47  ? 3671 LEU A CD1   1 
ATOM   15380 C  CD2   . LEU A 1 3671 ? 205.973 220.125 179.777 1.00 72.13  ? 3671 LEU A CD2   1 
ATOM   15381 N  N     . SER A 1 3672 ? 201.711 221.565 179.076 1.00 70.67  ? 3672 SER A N     1 
ATOM   15382 C  CA    . SER A 1 3672 ? 201.478 222.381 177.897 1.00 68.11  ? 3672 SER A CA    1 
ATOM   15383 C  C     . SER A 1 3672 ? 202.769 223.065 177.460 1.00 69.52  ? 3672 SER A C     1 
ATOM   15384 O  O     . SER A 1 3672 ? 203.566 223.480 178.309 1.00 73.11  ? 3672 SER A O     1 
ATOM   15385 C  CB    . SER A 1 3672 ? 200.408 223.443 178.168 1.00 71.64  ? 3672 SER A CB    1 
ATOM   15386 O  OG    . SER A 1 3672 ? 200.198 224.263 177.034 1.00 73.68  ? 3672 SER A OG    1 
ATOM   15387 N  N     . PRO A 1 3673 ? 203.008 223.195 176.152 1.00 70.40  ? 3673 PRO A N     1 
ATOM   15388 C  CA    . PRO A 1 3673 ? 204.287 223.760 175.693 1.00 69.36  ? 3673 PRO A CA    1 
ATOM   15389 C  C     . PRO A 1 3673 ? 204.460 225.239 175.995 1.00 68.90  ? 3673 PRO A C     1 
ATOM   15390 O  O     . PRO A 1 3673 ? 205.590 225.735 175.918 1.00 68.93  ? 3673 PRO A O     1 
ATOM   15391 C  CB    . PRO A 1 3673 ? 204.264 223.500 174.181 1.00 67.63  ? 3673 PRO A CB    1 
ATOM   15392 C  CG    . PRO A 1 3673 ? 202.822 223.397 173.839 1.00 70.57  ? 3673 PRO A CG    1 
ATOM   15393 C  CD    . PRO A 1 3673 ? 202.151 222.779 175.029 1.00 71.34  ? 3673 PRO A CD    1 
ATOM   15394 N  N     . SER A 1 3674 ? 203.392 225.959 176.327 1.00 68.22  ? 3674 SER A N     1 
ATOM   15395 C  CA    . SER A 1 3674 ? 203.476 227.388 176.597 1.00 66.26  ? 3674 SER A CA    1 
ATOM   15396 C  C     . SER A 1 3674 ? 203.644 227.709 178.076 1.00 68.62  ? 3674 SER A C     1 
ATOM   15397 O  O     . SER A 1 3674 ? 203.691 228.889 178.437 1.00 68.29  ? 3674 SER A O     1 
ATOM   15398 C  CB    . SER A 1 3674 ? 202.234 228.101 176.055 1.00 65.08  ? 3674 SER A CB    1 
ATOM   15399 O  OG    . SER A 1 3674 ? 201.073 227.707 176.764 1.00 69.28  ? 3674 SER A OG    1 
ATOM   15400 N  N     . PHE A 1 3675 ? 203.727 226.698 178.936 1.00 63.12  ? 3675 PHE A N     1 
ATOM   15401 C  CA    . PHE A 1 3675 ? 203.929 226.935 180.358 1.00 57.46  ? 3675 PHE A CA    1 
ATOM   15402 C  C     . PHE A 1 3675 ? 205.334 227.459 180.621 1.00 63.76  ? 3675 PHE A C     1 
ATOM   15403 O  O     . PHE A 1 3675 ? 206.307 227.020 180.001 1.00 65.82  ? 3675 PHE A O     1 
ATOM   15404 C  CB    . PHE A 1 3675 ? 203.691 225.649 181.147 1.00 57.13  ? 3675 PHE A CB    1 
ATOM   15405 C  CG    . PHE A 1 3675 ? 204.272 225.665 182.533 1.00 59.06  ? 3675 PHE A CG    1 
ATOM   15406 C  CD1   . PHE A 1 3675 ? 203.613 226.307 183.567 1.00 63.02  ? 3675 PHE A CD1   1 
ATOM   15407 C  CD2   . PHE A 1 3675 ? 205.470 225.026 182.805 1.00 55.10  ? 3675 PHE A CD2   1 
ATOM   15408 C  CE1   . PHE A 1 3675 ? 204.142 226.318 184.841 1.00 58.81  ? 3675 PHE A CE1   1 
ATOM   15409 C  CE2   . PHE A 1 3675 ? 206.002 225.037 184.076 1.00 53.75  ? 3675 PHE A CE2   1 
ATOM   15410 C  CZ    . PHE A 1 3675 ? 205.336 225.680 185.096 1.00 55.45  ? 3675 PHE A CZ    1 
ATOM   15411 N  N     . VAL A 1 3676 ? 205.435 228.408 181.547 1.00 58.63  ? 3676 VAL A N     1 
ATOM   15412 C  CA    . VAL A 1 3676 ? 206.717 228.952 181.980 1.00 51.60  ? 3676 VAL A CA    1 
ATOM   15413 C  C     . VAL A 1 3676 ? 206.554 229.462 183.403 1.00 48.31  ? 3676 VAL A C     1 
ATOM   15414 O  O     . VAL A 1 3676 ? 205.560 230.113 183.731 1.00 57.53  ? 3676 VAL A O     1 
ATOM   15415 C  CB    . VAL A 1 3676 ? 207.214 230.058 181.023 1.00 52.05  ? 3676 VAL A CB    1 
ATOM   15416 C  CG1   . VAL A 1 3676 ? 206.161 231.141 180.854 1.00 56.46  ? 3676 VAL A CG1   1 
ATOM   15417 C  CG2   . VAL A 1 3676 ? 208.519 230.649 181.521 1.00 50.95  ? 3676 VAL A CG2   1 
ATOM   15418 N  N     . ILE A 1 3677 ? 207.524 229.152 184.257 1.00 45.11  ? 3677 ILE A N     1 
ATOM   15419 C  CA    . ILE A 1 3677 ? 207.469 229.520 185.666 1.00 47.90  ? 3677 ILE A CA    1 
ATOM   15420 C  C     . ILE A 1 3677 ? 208.686 230.369 186.004 1.00 52.98  ? 3677 ILE A C     1 
ATOM   15421 O  O     . ILE A 1 3677 ? 209.804 230.074 185.569 1.00 52.44  ? 3677 ILE A O     1 
ATOM   15422 C  CB    . ILE A 1 3677 ? 207.383 228.277 186.577 1.00 45.94  ? 3677 ILE A CB    1 
ATOM   15423 C  CG1   . ILE A 1 3677 ? 207.345 228.689 188.048 1.00 45.86  ? 3677 ILE A CG1   1 
ATOM   15424 C  CG2   . ILE A 1 3677 ? 208.532 227.322 186.307 1.00 48.43  ? 3677 ILE A CG2   1 
ATOM   15425 C  CD1   . ILE A 1 3677 ? 206.943 227.577 188.976 1.00 49.54  ? 3677 ILE A CD1   1 
ATOM   15426 N  N     . PHE A 1 3678 ? 208.457 231.442 186.757 1.00 52.35  ? 3678 PHE A N     1 
ATOM   15427 C  CA    . PHE A 1 3678 ? 209.514 232.324 187.229 1.00 44.21  ? 3678 PHE A CA    1 
ATOM   15428 C  C     . PHE A 1 3678 ? 209.553 232.278 188.747 1.00 50.66  ? 3678 PHE A C     1 
ATOM   15429 O  O     . PHE A 1 3678 ? 208.525 232.467 189.403 1.00 59.57  ? 3678 PHE A O     1 
ATOM   15430 C  CB    . PHE A 1 3678 ? 209.294 233.764 186.757 1.00 47.62  ? 3678 PHE A CB    1 
ATOM   15431 C  CG    . PHE A 1 3678 ? 209.368 233.936 185.269 1.00 51.43  ? 3678 PHE A CG    1 
ATOM   15432 C  CD1   . PHE A 1 3678 ? 208.241 233.781 184.484 1.00 46.36  ? 3678 PHE A CD1   1 
ATOM   15433 C  CD2   . PHE A 1 3678 ? 210.565 234.259 184.656 1.00 49.88  ? 3678 PHE A CD2   1 
ATOM   15434 C  CE1   . PHE A 1 3678 ? 208.307 233.937 183.119 1.00 50.49  ? 3678 PHE A CE1   1 
ATOM   15435 C  CE2   . PHE A 1 3678 ? 210.636 234.419 183.290 1.00 45.12  ? 3678 PHE A CE2   1 
ATOM   15436 C  CZ    . PHE A 1 3678 ? 209.505 234.258 182.521 1.00 51.71  ? 3678 PHE A CZ    1 
ATOM   15437 N  N     . LEU A 1 3679 ? 210.733 232.026 189.302 1.00 46.84  ? 3679 LEU A N     1 
ATOM   15438 C  CA    . LEU A 1 3679 ? 210.932 232.027 190.744 1.00 47.43  ? 3679 LEU A CA    1 
ATOM   15439 C  C     . LEU A 1 3679 ? 211.625 233.321 191.143 1.00 49.35  ? 3679 LEU A C     1 
ATOM   15440 O  O     . LEU A 1 3679 ? 212.592 233.736 190.498 1.00 57.78  ? 3679 LEU A O     1 
ATOM   15441 C  CB    . LEU A 1 3679 ? 211.759 230.819 191.185 1.00 45.96  ? 3679 LEU A CB    1 
ATOM   15442 C  CG    . LEU A 1 3679 ? 211.350 229.463 190.611 1.00 44.73  ? 3679 LEU A CG    1 
ATOM   15443 C  CD1   . LEU A 1 3679 ? 212.270 228.371 191.121 1.00 49.47  ? 3679 LEU A CD1   1 
ATOM   15444 C  CD2   . LEU A 1 3679 ? 209.909 229.151 190.960 1.00 47.39  ? 3679 LEU A CD2   1 
ATOM   15445 N  N     . SER A 1 3680 ? 211.125 233.963 192.195 1.00 44.95  ? 3680 SER A N     1 
ATOM   15446 C  CA    . SER A 1 3680 ? 211.656 235.249 192.616 1.00 48.13  ? 3680 SER A CA    1 
ATOM   15447 C  C     . SER A 1 3680 ? 211.835 235.273 194.125 1.00 47.14  ? 3680 SER A C     1 
ATOM   15448 O  O     . SER A 1 3680 ? 211.158 234.552 194.860 1.00 55.25  ? 3680 SER A O     1 
ATOM   15449 C  CB    . SER A 1 3680 ? 210.748 236.405 192.176 1.00 55.85  ? 3680 SER A CB    1 
ATOM   15450 O  OG    . SER A 1 3680 ? 209.412 236.193 192.588 1.00 58.26  ? 3680 SER A OG    1 
ATOM   15451 N  N     . THR A 1 3681 ? 212.768 236.109 194.575 1.00 54.13  ? 3681 THR A N     1 
ATOM   15452 C  CA    . THR A 1 3681 ? 213.003 236.326 195.993 1.00 54.78  ? 3681 THR A CA    1 
ATOM   15453 C  C     . THR A 1 3681 ? 213.442 237.767 196.200 1.00 58.40  ? 3681 THR A C     1 
ATOM   15454 O  O     . THR A 1 3681 ? 214.029 238.387 195.310 1.00 58.77  ? 3681 THR A O     1 
ATOM   15455 C  CB    . THR A 1 3681 ? 214.058 235.366 196.556 1.00 53.56  ? 3681 THR A CB    1 
ATOM   15456 O  OG1   . THR A 1 3681 ? 214.195 235.575 197.966 1.00 63.32  ? 3681 THR A OG1   1 
ATOM   15457 C  CG2   . THR A 1 3681 ? 215.402 235.589 195.885 1.00 54.41  ? 3681 THR A CG2   1 
ATOM   15458 N  N     . ARG A 1 3682 ? 213.142 238.297 197.382 1.00 58.53  ? 3682 ARG A N     1 
ATOM   15459 C  CA    . ARG A 1 3682 ? 213.541 239.645 197.753 1.00 50.82  ? 3682 ARG A CA    1 
ATOM   15460 C  C     . ARG A 1 3682 ? 214.748 239.670 198.677 1.00 55.03  ? 3682 ARG A C     1 
ATOM   15461 O  O     . ARG A 1 3682 ? 215.170 240.752 199.092 1.00 63.25  ? 3682 ARG A O     1 
ATOM   15462 C  CB    . ARG A 1 3682 ? 212.375 240.378 198.419 1.00 56.06  ? 3682 ARG A CB    1 
ATOM   15463 C  CG    . ARG A 1 3682 ? 211.248 240.753 197.478 1.00 55.91  ? 3682 ARG A CG    1 
ATOM   15464 C  CD    . ARG A 1 3682 ? 210.153 241.500 198.218 1.00 58.28  ? 3682 ARG A CD    1 
ATOM   15465 N  NE    . ARG A 1 3682 ? 209.520 240.671 199.237 1.00 62.51  ? 3682 ARG A NE    1 
ATOM   15466 C  CZ    . ARG A 1 3682 ? 209.757 240.770 200.537 1.00 61.42  ? 3682 ARG A CZ    1 
ATOM   15467 N  NH1   . ARG A 1 3682 ? 210.613 241.656 201.018 1.00 60.59  ? 3682 ARG A NH1   1 
ATOM   15468 N  NH2   . ARG A 1 3682 ? 209.121 239.958 201.377 1.00 56.79  ? 3682 ARG A NH2   1 
ATOM   15469 N  N     . ASP A 1 3683 ? 215.311 238.511 199.009 1.00 59.90  ? 3683 ASP A N     1 
ATOM   15470 C  CA    . ASP A 1 3683 ? 216.445 238.447 199.916 1.00 63.34  ? 3683 ASP A CA    1 
ATOM   15471 C  C     . ASP A 1 3683 ? 217.713 238.213 199.114 1.00 64.36  ? 3683 ASP A C     1 
ATOM   15472 O  O     . ASP A 1 3683 ? 217.912 237.102 198.601 1.00 67.96  ? 3683 ASP A O     1 
ATOM   15473 C  CB    . ASP A 1 3683 ? 216.250 237.333 200.941 1.00 64.93  ? 3683 ASP A CB    1 
ATOM   15474 C  CG    . ASP A 1 3683 ? 217.205 237.443 202.113 1.00 68.48  ? 3683 ASP A CG    1 
ATOM   15475 O  OD1   . ASP A 1 3683 ? 217.963 238.433 202.177 1.00 70.91  ? 3683 ASP A OD1   1 
ATOM   15476 O  OD2   . ASP A 1 3683 ? 217.198 236.538 202.973 1.00 68.67  ? 3683 ASP A OD2   1 
ATOM   15477 N  N     . PRO A 1 3684 ? 218.594 239.208 198.974 1.00 67.42  ? 3684 PRO A N     1 
ATOM   15478 C  CA    . PRO A 1 3684 ? 219.876 238.966 198.302 1.00 67.04  ? 3684 PRO A CA    1 
ATOM   15479 C  C     . PRO A 1 3684 ? 220.870 238.200 199.153 1.00 69.10  ? 3684 PRO A C     1 
ATOM   15480 O  O     . PRO A 1 3684 ? 221.917 237.789 198.633 1.00 71.48  ? 3684 PRO A O     1 
ATOM   15481 C  CB    . PRO A 1 3684 ? 220.383 240.382 198.009 1.00 68.31  ? 3684 PRO A CB    1 
ATOM   15482 C  CG    . PRO A 1 3684 ? 219.791 241.210 199.092 1.00 65.73  ? 3684 PRO A CG    1 
ATOM   15483 C  CD    . PRO A 1 3684 ? 218.446 240.610 199.401 1.00 66.86  ? 3684 PRO A CD    1 
ATOM   15484 N  N     . THR A 1 3685 ? 220.578 237.997 200.436 1.00 73.70  ? 3685 THR A N     1 
ATOM   15485 C  CA    . THR A 1 3685 ? 221.475 237.311 201.354 1.00 72.00  ? 3685 THR A CA    1 
ATOM   15486 C  C     . THR A 1 3685 ? 221.084 235.857 201.586 1.00 70.43  ? 3685 THR A C     1 
ATOM   15487 O  O     . THR A 1 3685 ? 221.663 235.204 202.459 1.00 70.46  ? 3685 THR A O     1 
ATOM   15488 C  CB    . THR A 1 3685 ? 221.528 238.050 202.692 1.00 74.19  ? 3685 THR A CB    1 
ATOM   15489 O  OG1   . THR A 1 3685 ? 220.211 238.123 203.252 1.00 71.64  ? 3685 THR A OG1   1 
ATOM   15490 C  CG2   . THR A 1 3685 ? 222.075 239.456 202.504 1.00 70.54  ? 3685 THR A CG2   1 
ATOM   15491 N  N     . VAL A 1 3686 ? 220.124 235.339 200.832 1.00 74.34  ? 3686 VAL A N     1 
ATOM   15492 C  CA    . VAL A 1 3686 ? 219.676 233.964 201.013 1.00 74.09  ? 3686 VAL A CA    1 
ATOM   15493 C  C     . VAL A 1 3686 ? 220.643 233.019 200.314 1.00 74.07  ? 3686 VAL A C     1 
ATOM   15494 O  O     . VAL A 1 3686 ? 221.218 233.345 199.268 1.00 75.30  ? 3686 VAL A O     1 
ATOM   15495 C  CB    . VAL A 1 3686 ? 218.234 233.794 200.502 1.00 73.70  ? 3686 VAL A CB    1 
ATOM   15496 C  CG1   . VAL A 1 3686 ? 218.191 233.810 198.989 1.00 73.58  ? 3686 VAL A CG1   1 
ATOM   15497 C  CG2   . VAL A 1 3686 ? 217.624 232.511 201.045 1.00 72.40  ? 3686 VAL A CG2   1 
ATOM   15498 N  N     . GLU A 1 3687 ? 220.847 231.850 200.913 1.00 76.67  ? 3687 GLU A N     1 
ATOM   15499 C  CA    . GLU A 1 3687 ? 221.745 230.830 200.392 1.00 74.98  ? 3687 GLU A CA    1 
ATOM   15500 C  C     . GLU A 1 3687 ? 220.925 229.626 199.955 1.00 73.59  ? 3687 GLU A C     1 
ATOM   15501 O  O     . GLU A 1 3687 ? 220.096 229.125 200.721 1.00 75.26  ? 3687 GLU A O     1 
ATOM   15502 C  CB    . GLU A 1 3687 ? 222.776 230.424 201.447 1.00 75.15  ? 3687 GLU A CB    1 
ATOM   15503 C  CG    . GLU A 1 3687 ? 223.729 229.327 201.008 1.00 76.74  ? 3687 GLU A CG    1 
ATOM   15504 C  CD    . GLU A 1 3687 ? 224.334 228.584 202.183 1.00 79.23  ? 3687 GLU A CD    1 
ATOM   15505 O  OE1   . GLU A 1 3687 ? 224.524 229.209 203.248 1.00 75.83  ? 3687 GLU A OE1   1 
ATOM   15506 O  OE2   . GLU A 1 3687 ? 224.617 227.376 202.044 1.00 79.67  ? 3687 GLU A OE2   1 
ATOM   15507 N  N     . PHE A 1 3688 ? 221.155 229.167 198.729 1.00 61.79  ? 3688 PHE A N     1 
ATOM   15508 C  CA    . PHE A 1 3688 ? 220.376 228.068 198.189 1.00 65.78  ? 3688 PHE A CA    1 
ATOM   15509 C  C     . PHE A 1 3688 ? 221.191 226.780 198.172 1.00 68.38  ? 3688 PHE A C     1 
ATOM   15510 O  O     . PHE A 1 3688 ? 222.408 226.809 197.963 1.00 67.55  ? 3688 PHE A O     1 
ATOM   15511 C  CB    . PHE A 1 3688 ? 219.898 228.378 196.765 1.00 62.84  ? 3688 PHE A CB    1 
ATOM   15512 C  CG    . PHE A 1 3688 ? 218.920 229.511 196.687 1.00 64.64  ? 3688 PHE A CG    1 
ATOM   15513 C  CD1   . PHE A 1 3688 ? 217.604 229.335 197.073 1.00 65.93  ? 3688 PHE A CD1   1 
ATOM   15514 C  CD2   . PHE A 1 3688 ? 219.313 230.751 196.218 1.00 60.90  ? 3688 PHE A CD2   1 
ATOM   15515 C  CE1   . PHE A 1 3688 ? 216.701 230.374 196.998 1.00 63.63  ? 3688 PHE A CE1   1 
ATOM   15516 C  CE2   . PHE A 1 3688 ? 218.415 231.793 196.141 1.00 59.82  ? 3688 PHE A CE2   1 
ATOM   15517 C  CZ    . PHE A 1 3688 ? 217.107 231.604 196.532 1.00 61.55  ? 3688 PHE A CZ    1 
ATOM   15518 N  N     . PRO A 1 3689 ? 220.552 225.636 198.396 1.00 63.58  ? 3689 PRO A N     1 
ATOM   15519 C  CA    . PRO A 1 3689 ? 221.261 224.356 198.313 1.00 58.93  ? 3689 PRO A CA    1 
ATOM   15520 C  C     . PRO A 1 3689 ? 221.680 224.064 196.884 1.00 59.46  ? 3689 PRO A C     1 
ATOM   15521 O  O     . PRO A 1 3689 ? 221.052 224.557 195.935 1.00 60.73  ? 3689 PRO A O     1 
ATOM   15522 C  CB    . PRO A 1 3689 ? 220.220 223.343 198.809 1.00 59.38  ? 3689 PRO A CB    1 
ATOM   15523 C  CG    . PRO A 1 3689 ? 218.907 224.002 198.563 1.00 59.41  ? 3689 PRO A CG    1 
ATOM   15524 C  CD    . PRO A 1 3689 ? 219.139 225.466 198.774 1.00 57.50  ? 3689 PRO A CD    1 
ATOM   15525 N  N     . PRO A 1 3690 ? 222.740 223.276 196.688 1.00 63.05  ? 3690 PRO A N     1 
ATOM   15526 C  CA    . PRO A 1 3690 ? 223.190 222.985 195.316 1.00 57.86  ? 3690 PRO A CA    1 
ATOM   15527 C  C     . PRO A 1 3690 ? 222.135 222.310 194.458 1.00 55.61  ? 3690 PRO A C     1 
ATOM   15528 O  O     . PRO A 1 3690 ? 222.134 222.497 193.234 1.00 57.29  ? 3690 PRO A O     1 
ATOM   15529 C  CB    . PRO A 1 3690 ? 224.408 222.076 195.532 1.00 52.12  ? 3690 PRO A CB    1 
ATOM   15530 C  CG    . PRO A 1 3690 ? 224.846 222.340 196.931 1.00 53.02  ? 3690 PRO A CG    1 
ATOM   15531 C  CD    . PRO A 1 3690 ? 223.603 222.644 197.699 1.00 58.30  ? 3690 PRO A CD    1 
ATOM   15532 N  N     . ASP A 1 3691 ? 221.235 221.529 195.059 1.00 50.34  ? 3691 ASP A N     1 
ATOM   15533 C  CA    . ASP A 1 3691 ? 220.193 220.875 194.275 1.00 49.84  ? 3691 ASP A CA    1 
ATOM   15534 C  C     . ASP A 1 3691 ? 219.281 221.896 193.605 1.00 55.63  ? 3691 ASP A C     1 
ATOM   15535 O  O     . ASP A 1 3691 ? 218.922 221.737 192.434 1.00 63.50  ? 3691 ASP A O     1 
ATOM   15536 C  CB    . ASP A 1 3691 ? 219.391 219.916 195.154 1.00 56.92  ? 3691 ASP A CB    1 
ATOM   15537 C  CG    . ASP A 1 3691 ? 218.725 220.609 196.323 1.00 67.41  ? 3691 ASP A CG    1 
ATOM   15538 O  OD1   . ASP A 1 3691 ? 217.626 221.173 196.135 1.00 70.14  ? 3691 ASP A OD1   1 
ATOM   15539 O  OD2   . ASP A 1 3691 ? 219.298 220.585 197.432 1.00 64.06  ? 3691 ASP A OD2   1 
ATOM   15540 N  N     . LEU A 1 3692 ? 218.899 222.951 194.326 1.00 53.71  ? 3692 LEU A N     1 
ATOM   15541 C  CA    . LEU A 1 3692 ? 218.118 224.018 193.710 1.00 49.24  ? 3692 LEU A CA    1 
ATOM   15542 C  C     . LEU A 1 3692 ? 218.970 224.894 192.804 1.00 50.50  ? 3692 LEU A C     1 
ATOM   15543 O  O     . LEU A 1 3692 ? 218.481 225.375 191.777 1.00 57.26  ? 3692 LEU A O     1 
ATOM   15544 C  CB    . LEU A 1 3692 ? 217.443 224.871 194.784 1.00 51.54  ? 3692 LEU A CB    1 
ATOM   15545 C  CG    . LEU A 1 3692 ? 216.572 226.023 194.278 1.00 49.48  ? 3692 LEU A CG    1 
ATOM   15546 C  CD1   . LEU A 1 3692 ? 215.536 225.519 193.289 1.00 47.18  ? 3692 LEU A CD1   1 
ATOM   15547 C  CD2   . LEU A 1 3692 ? 215.902 226.738 195.434 1.00 51.84  ? 3692 LEU A CD2   1 
ATOM   15548 N  N     . CYS A 1 3693 ? 220.239 225.110 193.159 1.00 45.47  ? 3693 CYS A N     1 
ATOM   15549 C  CA    . CYS A 1 3693 ? 221.125 225.901 192.315 1.00 41.82  ? 3693 CYS A CA    1 
ATOM   15550 C  C     . CYS A 1 3693 ? 221.368 225.252 190.961 1.00 50.15  ? 3693 CYS A C     1 
ATOM   15551 O  O     . CYS A 1 3693 ? 221.705 225.954 190.002 1.00 57.66  ? 3693 CYS A O     1 
ATOM   15552 C  CB    . CYS A 1 3693 ? 222.463 226.127 193.018 1.00 48.28  ? 3693 CYS A CB    1 
ATOM   15553 S  SG    . CYS A 1 3693 ? 222.370 227.147 194.499 1.00 63.46  ? 3693 CYS A SG    1 
ATOM   15554 N  N     . SER A 1 3694 ? 221.217 223.933 190.862 1.00 44.27  ? 3694 SER A N     1 
ATOM   15555 C  CA    . SER A 1 3694 ? 221.413 223.244 189.594 1.00 36.78  ? 3694 SER A CA    1 
ATOM   15556 C  C     . SER A 1 3694 ? 220.227 223.379 188.649 1.00 45.75  ? 3694 SER A C     1 
ATOM   15557 O  O     . SER A 1 3694 ? 220.418 223.357 187.429 1.00 48.24  ? 3694 SER A O     1 
ATOM   15558 C  CB    . SER A 1 3694 ? 221.697 221.760 189.839 1.00 40.14  ? 3694 SER A CB    1 
ATOM   15559 O  OG    . SER A 1 3694 ? 220.699 221.176 190.656 1.00 48.66  ? 3694 SER A OG    1 
ATOM   15560 N  N     . ARG A 1 3695 ? 219.012 223.525 189.177 1.00 47.87  ? 3695 ARG A N     1 
ATOM   15561 C  CA    . ARG A 1 3695 ? 217.807 223.483 188.359 1.00 42.24  ? 3695 ARG A CA    1 
ATOM   15562 C  C     . ARG A 1 3695 ? 217.360 224.844 187.841 1.00 46.31  ? 3695 ARG A C     1 
ATOM   15563 O  O     . ARG A 1 3695 ? 216.422 224.898 187.040 1.00 50.77  ? 3695 ARG A O     1 
ATOM   15564 C  CB    . ARG A 1 3695 ? 216.653 222.859 189.149 1.00 35.26  ? 3695 ARG A CB    1 
ATOM   15565 C  CG    . ARG A 1 3695 ? 217.002 221.585 189.885 1.00 37.00  ? 3695 ARG A CG    1 
ATOM   15566 C  CD    . ARG A 1 3695 ? 215.812 221.089 190.683 1.00 41.00  ? 3695 ARG A CD    1 
ATOM   15567 N  NE    . ARG A 1 3695 ? 216.209 220.481 191.946 1.00 49.08  ? 3695 ARG A NE    1 
ATOM   15568 C  CZ    . ARG A 1 3695 ? 216.509 219.200 192.101 1.00 53.96  ? 3695 ARG A CZ    1 
ATOM   15569 N  NH1   . ARG A 1 3695 ? 216.473 218.355 191.085 1.00 47.51  ? 3695 ARG A NH1   1 
ATOM   15570 N  NH2   . ARG A 1 3695 ? 216.853 218.754 193.305 1.00 52.26  ? 3695 ARG A NH2   1 
ATOM   15571 N  N     . VAL A 1 3696 ? 217.988 225.938 188.272 1.00 41.23  ? 3696 VAL A N     1 
ATOM   15572 C  CA    . VAL A 1 3696 ? 217.544 227.276 187.907 1.00 38.80  ? 3696 VAL A CA    1 
ATOM   15573 C  C     . VAL A 1 3696 ? 218.734 228.105 187.447 1.00 40.90  ? 3696 VAL A C     1 
ATOM   15574 O  O     . VAL A 1 3696 ? 219.889 227.809 187.758 1.00 46.69  ? 3696 VAL A O     1 
ATOM   15575 C  CB    . VAL A 1 3696 ? 216.826 227.994 189.070 1.00 37.51  ? 3696 VAL A CB    1 
ATOM   15576 C  CG1   . VAL A 1 3696 ? 215.586 227.224 189.498 1.00 32.59  ? 3696 VAL A CG1   1 
ATOM   15577 C  CG2   . VAL A 1 3696 ? 217.776 228.180 190.236 1.00 40.73  ? 3696 VAL A CG2   1 
ATOM   15578 N  N     . THR A 1 3697 ? 218.432 229.158 186.692 1.00 34.75  ? 3697 THR A N     1 
ATOM   15579 C  CA    . THR A 1 3697 ? 219.407 230.172 186.312 1.00 38.32  ? 3697 THR A CA    1 
ATOM   15580 C  C     . THR A 1 3697 ? 219.161 231.404 187.170 1.00 37.99  ? 3697 THR A C     1 
ATOM   15581 O  O     . THR A 1 3697 ? 218.052 231.945 187.179 1.00 43.71  ? 3697 THR A O     1 
ATOM   15582 C  CB    . THR A 1 3697 ? 219.304 230.525 184.828 1.00 34.21  ? 3697 THR A CB    1 
ATOM   15583 O  OG1   . THR A 1 3697 ? 218.008 231.063 184.548 1.00 34.64  ? 3697 THR A OG1   1 
ATOM   15584 C  CG2   . THR A 1 3697 ? 219.527 229.297 183.969 1.00 48.43  ? 3697 THR A CG2   1 
ATOM   15585 N  N     . PHE A 1 3698 ? 220.187 231.840 187.892 1.00 40.15  ? 3698 PHE A N     1 
ATOM   15586 C  CA    . PHE A 1 3698 ? 220.047 232.989 188.772 1.00 33.01  ? 3698 PHE A CA    1 
ATOM   15587 C  C     . PHE A 1 3698 ? 220.101 234.278 187.966 1.00 43.33  ? 3698 PHE A C     1 
ATOM   15588 O  O     . PHE A 1 3698 ? 220.999 234.468 187.141 1.00 50.78  ? 3698 PHE A O     1 
ATOM   15589 C  CB    . PHE A 1 3698 ? 221.139 232.981 189.837 1.00 33.71  ? 3698 PHE A CB    1 
ATOM   15590 C  CG    . PHE A 1 3698 ? 220.982 231.892 190.851 1.00 33.08  ? 3698 PHE A CG    1 
ATOM   15591 C  CD1   . PHE A 1 3698 ? 220.026 231.990 191.844 1.00 36.78  ? 3698 PHE A CD1   1 
ATOM   15592 C  CD2   . PHE A 1 3698 ? 221.784 230.768 190.808 1.00 38.34  ? 3698 PHE A CD2   1 
ATOM   15593 C  CE1   . PHE A 1 3698 ? 219.876 230.989 192.776 1.00 41.41  ? 3698 PHE A CE1   1 
ATOM   15594 C  CE2   . PHE A 1 3698 ? 221.638 229.765 191.738 1.00 46.79  ? 3698 PHE A CE2   1 
ATOM   15595 C  CZ    . PHE A 1 3698 ? 220.683 229.875 192.723 1.00 45.22  ? 3698 PHE A CZ    1 
ATOM   15596 N  N     . VAL A 1 3699 ? 219.139 235.157 188.204 1.00 44.59  ? 3699 VAL A N     1 
ATOM   15597 C  CA    . VAL A 1 3699 ? 219.087 236.469 187.568 1.00 37.22  ? 3699 VAL A CA    1 
ATOM   15598 C  C     . VAL A 1 3699 ? 219.110 237.487 188.702 1.00 35.94  ? 3699 VAL A C     1 
ATOM   15599 O  O     . VAL A 1 3699 ? 218.074 237.842 189.268 1.00 46.16  ? 3699 VAL A O     1 
ATOM   15600 C  CB    . VAL A 1 3699 ? 217.855 236.640 186.677 1.00 34.00  ? 3699 VAL A CB    1 
ATOM   15601 C  CG1   . VAL A 1 3699 ? 217.926 237.949 185.933 1.00 38.84  ? 3699 VAL A CG1   1 
ATOM   15602 C  CG2   . VAL A 1 3699 ? 217.738 235.482 185.705 1.00 36.45  ? 3699 VAL A CG2   1 
ATOM   15603 N  N     . ASN A 1 3700 ? 220.303 237.965 189.043 1.00 32.81  ? 3700 ASN A N     1 
ATOM   15604 C  CA    . ASN A 1 3700 ? 220.503 238.820 190.208 1.00 33.53  ? 3700 ASN A CA    1 
ATOM   15605 C  C     . ASN A 1 3700 ? 220.359 240.280 189.795 1.00 40.24  ? 3700 ASN A C     1 
ATOM   15606 O  O     . ASN A 1 3700 ? 221.226 240.825 189.104 1.00 44.92  ? 3700 ASN A O     1 
ATOM   15607 C  CB    . ASN A 1 3700 ? 221.875 238.560 190.824 1.00 40.86  ? 3700 ASN A CB    1 
ATOM   15608 C  CG    . ASN A 1 3700 ? 221.926 238.890 192.299 1.00 38.43  ? 3700 ASN A CG    1 
ATOM   15609 O  OD1   . ASN A 1 3700 ? 221.049 239.572 192.825 1.00 43.76  ? 3700 ASN A OD1   1 
ATOM   15610 N  ND2   . ASN A 1 3700 ? 222.960 238.411 192.975 1.00 39.68  ? 3700 ASN A ND2   1 
ATOM   15611 N  N     . PHE A 1 3701 ? 219.269 240.916 190.221 1.00 34.44  ? 3701 PHE A N     1 
ATOM   15612 C  CA    . PHE A 1 3701 ? 219.068 242.348 190.003 1.00 34.88  ? 3701 PHE A CA    1 
ATOM   15613 C  C     . PHE A 1 3701 ? 219.725 243.095 191.154 1.00 39.42  ? 3701 PHE A C     1 
ATOM   15614 O  O     . PHE A 1 3701 ? 219.108 243.361 192.185 1.00 43.37  ? 3701 PHE A O     1 
ATOM   15615 C  CB    . PHE A 1 3701 ? 217.587 242.689 189.894 1.00 39.62  ? 3701 PHE A CB    1 
ATOM   15616 C  CG    . PHE A 1 3701 ? 216.958 242.281 188.595 1.00 43.34  ? 3701 PHE A CG    1 
ATOM   15617 C  CD1   . PHE A 1 3701 ? 216.594 240.967 188.365 1.00 38.00  ? 3701 PHE A CD1   1 
ATOM   15618 C  CD2   . PHE A 1 3701 ? 216.731 243.216 187.602 1.00 41.48  ? 3701 PHE A CD2   1 
ATOM   15619 C  CE1   . PHE A 1 3701 ? 216.014 240.597 187.171 1.00 37.73  ? 3701 PHE A CE1   1 
ATOM   15620 C  CE2   . PHE A 1 3701 ? 216.153 242.850 186.406 1.00 37.15  ? 3701 PHE A CE2   1 
ATOM   15621 C  CZ    . PHE A 1 3701 ? 215.793 241.540 186.191 1.00 40.79  ? 3701 PHE A CZ    1 
ATOM   15622 N  N     . THR A 1 3702 ? 220.997 243.438 190.978 1.00 41.27  ? 3702 THR A N     1 
ATOM   15623 C  CA    . THR A 1 3702 ? 221.726 244.204 191.973 1.00 35.91  ? 3702 THR A CA    1 
ATOM   15624 C  C     . THR A 1 3702 ? 221.609 245.696 191.668 1.00 44.18  ? 3702 THR A C     1 
ATOM   15625 O  O     . THR A 1 3702 ? 220.943 246.116 190.719 1.00 46.13  ? 3702 THR A O     1 
ATOM   15626 C  CB    . THR A 1 3702 ? 223.191 243.775 192.020 1.00 38.13  ? 3702 THR A CB    1 
ATOM   15627 O  OG1   . THR A 1 3702 ? 223.848 244.188 190.817 1.00 48.29  ? 3702 THR A OG1   1 
ATOM   15628 C  CG2   . THR A 1 3702 ? 223.303 242.270 192.154 1.00 39.55  ? 3702 THR A CG2   1 
ATOM   15629 N  N     . VAL A 1 3703 ? 222.266 246.510 192.488 1.00 46.16  ? 3703 VAL A N     1 
ATOM   15630 C  CA    . VAL A 1 3703 ? 222.327 247.952 192.289 1.00 46.20  ? 3703 VAL A CA    1 
ATOM   15631 C  C     . VAL A 1 3703 ? 223.757 248.324 191.935 1.00 47.14  ? 3703 VAL A C     1 
ATOM   15632 O  O     . VAL A 1 3703 ? 224.695 247.978 192.664 1.00 51.27  ? 3703 VAL A O     1 
ATOM   15633 C  CB    . VAL A 1 3703 ? 221.856 248.710 193.541 1.00 47.72  ? 3703 VAL A CB    1 
ATOM   15634 C  CG1   . VAL A 1 3703 ? 222.027 250.204 193.348 1.00 44.05  ? 3703 VAL A CG1   1 
ATOM   15635 C  CG2   . VAL A 1 3703 ? 220.411 248.372 193.853 1.00 51.30  ? 3703 VAL A CG2   1 
ATOM   15636 N  N     . THR A 1 3704 ? 223.929 249.021 190.819 1.00 41.57  ? 3704 THR A N     1 
ATOM   15637 C  CA    . THR A 1 3704 ? 225.240 249.456 190.367 1.00 46.07  ? 3704 THR A CA    1 
ATOM   15638 C  C     . THR A 1 3704 ? 225.432 250.937 190.665 1.00 43.51  ? 3704 THR A C     1 
ATOM   15639 O  O     . THR A 1 3704 ? 224.471 251.674 190.895 1.00 47.70  ? 3704 THR A O     1 
ATOM   15640 C  CB    . THR A 1 3704 ? 225.421 249.197 188.871 1.00 51.27  ? 3704 THR A CB    1 
ATOM   15641 O  OG1   . THR A 1 3704 ? 224.507 250.012 188.128 1.00 50.15  ? 3704 THR A OG1   1 
ATOM   15642 C  CG2   . THR A 1 3704 ? 225.157 247.738 188.551 1.00 50.74  ? 3704 THR A CG2   1 
ATOM   15643 N  N     . ARG A 1 3705 ? 226.696 251.364 190.674 1.00 47.16  ? 3705 ARG A N     1 
ATOM   15644 C  CA    . ARG A 1 3705 ? 226.999 252.764 190.947 1.00 42.09  ? 3705 ARG A CA    1 
ATOM   15645 C  C     . ARG A 1 3705 ? 226.453 253.674 189.855 1.00 48.23  ? 3705 ARG A C     1 
ATOM   15646 O  O     . ARG A 1 3705 ? 225.889 254.733 190.147 1.00 54.90  ? 3705 ARG A O     1 
ATOM   15647 C  CB    . ARG A 1 3705 ? 228.507 252.956 191.097 1.00 43.44  ? 3705 ARG A CB    1 
ATOM   15648 C  CG    . ARG A 1 3705 ? 229.190 251.848 191.874 1.00 48.99  ? 3705 ARG A CG    1 
ATOM   15649 C  CD    . ARG A 1 3705 ? 230.569 252.264 192.352 1.00 50.20  ? 3705 ARG A CD    1 
ATOM   15650 N  NE    . ARG A 1 3705 ? 230.504 253.238 193.434 1.00 53.72  ? 3705 ARG A NE    1 
ATOM   15651 C  CZ    . ARG A 1 3705 ? 230.960 253.023 194.660 1.00 54.94  ? 3705 ARG A CZ    1 
ATOM   15652 N  NH1   . ARG A 1 3705 ? 231.498 251.865 195.004 1.00 44.30  ? 3705 ARG A NH1   1 
ATOM   15653 N  NH2   . ARG A 1 3705 ? 230.870 253.993 195.565 1.00 52.58  ? 3705 ARG A NH2   1 
ATOM   15654 N  N     . SER A 1 3706 ? 226.611 253.281 188.590 1.00 45.75  ? 3706 SER A N     1 
ATOM   15655 C  CA    . SER A 1 3706 ? 226.178 254.135 187.488 1.00 41.43  ? 3706 SER A CA    1 
ATOM   15656 C  C     . SER A 1 3706 ? 224.665 254.316 187.486 1.00 44.95  ? 3706 SER A C     1 
ATOM   15657 O  O     . SER A 1 3706 ? 224.160 255.429 187.293 1.00 54.46  ? 3706 SER A O     1 
ATOM   15658 C  CB    . SER A 1 3706 ? 226.657 253.550 186.160 1.00 48.26  ? 3706 SER A CB    1 
ATOM   15659 O  OG    . SER A 1 3706 ? 226.219 252.212 186.005 1.00 55.20  ? 3706 SER A OG    1 
ATOM   15660 N  N     . SER A 1 3707 ? 223.921 253.228 187.694 1.00 40.05  ? 3707 SER A N     1 
ATOM   15661 C  CA    . SER A 1 3707 ? 222.465 253.317 187.695 1.00 40.87  ? 3707 SER A CA    1 
ATOM   15662 C  C     . SER A 1 3707 ? 221.969 254.175 188.851 1.00 46.25  ? 3707 SER A C     1 
ATOM   15663 O  O     . SER A 1 3707 ? 221.041 254.976 188.692 1.00 53.65  ? 3707 SER A O     1 
ATOM   15664 C  CB    . SER A 1 3707 ? 221.853 251.919 187.760 1.00 45.01  ? 3707 SER A CB    1 
ATOM   15665 O  OG    . SER A 1 3707 ? 222.247 251.244 188.940 1.00 47.62  ? 3707 SER A OG    1 
ATOM   15666 N  N     . LEU A 1 3708 ? 222.577 254.021 190.029 1.00 40.34  ? 3708 LEU A N     1 
ATOM   15667 C  CA    . LEU A 1 3708 ? 222.180 254.837 191.170 1.00 36.81  ? 3708 LEU A CA    1 
ATOM   15668 C  C     . LEU A 1 3708 ? 222.530 256.304 190.954 1.00 47.20  ? 3708 LEU A C     1 
ATOM   15669 O  O     . LEU A 1 3708 ? 221.763 257.191 191.340 1.00 56.56  ? 3708 LEU A O     1 
ATOM   15670 C  CB    . LEU A 1 3708 ? 222.830 254.315 192.447 1.00 39.54  ? 3708 LEU A CB    1 
ATOM   15671 C  CG    . LEU A 1 3708 ? 222.296 254.964 193.722 1.00 39.44  ? 3708 LEU A CG    1 
ATOM   15672 C  CD1   . LEU A 1 3708 ? 220.836 254.614 193.930 1.00 45.04  ? 3708 LEU A CD1   1 
ATOM   15673 C  CD2   . LEU A 1 3708 ? 223.120 254.543 194.911 1.00 40.92  ? 3708 LEU A CD2   1 
ATOM   15674 N  N     . GLN A 1 3709 ? 223.687 256.580 190.348 1.00 41.47  ? 3709 GLN A N     1 
ATOM   15675 C  CA    . GLN A 1 3709 ? 224.041 257.959 190.029 1.00 37.04  ? 3709 GLN A CA    1 
ATOM   15676 C  C     . GLN A 1 3709 ? 223.032 258.569 189.069 1.00 49.53  ? 3709 GLN A C     1 
ATOM   15677 O  O     . GLN A 1 3709 ? 222.603 259.713 189.248 1.00 61.05  ? 3709 GLN A O     1 
ATOM   15678 C  CB    . GLN A 1 3709 ? 225.446 258.022 189.432 1.00 36.52  ? 3709 GLN A CB    1 
ATOM   15679 C  CG    . GLN A 1 3709 ? 226.554 257.789 190.429 1.00 48.15  ? 3709 GLN A CG    1 
ATOM   15680 C  CD    . GLN A 1 3709 ? 227.922 257.801 189.790 1.00 53.98  ? 3709 GLN A CD    1 
ATOM   15681 O  OE1   . GLN A 1 3709 ? 228.061 258.088 188.603 1.00 54.58  ? 3709 GLN A OE1   1 
ATOM   15682 N  NE2   . GLN A 1 3709 ? 228.944 257.478 190.573 1.00 51.24  ? 3709 GLN A NE2   1 
ATOM   15683 N  N     . SER A 1 3710 ? 222.638 257.816 188.041 1.00 43.75  ? 3710 SER A N     1 
ATOM   15684 C  CA    . SER A 1 3710 ? 221.644 258.319 187.100 1.00 41.14  ? 3710 SER A CA    1 
ATOM   15685 C  C     . SER A 1 3710 ? 220.308 258.565 187.789 1.00 47.46  ? 3710 SER A C     1 
ATOM   15686 O  O     . SER A 1 3710 ? 219.655 259.589 187.551 1.00 58.27  ? 3710 SER A O     1 
ATOM   15687 C  CB    . SER A 1 3710 ? 221.479 257.339 185.941 1.00 45.81  ? 3710 SER A CB    1 
ATOM   15688 O  OG    . SER A 1 3710 ? 222.731 257.038 185.353 1.00 51.67  ? 3710 SER A OG    1 
ATOM   15689 N  N     . GLN A 1 3711 ? 219.890 257.639 188.653 1.00 39.31  ? 3711 GLN A N     1 
ATOM   15690 C  CA    . GLN A 1 3711 ? 218.617 257.785 189.351 1.00 43.74  ? 3711 GLN A CA    1 
ATOM   15691 C  C     . GLN A 1 3711 ? 218.622 259.005 190.266 1.00 45.79  ? 3711 GLN A C     1 
ATOM   15692 O  O     . GLN A 1 3711 ? 217.663 259.786 190.280 1.00 53.54  ? 3711 GLN A O     1 
ATOM   15693 C  CB    . GLN A 1 3711 ? 218.322 256.509 190.138 1.00 45.67  ? 3711 GLN A CB    1 
ATOM   15694 C  CG    . GLN A 1 3711 ? 217.136 256.590 191.074 1.00 51.27  ? 3711 GLN A CG    1 
ATOM   15695 C  CD    . GLN A 1 3711 ? 216.901 255.285 191.808 1.00 55.28  ? 3711 GLN A CD    1 
ATOM   15696 O  OE1   . GLN A 1 3711 ? 217.617 254.306 191.600 1.00 45.36  ? 3711 GLN A OE1   1 
ATOM   15697 N  NE2   . GLN A 1 3711 ? 215.893 255.263 192.671 1.00 52.09  ? 3711 GLN A NE2   1 
ATOM   15698 N  N     . CYS A 1 3712 ? 219.702 259.197 191.023 1.00 45.45  ? 3712 CYS A N     1 
ATOM   15699 C  CA    . CYS A 1 3712 ? 219.796 260.345 191.915 1.00 38.32  ? 3712 CYS A CA    1 
ATOM   15700 C  C     . CYS A 1 3712 ? 219.917 261.656 191.150 1.00 44.65  ? 3712 CYS A C     1 
ATOM   15701 O  O     . CYS A 1 3712 ? 219.366 262.673 191.586 1.00 55.24  ? 3712 CYS A O     1 
ATOM   15702 C  CB    . CYS A 1 3712 ? 220.981 260.173 192.864 1.00 44.56  ? 3712 CYS A CB    1 
ATOM   15703 S  SG    . CYS A 1 3712 ? 220.758 258.855 194.078 1.00 58.86  ? 3712 CYS A SG    1 
ATOM   15704 N  N     . LEU A 1 3713 ? 220.628 261.659 190.020 1.00 50.07  ? 3713 LEU A N     1 
ATOM   15705 C  CA    . LEU A 1 3713 ? 220.703 262.860 189.198 1.00 47.72  ? 3713 LEU A CA    1 
ATOM   15706 C  C     . LEU A 1 3713 ? 219.335 263.226 188.645 1.00 49.17  ? 3713 LEU A C     1 
ATOM   15707 O  O     . LEU A 1 3713 ? 218.952 264.401 188.642 1.00 55.62  ? 3713 LEU A O     1 
ATOM   15708 C  CB    . LEU A 1 3713 ? 221.705 262.656 188.064 1.00 44.49  ? 3713 LEU A CB    1 
ATOM   15709 C  CG    . LEU A 1 3713 ? 221.768 263.753 187.002 1.00 50.71  ? 3713 LEU A CG    1 
ATOM   15710 C  CD1   . LEU A 1 3713 ? 222.199 265.068 187.616 1.00 51.20  ? 3713 LEU A CD1   1 
ATOM   15711 C  CD2   . LEU A 1 3713 ? 222.705 263.351 185.881 1.00 47.70  ? 3713 LEU A CD2   1 
ATOM   15712 N  N     . ASN A 1 3714 ? 218.577 262.232 188.178 1.00 50.33  ? 3714 ASN A N     1 
ATOM   15713 C  CA    . ASN A 1 3714 ? 217.222 262.503 187.716 1.00 48.40  ? 3714 ASN A CA    1 
ATOM   15714 C  C     . ASN A 1 3714 ? 216.343 263.020 188.845 1.00 53.77  ? 3714 ASN A C     1 
ATOM   15715 O  O     . ASN A 1 3714 ? 215.544 263.938 188.634 1.00 61.98  ? 3714 ASN A O     1 
ATOM   15716 C  CB    . ASN A 1 3714 ? 216.614 261.246 187.099 1.00 48.26  ? 3714 ASN A CB    1 
ATOM   15717 C  CG    . ASN A 1 3714 ? 217.324 260.820 185.831 1.00 55.01  ? 3714 ASN A CG    1 
ATOM   15718 O  OD1   . ASN A 1 3714 ? 218.199 261.524 185.330 1.00 56.48  ? 3714 ASN A OD1   1 
ATOM   15719 N  ND2   . ASN A 1 3714 ? 216.952 259.659 185.307 1.00 56.08  ? 3714 ASN A ND2   1 
ATOM   15720 N  N     . GLU A 1 3715 ? 216.477 262.454 190.046 1.00 51.11  ? 3715 GLU A N     1 
ATOM   15721 C  CA    . GLU A 1 3715 ? 215.668 262.915 191.170 1.00 49.60  ? 3715 GLU A CA    1 
ATOM   15722 C  C     . GLU A 1 3715 ? 216.000 264.354 191.551 1.00 50.15  ? 3715 GLU A C     1 
ATOM   15723 O  O     . GLU A 1 3715 ? 215.094 265.155 191.810 1.00 59.17  ? 3715 GLU A O     1 
ATOM   15724 C  CB    . GLU A 1 3715 ? 215.852 261.985 192.366 1.00 52.09  ? 3715 GLU A CB    1 
ATOM   15725 C  CG    . GLU A 1 3715 ? 214.863 262.230 193.488 1.00 56.76  ? 3715 GLU A CG    1 
ATOM   15726 C  CD    . GLU A 1 3715 ? 213.429 261.999 193.060 1.00 65.11  ? 3715 GLU A CD    1 
ATOM   15727 O  OE1   . GLU A 1 3715 ? 213.183 261.051 192.285 1.00 65.20  ? 3715 GLU A OE1   1 
ATOM   15728 O  OE2   . GLU A 1 3715 ? 212.547 262.768 193.494 1.00 63.08  ? 3715 GLU A OE2   1 
ATOM   15729 N  N     . VAL A 1 3716 ? 217.287 264.707 191.591 1.00 46.65  ? 3716 VAL A N     1 
ATOM   15730 C  CA    . VAL A 1 3716 ? 217.651 266.076 191.949 1.00 46.99  ? 3716 VAL A CA    1 
ATOM   15731 C  C     . VAL A 1 3716 ? 217.244 267.047 190.846 1.00 52.85  ? 3716 VAL A C     1 
ATOM   15732 O  O     . VAL A 1 3716 ? 216.859 268.188 191.123 1.00 59.21  ? 3716 VAL A O     1 
ATOM   15733 C  CB    . VAL A 1 3716 ? 219.150 266.187 192.288 1.00 49.27  ? 3716 VAL A CB    1 
ATOM   15734 C  CG1   . VAL A 1 3716 ? 220.017 266.027 191.057 1.00 53.24  ? 3716 VAL A CG1   1 
ATOM   15735 C  CG2   . VAL A 1 3716 ? 219.434 267.515 192.968 1.00 49.75  ? 3716 VAL A CG2   1 
ATOM   15736 N  N     . LEU A 1 3717 ? 217.321 266.619 189.582 1.00 53.41  ? 3717 LEU A N     1 
ATOM   15737 C  CA    . LEU A 1 3717 ? 216.846 267.469 188.496 1.00 47.06  ? 3717 LEU A CA    1 
ATOM   15738 C  C     . LEU A 1 3717 ? 215.347 267.705 188.604 1.00 55.12  ? 3717 LEU A C     1 
ATOM   15739 O  O     . LEU A 1 3717 ? 214.873 268.827 188.403 1.00 63.60  ? 3717 LEU A O     1 
ATOM   15740 C  CB    . LEU A 1 3717 ? 217.194 266.844 187.147 1.00 53.69  ? 3717 LEU A CB    1 
ATOM   15741 C  CG    . LEU A 1 3717 ? 218.540 267.233 186.534 1.00 60.64  ? 3717 LEU A CG    1 
ATOM   15742 C  CD1   . LEU A 1 3717 ? 218.725 266.547 185.191 1.00 57.72  ? 3717 LEU A CD1   1 
ATOM   15743 C  CD2   . LEU A 1 3717 ? 218.645 268.738 186.384 1.00 58.95  ? 3717 LEU A CD2   1 
ATOM   15744 N  N     . LYS A 1 3718 ? 214.586 266.658 188.922 1.00 55.34  ? 3718 LYS A N     1 
ATOM   15745 C  CA    . LYS A 1 3718 ? 213.144 266.810 189.081 1.00 52.54  ? 3718 LYS A CA    1 
ATOM   15746 C  C     . LYS A 1 3718 ? 212.810 267.720 190.255 1.00 56.02  ? 3718 LYS A C     1 
ATOM   15747 O  O     . LYS A 1 3718 ? 211.896 268.548 190.167 1.00 62.38  ? 3718 LYS A O     1 
ATOM   15748 C  CB    . LYS A 1 3718 ? 212.493 265.440 189.263 1.00 53.78  ? 3718 LYS A CB    1 
ATOM   15749 C  CG    . LYS A 1 3718 ? 210.980 265.474 189.346 1.00 57.67  ? 3718 LYS A CG    1 
ATOM   15750 C  CD    . LYS A 1 3718 ? 210.408 264.071 189.456 1.00 63.27  ? 3718 LYS A CD    1 
ATOM   15751 C  CE    . LYS A 1 3718 ? 208.891 264.097 189.539 1.00 63.73  ? 3718 LYS A CE    1 
ATOM   15752 N  NZ    . LYS A 1 3718 ? 208.320 262.726 189.630 1.00 60.61  ? 3718 LYS A NZ    1 
ATOM   15753 N  N     . ALA A 1 3719 ? 213.535 267.579 191.365 1.00 53.22  ? 3719 ALA A N     1 
ATOM   15754 C  CA    . ALA A 1 3719 ? 213.219 268.362 192.555 1.00 51.11  ? 3719 ALA A CA    1 
ATOM   15755 C  C     . ALA A 1 3719 ? 213.613 269.825 192.390 1.00 54.00  ? 3719 ALA A C     1 
ATOM   15756 O  O     . ALA A 1 3719 ? 212.840 270.723 192.741 1.00 58.03  ? 3719 ALA A O     1 
ATOM   15757 C  CB    . ALA A 1 3719 ? 213.906 267.758 193.777 1.00 51.14  ? 3719 ALA A CB    1 
ATOM   15758 N  N     . GLU A 1 3720 ? 214.806 270.086 191.859 1.00 57.03  ? 3720 GLU A N     1 
ATOM   15759 C  CA    . GLU A 1 3720 ? 215.341 271.441 191.817 1.00 55.62  ? 3720 GLU A CA    1 
ATOM   15760 C  C     . GLU A 1 3720 ? 214.988 272.180 190.532 1.00 60.65  ? 3720 GLU A C     1 
ATOM   15761 O  O     . GLU A 1 3720 ? 214.738 273.389 190.566 1.00 67.70  ? 3720 GLU A O     1 
ATOM   15762 C  CB    . GLU A 1 3720 ? 216.861 271.407 191.990 1.00 54.59  ? 3720 GLU A CB    1 
ATOM   15763 C  CG    . GLU A 1 3720 ? 217.315 271.110 193.408 1.00 60.98  ? 3720 GLU A CG    1 
ATOM   15764 C  CD    . GLU A 1 3720 ? 216.762 272.096 194.415 1.00 62.53  ? 3720 GLU A CD    1 
ATOM   15765 O  OE1   . GLU A 1 3720 ? 217.059 273.302 194.291 1.00 65.63  ? 3720 GLU A OE1   1 
ATOM   15766 O  OE2   . GLU A 1 3720 ? 216.031 271.667 195.332 1.00 58.24  ? 3720 GLU A OE2   1 
ATOM   15767 N  N     . ARG A 1 3721 ? 214.964 271.484 189.398 1.00 62.92  ? 3721 ARG A N     1 
ATOM   15768 C  CA    . ARG A 1 3721 ? 214.690 272.090 188.095 1.00 59.06  ? 3721 ARG A CA    1 
ATOM   15769 C  C     . ARG A 1 3721 ? 213.588 271.299 187.403 1.00 59.80  ? 3721 ARG A C     1 
ATOM   15770 O  O     . ARG A 1 3721 ? 213.841 270.580 186.430 1.00 67.71  ? 3721 ARG A O     1 
ATOM   15771 C  CB    . ARG A 1 3721 ? 215.953 272.127 187.235 1.00 58.90  ? 3721 ARG A CB    1 
ATOM   15772 C  CG    . ARG A 1 3721 ? 217.178 272.674 187.940 1.00 58.04  ? 3721 ARG A CG    1 
ATOM   15773 C  CD    . ARG A 1 3721 ? 217.091 274.174 188.134 1.00 64.09  ? 3721 ARG A CD    1 
ATOM   15774 N  NE    . ARG A 1 3721 ? 217.646 274.900 186.998 1.00 66.49  ? 3721 ARG A NE    1 
ATOM   15775 C  CZ    . ARG A 1 3721 ? 218.942 275.075 186.782 1.00 64.62  ? 3721 ARG A CZ    1 
ATOM   15776 N  NH1   . ARG A 1 3721 ? 219.853 274.590 187.609 1.00 61.51  ? 3721 ARG A NH1   1 
ATOM   15777 N  NH2   . ARG A 1 3721 ? 219.334 275.754 185.709 1.00 65.72  ? 3721 ARG A NH2   1 
ATOM   15778 N  N     . PRO A 1 3722 ? 212.349 271.404 187.887 1.00 64.79  ? 3722 PRO A N     1 
ATOM   15779 C  CA    . PRO A 1 3722 ? 211.271 270.585 187.307 1.00 70.57  ? 3722 PRO A CA    1 
ATOM   15780 C  C     . PRO A 1 3722 ? 211.037 270.843 185.829 1.00 72.44  ? 3722 PRO A C     1 
ATOM   15781 O  O     . PRO A 1 3722 ? 210.723 269.901 185.090 1.00 72.66  ? 3722 PRO A O     1 
ATOM   15782 C  CB    . PRO A 1 3722 ? 210.047 270.971 188.151 1.00 68.31  ? 3722 PRO A CB    1 
ATOM   15783 C  CG    . PRO A 1 3722 ? 210.375 272.312 188.709 1.00 66.96  ? 3722 PRO A CG    1 
ATOM   15784 C  CD    . PRO A 1 3722 ? 211.854 272.314 188.933 1.00 67.10  ? 3722 PRO A CD    1 
ATOM   15785 N  N     . ASP A 1 3723 ? 211.182 272.089 185.373 1.00 74.62  ? 3723 ASP A N     1 
ATOM   15786 C  CA    . ASP A 1 3723 ? 211.016 272.377 183.952 1.00 69.99  ? 3723 ASP A CA    1 
ATOM   15787 C  C     . ASP A 1 3723 ? 212.111 271.719 183.119 1.00 72.30  ? 3723 ASP A C     1 
ATOM   15788 O  O     . ASP A 1 3723 ? 211.833 271.151 182.056 1.00 75.87  ? 3723 ASP A O     1 
ATOM   15789 C  CB    . ASP A 1 3723 ? 210.975 273.890 183.723 1.00 73.34  ? 3723 ASP A CB    1 
ATOM   15790 C  CG    . ASP A 1 3723 ? 212.262 274.587 184.127 1.00 76.74  ? 3723 ASP A CG    1 
ATOM   15791 O  OD1   . ASP A 1 3723 ? 213.187 273.916 184.627 1.00 78.42  ? 3723 ASP A OD1   1 
ATOM   15792 O  OD2   . ASP A 1 3723 ? 212.350 275.819 183.939 1.00 77.91  ? 3723 ASP A OD2   1 
ATOM   15793 N  N     . VAL A 1 3724 ? 213.357 271.773 183.591 1.00 68.89  ? 3724 VAL A N     1 
ATOM   15794 C  CA    . VAL A 1 3724 ? 214.443 271.103 182.883 1.00 67.80  ? 3724 VAL A CA    1 
ATOM   15795 C  C     . VAL A 1 3724 ? 214.214 269.598 182.864 1.00 68.46  ? 3724 VAL A C     1 
ATOM   15796 O  O     . VAL A 1 3724 ? 214.482 268.932 181.860 1.00 75.13  ? 3724 VAL A O     1 
ATOM   15797 C  CB    . VAL A 1 3724 ? 215.800 271.465 183.514 1.00 68.81  ? 3724 VAL A CB    1 
ATOM   15798 C  CG1   . VAL A 1 3724 ? 216.928 270.764 182.781 1.00 66.93  ? 3724 VAL A CG1   1 
ATOM   15799 C  CG2   . VAL A 1 3724 ? 216.012 272.966 183.488 1.00 69.62  ? 3724 VAL A CG2   1 
ATOM   15800 N  N     . ASP A 1 3725 ? 213.712 269.038 183.966 1.00 64.28  ? 3725 ASP A N     1 
ATOM   15801 C  CA    . ASP A 1 3725 ? 213.468 267.600 184.012 1.00 68.69  ? 3725 ASP A CA    1 
ATOM   15802 C  C     . ASP A 1 3725 ? 212.363 267.186 183.048 1.00 73.86  ? 3725 ASP A C     1 
ATOM   15803 O  O     . ASP A 1 3725 ? 212.480 266.162 182.364 1.00 81.37  ? 3725 ASP A O     1 
ATOM   15804 C  CB    . ASP A 1 3725 ? 213.121 267.168 185.434 1.00 71.89  ? 3725 ASP A CB    1 
ATOM   15805 C  CG    . ASP A 1 3725 ? 212.808 265.690 185.528 1.00 78.14  ? 3725 ASP A CG    1 
ATOM   15806 O  OD1   . ASP A 1 3725 ? 213.691 264.873 185.191 1.00 69.24  ? 3725 ASP A OD1   1 
ATOM   15807 O  OD2   . ASP A 1 3725 ? 211.679 265.346 185.937 1.00 80.28  ? 3725 ASP A OD2   1 
ATOM   15808 N  N     . GLU A 1 3726 ? 211.272 267.955 182.990 1.00 74.78  ? 3726 GLU A N     1 
ATOM   15809 C  CA    . GLU A 1 3726 ? 210.201 267.614 182.058 1.00 73.13  ? 3726 GLU A CA    1 
ATOM   15810 C  C     . GLU A 1 3726 ? 210.659 267.784 180.615 1.00 73.18  ? 3726 GLU A C     1 
ATOM   15811 O  O     . GLU A 1 3726 ? 210.306 266.976 179.746 1.00 75.08  ? 3726 GLU A O     1 
ATOM   15812 C  CB    . GLU A 1 3726 ? 208.950 268.449 182.351 1.00 74.04  ? 3726 GLU A CB    1 
ATOM   15813 C  CG    . GLU A 1 3726 ? 208.980 269.882 181.849 1.00 76.56  ? 3726 GLU A CG    1 
ATOM   15814 C  CD    . GLU A 1 3726 ? 207.610 270.530 181.845 1.00 79.31  ? 3726 GLU A CD    1 
ATOM   15815 O  OE1   . GLU A 1 3726 ? 206.604 269.795 181.768 1.00 78.36  ? 3726 GLU A OE1   1 
ATOM   15816 O  OE2   . GLU A 1 3726 ? 207.540 271.775 181.917 1.00 76.77  ? 3726 GLU A OE2   1 
ATOM   15817 N  N     . LYS A 1 3727 ? 211.471 268.811 180.346 1.00 75.92  ? 3727 LYS A N     1 
ATOM   15818 C  CA    . LYS A 1 3727 ? 212.054 268.966 179.019 1.00 75.75  ? 3727 LYS A CA    1 
ATOM   15819 C  C     . LYS A 1 3727 ? 212.926 267.771 178.666 1.00 76.00  ? 3727 LYS A C     1 
ATOM   15820 O  O     . LYS A 1 3727 ? 212.860 267.256 177.546 1.00 81.35  ? 3727 LYS A O     1 
ATOM   15821 C  CB    . LYS A 1 3727 ? 212.864 270.260 178.959 1.00 74.00  ? 3727 LYS A CB    1 
ATOM   15822 C  CG    . LYS A 1 3727 ? 213.415 270.599 177.590 1.00 75.75  ? 3727 LYS A CG    1 
ATOM   15823 C  CD    . LYS A 1 3727 ? 214.257 271.863 177.647 1.00 76.90  ? 3727 LYS A CD    1 
ATOM   15824 C  CE    . LYS A 1 3727 ? 213.390 273.095 177.825 1.00 77.01  ? 3727 LYS A CE    1 
ATOM   15825 N  NZ    . LYS A 1 3727 ? 214.191 274.348 177.774 1.00 77.69  ? 3727 LYS A NZ    1 
ATOM   15826 N  N     . ARG A 1 3728 ? 213.734 267.306 179.619 1.00 75.78  ? 3728 ARG A N     1 
ATOM   15827 C  CA    . ARG A 1 3728 ? 214.594 266.152 179.387 1.00 77.42  ? 3728 ARG A CA    1 
ATOM   15828 C  C     . ARG A 1 3728 ? 213.779 264.894 179.110 1.00 78.71  ? 3728 ARG A C     1 
ATOM   15829 O  O     . ARG A 1 3728 ? 214.120 264.113 178.216 1.00 81.29  ? 3728 ARG A O     1 
ATOM   15830 C  CB    . ARG A 1 3728 ? 215.511 265.950 180.592 1.00 76.19  ? 3728 ARG A CB    1 
ATOM   15831 C  CG    . ARG A 1 3728 ? 216.483 264.797 180.467 1.00 79.72  ? 3728 ARG A CG    1 
ATOM   15832 C  CD    . ARG A 1 3728 ? 216.948 264.356 181.843 1.00 77.53  ? 3728 ARG A CD    1 
ATOM   15833 N  NE    . ARG A 1 3728 ? 216.053 263.364 182.425 1.00 77.94  ? 3728 ARG A NE    1 
ATOM   15834 C  CZ    . ARG A 1 3728 ? 216.212 262.054 182.310 1.00 81.27  ? 3728 ARG A CZ    1 
ATOM   15835 N  NH1   . ARG A 1 3728 ? 217.241 261.537 181.660 1.00 77.82  ? 3728 ARG A NH1   1 
ATOM   15836 N  NH2   . ARG A 1 3728 ? 215.317 261.241 182.865 1.00 79.09  ? 3728 ARG A NH2   1 
ATOM   15837 N  N     . SER A 1 3729 ? 212.707 264.675 179.873 1.00 73.82  ? 3729 SER A N     1 
ATOM   15838 C  CA    . SER A 1 3729 ? 211.870 263.499 179.643 1.00 75.69  ? 3729 SER A CA    1 
ATOM   15839 C  C     . SER A 1 3729 ? 211.208 263.550 178.270 1.00 81.46  ? 3729 SER A C     1 
ATOM   15840 O  O     . SER A 1 3729 ? 211.174 262.541 177.547 1.00 81.84  ? 3729 SER A O     1 
ATOM   15841 C  CB    . SER A 1 3729 ? 210.816 263.381 180.742 1.00 79.34  ? 3729 SER A CB    1 
ATOM   15842 O  OG    . SER A 1 3729 ? 211.417 263.346 182.024 1.00 82.91  ? 3729 SER A OG    1 
ATOM   15843 N  N     . ASP A 1 3730 ? 210.684 264.719 177.889 1.00 84.04  ? 3730 ASP A N     1 
ATOM   15844 C  CA    . ASP A 1 3730 ? 210.095 264.862 176.563 1.00 80.17  ? 3730 ASP A CA    1 
ATOM   15845 C  C     . ASP A 1 3730 ? 211.134 264.621 175.477 1.00 78.34  ? 3730 ASP A C     1 
ATOM   15846 O  O     . ASP A 1 3730 ? 210.840 263.996 174.451 1.00 82.84  ? 3730 ASP A O     1 
ATOM   15847 C  CB    . ASP A 1 3730 ? 209.469 266.248 176.413 1.00 81.57  ? 3730 ASP A CB    1 
ATOM   15848 C  CG    . ASP A 1 3730 ? 208.316 266.473 177.372 1.00 85.10  ? 3730 ASP A CG    1 
ATOM   15849 O  OD1   . ASP A 1 3730 ? 207.946 265.524 178.094 1.00 83.01  ? 3730 ASP A OD1   1 
ATOM   15850 O  OD2   . ASP A 1 3730 ? 207.780 267.600 177.404 1.00 83.99  ? 3730 ASP A OD2   1 
ATOM   15851 N  N     . LEU A 1 3731 ? 212.360 265.103 175.689 1.00 75.97  ? 3731 LEU A N     1 
ATOM   15852 C  CA    . LEU A 1 3731 ? 213.411 264.903 174.698 1.00 78.46  ? 3731 LEU A CA    1 
ATOM   15853 C  C     . LEU A 1 3731 ? 213.798 263.434 174.584 1.00 80.71  ? 3731 LEU A C     1 
ATOM   15854 O  O     . LEU A 1 3731 ? 214.080 262.952 173.485 1.00 81.83  ? 3731 LEU A O     1 
ATOM   15855 C  CB    . LEU A 1 3731 ? 214.630 265.756 175.039 1.00 80.80  ? 3731 LEU A CB    1 
ATOM   15856 C  CG    . LEU A 1 3731 ? 214.476 267.262 174.837 1.00 80.41  ? 3731 LEU A CG    1 
ATOM   15857 C  CD1   . LEU A 1 3731 ? 215.421 268.019 175.749 1.00 80.08  ? 3731 LEU A CD1   1 
ATOM   15858 C  CD2   . LEU A 1 3731 ? 214.709 267.636 173.393 1.00 79.31  ? 3731 LEU A CD2   1 
ATOM   15859 N  N     . LEU A 1 3732 ? 213.831 262.707 175.704 1.00 83.32  ? 3732 LEU A N     1 
ATOM   15860 C  CA    . LEU A 1 3732 ? 214.093 261.270 175.630 1.00 83.50  ? 3732 LEU A CA    1 
ATOM   15861 C  C     . LEU A 1 3732 ? 212.999 260.548 174.856 1.00 82.75  ? 3732 LEU A C     1 
ATOM   15862 O  O     . LEU A 1 3732 ? 213.285 259.670 174.028 1.00 82.05  ? 3732 LEU A O     1 
ATOM   15863 C  CB    . LEU A 1 3732 ? 214.228 260.664 177.029 1.00 82.48  ? 3732 LEU A CB    1 
ATOM   15864 C  CG    . LEU A 1 3732 ? 215.206 261.246 178.045 1.00 80.74  ? 3732 LEU A CG    1 
ATOM   15865 C  CD1   . LEU A 1 3732 ? 215.267 260.352 179.266 1.00 78.39  ? 3732 LEU A CD1   1 
ATOM   15866 C  CD2   . LEU A 1 3732 ? 216.580 261.383 177.429 1.00 78.31  ? 3732 LEU A CD2   1 
ATOM   15867 N  N     . LYS A 1 3733 ? 211.737 260.896 175.118 1.00 82.33  ? 3733 LYS A N     1 
ATOM   15868 C  CA    . LYS A 1 3733 ? 210.642 260.271 174.381 1.00 81.16  ? 3733 LYS A CA    1 
ATOM   15869 C  C     . LYS A 1 3733 ? 210.748 260.565 172.889 1.00 82.79  ? 3733 LYS A C     1 
ATOM   15870 O  O     . LYS A 1 3733 ? 210.557 259.669 172.054 1.00 83.10  ? 3733 LYS A O     1 
ATOM   15871 C  CB    . LYS A 1 3733 ? 209.300 260.746 174.933 1.00 82.63  ? 3733 LYS A CB    1 
ATOM   15872 C  CG    . LYS A 1 3733 ? 208.108 259.936 174.455 1.00 82.08  ? 3733 LYS A CG    1 
ATOM   15873 C  CD    . LYS A 1 3733 ? 206.800 260.493 174.998 1.00 82.35  ? 3733 LYS A CD    1 
ATOM   15874 C  CE    . LYS A 1 3733 ? 206.784 262.014 174.975 1.00 85.45  ? 3733 LYS A CE    1 
ATOM   15875 N  NZ    . LYS A 1 3733 ? 206.812 262.553 173.587 1.00 82.23  ? 3733 LYS A NZ    1 
ATOM   15876 N  N     . LEU A 1 3734 ? 211.066 261.814 172.537 1.00 81.99  ? 3734 LEU A N     1 
ATOM   15877 C  CA    . LEU A 1 3734 ? 211.234 262.172 171.133 1.00 80.01  ? 3734 LEU A CA    1 
ATOM   15878 C  C     . LEU A 1 3734 ? 212.419 261.447 170.506 1.00 81.08  ? 3734 LEU A C     1 
ATOM   15879 O  O     . LEU A 1 3734 ? 212.345 261.026 169.350 1.00 85.45  ? 3734 LEU A O     1 
ATOM   15880 C  CB    . LEU A 1 3734 ? 211.389 263.685 170.986 1.00 80.20  ? 3734 LEU A CB    1 
ATOM   15881 C  CG    . LEU A 1 3734 ? 210.122 264.459 170.617 1.00 80.89  ? 3734 LEU A CG    1 
ATOM   15882 C  CD1   . LEU A 1 3734 ? 209.100 264.418 171.741 1.00 82.00  ? 3734 LEU A CD1   1 
ATOM   15883 C  CD2   . LEU A 1 3734 ? 210.460 265.896 170.249 1.00 81.10  ? 3734 LEU A CD2   1 
ATOM   15884 N  N     . GLN A 1 3735 ? 213.524 261.304 171.242 1.00 78.55  ? 3735 GLN A N     1 
ATOM   15885 C  CA    . GLN A 1 3735 ? 214.667 260.554 170.727 1.00 77.65  ? 3735 GLN A CA    1 
ATOM   15886 C  C     . GLN A 1 3735 ? 214.280 259.118 170.415 1.00 77.93  ? 3735 GLN A C     1 
ATOM   15887 O  O     . GLN A 1 3735 ? 214.615 258.590 169.346 1.00 77.31  ? 3735 GLN A O     1 
ATOM   15888 C  CB    . GLN A 1 3735 ? 215.812 260.570 171.740 1.00 82.08  ? 3735 GLN A CB    1 
ATOM   15889 C  CG    . GLN A 1 3735 ? 216.554 261.883 171.881 1.00 80.73  ? 3735 GLN A CG    1 
ATOM   15890 C  CD    . GLN A 1 3735 ? 217.471 262.166 170.714 1.00 82.37  ? 3735 GLN A CD    1 
ATOM   15891 O  OE1   . GLN A 1 3735 ? 217.842 261.262 169.966 1.00 80.95  ? 3735 GLN A OE1   1 
ATOM   15892 N  NE2   . GLN A 1 3735 ? 217.869 263.421 170.570 1.00 81.32  ? 3735 GLN A NE2   1 
ATOM   15893 N  N     . GLY A 1 3736 ? 213.574 258.469 171.342 1.00 79.83  ? 3736 GLY A N     1 
ATOM   15894 C  CA    . GLY A 1 3736 ? 213.155 257.098 171.107 1.00 80.79  ? 3736 GLY A CA    1 
ATOM   15895 C  C     . GLY A 1 3736 ? 212.233 256.973 169.910 1.00 83.62  ? 3736 GLY A C     1 
ATOM   15896 O  O     . GLY A 1 3736 ? 212.413 256.091 169.064 1.00 81.08  ? 3736 GLY A O     1 
ATOM   15897 N  N     . GLU A 1 3737 ? 211.241 257.864 169.814 1.00 84.97  ? 3737 GLU A N     1 
ATOM   15898 C  CA    . GLU A 1 3737 ? 210.311 257.818 168.689 1.00 82.56  ? 3737 GLU A CA    1 
ATOM   15899 C  C     . GLU A 1 3737 ? 211.020 258.087 167.367 1.00 81.22  ? 3737 GLU A C     1 
ATOM   15900 O  O     . GLU A 1 3737 ? 210.742 257.422 166.363 1.00 83.84  ? 3737 GLU A O     1 
ATOM   15901 C  CB    . GLU A 1 3737 ? 209.175 258.816 168.906 1.00 82.44  ? 3737 GLU A CB    1 
ATOM   15902 C  CG    . GLU A 1 3737 ? 208.258 258.461 170.066 1.00 83.85  ? 3737 GLU A CG    1 
ATOM   15903 C  CD    . GLU A 1 3737 ? 207.154 259.478 170.270 1.00 86.51  ? 3737 GLU A CD    1 
ATOM   15904 O  OE1   . GLU A 1 3737 ? 207.172 260.525 169.590 1.00 87.93  ? 3737 GLU A OE1   1 
ATOM   15905 O  OE2   . GLU A 1 3737 ? 206.268 259.231 171.115 1.00 84.69  ? 3737 GLU A OE2   1 
ATOM   15906 N  N     . PHE A 1 3738 ? 211.939 259.054 167.345 1.00 77.44  ? 3738 PHE A N     1 
ATOM   15907 C  CA    . PHE A 1 3738 ? 212.669 259.367 166.122 1.00 78.16  ? 3738 PHE A CA    1 
ATOM   15908 C  C     . PHE A 1 3738 ? 213.545 258.205 165.681 1.00 78.48  ? 3738 PHE A C     1 
ATOM   15909 O  O     . PHE A 1 3738 ? 213.627 257.905 164.486 1.00 80.68  ? 3738 PHE A O     1 
ATOM   15910 C  CB    . PHE A 1 3738 ? 213.519 260.620 166.318 1.00 77.83  ? 3738 PHE A CB    1 
ATOM   15911 C  CG    . PHE A 1 3738 ? 212.723 261.879 166.479 1.00 80.71  ? 3738 PHE A CG    1 
ATOM   15912 C  CD1   . PHE A 1 3738 ? 211.379 261.915 166.150 1.00 79.16  ? 3738 PHE A CD1   1 
ATOM   15913 C  CD2   . PHE A 1 3738 ? 213.322 263.032 166.955 1.00 82.08  ? 3738 PHE A CD2   1 
ATOM   15914 C  CE1   . PHE A 1 3738 ? 210.648 263.074 166.297 1.00 79.07  ? 3738 PHE A CE1   1 
ATOM   15915 C  CE2   . PHE A 1 3738 ? 212.597 264.194 167.104 1.00 80.58  ? 3738 PHE A CE2   1 
ATOM   15916 C  CZ    . PHE A 1 3738 ? 211.258 264.216 166.774 1.00 81.22  ? 3738 PHE A CZ    1 
ATOM   15917 N  N     . GLN A 1 3739 ? 214.226 257.549 166.622 1.00 76.82  ? 3739 GLN A N     1 
ATOM   15918 C  CA    . GLN A 1 3739 ? 215.069 256.422 166.237 1.00 77.99  ? 3739 GLN A CA    1 
ATOM   15919 C  C     . GLN A 1 3739 ? 214.229 255.239 165.772 1.00 77.37  ? 3739 GLN A C     1 
ATOM   15920 O  O     . GLN A 1 3739 ? 214.602 254.545 164.817 1.00 73.74  ? 3739 GLN A O     1 
ATOM   15921 C  CB    . GLN A 1 3739 ? 215.992 256.031 167.389 1.00 80.60  ? 3739 GLN A CB    1 
ATOM   15922 C  CG    . GLN A 1 3739 ? 217.050 257.084 167.713 1.00 80.04  ? 3739 GLN A CG    1 
ATOM   15923 C  CD    . GLN A 1 3739 ? 218.212 257.093 166.727 1.00 78.73  ? 3739 GLN A CD    1 
ATOM   15924 O  OE1   . GLN A 1 3739 ? 218.082 256.660 165.583 1.00 75.03  ? 3739 GLN A OE1   1 
ATOM   15925 N  NE2   . GLN A 1 3739 ? 219.356 257.599 167.172 1.00 76.83  ? 3739 GLN A NE2   1 
ATOM   15926 N  N     . LEU A 1 3740 ? 213.082 255.003 166.418 1.00 77.45  ? 3740 LEU A N     1 
ATOM   15927 C  CA    . LEU A 1 3740 ? 212.163 253.982 165.924 1.00 74.00  ? 3740 LEU A CA    1 
ATOM   15928 C  C     . LEU A 1 3740 ? 211.711 254.293 164.505 1.00 78.21  ? 3740 LEU A C     1 
ATOM   15929 O  O     . LEU A 1 3740 ? 211.666 253.402 163.647 1.00 79.16  ? 3740 LEU A O     1 
ATOM   15930 C  CB    . LEU A 1 3740 ? 210.957 253.868 166.853 1.00 75.85  ? 3740 LEU A CB    1 
ATOM   15931 C  CG    . LEU A 1 3740 ? 209.933 252.793 166.490 1.00 79.84  ? 3740 LEU A CG    1 
ATOM   15932 C  CD1   . LEU A 1 3740 ? 210.546 251.407 166.547 1.00 78.88  ? 3740 LEU A CD1   1 
ATOM   15933 C  CD2   . LEU A 1 3740 ? 208.727 252.886 167.409 1.00 77.89  ? 3740 LEU A CD2   1 
ATOM   15934 N  N     . ARG A 1 3741 ? 211.380 255.558 164.239 1.00 83.56  ? 3741 ARG A N     1 
ATOM   15935 C  CA    . ARG A 1 3741 ? 210.946 255.945 162.903 1.00 79.12  ? 3741 ARG A CA    1 
ATOM   15936 C  C     . ARG A 1 3741 ? 212.064 255.759 161.884 1.00 76.25  ? 3741 ARG A C     1 
ATOM   15937 O  O     . ARG A 1 3741 ? 211.817 255.293 160.770 1.00 78.66  ? 3741 ARG A O     1 
ATOM   15938 C  CB    . ARG A 1 3741 ? 210.455 257.391 162.909 1.00 77.44  ? 3741 ARG A CB    1 
ATOM   15939 C  CG    . ARG A 1 3741 ? 209.611 257.752 161.700 1.00 79.30  ? 3741 ARG A CG    1 
ATOM   15940 C  CD    . ARG A 1 3741 ? 208.557 256.683 161.450 1.00 80.80  ? 3741 ARG A CD    1 
ATOM   15941 N  NE    . ARG A 1 3741 ? 208.180 256.584 160.045 1.00 82.79  ? 3741 ARG A NE    1 
ATOM   15942 C  CZ    . ARG A 1 3741 ? 207.370 255.657 159.552 1.00 82.00  ? 3741 ARG A CZ    1 
ATOM   15943 N  NH1   . ARG A 1 3741 ? 206.845 254.718 160.322 1.00 77.04  ? 3741 ARG A NH1   1 
ATOM   15944 N  NH2   . ARG A 1 3741 ? 207.081 255.672 158.254 1.00 80.19  ? 3741 ARG A NH2   1 
ATOM   15945 N  N     . LEU A 1 3742 ? 213.297 256.128 162.242 1.00 71.50  ? 3742 LEU A N     1 
ATOM   15946 C  CA    . LEU A 1 3742 ? 214.418 255.970 161.319 1.00 70.57  ? 3742 LEU A CA    1 
ATOM   15947 C  C     . LEU A 1 3742 ? 214.679 254.501 161.008 1.00 75.25  ? 3742 LEU A C     1 
ATOM   15948 O  O     . LEU A 1 3742 ? 214.933 254.138 159.852 1.00 77.27  ? 3742 LEU A O     1 
ATOM   15949 C  CB    . LEU A 1 3742 ? 215.673 256.627 161.894 1.00 74.92  ? 3742 LEU A CB    1 
ATOM   15950 C  CG    . LEU A 1 3742 ? 215.977 258.055 161.435 1.00 76.16  ? 3742 LEU A CG    1 
ATOM   15951 C  CD1   . LEU A 1 3742 ? 217.272 258.557 162.049 1.00 74.07  ? 3742 LEU A CD1   1 
ATOM   15952 C  CD2   . LEU A 1 3742 ? 216.044 258.125 159.920 1.00 74.99  ? 3742 LEU A CD2   1 
ATOM   15953 N  N     . ARG A 1 3743 ? 214.622 253.640 162.027 1.00 73.76  ? 3743 ARG A N     1 
ATOM   15954 C  CA    . ARG A 1 3743 ? 214.762 252.207 161.790 1.00 72.45  ? 3743 ARG A CA    1 
ATOM   15955 C  C     . ARG A 1 3743 ? 213.661 251.688 160.875 1.00 74.68  ? 3743 ARG A C     1 
ATOM   15956 O  O     . ARG A 1 3743 ? 213.926 250.923 159.939 1.00 74.41  ? 3743 ARG A O     1 
ATOM   15957 C  CB    . ARG A 1 3743 ? 214.755 251.455 163.120 1.00 75.37  ? 3743 ARG A CB    1 
ATOM   15958 C  CG    . ARG A 1 3743 ? 215.958 251.722 164.003 1.00 76.78  ? 3743 ARG A CG    1 
ATOM   15959 C  CD    . ARG A 1 3743 ? 215.824 250.952 165.298 1.00 70.45  ? 3743 ARG A CD    1 
ATOM   15960 N  NE    . ARG A 1 3743 ? 214.730 251.479 166.104 1.00 72.58  ? 3743 ARG A NE    1 
ATOM   15961 C  CZ    . ARG A 1 3743 ? 214.284 250.921 167.220 1.00 73.93  ? 3743 ARG A CZ    1 
ATOM   15962 N  NH1   . ARG A 1 3743 ? 214.682 249.721 167.597 1.00 81.11  ? 3743 ARG A NH1   1 
ATOM   15963 N  NH2   . ARG A 1 3743 ? 213.398 251.575 167.965 1.00 75.60  ? 3743 ARG A NH2   1 
ATOM   15964 N  N     . GLN A 1 3744 ? 212.415 252.096 161.129 1.00 78.97  ? 3744 GLN A N     1 
ATOM   15965 C  CA    . GLN A 1 3744 ? 211.310 251.643 160.292 1.00 73.32  ? 3744 GLN A CA    1 
ATOM   15966 C  C     . GLN A 1 3744 ? 211.486 252.113 158.855 1.00 76.74  ? 3744 GLN A C     1 
ATOM   15967 O  O     . GLN A 1 3744 ? 211.252 251.352 157.910 1.00 78.75  ? 3744 GLN A O     1 
ATOM   15968 C  CB    . GLN A 1 3744 ? 209.978 252.131 160.863 1.00 74.45  ? 3744 GLN A CB    1 
ATOM   15969 C  CG    . GLN A 1 3744 ? 209.542 251.398 162.119 1.00 78.50  ? 3744 GLN A CG    1 
ATOM   15970 C  CD    . GLN A 1 3744 ? 208.072 251.595 162.426 1.00 80.42  ? 3744 GLN A CD    1 
ATOM   15971 O  OE1   . GLN A 1 3744 ? 207.706 252.352 163.325 1.00 80.11  ? 3744 GLN A OE1   1 
ATOM   15972 N  NE2   . GLN A 1 3744 ? 207.217 250.908 161.677 1.00 78.11  ? 3744 GLN A NE2   1 
ATOM   15973 N  N     . LEU A 1 3745 ? 211.907 253.365 158.671 1.00 81.83  ? 3745 LEU A N     1 
ATOM   15974 C  CA    . LEU A 1 3745 ? 212.112 253.898 157.329 1.00 79.03  ? 3745 LEU A CA    1 
ATOM   15975 C  C     . LEU A 1 3745 ? 213.209 253.141 156.597 1.00 79.21  ? 3745 LEU A C     1 
ATOM   15976 O  O     . LEU A 1 3745 ? 213.053 252.789 155.424 1.00 82.78  ? 3745 LEU A O     1 
ATOM   15977 C  CB    . LEU A 1 3745 ? 212.451 255.385 157.401 1.00 79.43  ? 3745 LEU A CB    1 
ATOM   15978 C  CG    . LEU A 1 3745 ? 211.342 256.323 157.866 1.00 80.47  ? 3745 LEU A CG    1 
ATOM   15979 C  CD1   . LEU A 1 3745 ? 211.869 257.736 157.922 1.00 81.27  ? 3745 LEU A CD1   1 
ATOM   15980 C  CD2   . LEU A 1 3745 ? 210.141 256.228 156.944 1.00 79.14  ? 3745 LEU A CD2   1 
ATOM   15981 N  N     . GLU A 1 3746 ? 214.331 252.884 157.272 1.00 81.13  ? 3746 GLU A N     1 
ATOM   15982 C  CA    . GLU A 1 3746 ? 215.430 252.172 156.625 1.00 85.52  ? 3746 GLU A CA    1 
ATOM   15983 C  C     . GLU A 1 3746 ? 215.016 250.756 156.243 1.00 84.50  ? 3746 GLU A C     1 
ATOM   15984 O  O     . GLU A 1 3746 ? 215.279 250.294 155.123 1.00 83.74  ? 3746 GLU A O     1 
ATOM   15985 C  CB    . GLU A 1 3746 ? 216.649 252.149 157.547 1.00 85.19  ? 3746 GLU A CB    1 
ATOM   15986 C  CG    . GLU A 1 3746 ? 217.829 251.380 156.990 1.00 83.88  ? 3746 GLU A CG    1 
ATOM   15987 C  CD    . GLU A 1 3746 ? 218.170 251.793 155.577 1.00 85.40  ? 3746 GLU A CD    1 
ATOM   15988 O  OE1   . GLU A 1 3746 ? 218.486 252.982 155.364 1.00 85.48  ? 3746 GLU A OE1   1 
ATOM   15989 O  OE2   . GLU A 1 3746 ? 218.119 250.930 154.677 1.00 84.82  ? 3746 GLU A OE2   1 
ATOM   15990 N  N     . LYS A 1 3747 ? 214.353 250.053 157.164 1.00 81.81  ? 3747 LYS A N     1 
ATOM   15991 C  CA    . LYS A 1 3747 ? 213.943 248.680 156.894 1.00 81.11  ? 3747 LYS A CA    1 
ATOM   15992 C  C     . LYS A 1 3747 ? 212.920 248.628 155.766 1.00 81.65  ? 3747 LYS A C     1 
ATOM   15993 O  O     . LYS A 1 3747 ? 212.997 247.767 154.881 1.00 82.07  ? 3747 LYS A O     1 
ATOM   15994 C  CB    . LYS A 1 3747 ? 213.392 248.049 158.173 1.00 80.67  ? 3747 LYS A CB    1 
ATOM   15995 C  CG    . LYS A 1 3747 ? 212.923 246.613 158.036 1.00 81.06  ? 3747 LYS A CG    1 
ATOM   15996 C  CD    . LYS A 1 3747 ? 212.367 246.112 159.361 1.00 83.81  ? 3747 LYS A CD    1 
ATOM   15997 C  CE    . LYS A 1 3747 ? 211.852 244.688 159.258 1.00 83.36  ? 3747 LYS A CE    1 
ATOM   15998 N  NZ    . LYS A 1 3747 ? 211.281 244.209 160.546 1.00 83.21  ? 3747 LYS A NZ    1 
ATOM   15999 N  N     . SER A 1 3748 ? 211.961 249.558 155.769 1.00 85.17  ? 3748 SER A N     1 
ATOM   16000 C  CA    . SER A 1 3748 ? 210.954 249.590 154.715 1.00 81.40  ? 3748 SER A CA    1 
ATOM   16001 C  C     . SER A 1 3748 ? 211.571 249.948 153.372 1.00 81.06  ? 3748 SER A C     1 
ATOM   16002 O  O     . SER A 1 3748 ? 211.177 249.400 152.338 1.00 84.82  ? 3748 SER A O     1 
ATOM   16003 C  CB    . SER A 1 3748 ? 209.846 250.579 155.077 1.00 83.68  ? 3748 SER A CB    1 
ATOM   16004 O  OG    . SER A 1 3748 ? 210.353 251.898 155.167 1.00 86.97  ? 3748 SER A OG    1 
ATOM   16005 N  N     . LEU A 1 3749 ? 212.536 250.870 153.362 1.00 78.82  ? 3749 LEU A N     1 
ATOM   16006 C  CA    . LEU A 1 3749 ? 213.220 251.218 152.123 1.00 82.68  ? 3749 LEU A CA    1 
ATOM   16007 C  C     . LEU A 1 3749 ? 213.945 250.011 151.549 1.00 85.05  ? 3749 LEU A C     1 
ATOM   16008 O  O     . LEU A 1 3749 ? 213.844 249.723 150.350 1.00 89.05  ? 3749 LEU A O     1 
ATOM   16009 C  CB    . LEU A 1 3749 ? 214.202 252.363 152.372 1.00 84.36  ? 3749 LEU A CB    1 
ATOM   16010 C  CG    . LEU A 1 3749 ? 215.019 252.852 151.175 1.00 85.00  ? 3749 LEU A CG    1 
ATOM   16011 C  CD1   . LEU A 1 3749 ? 214.229 253.869 150.373 1.00 85.83  ? 3749 LEU A CD1   1 
ATOM   16012 C  CD2   . LEU A 1 3749 ? 216.346 253.439 151.627 1.00 85.86  ? 3749 LEU A CD2   1 
ATOM   16013 N  N     . LEU A 1 3750 ? 214.676 249.282 152.395 1.00 86.64  ? 3750 LEU A N     1 
ATOM   16014 C  CA    . LEU A 1 3750 ? 215.399 248.114 151.905 1.00 86.54  ? 3750 LEU A CA    1 
ATOM   16015 C  C     . LEU A 1 3750 ? 214.438 247.039 151.410 1.00 84.96  ? 3750 LEU A C     1 
ATOM   16016 O  O     . LEU A 1 3750 ? 214.663 246.432 150.355 1.00 84.00  ? 3750 LEU A O     1 
ATOM   16017 C  CB    . LEU A 1 3750 ? 216.317 247.565 152.995 1.00 85.39  ? 3750 LEU A CB    1 
ATOM   16018 C  CG    . LEU A 1 3750 ? 217.185 246.375 152.585 1.00 88.11  ? 3750 LEU A CG    1 
ATOM   16019 C  CD1   . LEU A 1 3750 ? 218.138 246.773 151.471 1.00 84.76  ? 3750 LEU A CD1   1 
ATOM   16020 C  CD2   . LEU A 1 3750 ? 217.955 245.848 153.781 1.00 87.51  ? 3750 LEU A CD2   1 
ATOM   16021 N  N     . GLN A 1 3751 ? 213.348 246.802 152.144 1.00 86.83  ? 3751 GLN A N     1 
ATOM   16022 C  CA    . GLN A 1 3751 ? 212.378 245.799 151.714 1.00 83.42  ? 3751 GLN A CA    1 
ATOM   16023 C  C     . GLN A 1 3751 ? 211.731 246.183 150.390 1.00 85.98  ? 3751 GLN A C     1 
ATOM   16024 O  O     . GLN A 1 3751 ? 211.585 245.344 149.497 1.00 90.26  ? 3751 GLN A O     1 
ATOM   16025 C  CB    . GLN A 1 3751 ? 211.313 245.588 152.789 1.00 82.93  ? 3751 GLN A CB    1 
ATOM   16026 C  CG    . GLN A 1 3751 ? 211.838 244.951 154.057 1.00 87.30  ? 3751 GLN A CG    1 
ATOM   16027 C  CD    . GLN A 1 3751 ? 210.753 244.743 155.088 1.00 90.24  ? 3751 GLN A CD    1 
ATOM   16028 O  OE1   . GLN A 1 3751 ? 209.603 245.129 154.882 1.00 91.34  ? 3751 GLN A OE1   1 
ATOM   16029 N  NE2   . GLN A 1 3751 ? 211.110 244.116 156.201 1.00 88.00  ? 3751 GLN A NE2   1 
ATOM   16030 N  N     . ALA A 1 3752 ? 211.331 247.448 150.244 1.00 87.47  ? 3752 ALA A N     1 
ATOM   16031 C  CA    . ALA A 1 3752 ? 210.697 247.882 149.003 1.00 86.18  ? 3752 ALA A CA    1 
ATOM   16032 C  C     . ALA A 1 3752 ? 211.671 247.815 147.836 1.00 88.37  ? 3752 ALA A C     1 
ATOM   16033 O  O     . ALA A 1 3752 ? 211.282 247.476 146.712 1.00 87.79  ? 3752 ALA A O     1 
ATOM   16034 C  CB    . ALA A 1 3752 ? 210.145 249.298 149.162 1.00 82.72  ? 3752 ALA A CB    1 
ATOM   16035 N  N     . LEU A 1 3753 ? 212.942 248.140 148.081 1.00 87.68  ? 3753 LEU A N     1 
ATOM   16036 C  CA    . LEU A 1 3753 ? 213.944 248.042 147.028 1.00 83.11  ? 3753 LEU A CA    1 
ATOM   16037 C  C     . LEU A 1 3753 ? 214.219 246.589 146.660 1.00 83.99  ? 3753 LEU A C     1 
ATOM   16038 O  O     . LEU A 1 3753 ? 214.627 246.301 145.531 1.00 86.64  ? 3753 LEU A O     1 
ATOM   16039 C  CB    . LEU A 1 3753 ? 215.223 248.751 147.470 1.00 85.10  ? 3753 LEU A CB    1 
ATOM   16040 C  CG    . LEU A 1 3753 ? 216.366 248.884 146.469 1.00 87.83  ? 3753 LEU A CG    1 
ATOM   16041 C  CD1   . LEU A 1 3753 ? 216.203 250.159 145.670 1.00 87.00  ? 3753 LEU A CD1   1 
ATOM   16042 C  CD2   . LEU A 1 3753 ? 217.683 248.899 147.199 1.00 88.69  ? 3753 LEU A CD2   1 
ATOM   16043 N  N     . ASN A 1 3754 ? 214.023 245.663 147.603 1.00 89.94  ? 3754 ASN A N     1 
ATOM   16044 C  CA    . ASN A 1 3754 ? 214.121 244.243 147.276 1.00 91.57  ? 3754 ASN A CA    1 
ATOM   16045 C  C     . ASN A 1 3754 ? 212.888 243.740 146.527 1.00 89.66  ? 3754 ASN A C     1 
ATOM   16046 O  O     . ASN A 1 3754 ? 212.998 242.847 145.680 1.00 89.40  ? 3754 ASN A O     1 
ATOM   16047 C  CB    . ASN A 1 3754 ? 214.332 243.419 148.548 1.00 90.44  ? 3754 ASN A CB    1 
ATOM   16048 C  CG    . ASN A 1 3754 ? 215.729 243.567 149.118 1.00 91.73  ? 3754 ASN A CG    1 
ATOM   16049 O  OD1   . ASN A 1 3754 ? 216.588 244.222 148.528 1.00 90.62  ? 3754 ASN A OD1   1 
ATOM   16050 N  ND2   . ASN A 1 3754 ? 215.963 242.957 150.272 1.00 91.26  ? 3754 ASN A ND2   1 
ATOM   16051 N  N     . GLU A 1 3755 ? 211.709 244.292 146.831 1.00 92.75  ? 3755 GLU A N     1 
ATOM   16052 C  CA    . GLU A 1 3755 ? 210.471 243.781 146.247 1.00 91.80  ? 3755 GLU A CA    1 
ATOM   16053 C  C     . GLU A 1 3755 ? 210.307 244.182 144.786 1.00 91.61  ? 3755 GLU A C     1 
ATOM   16054 O  O     . GLU A 1 3755 ? 209.487 243.588 144.077 1.00 90.25  ? 3755 GLU A O     1 
ATOM   16055 C  CB    . GLU A 1 3755 ? 209.260 244.265 147.048 1.00 89.66  ? 3755 GLU A CB    1 
ATOM   16056 C  CG    . GLU A 1 3755 ? 209.169 243.739 148.471 1.00 91.49  ? 3755 GLU A CG    1 
ATOM   16057 C  CD    . GLU A 1 3755 ? 209.518 242.269 148.580 1.00 94.16  ? 3755 GLU A CD    1 
ATOM   16058 O  OE1   . GLU A 1 3755 ? 208.842 241.447 147.925 1.00 94.86  ? 3755 GLU A OE1   1 
ATOM   16059 O  OE2   . GLU A 1 3755 ? 210.461 241.933 149.326 1.00 91.30  ? 3755 GLU A OE2   1 
ATOM   16060 N  N     . VAL A 1 3756 ? 211.055 245.186 144.320 1.00 92.96  ? 3756 VAL A N     1 
ATOM   16061 C  CA    . VAL A 1 3756 ? 210.869 245.652 142.951 1.00 92.83  ? 3756 VAL A CA    1 
ATOM   16062 C  C     . VAL A 1 3756 ? 211.302 244.556 141.974 1.00 96.13  ? 3756 VAL A C     1 
ATOM   16063 O  O     . VAL A 1 3756 ? 212.145 243.703 142.279 1.00 95.13  ? 3756 VAL A O     1 
ATOM   16064 C  CB    . VAL A 1 3756 ? 211.640 246.960 142.701 1.00 94.10  ? 3756 VAL A CB    1 
ATOM   16065 C  CG1   . VAL A 1 3756 ? 213.141 246.727 142.770 1.00 92.85  ? 3756 VAL A CG1   1 
ATOM   16066 C  CG2   . VAL A 1 3756 ? 211.232 247.604 141.380 1.00 94.01  ? 3756 VAL A CG2   1 
ATOM   16067 N  N     . LYS A 1 3757 ? 210.705 244.582 140.784 1.00 97.00  ? 3757 LYS A N     1 
ATOM   16068 C  CA    . LYS A 1 3757 ? 210.932 243.566 139.764 1.00 95.66  ? 3757 LYS A CA    1 
ATOM   16069 C  C     . LYS A 1 3757 ? 212.198 243.807 138.952 1.00 95.84  ? 3757 LYS A C     1 
ATOM   16070 O  O     . LYS A 1 3757 ? 212.322 243.260 137.851 1.00 94.25  ? 3757 LYS A O     1 
ATOM   16071 C  CB    . LYS A 1 3757 ? 209.725 243.489 138.822 1.00 94.24  ? 3757 LYS A CB    1 
ATOM   16072 C  CG    . LYS A 1 3757 ? 208.372 243.519 139.520 1.00 93.92  ? 3757 LYS A CG    1 
ATOM   16073 C  CD    . LYS A 1 3757 ? 208.258 242.440 140.590 1.00 94.13  ? 3757 LYS A CD    1 
ATOM   16074 C  CE    . LYS A 1 3757 ? 208.376 241.045 139.992 1.00 92.98  ? 3757 LYS A CE    1 
ATOM   16075 N  NZ    . LYS A 1 3757 ? 208.272 239.986 141.033 1.00 91.86  ? 3757 LYS A NZ    1 
ATOM   16076 N  N     . GLY A 1 3758 ? 213.132 244.605 139.459 1.00 98.77  ? 3758 GLY A N     1 
ATOM   16077 C  CA    . GLY A 1 3758 ? 214.361 244.884 138.750 1.00 98.11  ? 3758 GLY A CA    1 
ATOM   16078 C  C     . GLY A 1 3758 ? 214.349 246.130 137.896 1.00 99.94  ? 3758 GLY A C     1 
ATOM   16079 O  O     . GLY A 1 3758 ? 215.388 246.471 137.318 1.00 99.17  ? 3758 GLY A O     1 
ATOM   16080 N  N     . ARG A 1 3759 ? 213.213 246.821 137.795 1.00 103.66 ? 3759 ARG A N     1 
ATOM   16081 C  CA    . ARG A 1 3759 ? 213.096 248.038 136.996 1.00 103.92 ? 3759 ARG A CA    1 
ATOM   16082 C  C     . ARG A 1 3759 ? 212.375 249.104 137.825 1.00 103.78 ? 3759 ARG A C     1 
ATOM   16083 O  O     . ARG A 1 3759 ? 211.149 249.222 137.792 1.00 102.66 ? 3759 ARG A O     1 
ATOM   16084 C  CB    . ARG A 1 3759 ? 212.370 247.762 135.679 1.00 104.28 ? 3759 ARG A CB    1 
ATOM   16085 C  CG    . ARG A 1 3759 ? 213.207 247.024 134.645 1.00 103.36 ? 3759 ARG A CG    1 
ATOM   16086 C  CD    . ARG A 1 3759 ? 214.539 247.719 134.396 1.00 102.79 ? 3759 ARG A CD    1 
ATOM   16087 N  NE    . ARG A 1 3759 ? 214.380 249.152 134.178 1.00 106.60 ? 3759 ARG A NE    1 
ATOM   16088 C  CZ    . ARG A 1 3759 ? 214.623 249.767 133.029 1.00 105.72 ? 3759 ARG A CZ    1 
ATOM   16089 N  NH1   . ARG A 1 3759 ? 215.034 249.102 131.962 1.00 105.46 ? 3759 ARG A NH1   1 
ATOM   16090 N  NH2   . ARG A 1 3759 ? 214.452 251.084 132.949 1.00 100.65 ? 3759 ARG A NH2   1 
ATOM   16091 N  N     . ILE A 1 3760 ? 213.154 249.884 138.577 1.00 103.67 ? 3760 ILE A N     1 
ATOM   16092 C  CA    . ILE A 1 3760 ? 212.583 250.999 139.329 1.00 105.39 ? 3760 ILE A CA    1 
ATOM   16093 C  C     . ILE A 1 3760 ? 212.139 252.103 138.376 1.00 106.57 ? 3760 ILE A C     1 
ATOM   16094 O  O     . ILE A 1 3760 ? 211.107 252.751 138.585 1.00 106.56 ? 3760 ILE A O     1 
ATOM   16095 C  CB    . ILE A 1 3760 ? 213.590 251.516 140.372 1.00 103.77 ? 3760 ILE A CB    1 
ATOM   16096 C  CG1   . ILE A 1 3760 ? 213.915 250.418 141.382 1.00 103.07 ? 3760 ILE A CG1   1 
ATOM   16097 C  CG2   . ILE A 1 3760 ? 213.041 252.730 141.097 1.00 103.10 ? 3760 ILE A CG2   1 
ATOM   16098 C  CD1   . ILE A 1 3760 ? 214.931 250.833 142.409 1.00 102.14 ? 3760 ILE A CD1   1 
ATOM   16099 N  N     . LEU A 1 3761 ? 212.913 252.328 137.311 1.00 104.41 ? 3761 LEU A N     1 
ATOM   16100 C  CA    . LEU A 1 3761 ? 212.565 253.363 136.341 1.00 104.04 ? 3761 LEU A CA    1 
ATOM   16101 C  C     . LEU A 1 3761 ? 211.223 253.081 135.678 1.00 104.83 ? 3761 LEU A C     1 
ATOM   16102 O  O     . LEU A 1 3761 ? 210.433 254.001 135.439 1.00 104.74 ? 3761 LEU A O     1 
ATOM   16103 C  CB    . LEU A 1 3761 ? 213.658 253.479 135.276 1.00 104.74 ? 3761 LEU A CB    1 
ATOM   16104 C  CG    . LEU A 1 3761 ? 214.924 254.273 135.600 1.00 105.45 ? 3761 LEU A CG    1 
ATOM   16105 C  CD1   . LEU A 1 3761 ? 215.873 253.457 136.452 1.00 104.02 ? 3761 LEU A CD1   1 
ATOM   16106 C  CD2   . LEU A 1 3761 ? 215.605 254.724 134.318 1.00 103.67 ? 3761 LEU A CD2   1 
ATOM   16107 N  N     . ASP A 1 3762 ? 210.951 251.812 135.367 1.00 104.21 ? 3762 ASP A N     1 
ATOM   16108 C  CA    . ASP A 1 3762 ? 209.740 251.471 134.628 1.00 105.98 ? 3762 ASP A CA    1 
ATOM   16109 C  C     . ASP A 1 3762 ? 208.483 251.724 135.453 1.00 106.75 ? 3762 ASP A C     1 
ATOM   16110 O  O     . ASP A 1 3762 ? 207.470 252.190 134.920 1.00 104.54 ? 3762 ASP A O     1 
ATOM   16111 C  CB    . ASP A 1 3762 ? 209.803 250.016 134.169 1.00 103.52 ? 3762 ASP A CB    1 
ATOM   16112 C  CG    . ASP A 1 3762 ? 210.943 249.762 133.202 1.00 104.57 ? 3762 ASP A CG    1 
ATOM   16113 O  OD1   . ASP A 1 3762 ? 211.687 250.718 132.900 1.00 104.48 ? 3762 ASP A OD1   1 
ATOM   16114 O  OD2   . ASP A 1 3762 ? 211.094 248.611 132.743 1.00 103.75 ? 3762 ASP A OD2   1 
ATOM   16115 N  N     . ASP A 1 3763 ? 208.525 251.426 136.749 1.00 103.82 ? 3763 ASP A N     1 
ATOM   16116 C  CA    . ASP A 1 3763 ? 207.362 251.553 137.622 1.00 103.04 ? 3763 ASP A CA    1 
ATOM   16117 C  C     . ASP A 1 3763 ? 207.483 252.850 138.416 1.00 103.07 ? 3763 ASP A C     1 
ATOM   16118 O  O     . ASP A 1 3763 ? 208.407 253.011 139.219 1.00 103.10 ? 3763 ASP A O     1 
ATOM   16119 C  CB    . ASP A 1 3763 ? 207.250 250.346 138.551 1.00 102.84 ? 3763 ASP A CB    1 
ATOM   16120 C  CG    . ASP A 1 3763 ? 205.951 250.328 139.327 1.00 102.07 ? 3763 ASP A CG    1 
ATOM   16121 O  OD1   . ASP A 1 3763 ? 204.878 250.276 138.691 1.00 100.65 ? 3763 ASP A OD1   1 
ATOM   16122 O  OD2   . ASP A 1 3763 ? 206.002 250.362 140.574 1.00 103.62 ? 3763 ASP A OD2   1 
ATOM   16123 N  N     . ASP A 1 3764 ? 206.545 253.774 138.191 1.00 105.16 ? 3764 ASP A N     1 
ATOM   16124 C  CA    . ASP A 1 3764 ? 206.595 255.056 138.886 1.00 105.40 ? 3764 ASP A CA    1 
ATOM   16125 C  C     . ASP A 1 3764 ? 206.178 254.918 140.345 1.00 106.07 ? 3764 ASP A C     1 
ATOM   16126 O  O     . ASP A 1 3764 ? 206.540 255.754 141.181 1.00 106.63 ? 3764 ASP A O     1 
ATOM   16127 C  CB    . ASP A 1 3764 ? 205.713 256.080 138.171 1.00 103.09 ? 3764 ASP A CB    1 
ATOM   16128 C  CG    . ASP A 1 3764 ? 206.332 256.580 136.881 1.00 105.07 ? 3764 ASP A CG    1 
ATOM   16129 O  OD1   . ASP A 1 3764 ? 207.449 256.132 136.544 1.00 106.10 ? 3764 ASP A OD1   1 
ATOM   16130 O  OD2   . ASP A 1 3764 ? 205.705 257.424 136.207 1.00 103.84 ? 3764 ASP A OD2   1 
ATOM   16131 N  N     . THR A 1 3765 ? 205.412 253.875 140.671 1.00 99.45  ? 3765 THR A N     1 
ATOM   16132 C  CA    . THR A 1 3765 ? 204.992 253.660 142.052 1.00 101.51 ? 3765 THR A CA    1 
ATOM   16133 C  C     . THR A 1 3765 ? 206.193 253.428 142.961 1.00 101.02 ? 3765 THR A C     1 
ATOM   16134 O  O     . THR A 1 3765 ? 206.276 253.980 144.066 1.00 100.00 ? 3765 THR A O     1 
ATOM   16135 C  CB    . THR A 1 3765 ? 204.024 252.476 142.127 1.00 101.36 ? 3765 THR A CB    1 
ATOM   16136 O  OG1   . THR A 1 3765 ? 202.943 252.681 141.208 1.00 99.31  ? 3765 THR A OG1   1 
ATOM   16137 C  CG2   . THR A 1 3765 ? 203.463 252.333 143.534 1.00 98.73  ? 3765 THR A CG2   1 
ATOM   16138 N  N     . ILE A 1 3766 ? 207.145 252.615 142.497 1.00 99.67  ? 3766 ILE A N     1 
ATOM   16139 C  CA    . ILE A 1 3766 ? 208.350 252.357 143.276 1.00 101.19 ? 3766 ILE A CA    1 
ATOM   16140 C  C     . ILE A 1 3766 ? 209.161 253.635 143.446 1.00 99.40  ? 3766 ILE A C     1 
ATOM   16141 O  O     . ILE A 1 3766 ? 209.700 253.902 144.527 1.00 101.70 ? 3766 ILE A O     1 
ATOM   16142 C  CB    . ILE A 1 3766 ? 209.179 251.238 142.620 1.00 100.79 ? 3766 ILE A CB    1 
ATOM   16143 C  CG1   . ILE A 1 3766 ? 208.416 249.914 142.671 1.00 98.75  ? 3766 ILE A CG1   1 
ATOM   16144 C  CG2   . ILE A 1 3766 ? 210.527 251.094 143.306 1.00 98.06  ? 3766 ILE A CG2   1 
ATOM   16145 C  CD1   . ILE A 1 3766 ? 208.103 249.447 144.075 1.00 96.52  ? 3766 ILE A CD1   1 
ATOM   16146 N  N     . ILE A 1 3767 ? 209.258 254.445 142.389 1.00 93.03  ? 3767 ILE A N     1 
ATOM   16147 C  CA    . ILE A 1 3767 ? 210.001 255.700 142.483 1.00 97.85  ? 3767 ILE A CA    1 
ATOM   16148 C  C     . ILE A 1 3767 ? 209.353 256.625 143.504 1.00 95.91  ? 3767 ILE A C     1 
ATOM   16149 O  O     . ILE A 1 3767 ? 210.039 257.252 144.322 1.00 95.91  ? 3767 ILE A O     1 
ATOM   16150 C  CB    . ILE A 1 3767 ? 210.101 256.368 141.099 1.00 99.57  ? 3767 ILE A CB    1 
ATOM   16151 C  CG1   . ILE A 1 3767 ? 210.963 255.527 140.159 1.00 97.01  ? 3767 ILE A CG1   1 
ATOM   16152 C  CG2   . ILE A 1 3767 ? 210.698 257.758 141.226 1.00 97.24  ? 3767 ILE A CG2   1 
ATOM   16153 C  CD1   . ILE A 1 3767 ? 211.131 256.130 138.784 1.00 95.66  ? 3767 ILE A CD1   1 
ATOM   16154 N  N     . THR A 1 3768 ? 208.021 256.727 143.473 1.00 92.90  ? 3768 THR A N     1 
ATOM   16155 C  CA    . THR A 1 3768 ? 207.322 257.574 144.433 1.00 97.51  ? 3768 THR A CA    1 
ATOM   16156 C  C     . THR A 1 3768 ? 207.534 257.085 145.858 1.00 97.63  ? 3768 THR A C     1 
ATOM   16157 O  O     . THR A 1 3768 ? 207.761 257.890 146.769 1.00 95.77  ? 3768 THR A O     1 
ATOM   16158 C  CB    . THR A 1 3768 ? 205.829 257.629 144.107 1.00 96.09  ? 3768 THR A CB    1 
ATOM   16159 O  OG1   . THR A 1 3768 ? 205.321 256.298 143.954 1.00 94.19  ? 3768 THR A OG1   1 
ATOM   16160 C  CG2   . THR A 1 3768 ? 205.590 258.411 142.825 1.00 93.84  ? 3768 THR A CG2   1 
ATOM   16161 N  N     . THR A 1 3769 ? 207.464 255.767 146.074 1.00 94.37  ? 3769 THR A N     1 
ATOM   16162 C  CA    . THR A 1 3769 ? 207.691 255.237 147.416 1.00 93.00  ? 3769 THR A CA    1 
ATOM   16163 C  C     . THR A 1 3769 ? 209.108 255.527 147.895 1.00 91.74  ? 3769 THR A C     1 
ATOM   16164 O  O     . THR A 1 3769 ? 209.310 255.920 149.051 1.00 94.76  ? 3769 THR A O     1 
ATOM   16165 C  CB    . THR A 1 3769 ? 207.419 253.733 147.451 1.00 92.16  ? 3769 THR A CB    1 
ATOM   16166 O  OG1   . THR A 1 3769 ? 208.186 253.083 146.431 1.00 91.66  ? 3769 THR A OG1   1 
ATOM   16167 C  CG2   . THR A 1 3769 ? 205.938 253.450 147.237 1.00 92.37  ? 3769 THR A CG2   1 
ATOM   16168 N  N     . LEU A 1 3770 ? 210.101 255.344 147.020 1.00 88.48  ? 3770 LEU A N     1 
ATOM   16169 C  CA    . LEU A 1 3770 ? 211.482 255.611 147.410 1.00 89.88  ? 3770 LEU A CA    1 
ATOM   16170 C  C     . LEU A 1 3770 ? 211.682 257.080 147.756 1.00 92.61  ? 3770 LEU A C     1 
ATOM   16171 O  O     . LEU A 1 3770 ? 212.323 257.406 148.764 1.00 96.68  ? 3770 LEU A O     1 
ATOM   16172 C  CB    . LEU A 1 3770 ? 212.439 255.190 146.295 1.00 89.05  ? 3770 LEU A CB    1 
ATOM   16173 C  CG    . LEU A 1 3770 ? 212.498 253.701 145.951 1.00 91.76  ? 3770 LEU A CG    1 
ATOM   16174 C  CD1   . LEU A 1 3770 ? 213.539 253.440 144.874 1.00 92.67  ? 3770 LEU A CD1   1 
ATOM   16175 C  CD2   . LEU A 1 3770 ? 212.771 252.860 147.185 1.00 90.91  ? 3770 LEU A CD2   1 
ATOM   16176 N  N     . GLU A 1 3771 ? 211.138 257.983 146.936 1.00 93.55  ? 3771 GLU A N     1 
ATOM   16177 C  CA    . GLU A 1 3771 ? 211.284 259.408 147.213 1.00 91.51  ? 3771 GLU A CA    1 
ATOM   16178 C  C     . GLU A 1 3771 ? 210.581 259.798 148.507 1.00 92.09  ? 3771 GLU A C     1 
ATOM   16179 O  O     . GLU A 1 3771 ? 211.113 260.593 149.291 1.00 91.05  ? 3771 GLU A O     1 
ATOM   16180 C  CB    . GLU A 1 3771 ? 210.757 260.235 146.040 1.00 92.14  ? 3771 GLU A CB    1 
ATOM   16181 C  CG    . GLU A 1 3771 ? 211.502 260.003 144.735 1.00 94.83  ? 3771 GLU A CG    1 
ATOM   16182 C  CD    . GLU A 1 3771 ? 211.411 261.186 143.792 1.00 96.94  ? 3771 GLU A CD    1 
ATOM   16183 O  OE1   . GLU A 1 3771 ? 210.282 261.546 143.395 1.00 96.34  ? 3771 GLU A OE1   1 
ATOM   16184 O  OE2   . GLU A 1 3771 ? 212.467 261.754 143.446 1.00 94.04  ? 3771 GLU A OE2   1 
ATOM   16185 N  N     . ASN A 1 3772 ? 209.385 259.253 148.751 1.00 91.05  ? 3772 ASN A N     1 
ATOM   16186 C  CA    . ASN A 1 3772 ? 208.676 259.558 149.989 1.00 93.69  ? 3772 ASN A CA    1 
ATOM   16187 C  C     . ASN A 1 3772 ? 209.458 259.082 151.205 1.00 92.91  ? 3772 ASN A C     1 
ATOM   16188 O  O     . ASN A 1 3772 ? 209.597 259.817 152.192 1.00 94.36  ? 3772 ASN A O     1 
ATOM   16189 C  CB    . ASN A 1 3772 ? 207.285 258.923 149.967 1.00 91.48  ? 3772 ASN A CB    1 
ATOM   16190 C  CG    . ASN A 1 3772 ? 206.314 259.675 149.080 1.00 95.01  ? 3772 ASN A CG    1 
ATOM   16191 O  OD1   . ASN A 1 3772 ? 206.638 260.732 148.540 1.00 97.15  ? 3772 ASN A OD1   1 
ATOM   16192 N  ND2   . ASN A 1 3772 ? 205.112 259.130 148.925 1.00 92.95  ? 3772 ASN A ND2   1 
ATOM   16193 N  N     . LEU A 1 3773 ? 209.984 257.856 151.149 1.00 88.17  ? 3773 LEU A N     1 
ATOM   16194 C  CA    . LEU A 1 3773 ? 210.758 257.338 152.271 1.00 87.90  ? 3773 LEU A CA    1 
ATOM   16195 C  C     . LEU A 1 3773 ? 212.018 258.163 152.500 1.00 90.12  ? 3773 LEU A C     1 
ATOM   16196 O  O     . LEU A 1 3773 ? 212.372 258.456 153.647 1.00 92.62  ? 3773 LEU A O     1 
ATOM   16197 C  CB    . LEU A 1 3773 ? 211.105 255.869 152.035 1.00 87.04  ? 3773 LEU A CB    1 
ATOM   16198 C  CG    . LEU A 1 3773 ? 209.927 254.897 152.119 1.00 89.33  ? 3773 LEU A CG    1 
ATOM   16199 C  CD1   . LEU A 1 3773 ? 210.357 253.489 151.749 1.00 87.33  ? 3773 LEU A CD1   1 
ATOM   16200 C  CD2   . LEU A 1 3773 ? 209.309 254.922 153.506 1.00 88.39  ? 3773 LEU A CD2   1 
ATOM   16201 N  N     . LYS A 1 3774 ? 212.703 258.557 151.424 1.00 89.28  ? 3774 LYS A N     1 
ATOM   16202 C  CA    . LYS A 1 3774 ? 213.920 259.348 151.582 1.00 88.95  ? 3774 LYS A CA    1 
ATOM   16203 C  C     . LYS A 1 3774 ? 213.620 260.729 152.155 1.00 89.71  ? 3774 LYS A C     1 
ATOM   16204 O  O     . LYS A 1 3774 ? 214.373 261.234 152.997 1.00 90.92  ? 3774 LYS A O     1 
ATOM   16205 C  CB    . LYS A 1 3774 ? 214.647 259.463 150.244 1.00 87.46  ? 3774 LYS A CB    1 
ATOM   16206 C  CG    . LYS A 1 3774 ? 215.759 258.447 150.061 1.00 87.77  ? 3774 LYS A CG    1 
ATOM   16207 C  CD    . LYS A 1 3774 ? 216.904 258.695 151.029 1.00 90.57  ? 3774 LYS A CD    1 
ATOM   16208 C  CE    . LYS A 1 3774 ? 217.375 260.140 150.977 1.00 90.95  ? 3774 LYS A CE    1 
ATOM   16209 N  NZ    . LYS A 1 3774 ? 218.688 260.322 151.656 1.00 90.53  ? 3774 LYS A NZ    1 
ATOM   16210 N  N     . ARG A 1 3775 ? 212.530 261.360 151.710 1.00 88.97  ? 3775 ARG A N     1 
ATOM   16211 C  CA    . ARG A 1 3775 ? 212.161 262.666 152.247 1.00 90.67  ? 3775 ARG A CA    1 
ATOM   16212 C  C     . ARG A 1 3775 ? 211.800 262.571 153.724 1.00 91.99  ? 3775 ARG A C     1 
ATOM   16213 O  O     . ARG A 1 3775 ? 212.201 263.425 154.531 1.00 92.23  ? 3775 ARG A O     1 
ATOM   16214 C  CB    . ARG A 1 3775 ? 211.002 263.247 151.440 1.00 91.26  ? 3775 ARG A CB    1 
ATOM   16215 C  CG    . ARG A 1 3775 ? 210.739 264.721 151.677 1.00 89.22  ? 3775 ARG A CG    1 
ATOM   16216 C  CD    . ARG A 1 3775 ? 209.682 265.237 150.716 1.00 90.64  ? 3775 ARG A CD    1 
ATOM   16217 N  NE    . ARG A 1 3775 ? 209.901 264.747 149.360 1.00 93.03  ? 3775 ARG A NE    1 
ATOM   16218 C  CZ    . ARG A 1 3775 ? 209.026 264.027 148.672 1.00 92.89  ? 3775 ARG A CZ    1 
ATOM   16219 N  NH1   . ARG A 1 3775 ? 207.856 263.682 149.186 1.00 90.70  ? 3775 ARG A NH1   1 
ATOM   16220 N  NH2   . ARG A 1 3775 ? 209.333 263.639 147.437 1.00 88.44  ? 3775 ARG A NH2   1 
ATOM   16221 N  N     . GLU A 1 3776 ? 211.046 261.534 154.098 1.00 86.76  ? 3776 GLU A N     1 
ATOM   16222 C  CA    . GLU A 1 3776 ? 210.716 261.334 155.504 1.00 85.47  ? 3776 GLU A CA    1 
ATOM   16223 C  C     . GLU A 1 3776 ? 211.975 261.098 156.330 1.00 87.17  ? 3776 GLU A C     1 
ATOM   16224 O  O     . GLU A 1 3776 ? 212.104 261.630 157.439 1.00 87.32  ? 3776 GLU A O     1 
ATOM   16225 C  CB    . GLU A 1 3776 ? 209.739 260.166 155.647 1.00 85.20  ? 3776 GLU A CB    1 
ATOM   16226 C  CG    . GLU A 1 3776 ? 209.280 259.884 157.070 1.00 89.03  ? 3776 GLU A CG    1 
ATOM   16227 C  CD    . GLU A 1 3776 ? 208.459 261.010 157.664 1.00 91.10  ? 3776 GLU A CD    1 
ATOM   16228 O  OE1   . GLU A 1 3776 ? 207.832 261.764 156.892 1.00 93.23  ? 3776 GLU A OE1   1 
ATOM   16229 O  OE2   . GLU A 1 3776 ? 208.441 261.138 158.907 1.00 88.81  ? 3776 GLU A OE2   1 
ATOM   16230 N  N     . ALA A 1 3777 ? 212.921 260.320 155.796 1.00 86.57  ? 3777 ALA A N     1 
ATOM   16231 C  CA    . ALA A 1 3777 ? 214.177 260.080 156.501 1.00 85.99  ? 3777 ALA A CA    1 
ATOM   16232 C  C     . ALA A 1 3777 ? 214.966 261.369 156.689 1.00 87.50  ? 3777 ALA A C     1 
ATOM   16233 O  O     . ALA A 1 3777 ? 215.533 261.605 157.761 1.00 93.40  ? 3777 ALA A O     1 
ATOM   16234 C  CB    . ALA A 1 3777 ? 215.012 259.046 155.748 1.00 82.60  ? 3777 ALA A CB    1 
ATOM   16235 N  N     . ALA A 1 3778 ? 215.019 262.213 155.657 1.00 81.22  ? 3778 ALA A N     1 
ATOM   16236 C  CA    . ALA A 1 3778 ? 215.740 263.477 155.777 1.00 81.92  ? 3778 ALA A CA    1 
ATOM   16237 C  C     . ALA A 1 3778 ? 215.111 264.380 156.832 1.00 84.23  ? 3778 ALA A C     1 
ATOM   16238 O  O     . ALA A 1 3778 ? 215.822 264.974 157.657 1.00 81.40  ? 3778 ALA A O     1 
ATOM   16239 C  CB    . ALA A 1 3778 ? 215.788 264.184 154.423 1.00 80.72  ? 3778 ALA A CB    1 
ATOM   16240 N  N     . GLU A 1 3779 ? 213.779 264.495 156.828 1.00 88.71  ? 3779 GLU A N     1 
ATOM   16241 C  CA    . GLU A 1 3779 ? 213.136 265.365 157.808 1.00 88.78  ? 3779 GLU A CA    1 
ATOM   16242 C  C     . GLU A 1 3779 ? 213.295 264.813 159.223 1.00 90.83  ? 3779 GLU A C     1 
ATOM   16243 O  O     . GLU A 1 3779 ? 213.491 265.580 160.178 1.00 89.51  ? 3779 GLU A O     1 
ATOM   16244 C  CB    . GLU A 1 3779 ? 211.662 265.580 157.450 1.00 87.04  ? 3779 GLU A CB    1 
ATOM   16245 C  CG    . GLU A 1 3779 ? 210.697 264.513 157.933 1.00 89.84  ? 3779 GLU A CG    1 
ATOM   16246 C  CD    . GLU A 1 3779 ? 209.246 264.907 157.717 1.00 93.18  ? 3779 GLU A CD    1 
ATOM   16247 O  OE1   . GLU A 1 3779 ? 209.002 265.948 157.072 1.00 91.07  ? 3779 GLU A OE1   1 
ATOM   16248 O  OE2   . GLU A 1 3779 ? 208.351 264.182 158.199 1.00 89.72  ? 3779 GLU A OE2   1 
ATOM   16249 N  N     . VAL A 1 3780 ? 213.257 263.487 159.376 1.00 88.40  ? 3780 VAL A N     1 
ATOM   16250 C  CA    . VAL A 1 3780 ? 213.459 262.896 160.694 1.00 85.17  ? 3780 VAL A CA    1 
ATOM   16251 C  C     . VAL A 1 3780 ? 214.893 263.112 161.162 1.00 83.56  ? 3780 VAL A C     1 
ATOM   16252 O  O     . VAL A 1 3780 ? 215.137 263.356 162.347 1.00 88.22  ? 3780 VAL A O     1 
ATOM   16253 C  CB    . VAL A 1 3780 ? 213.075 261.405 160.678 1.00 82.72  ? 3780 VAL A CB    1 
ATOM   16254 C  CG1   . VAL A 1 3780 ? 213.561 260.715 161.937 1.00 84.77  ? 3780 VAL A CG1   1 
ATOM   16255 C  CG2   . VAL A 1 3780 ? 211.569 261.256 160.555 1.00 86.23  ? 3780 VAL A CG2   1 
ATOM   16256 N  N     . THR A 1 3781 ? 215.862 263.040 160.246 1.00 78.94  ? 3781 THR A N     1 
ATOM   16257 C  CA    . THR A 1 3781 ? 217.249 263.310 160.617 1.00 82.02  ? 3781 THR A CA    1 
ATOM   16258 C  C     . THR A 1 3781 ? 217.428 264.751 161.081 1.00 87.40  ? 3781 THR A C     1 
ATOM   16259 O  O     . THR A 1 3781 ? 218.129 265.013 162.068 1.00 87.47  ? 3781 THR A O     1 
ATOM   16260 C  CB    . THR A 1 3781 ? 218.175 263.008 159.439 1.00 84.20  ? 3781 THR A CB    1 
ATOM   16261 O  OG1   . THR A 1 3781 ? 218.062 261.625 159.082 1.00 84.23  ? 3781 THR A OG1   1 
ATOM   16262 C  CG2   . THR A 1 3781 ? 219.620 263.314 159.800 1.00 82.58  ? 3781 THR A CG2   1 
ATOM   16263 N  N     . ARG A 1 3782 ? 216.804 265.701 160.380 1.00 89.55  ? 3782 ARG A N     1 
ATOM   16264 C  CA    . ARG A 1 3782 ? 216.879 267.096 160.814 1.00 89.88  ? 3782 ARG A CA    1 
ATOM   16265 C  C     . ARG A 1 3782 ? 216.252 267.279 162.195 1.00 88.12  ? 3782 ARG A C     1 
ATOM   16266 O  O     . ARG A 1 3782 ? 216.804 267.986 163.057 1.00 86.49  ? 3782 ARG A O     1 
ATOM   16267 C  CB    . ARG A 1 3782 ? 216.203 268.000 159.783 1.00 88.04  ? 3782 ARG A CB    1 
ATOM   16268 C  CG    . ARG A 1 3782 ? 215.902 269.404 160.280 1.00 87.85  ? 3782 ARG A CG    1 
ATOM   16269 C  CD    . ARG A 1 3782 ? 214.977 270.146 159.324 1.00 86.08  ? 3782 ARG A CD    1 
ATOM   16270 N  NE    . ARG A 1 3782 ? 213.727 269.434 159.079 1.00 90.51  ? 3782 ARG A NE    1 
ATOM   16271 C  CZ    . ARG A 1 3782 ? 212.756 269.284 159.970 1.00 90.64  ? 3782 ARG A CZ    1 
ATOM   16272 N  NH1   . ARG A 1 3782 ? 212.844 269.798 161.185 1.00 87.54  ? 3782 ARG A NH1   1 
ATOM   16273 N  NH2   . ARG A 1 3782 ? 211.664 268.606 159.629 1.00 87.41  ? 3782 ARG A NH2   1 
ATOM   16274 N  N     . LYS A 1 3783 ? 215.102 266.640 162.426 1.00 83.08  ? 3783 LYS A N     1 
ATOM   16275 C  CA    . LYS A 1 3783 ? 214.467 266.720 163.738 1.00 87.15  ? 3783 LYS A CA    1 
ATOM   16276 C  C     . LYS A 1 3783 ? 215.351 266.103 164.818 1.00 87.19  ? 3783 LYS A C     1 
ATOM   16277 O  O     . LYS A 1 3783 ? 215.420 266.615 165.942 1.00 88.41  ? 3783 LYS A O     1 
ATOM   16278 C  CB    . LYS A 1 3783 ? 213.099 266.041 163.697 1.00 86.74  ? 3783 LYS A CB    1 
ATOM   16279 C  CG    . LYS A 1 3783 ? 211.987 266.942 163.185 1.00 86.74  ? 3783 LYS A CG    1 
ATOM   16280 C  CD    . LYS A 1 3783 ? 210.624 266.476 163.664 1.00 86.93  ? 3783 LYS A CD    1 
ATOM   16281 C  CE    . LYS A 1 3783 ? 210.187 265.211 162.947 1.00 88.55  ? 3783 LYS A CE    1 
ATOM   16282 N  NZ    . LYS A 1 3783 ? 209.486 265.518 161.670 1.00 88.48  ? 3783 LYS A NZ    1 
ATOM   16283 N  N     . VAL A 1 3784 ? 216.036 265.004 164.493 1.00 86.06  ? 3784 VAL A N     1 
ATOM   16284 C  CA    . VAL A 1 3784 ? 216.961 264.386 165.440 1.00 86.38  ? 3784 VAL A CA    1 
ATOM   16285 C  C     . VAL A 1 3784 ? 218.094 265.343 165.780 1.00 86.41  ? 3784 VAL A C     1 
ATOM   16286 O  O     . VAL A 1 3784 ? 218.495 265.464 166.942 1.00 90.81  ? 3784 VAL A O     1 
ATOM   16287 C  CB    . VAL A 1 3784 ? 217.494 263.053 164.882 1.00 85.78  ? 3784 VAL A CB    1 
ATOM   16288 C  CG1   . VAL A 1 3784 ? 218.665 262.560 165.713 1.00 83.68  ? 3784 VAL A CG1   1 
ATOM   16289 C  CG2   . VAL A 1 3784 ? 216.399 262.011 164.872 1.00 84.86  ? 3784 VAL A CG2   1 
ATOM   16290 N  N     . GLU A 1 3785 ? 218.630 266.035 164.775 1.00 86.54  ? 3785 GLU A N     1 
ATOM   16291 C  CA    . GLU A 1 3785 ? 219.708 266.986 165.036 1.00 89.77  ? 3785 GLU A CA    1 
ATOM   16292 C  C     . GLU A 1 3785 ? 219.250 268.095 165.981 1.00 92.37  ? 3785 GLU A C     1 
ATOM   16293 O  O     . GLU A 1 3785 ? 219.939 268.427 166.959 1.00 92.12  ? 3785 GLU A O     1 
ATOM   16294 C  CB    . GLU A 1 3785 ? 220.216 267.572 163.719 1.00 89.74  ? 3785 GLU A CB    1 
ATOM   16295 C  CG    . GLU A 1 3785 ? 221.184 268.730 163.885 1.00 90.50  ? 3785 GLU A CG    1 
ATOM   16296 C  CD    . GLU A 1 3785 ? 221.585 269.348 162.559 1.00 94.56  ? 3785 GLU A CD    1 
ATOM   16297 O  OE1   . GLU A 1 3785 ? 221.112 268.864 161.509 1.00 94.17  ? 3785 GLU A OE1   1 
ATOM   16298 O  OE2   . GLU A 1 3785 ? 222.374 270.316 162.564 1.00 91.93  ? 3785 GLU A OE2   1 
ATOM   16299 N  N     . GLU A 1 3786 ? 218.073 268.672 165.718 1.00 90.72  ? 3786 GLU A N     1 
ATOM   16300 C  CA    . GLU A 1 3786 ? 217.629 269.781 166.561 1.00 88.45  ? 3786 GLU A CA    1 
ATOM   16301 C  C     . GLU A 1 3786 ? 217.294 269.312 167.978 1.00 91.29  ? 3786 GLU A C     1 
ATOM   16302 O  O     . GLU A 1 3786 ? 217.618 269.997 168.963 1.00 92.38  ? 3786 GLU A O     1 
ATOM   16303 C  CB    . GLU A 1 3786 ? 216.445 270.506 165.915 1.00 88.82  ? 3786 GLU A CB    1 
ATOM   16304 C  CG    . GLU A 1 3786 ? 215.182 269.690 165.749 1.00 91.25  ? 3786 GLU A CG    1 
ATOM   16305 C  CD    . GLU A 1 3786 ? 214.190 270.349 164.812 1.00 92.69  ? 3786 GLU A CD    1 
ATOM   16306 O  OE1   . GLU A 1 3786 ? 214.546 271.377 164.199 1.00 92.10  ? 3786 GLU A OE1   1 
ATOM   16307 O  OE2   . GLU A 1 3786 ? 213.055 269.843 164.693 1.00 92.06  ? 3786 GLU A OE2   1 
ATOM   16308 N  N     . THR A 1 3787 ? 216.671 268.136 168.112 1.00 88.15  ? 3787 THR A N     1 
ATOM   16309 C  CA    . THR A 1 3787 ? 216.386 267.634 169.451 1.00 86.02  ? 3787 THR A CA    1 
ATOM   16310 C  C     . THR A 1 3787 ? 217.669 267.243 170.177 1.00 86.25  ? 3787 THR A C     1 
ATOM   16311 O  O     . THR A 1 3787 ? 217.726 267.309 171.407 1.00 91.54  ? 3787 THR A O     1 
ATOM   16312 C  CB    . THR A 1 3787 ? 215.397 266.464 169.390 1.00 88.06  ? 3787 THR A CB    1 
ATOM   16313 O  OG1   . THR A 1 3787 ? 214.982 266.114 170.714 1.00 91.58  ? 3787 THR A OG1   1 
ATOM   16314 C  CG2   . THR A 1 3787 ? 216.016 265.253 168.749 1.00 87.31  ? 3787 THR A CG2   1 
ATOM   16315 N  N     . ASP A 1 3788 ? 218.723 266.880 169.438 1.00 85.44  ? 3788 ASP A N     1 
ATOM   16316 C  CA    . ASP A 1 3788 ? 220.025 266.668 170.066 1.00 86.36  ? 3788 ASP A CA    1 
ATOM   16317 C  C     . ASP A 1 3788 ? 220.599 267.972 170.603 1.00 86.86  ? 3788 ASP A C     1 
ATOM   16318 O  O     . ASP A 1 3788 ? 221.220 267.993 171.673 1.00 90.68  ? 3788 ASP A O     1 
ATOM   16319 C  CB    . ASP A 1 3788 ? 220.996 266.030 169.073 1.00 84.59  ? 3788 ASP A CB    1 
ATOM   16320 C  CG    . ASP A 1 3788 ? 220.717 264.559 168.847 1.00 91.25  ? 3788 ASP A CG    1 
ATOM   16321 O  OD1   . ASP A 1 3788 ? 219.790 264.020 169.487 1.00 89.41  ? 3788 ASP A OD1   1 
ATOM   16322 O  OD2   . ASP A 1 3788 ? 221.429 263.938 168.030 1.00 92.31  ? 3788 ASP A OD2   1 
ATOM   16323 N  N     . ILE A 1 3789 ? 220.423 269.069 169.864 1.00 84.33  ? 3789 ILE A N     1 
ATOM   16324 C  CA    . ILE A 1 3789 ? 220.876 270.366 170.373 1.00 87.69  ? 3789 ILE A CA    1 
ATOM   16325 C  C     . ILE A 1 3789 ? 220.149 270.712 171.671 1.00 88.46  ? 3789 ILE A C     1 
ATOM   16326 O  O     . ILE A 1 3789 ? 220.759 271.165 172.653 1.00 87.05  ? 3789 ILE A O     1 
ATOM   16327 C  CB    . ILE A 1 3789 ? 220.691 271.464 169.310 1.00 87.70  ? 3789 ILE A CB    1 
ATOM   16328 C  CG1   . ILE A 1 3789 ? 221.321 271.039 167.985 1.00 87.49  ? 3789 ILE A CG1   1 
ATOM   16329 C  CG2   . ILE A 1 3789 ? 221.296 272.773 169.787 1.00 84.69  ? 3789 ILE A CG2   1 
ATOM   16330 C  CD1   . ILE A 1 3789 ? 221.086 272.016 166.856 1.00 85.20  ? 3789 ILE A CD1   1 
ATOM   16331 N  N     . VAL A 1 3790 ? 218.832 270.496 171.699 1.00 84.80  ? 3790 VAL A N     1 
ATOM   16332 C  CA    . VAL A 1 3790 ? 218.078 270.765 172.926 1.00 83.20  ? 3790 VAL A CA    1 
ATOM   16333 C  C     . VAL A 1 3790 ? 218.533 269.837 174.054 1.00 83.53  ? 3790 VAL A C     1 
ATOM   16334 O  O     . VAL A 1 3790 ? 218.599 270.237 175.228 1.00 85.36  ? 3790 VAL A O     1 
ATOM   16335 C  CB    . VAL A 1 3790 ? 216.566 270.651 172.664 1.00 84.79  ? 3790 VAL A CB    1 
ATOM   16336 C  CG1   . VAL A 1 3790 ? 215.784 271.118 173.879 1.00 83.00  ? 3790 VAL A CG1   1 
ATOM   16337 C  CG2   . VAL A 1 3790 ? 216.182 271.466 171.442 1.00 85.49  ? 3790 VAL A CG2   1 
ATOM   16338 N  N     . MET A 1 3791 ? 218.856 268.585 173.717 1.00 84.85  ? 3791 MET A N     1 
ATOM   16339 C  CA    . MET A 1 3791 ? 219.396 267.655 174.704 1.00 82.94  ? 3791 MET A CA    1 
ATOM   16340 C  C     . MET A 1 3791 ? 220.692 268.178 175.304 1.00 83.87  ? 3791 MET A C     1 
ATOM   16341 O  O     . MET A 1 3791 ? 220.921 268.055 176.511 1.00 86.19  ? 3791 MET A O     1 
ATOM   16342 C  CB    . MET A 1 3791 ? 219.634 266.291 174.060 1.00 82.80  ? 3791 MET A CB    1 
ATOM   16343 C  CG    . MET A 1 3791 ? 220.087 265.217 175.031 1.00 86.50  ? 3791 MET A CG    1 
ATOM   16344 S  SD    . MET A 1 3791 ? 218.843 264.852 176.274 1.00 96.81  ? 3791 MET A SD    1 
ATOM   16345 C  CE    . MET A 1 3791 ? 217.660 263.973 175.262 1.00 87.88  ? 3791 MET A CE    1 
ATOM   16346 N  N     . GLN A 1 3792 ? 221.565 268.739 174.467 1.00 81.79  ? 3792 GLN A N     1 
ATOM   16347 C  CA    . GLN A 1 3792 ? 222.803 269.325 174.973 1.00 83.53  ? 3792 GLN A CA    1 
ATOM   16348 C  C     . GLN A 1 3792 ? 222.510 270.494 175.904 1.00 83.64  ? 3792 GLN A C     1 
ATOM   16349 O  O     . GLN A 1 3792 ? 223.179 270.667 176.935 1.00 85.14  ? 3792 GLN A O     1 
ATOM   16350 C  CB    . GLN A 1 3792 ? 223.688 269.769 173.810 1.00 82.84  ? 3792 GLN A CB    1 
ATOM   16351 C  CG    . GLN A 1 3792 ? 225.033 270.321 174.240 1.00 82.97  ? 3792 GLN A CG    1 
ATOM   16352 C  CD    . GLN A 1 3792 ? 225.912 269.265 174.875 1.00 85.95  ? 3792 GLN A CD    1 
ATOM   16353 O  OE1   . GLN A 1 3792 ? 225.968 268.127 174.410 1.00 84.73  ? 3792 GLN A OE1   1 
ATOM   16354 N  NE2   . GLN A 1 3792 ? 226.603 269.635 175.946 1.00 83.67  ? 3792 GLN A NE2   1 
ATOM   16355 N  N     . GLU A 1 3793 ? 221.513 271.309 175.555 1.00 81.91  ? 3793 GLU A N     1 
ATOM   16356 C  CA    . GLU A 1 3793 ? 221.119 272.407 176.435 1.00 82.04  ? 3793 GLU A CA    1 
ATOM   16357 C  C     . GLU A 1 3793 ? 220.696 271.890 177.807 1.00 79.60  ? 3793 GLU A C     1 
ATOM   16358 O  O     . GLU A 1 3793 ? 221.023 272.488 178.838 1.00 76.98  ? 3793 GLU A O     1 
ATOM   16359 C  CB    . GLU A 1 3793 ? 219.994 273.222 175.797 1.00 81.66  ? 3793 GLU A CB    1 
ATOM   16360 C  CG    . GLU A 1 3793 ? 220.440 274.106 174.644 1.00 83.68  ? 3793 GLU A CG    1 
ATOM   16361 C  CD    . GLU A 1 3793 ? 221.440 275.163 175.073 1.00 84.02  ? 3793 GLU A CD    1 
ATOM   16362 O  OE1   . GLU A 1 3793 ? 221.362 275.626 176.231 1.00 84.27  ? 3793 GLU A OE1   1 
ATOM   16363 O  OE2   . GLU A 1 3793 ? 222.303 275.533 174.251 1.00 82.26  ? 3793 GLU A OE2   1 
ATOM   16364 N  N     . VAL A 1 3794 ? 219.956 270.780 177.836 1.00 79.00  ? 3794 VAL A N     1 
ATOM   16365 C  CA    . VAL A 1 3794 ? 219.522 270.209 179.115 1.00 75.58  ? 3794 VAL A CA    1 
ATOM   16366 C  C     . VAL A 1 3794 ? 220.709 269.622 179.877 1.00 77.08  ? 3794 VAL A C     1 
ATOM   16367 O  O     . VAL A 1 3794 ? 220.816 269.750 181.107 1.00 81.31  ? 3794 VAL A O     1 
ATOM   16368 C  CB    . VAL A 1 3794 ? 218.423 269.157 178.884 1.00 76.27  ? 3794 VAL A CB    1 
ATOM   16369 C  CG1   . VAL A 1 3794 ? 218.099 268.437 180.178 1.00 77.68  ? 3794 VAL A CG1   1 
ATOM   16370 C  CG2   . VAL A 1 3794 ? 217.183 269.816 178.320 1.00 77.56  ? 3794 VAL A CG2   1 
ATOM   16371 N  N     . GLU A 1 3795 ? 221.612 268.954 179.158 1.00 75.88  ? 3795 GLU A N     1 
ATOM   16372 C  CA    . GLU A 1 3795 ? 222.767 268.334 179.796 1.00 74.76  ? 3795 GLU A CA    1 
ATOM   16373 C  C     . GLU A 1 3795 ? 223.652 269.381 180.458 1.00 74.31  ? 3795 GLU A C     1 
ATOM   16374 O  O     . GLU A 1 3795 ? 224.252 269.134 181.512 1.00 76.20  ? 3795 GLU A O     1 
ATOM   16375 C  CB    . GLU A 1 3795 ? 223.561 267.525 178.769 1.00 73.75  ? 3795 GLU A CB    1 
ATOM   16376 C  CG    . GLU A 1 3795 ? 224.952 267.127 179.233 1.00 77.31  ? 3795 GLU A CG    1 
ATOM   16377 C  CD    . GLU A 1 3795 ? 225.769 266.475 178.138 1.00 82.13  ? 3795 GLU A CD    1 
ATOM   16378 O  OE1   . GLU A 1 3795 ? 225.245 266.320 177.015 1.00 83.15  ? 3795 GLU A OE1   1 
ATOM   16379 O  OE2   . GLU A 1 3795 ? 226.938 266.122 178.400 1.00 80.26  ? 3795 GLU A OE2   1 
ATOM   16380 N  N     . THR A 1 3796 ? 223.751 270.562 179.843 1.00 73.20  ? 3796 THR A N     1 
ATOM   16381 C  CA    . THR A 1 3796 ? 224.518 271.646 180.450 1.00 75.49  ? 3796 THR A CA    1 
ATOM   16382 C  C     . THR A 1 3796 ? 223.987 271.979 181.840 1.00 75.13  ? 3796 THR A C     1 
ATOM   16383 O  O     . THR A 1 3796 ? 224.760 272.186 182.783 1.00 76.71  ? 3796 THR A O     1 
ATOM   16384 C  CB    . THR A 1 3796 ? 224.489 272.881 179.548 1.00 79.08  ? 3796 THR A CB    1 
ATOM   16385 O  OG1   . THR A 1 3796 ? 225.205 272.607 178.337 1.00 78.51  ? 3796 THR A OG1   1 
ATOM   16386 C  CG2   . THR A 1 3796 ? 225.126 274.072 180.246 1.00 74.35  ? 3796 THR A CG2   1 
ATOM   16387 N  N     . VAL A 1 3797 ? 222.661 272.024 181.987 1.00 67.55  ? 3797 VAL A N     1 
ATOM   16388 C  CA    . VAL A 1 3797 ? 222.063 272.261 183.298 1.00 64.57  ? 3797 VAL A CA    1 
ATOM   16389 C  C     . VAL A 1 3797 ? 222.360 271.101 184.240 1.00 65.79  ? 3797 VAL A C     1 
ATOM   16390 O  O     . VAL A 1 3797 ? 222.675 271.304 185.419 1.00 70.01  ? 3797 VAL A O     1 
ATOM   16391 C  CB    . VAL A 1 3797 ? 220.549 272.502 183.158 1.00 66.28  ? 3797 VAL A CB    1 
ATOM   16392 C  CG1   . VAL A 1 3797 ? 219.873 272.454 184.516 1.00 65.62  ? 3797 VAL A CG1   1 
ATOM   16393 C  CG2   . VAL A 1 3797 ? 220.285 273.833 182.480 1.00 66.31  ? 3797 VAL A CG2   1 
ATOM   16394 N  N     . SER A 1 3798 ? 222.264 269.866 183.738 1.00 63.96  ? 3798 SER A N     1 
ATOM   16395 C  CA    . SER A 1 3798 ? 222.445 268.703 184.610 1.00 60.67  ? 3798 SER A CA    1 
ATOM   16396 C  C     . SER A 1 3798 ? 223.872 268.615 185.154 1.00 63.09  ? 3798 SER A C     1 
ATOM   16397 O  O     . SER A 1 3798 ? 224.096 268.092 186.258 1.00 66.79  ? 3798 SER A O     1 
ATOM   16398 C  CB    . SER A 1 3798 ? 222.077 267.423 183.863 1.00 62.01  ? 3798 SER A CB    1 
ATOM   16399 O  OG    . SER A 1 3798 ? 222.993 267.156 182.818 1.00 65.41  ? 3798 SER A OG    1 
ATOM   16400 N  N     . GLN A 1 3799 ? 224.848 269.127 184.395 1.00 64.48  ? 3799 GLN A N     1 
ATOM   16401 C  CA    . GLN A 1 3799 ? 226.248 269.011 184.808 1.00 60.57  ? 3799 GLN A CA    1 
ATOM   16402 C  C     . GLN A 1 3799 ? 226.496 269.651 186.168 1.00 62.43  ? 3799 GLN A C     1 
ATOM   16403 O  O     . GLN A 1 3799 ? 227.416 269.250 186.889 1.00 64.45  ? 3799 GLN A O     1 
ATOM   16404 C  CB    . GLN A 1 3799 ? 227.172 269.625 183.757 1.00 62.65  ? 3799 GLN A CB    1 
ATOM   16405 C  CG    . GLN A 1 3799 ? 227.161 268.893 182.437 1.00 69.49  ? 3799 GLN A CG    1 
ATOM   16406 C  CD    . GLN A 1 3799 ? 227.654 267.468 182.569 1.00 71.55  ? 3799 GLN A CD    1 
ATOM   16407 O  OE1   . GLN A 1 3799 ? 226.879 266.520 182.460 1.00 68.98  ? 3799 GLN A OE1   1 
ATOM   16408 N  NE2   . GLN A 1 3799 ? 228.950 267.310 182.807 1.00 67.37  ? 3799 GLN A NE2   1 
ATOM   16409 N  N     . GLN A 1 3800 ? 225.697 270.652 186.535 1.00 60.99  ? 3800 GLN A N     1 
ATOM   16410 C  CA    . GLN A 1 3800 ? 225.827 271.233 187.865 1.00 60.44  ? 3800 GLN A CA    1 
ATOM   16411 C  C     . GLN A 1 3800 ? 225.407 270.243 188.945 1.00 62.37  ? 3800 GLN A C     1 
ATOM   16412 O  O     . GLN A 1 3800 ? 225.898 270.311 190.077 1.00 57.64  ? 3800 GLN A O     1 
ATOM   16413 C  CB    . GLN A 1 3800 ? 225.001 272.517 187.954 1.00 60.64  ? 3800 GLN A CB    1 
ATOM   16414 C  CG    . GLN A 1 3800 ? 225.024 273.194 189.312 1.00 61.49  ? 3800 GLN A CG    1 
ATOM   16415 C  CD    . GLN A 1 3800 ? 224.026 274.325 189.411 1.00 65.54  ? 3800 GLN A CD    1 
ATOM   16416 O  OE1   . GLN A 1 3800 ? 223.340 274.648 188.441 1.00 63.47  ? 3800 GLN A OE1   1 
ATOM   16417 N  NE2   . GLN A 1 3800 ? 223.937 274.934 190.586 1.00 66.05  ? 3800 GLN A NE2   1 
ATOM   16418 N  N     . TYR A 1 3801 ? 224.518 269.309 188.612 1.00 60.70  ? 3801 TYR A N     1 
ATOM   16419 C  CA    . TYR A 1 3801 ? 223.945 268.384 189.580 1.00 49.73  ? 3801 TYR A CA    1 
ATOM   16420 C  C     . TYR A 1 3801 ? 224.557 266.990 189.528 1.00 51.06  ? 3801 TYR A C     1 
ATOM   16421 O  O     . TYR A 1 3801 ? 224.177 266.137 190.334 1.00 55.59  ? 3801 TYR A O     1 
ATOM   16422 C  CB    . TYR A 1 3801 ? 222.433 268.295 189.376 1.00 54.22  ? 3801 TYR A CB    1 
ATOM   16423 C  CG    . TYR A 1 3801 ? 221.697 269.549 189.773 1.00 55.19  ? 3801 TYR A CG    1 
ATOM   16424 C  CD1   . TYR A 1 3801 ? 222.213 270.401 190.732 1.00 61.89  ? 3801 TYR A CD1   1 
ATOM   16425 C  CD2   . TYR A 1 3801 ? 220.494 269.888 189.178 1.00 57.51  ? 3801 TYR A CD2   1 
ATOM   16426 C  CE1   . TYR A 1 3801 ? 221.547 271.550 191.099 1.00 61.57  ? 3801 TYR A CE1   1 
ATOM   16427 C  CE2   . TYR A 1 3801 ? 219.822 271.036 189.537 1.00 59.57  ? 3801 TYR A CE2   1 
ATOM   16428 C  CZ    . TYR A 1 3801 ? 220.354 271.864 190.497 1.00 60.08  ? 3801 TYR A CZ    1 
ATOM   16429 O  OH    . TYR A 1 3801 ? 219.689 273.010 190.860 1.00 66.92  ? 3801 TYR A OH    1 
ATOM   16430 N  N     . LEU A 1 3802 ? 225.477 266.723 188.589 1.00 56.25  ? 3802 LEU A N     1 
ATOM   16431 C  CA    . LEU A 1 3802 ? 226.210 265.455 188.652 1.00 48.26  ? 3802 LEU A CA    1 
ATOM   16432 C  C     . LEU A 1 3802 ? 226.910 265.202 189.985 1.00 48.43  ? 3802 LEU A C     1 
ATOM   16433 O  O     . LEU A 1 3802 ? 226.784 264.082 190.511 1.00 54.08  ? 3802 LEU A O     1 
ATOM   16434 C  CB    . LEU A 1 3802 ? 227.200 265.337 187.489 1.00 50.67  ? 3802 LEU A CB    1 
ATOM   16435 C  CG    . LEU A 1 3802 ? 226.765 264.833 186.109 1.00 56.22  ? 3802 LEU A CG    1 
ATOM   16436 C  CD1   . LEU A 1 3802 ? 226.315 263.388 186.237 1.00 56.34  ? 3802 LEU A CD1   1 
ATOM   16437 C  CD2   . LEU A 1 3802 ? 225.667 265.638 185.489 1.00 56.56  ? 3802 LEU A CD2   1 
ATOM   16438 N  N     . PRO A 1 3803 ? 227.670 266.141 190.572 1.00 53.35  ? 3803 PRO A N     1 
ATOM   16439 C  CA    . PRO A 1 3803 ? 228.458 265.779 191.770 1.00 50.37  ? 3803 PRO A CA    1 
ATOM   16440 C  C     . PRO A 1 3803 ? 227.626 265.263 192.934 1.00 51.35  ? 3803 PRO A C     1 
ATOM   16441 O  O     . PRO A 1 3803 ? 228.075 264.371 193.669 1.00 50.59  ? 3803 PRO A O     1 
ATOM   16442 C  CB    . PRO A 1 3803 ? 229.172 267.091 192.123 1.00 41.80  ? 3803 PRO A CB    1 
ATOM   16443 C  CG    . PRO A 1 3803 ? 229.228 267.839 190.852 1.00 49.98  ? 3803 PRO A CG    1 
ATOM   16444 C  CD    . PRO A 1 3803 ? 227.939 267.531 190.162 1.00 52.85  ? 3803 PRO A CD    1 
ATOM   16445 N  N     . LEU A 1 3804 ? 226.419 265.799 193.124 1.00 41.12  ? 3804 LEU A N     1 
ATOM   16446 C  CA    . LEU A 1 3804 ? 225.563 265.313 194.199 1.00 32.69  ? 3804 LEU A CA    1 
ATOM   16447 C  C     . LEU A 1 3804 ? 225.159 263.863 193.969 1.00 46.85  ? 3804 LEU A C     1 
ATOM   16448 O  O     . LEU A 1 3804 ? 225.051 263.084 194.920 1.00 56.80  ? 3804 LEU A O     1 
ATOM   16449 C  CB    . LEU A 1 3804 ? 224.329 266.201 194.331 1.00 34.22  ? 3804 LEU A CB    1 
ATOM   16450 C  CG    . LEU A 1 3804 ? 223.360 265.805 195.442 1.00 45.51  ? 3804 LEU A CG    1 
ATOM   16451 C  CD1   . LEU A 1 3804 ? 223.949 266.125 196.801 1.00 45.21  ? 3804 LEU A CD1   1 
ATOM   16452 C  CD2   . LEU A 1 3804 ? 222.036 266.507 195.257 1.00 48.77  ? 3804 LEU A CD2   1 
ATOM   16453 N  N     . SER A 1 3805 ? 224.927 263.481 192.711 1.00 41.89  ? 3805 SER A N     1 
ATOM   16454 C  CA    . SER A 1 3805 ? 224.596 262.092 192.409 1.00 39.46  ? 3805 SER A CA    1 
ATOM   16455 C  C     . SER A 1 3805 ? 225.758 261.162 192.737 1.00 43.88  ? 3805 SER A C     1 
ATOM   16456 O  O     . SER A 1 3805 ? 225.555 260.065 193.274 1.00 54.07  ? 3805 SER A O     1 
ATOM   16457 C  CB    . SER A 1 3805 ? 224.197 261.960 190.941 1.00 41.52  ? 3805 SER A CB    1 
ATOM   16458 O  OG    . SER A 1 3805 ? 225.292 262.247 190.091 1.00 52.50  ? 3805 SER A OG    1 
ATOM   16459 N  N     . THR A 1 3806 ? 226.983 261.579 192.415 1.00 30.53  ? 3806 THR A N     1 
ATOM   16460 C  CA    . THR A 1 3806 ? 228.155 260.781 192.761 1.00 35.10  ? 3806 THR A CA    1 
ATOM   16461 C  C     . THR A 1 3806 ? 228.287 260.639 194.271 1.00 39.64  ? 3806 THR A C     1 
ATOM   16462 O  O     . THR A 1 3806 ? 228.587 259.553 194.784 1.00 52.12  ? 3806 THR A O     1 
ATOM   16463 C  CB    . THR A 1 3806 ? 229.413 261.414 192.169 1.00 38.28  ? 3806 THR A CB    1 
ATOM   16464 O  OG1   . THR A 1 3806 ? 229.263 261.544 190.750 1.00 49.30  ? 3806 THR A OG1   1 
ATOM   16465 C  CG2   . THR A 1 3806 ? 230.629 260.556 192.465 1.00 37.71  ? 3806 THR A CG2   1 
ATOM   16466 N  N     . ALA A 1 3807 ? 228.063 261.734 195.002 1.00 40.47  ? 3807 ALA A N     1 
ATOM   16467 C  CA    . ALA A 1 3807 ? 228.111 261.666 196.459 1.00 32.18  ? 3807 ALA A CA    1 
ATOM   16468 C  C     . ALA A 1 3807 ? 227.042 260.726 197.000 1.00 33.92  ? 3807 ALA A C     1 
ATOM   16469 O  O     . ALA A 1 3807 ? 227.292 259.968 197.942 1.00 43.62  ? 3807 ALA A O     1 
ATOM   16470 C  CB    . ALA A 1 3807 ? 227.952 263.062 197.055 1.00 37.95  ? 3807 ALA A CB    1 
ATOM   16471 N  N     . CYS A 1 3808 ? 225.842 260.768 196.421 1.00 40.39  ? 3808 CYS A N     1 
ATOM   16472 C  CA    . CYS A 1 3808 ? 224.767 259.883 196.857 1.00 35.84  ? 3808 CYS A CA    1 
ATOM   16473 C  C     . CYS A 1 3808 ? 225.123 258.422 196.625 1.00 42.16  ? 3808 CYS A C     1 
ATOM   16474 O  O     . CYS A 1 3808 ? 224.889 257.571 197.492 1.00 49.48  ? 3808 CYS A O     1 
ATOM   16475 C  CB    . CYS A 1 3808 ? 223.474 260.235 196.127 1.00 29.89  ? 3808 CYS A CB    1 
ATOM   16476 S  SG    . CYS A 1 3808 ? 222.718 261.767 196.673 1.00 56.87  ? 3808 CYS A SG    1 
ATOM   16477 N  N     . SER A 1 3809 ? 225.679 258.108 195.454 1.00 37.68  ? 3809 SER A N     1 
ATOM   16478 C  CA    . SER A 1 3809 ? 226.072 256.730 195.179 1.00 29.00  ? 3809 SER A CA    1 
ATOM   16479 C  C     . SER A 1 3809 ? 227.163 256.269 196.136 1.00 36.24  ? 3809 SER A C     1 
ATOM   16480 O  O     . SER A 1 3809 ? 227.114 255.143 196.648 1.00 51.41  ? 3809 SER A O     1 
ATOM   16481 C  CB    . SER A 1 3809 ? 226.532 256.591 193.731 1.00 33.64  ? 3809 SER A CB    1 
ATOM   16482 O  OG    . SER A 1 3809 ? 227.904 256.908 193.598 1.00 48.11  ? 3809 SER A OG    1 
ATOM   16483 N  N     . SER A 1 3810 ? 228.151 257.128 196.397 1.00 34.89  ? 3810 SER A N     1 
ATOM   16484 C  CA    . SER A 1 3810 ? 229.211 256.767 197.334 1.00 24.87  ? 3810 SER A CA    1 
ATOM   16485 C  C     . SER A 1 3810 ? 228.658 256.546 198.736 1.00 39.53  ? 3810 SER A C     1 
ATOM   16486 O  O     . SER A 1 3810 ? 229.064 255.606 199.428 1.00 45.96  ? 3810 SER A O     1 
ATOM   16487 C  CB    . SER A 1 3810 ? 230.290 257.847 197.346 1.00 31.78  ? 3810 SER A CB    1 
ATOM   16488 O  OG    . SER A 1 3810 ? 230.721 258.147 196.032 1.00 44.53  ? 3810 SER A OG    1 
ATOM   16489 N  N     . ILE A 1 3811 ? 227.725 257.395 199.169 1.00 39.42  ? 3811 ILE A N     1 
ATOM   16490 C  CA    . ILE A 1 3811 ? 227.132 257.243 200.493 1.00 30.72  ? 3811 ILE A CA    1 
ATOM   16491 C  C     . ILE A 1 3811 ? 226.359 255.934 200.585 1.00 34.91  ? 3811 ILE A C     1 
ATOM   16492 O  O     . ILE A 1 3811 ? 226.471 255.198 201.572 1.00 45.04  ? 3811 ILE A O     1 
ATOM   16493 C  CB    . ILE A 1 3811 ? 226.235 258.448 200.822 1.00 31.21  ? 3811 ILE A CB    1 
ATOM   16494 C  CG1   . ILE A 1 3811 ? 227.084 259.661 201.192 1.00 33.55  ? 3811 ILE A CG1   1 
ATOM   16495 C  CG2   . ILE A 1 3811 ? 225.282 258.113 201.953 1.00 38.42  ? 3811 ILE A CG2   1 
ATOM   16496 C  CD1   . ILE A 1 3811 ? 226.275 260.899 201.451 1.00 34.08  ? 3811 ILE A CD1   1 
ATOM   16497 N  N     . TYR A 1 3812 ? 225.563 255.622 199.560 1.00 35.65  ? 3812 TYR A N     1 
ATOM   16498 C  CA    . TYR A 1 3812 ? 224.790 254.386 199.600 1.00 27.27  ? 3812 TYR A CA    1 
ATOM   16499 C  C     . TYR A 1 3812 ? 225.697 253.166 199.597 1.00 32.11  ? 3812 TYR A C     1 
ATOM   16500 O  O     . TYR A 1 3812 ? 225.414 252.176 200.276 1.00 43.23  ? 3812 TYR A O     1 
ATOM   16501 C  CB    . TYR A 1 3812 ? 223.814 254.304 198.430 1.00 34.04  ? 3812 TYR A CB    1 
ATOM   16502 C  CG    . TYR A 1 3812 ? 223.237 252.914 198.279 1.00 38.69  ? 3812 TYR A CG    1 
ATOM   16503 C  CD1   . TYR A 1 3812 ? 222.276 252.443 199.163 1.00 42.77  ? 3812 TYR A CD1   1 
ATOM   16504 C  CD2   . TYR A 1 3812 ? 223.677 252.060 197.278 1.00 41.19  ? 3812 TYR A CD2   1 
ATOM   16505 C  CE1   . TYR A 1 3812 ? 221.758 251.172 199.040 1.00 40.97  ? 3812 TYR A CE1   1 
ATOM   16506 C  CE2   . TYR A 1 3812 ? 223.165 250.788 197.149 1.00 42.52  ? 3812 TYR A CE2   1 
ATOM   16507 C  CZ    . TYR A 1 3812 ? 222.206 250.350 198.031 1.00 44.21  ? 3812 TYR A CZ    1 
ATOM   16508 O  OH    . TYR A 1 3812 ? 221.692 249.081 197.904 1.00 48.59  ? 3812 TYR A OH    1 
ATOM   16509 N  N     . PHE A 1 3813 ? 226.783 253.205 198.825 1.00 39.39  ? 3813 PHE A N     1 
ATOM   16510 C  CA    . PHE A 1 3813 ? 227.657 252.040 198.771 1.00 31.41  ? 3813 PHE A CA    1 
ATOM   16511 C  C     . PHE A 1 3813 ? 228.573 251.945 199.983 1.00 39.36  ? 3813 PHE A C     1 
ATOM   16512 O  O     . PHE A 1 3813 ? 229.143 250.877 200.227 1.00 48.91  ? 3813 PHE A O     1 
ATOM   16513 C  CB    . PHE A 1 3813 ? 228.463 252.051 197.476 1.00 30.83  ? 3813 PHE A CB    1 
ATOM   16514 C  CG    . PHE A 1 3813 ? 227.727 251.450 196.319 1.00 39.75  ? 3813 PHE A CG    1 
ATOM   16515 C  CD1   . PHE A 1 3813 ? 227.742 250.084 196.109 1.00 44.98  ? 3813 PHE A CD1   1 
ATOM   16516 C  CD2   . PHE A 1 3813 ? 226.994 252.245 195.460 1.00 39.40  ? 3813 PHE A CD2   1 
ATOM   16517 C  CE1   . PHE A 1 3813 ? 227.055 249.527 195.055 1.00 38.66  ? 3813 PHE A CE1   1 
ATOM   16518 C  CE2   . PHE A 1 3813 ? 226.306 251.693 194.405 1.00 41.50  ? 3813 PHE A CE2   1 
ATOM   16519 C  CZ    . PHE A 1 3813 ? 226.337 250.333 194.202 1.00 43.09  ? 3813 PHE A CZ    1 
ATOM   16520 N  N     . THR A 1 3814 ? 228.736 253.031 200.739 1.00 41.06  ? 3814 THR A N     1 
ATOM   16521 C  CA    . THR A 1 3814 ? 229.337 252.918 202.063 1.00 36.20  ? 3814 THR A CA    1 
ATOM   16522 C  C     . THR A 1 3814 ? 228.351 252.310 203.054 1.00 30.04  ? 3814 THR A C     1 
ATOM   16523 O  O     . THR A 1 3814 ? 228.725 251.470 203.879 1.00 41.42  ? 3814 THR A O     1 
ATOM   16524 C  CB    . THR A 1 3814 ? 229.816 254.288 202.541 1.00 37.48  ? 3814 THR A CB    1 
ATOM   16525 O  OG1   . THR A 1 3814 ? 230.885 254.737 201.700 1.00 38.68  ? 3814 THR A OG1   1 
ATOM   16526 C  CG2   . THR A 1 3814 ? 230.310 254.217 203.975 1.00 39.30  ? 3814 THR A CG2   1 
ATOM   16527 N  N     . MET A 1 3815 ? 227.082 252.719 202.975 1.00 35.09  ? 3815 MET A N     1 
ATOM   16528 C  CA    . MET A 1 3815 ? 226.032 252.110 203.786 1.00 34.69  ? 3815 MET A CA    1 
ATOM   16529 C  C     . MET A 1 3815 ? 225.905 250.616 203.526 1.00 42.91  ? 3815 MET A C     1 
ATOM   16530 O  O     . MET A 1 3815 ? 225.682 249.840 204.461 1.00 47.58  ? 3815 MET A O     1 
ATOM   16531 C  CB    . MET A 1 3815 ? 224.697 252.793 203.495 1.00 39.39  ? 3815 MET A CB    1 
ATOM   16532 C  CG    . MET A 1 3815 ? 224.596 254.236 203.934 1.00 36.38  ? 3815 MET A CG    1 
ATOM   16533 S  SD    . MET A 1 3815 ? 223.011 254.929 203.436 1.00 61.06  ? 3815 MET A SD    1 
ATOM   16534 C  CE    . MET A 1 3815 ? 221.900 254.059 204.525 1.00 45.10  ? 3815 MET A CE    1 
ATOM   16535 N  N     . GLU A 1 3816 ? 226.030 250.200 202.265 1.00 41.52  ? 3816 GLU A N     1 
ATOM   16536 C  CA    . GLU A 1 3816 ? 225.816 248.803 201.908 1.00 37.46  ? 3816 GLU A CA    1 
ATOM   16537 C  C     . GLU A 1 3816 ? 226.924 247.913 202.457 1.00 44.39  ? 3816 GLU A C     1 
ATOM   16538 O  O     . GLU A 1 3816 ? 226.692 246.738 202.761 1.00 54.22  ? 3816 GLU A O     1 
ATOM   16539 C  CB    . GLU A 1 3816 ? 225.716 248.672 200.390 1.00 35.80  ? 3816 GLU A CB    1 
ATOM   16540 C  CG    . GLU A 1 3816 ? 225.043 247.404 199.905 1.00 52.07  ? 3816 GLU A CG    1 
ATOM   16541 C  CD    . GLU A 1 3816 ? 225.358 247.105 198.452 1.00 58.79  ? 3816 GLU A CD    1 
ATOM   16542 O  OE1   . GLU A 1 3816 ? 226.440 247.514 197.982 1.00 61.18  ? 3816 GLU A OE1   1 
ATOM   16543 O  OE2   . GLU A 1 3816 ? 224.524 246.465 197.777 1.00 51.27  ? 3816 GLU A OE2   1 
ATOM   16544 N  N     . SER A 1 3817 ? 228.133 248.449 202.587 1.00 37.74  ? 3817 SER A N     1 
ATOM   16545 C  CA    . SER A 1 3817 ? 229.260 247.695 203.114 1.00 39.78  ? 3817 SER A CA    1 
ATOM   16546 C  C     . SER A 1 3817 ? 229.388 247.801 204.627 1.00 38.41  ? 3817 SER A C     1 
ATOM   16547 O  O     . SER A 1 3817 ? 230.334 247.247 205.193 1.00 45.12  ? 3817 SER A O     1 
ATOM   16548 C  CB    . SER A 1 3817 ? 230.562 248.160 202.457 1.00 45.86  ? 3817 SER A CB    1 
ATOM   16549 O  OG    . SER A 1 3817 ? 230.983 249.403 202.988 1.00 45.96  ? 3817 SER A OG    1 
ATOM   16550 N  N     . LEU A 1 3818 ? 228.469 248.503 205.292 1.00 35.43  ? 3818 LEU A N     1 
ATOM   16551 C  CA    . LEU A 1 3818 ? 228.511 248.606 206.745 1.00 28.17  ? 3818 LEU A CA    1 
ATOM   16552 C  C     . LEU A 1 3818 ? 228.242 247.273 207.425 1.00 33.18  ? 3818 LEU A C     1 
ATOM   16553 O  O     . LEU A 1 3818 ? 228.612 247.101 208.590 1.00 41.65  ? 3818 LEU A O     1 
ATOM   16554 C  CB    . LEU A 1 3818 ? 227.500 249.644 207.229 1.00 37.44  ? 3818 LEU A CB    1 
ATOM   16555 C  CG    . LEU A 1 3818 ? 227.993 251.081 207.382 1.00 27.33  ? 3818 LEU A CG    1 
ATOM   16556 C  CD1   . LEU A 1 3818 ? 226.856 251.980 207.827 1.00 35.67  ? 3818 LEU A CD1   1 
ATOM   16557 C  CD2   . LEU A 1 3818 ? 229.134 251.143 208.370 1.00 31.27  ? 3818 LEU A CD2   1 
ATOM   16558 N  N     . LYS A 1 3819 ? 227.608 246.328 206.729 1.00 38.40  ? 3819 LYS A N     1 
ATOM   16559 C  CA    . LYS A 1 3819 ? 227.333 245.019 207.304 1.00 31.91  ? 3819 LYS A CA    1 
ATOM   16560 C  C     . LYS A 1 3819 ? 228.591 244.190 207.514 1.00 38.91  ? 3819 LYS A C     1 
ATOM   16561 O  O     . LYS A 1 3819 ? 228.524 243.154 208.183 1.00 45.23  ? 3819 LYS A O     1 
ATOM   16562 C  CB    . LYS A 1 3819 ? 226.352 244.256 206.414 1.00 30.80  ? 3819 LYS A CB    1 
ATOM   16563 C  CG    . LYS A 1 3819 ? 226.907 243.897 205.050 1.00 39.79  ? 3819 LYS A CG    1 
ATOM   16564 C  CD    . LYS A 1 3819 ? 225.937 243.027 204.276 1.00 42.17  ? 3819 LYS A CD    1 
ATOM   16565 C  CE    . LYS A 1 3819 ? 225.076 243.857 203.343 1.00 41.23  ? 3819 LYS A CE    1 
ATOM   16566 N  NZ    . LYS A 1 3819 ? 225.798 244.198 202.090 1.00 44.89  ? 3819 LYS A NZ    1 
ATOM   16567 N  N     . GLN A 1 3820 ? 229.728 244.613 206.961 1.00 38.91  ? 3820 GLN A N     1 
ATOM   16568 C  CA    . GLN A 1 3820 ? 230.972 243.884 207.162 1.00 35.04  ? 3820 GLN A CA    1 
ATOM   16569 C  C     . GLN A 1 3820 ? 231.550 244.096 208.554 1.00 44.65  ? 3820 GLN A C     1 
ATOM   16570 O  O     . GLN A 1 3820 ? 232.371 243.287 208.998 1.00 46.13  ? 3820 GLN A O     1 
ATOM   16571 C  CB    . GLN A 1 3820 ? 231.998 244.297 206.108 1.00 38.91  ? 3820 GLN A CB    1 
ATOM   16572 C  CG    . GLN A 1 3820 ? 231.479 244.228 204.686 1.00 38.44  ? 3820 GLN A CG    1 
ATOM   16573 C  CD    . GLN A 1 3820 ? 231.136 242.817 204.261 1.00 50.93  ? 3820 GLN A CD    1 
ATOM   16574 O  OE1   . GLN A 1 3820 ? 230.040 242.554 203.769 1.00 55.58  ? 3820 GLN A OE1   1 
ATOM   16575 N  NE2   . GLN A 1 3820 ? 232.075 241.898 204.450 1.00 43.76  ? 3820 GLN A NE2   1 
ATOM   16576 N  N     . ILE A 1 3821 ? 231.145 245.160 209.250 1.00 38.87  ? 3821 ILE A N     1 
ATOM   16577 C  CA    . ILE A 1 3821 ? 231.667 245.446 210.582 1.00 36.83  ? 3821 ILE A CA    1 
ATOM   16578 C  C     . ILE A 1 3821 ? 230.698 245.058 211.690 1.00 42.12  ? 3821 ILE A C     1 
ATOM   16579 O  O     . ILE A 1 3821 ? 231.107 245.009 212.861 1.00 51.12  ? 3821 ILE A O     1 
ATOM   16580 C  CB    . ILE A 1 3821 ? 232.055 246.933 210.720 1.00 36.90  ? 3821 ILE A CB    1 
ATOM   16581 C  CG1   . ILE A 1 3821 ? 230.808 247.807 210.835 1.00 37.67  ? 3821 ILE A CG1   1 
ATOM   16582 C  CG2   . ILE A 1 3821 ? 232.895 247.372 209.535 1.00 36.29  ? 3821 ILE A CG2   1 
ATOM   16583 C  CD1   . ILE A 1 3821 ? 231.111 249.267 211.067 1.00 33.41  ? 3821 ILE A CD1   1 
ATOM   16584 N  N     . HIS A 1 3822 ? 229.438 244.779 211.363 1.00 34.08  ? 3822 HIS A N     1 
ATOM   16585 C  CA    . HIS A 1 3822 ? 228.462 244.313 212.338 1.00 32.57  ? 3822 HIS A CA    1 
ATOM   16586 C  C     . HIS A 1 3822 ? 227.268 243.743 211.589 1.00 38.76  ? 3822 HIS A C     1 
ATOM   16587 O  O     . HIS A 1 3822 ? 226.842 244.301 210.577 1.00 46.60  ? 3822 HIS A O     1 
ATOM   16588 C  CB    . HIS A 1 3822 ? 228.016 245.441 213.274 1.00 30.25  ? 3822 HIS A CB    1 
ATOM   16589 C  CG    . HIS A 1 3822 ? 227.441 244.962 214.569 1.00 34.11  ? 3822 HIS A CG    1 
ATOM   16590 N  ND1   . HIS A 1 3822 ? 226.129 244.563 214.698 1.00 38.93  ? 3822 HIS A ND1   1 
ATOM   16591 C  CD2   . HIS A 1 3822 ? 227.998 244.820 215.795 1.00 39.19  ? 3822 HIS A CD2   1 
ATOM   16592 C  CE1   . HIS A 1 3822 ? 225.902 244.197 215.946 1.00 35.95  ? 3822 HIS A CE1   1 
ATOM   16593 N  NE2   . HIS A 1 3822 ? 227.020 244.342 216.632 1.00 39.36  ? 3822 HIS A NE2   1 
ATOM   16594 N  N     . PHE A 1 3823 ? 226.736 242.628 212.093 1.00 44.08  ? 3823 PHE A N     1 
ATOM   16595 C  CA    . PHE A 1 3823 ? 225.620 241.969 211.424 1.00 36.63  ? 3823 PHE A CA    1 
ATOM   16596 C  C     . PHE A 1 3823 ? 224.354 242.812 211.466 1.00 31.41  ? 3823 PHE A C     1 
ATOM   16597 O  O     . PHE A 1 3823 ? 223.487 242.668 210.598 1.00 42.07  ? 3823 PHE A O     1 
ATOM   16598 C  CB    . PHE A 1 3823 ? 225.362 240.603 212.057 1.00 34.05  ? 3823 PHE A CB    1 
ATOM   16599 C  CG    . PHE A 1 3823 ? 225.019 240.667 213.518 1.00 40.65  ? 3823 PHE A CG    1 
ATOM   16600 C  CD1   . PHE A 1 3823 ? 226.015 240.664 214.477 1.00 40.99  ? 3823 PHE A CD1   1 
ATOM   16601 C  CD2   . PHE A 1 3823 ? 223.701 240.726 213.931 1.00 35.99  ? 3823 PHE A CD2   1 
ATOM   16602 C  CE1   . PHE A 1 3823 ? 225.703 240.725 215.818 1.00 33.43  ? 3823 PHE A CE1   1 
ATOM   16603 C  CE2   . PHE A 1 3823 ? 223.386 240.788 215.268 1.00 37.70  ? 3823 PHE A CE2   1 
ATOM   16604 C  CZ    . PHE A 1 3823 ? 224.388 240.785 216.213 1.00 37.28  ? 3823 PHE A CZ    1 
ATOM   16605 N  N     . LEU A 1 3824 ? 224.226 243.688 212.460 1.00 32.37  ? 3824 LEU A N     1 
ATOM   16606 C  CA    . LEU A 1 3824 ? 223.016 244.478 212.637 1.00 34.60  ? 3824 LEU A CA    1 
ATOM   16607 C  C     . LEU A 1 3824 ? 222.902 245.618 211.635 1.00 38.71  ? 3824 LEU A C     1 
ATOM   16608 O  O     . LEU A 1 3824 ? 221.825 246.209 211.512 1.00 40.16  ? 3824 LEU A O     1 
ATOM   16609 C  CB    . LEU A 1 3824 ? 222.976 245.033 214.063 1.00 30.22  ? 3824 LEU A CB    1 
ATOM   16610 C  CG    . LEU A 1 3824 ? 221.714 245.721 214.579 1.00 32.51  ? 3824 LEU A CG    1 
ATOM   16611 C  CD1   . LEU A 1 3824 ? 220.577 244.726 214.694 1.00 38.80  ? 3824 LEU A CD1   1 
ATOM   16612 C  CD2   . LEU A 1 3824 ? 221.987 246.387 215.911 1.00 36.20  ? 3824 LEU A CD2   1 
ATOM   16613 N  N     . TYR A 1 3825 ? 223.972 245.930 210.906 1.00 37.28  ? 3825 TYR A N     1 
ATOM   16614 C  CA    . TYR A 1 3825 ? 223.989 247.091 210.018 1.00 29.67  ? 3825 TYR A CA    1 
ATOM   16615 C  C     . TYR A 1 3825 ? 223.514 246.677 208.625 1.00 36.75  ? 3825 TYR A C     1 
ATOM   16616 O  O     . TYR A 1 3825 ? 224.275 246.600 207.659 1.00 40.39  ? 3825 TYR A O     1 
ATOM   16617 C  CB    . TYR A 1 3825 ? 225.379 247.714 209.980 1.00 28.59  ? 3825 TYR A CB    1 
ATOM   16618 C  CG    . TYR A 1 3825 ? 225.926 248.132 211.331 1.00 28.83  ? 3825 TYR A CG    1 
ATOM   16619 C  CD1   . TYR A 1 3825 ? 225.109 248.201 212.452 1.00 32.17  ? 3825 TYR A CD1   1 
ATOM   16620 C  CD2   . TYR A 1 3825 ? 227.264 248.455 211.483 1.00 30.88  ? 3825 TYR A CD2   1 
ATOM   16621 C  CE1   . TYR A 1 3825 ? 225.609 248.575 213.680 1.00 23.32  ? 3825 TYR A CE1   1 
ATOM   16622 C  CE2   . TYR A 1 3825 ? 227.772 248.832 212.707 1.00 35.32  ? 3825 TYR A CE2   1 
ATOM   16623 C  CZ    . TYR A 1 3825 ? 226.941 248.888 213.801 1.00 31.40  ? 3825 TYR A CZ    1 
ATOM   16624 O  OH    . TYR A 1 3825 ? 227.445 249.264 215.022 1.00 38.87  ? 3825 TYR A OH    1 
ATOM   16625 N  N     . GLN A 1 3826 ? 222.216 246.406 208.540 1.00 34.05  ? 3826 GLN A N     1 
ATOM   16626 C  CA    . GLN A 1 3826 ? 221.564 246.055 207.286 1.00 26.76  ? 3826 GLN A CA    1 
ATOM   16627 C  C     . GLN A 1 3826 ? 220.707 247.229 206.836 1.00 38.64  ? 3826 GLN A C     1 
ATOM   16628 O  O     . GLN A 1 3826 ? 219.799 247.652 207.558 1.00 45.38  ? 3826 GLN A O     1 
ATOM   16629 C  CB    . GLN A 1 3826 ? 220.711 244.797 207.444 1.00 33.70  ? 3826 GLN A CB    1 
ATOM   16630 C  CG    . GLN A 1 3826 ? 221.437 243.620 208.065 1.00 39.16  ? 3826 GLN A CG    1 
ATOM   16631 C  CD    . GLN A 1 3826 ? 222.516 243.062 207.163 1.00 38.87  ? 3826 GLN A CD    1 
ATOM   16632 O  OE1   . GLN A 1 3826 ? 222.370 243.038 205.943 1.00 44.94  ? 3826 GLN A OE1   1 
ATOM   16633 N  NE2   . GLN A 1 3826 ? 223.610 242.610 207.762 1.00 32.60  ? 3826 GLN A NE2   1 
ATOM   16634 N  N     . TYR A 1 3827 ? 220.997 247.754 205.649 1.00 35.77  ? 3827 TYR A N     1 
ATOM   16635 C  CA    . TYR A 1 3827 ? 220.295 248.910 205.111 1.00 33.11  ? 3827 TYR A CA    1 
ATOM   16636 C  C     . TYR A 1 3827 ? 219.916 248.636 203.666 1.00 43.72  ? 3827 TYR A C     1 
ATOM   16637 O  O     . TYR A 1 3827 ? 220.757 248.206 202.871 1.00 51.24  ? 3827 TYR A O     1 
ATOM   16638 C  CB    . TYR A 1 3827 ? 221.159 250.171 205.207 1.00 32.83  ? 3827 TYR A CB    1 
ATOM   16639 C  CG    . TYR A 1 3827 ? 221.649 250.454 206.607 1.00 36.68  ? 3827 TYR A CG    1 
ATOM   16640 C  CD1   . TYR A 1 3827 ? 220.780 250.913 207.585 1.00 29.98  ? 3827 TYR A CD1   1 
ATOM   16641 C  CD2   . TYR A 1 3827 ? 222.976 250.252 206.954 1.00 33.94  ? 3827 TYR A CD2   1 
ATOM   16642 C  CE1   . TYR A 1 3827 ? 221.217 251.165 208.865 1.00 33.58  ? 3827 TYR A CE1   1 
ATOM   16643 C  CE2   . TYR A 1 3827 ? 223.422 250.504 208.233 1.00 34.98  ? 3827 TYR A CE2   1 
ATOM   16644 C  CZ    . TYR A 1 3827 ? 222.538 250.960 209.184 1.00 41.00  ? 3827 TYR A CZ    1 
ATOM   16645 O  OH    . TYR A 1 3827 ? 222.975 251.212 210.462 1.00 40.89  ? 3827 TYR A OH    1 
ATOM   16646 N  N     . SER A 1 3828 ? 218.656 248.883 203.331 1.00 38.52  ? 3828 SER A N     1 
ATOM   16647 C  CA    . SER A 1 3828 ? 218.170 248.675 201.979 1.00 38.05  ? 3828 SER A CA    1 
ATOM   16648 C  C     . SER A 1 3828 ? 218.331 249.946 201.151 1.00 38.78  ? 3828 SER A C     1 
ATOM   16649 O  O     . SER A 1 3828 ? 218.710 251.006 201.653 1.00 49.54  ? 3828 SER A O     1 
ATOM   16650 C  CB    . SER A 1 3828 ? 216.708 248.231 201.999 1.00 39.35  ? 3828 SER A CB    1 
ATOM   16651 O  OG    . SER A 1 3828 ? 215.922 249.102 202.790 1.00 41.22  ? 3828 SER A OG    1 
ATOM   16652 N  N     . LEU A 1 3829 ? 218.046 249.824 199.854 1.00 42.67  ? 3829 LEU A N     1 
ATOM   16653 C  CA    . LEU A 1 3829 ? 218.098 250.989 198.978 1.00 35.96  ? 3829 LEU A CA    1 
ATOM   16654 C  C     . LEU A 1 3829 ? 216.978 251.968 199.301 1.00 38.53  ? 3829 LEU A C     1 
ATOM   16655 O  O     . LEU A 1 3829 ? 217.143 253.181 199.138 1.00 48.40  ? 3829 LEU A O     1 
ATOM   16656 C  CB    . LEU A 1 3829 ? 218.025 250.551 197.517 1.00 41.51  ? 3829 LEU A CB    1 
ATOM   16657 C  CG    . LEU A 1 3829 ? 218.081 251.662 196.468 1.00 37.84  ? 3829 LEU A CG    1 
ATOM   16658 C  CD1   . LEU A 1 3829 ? 219.443 252.324 196.467 1.00 39.92  ? 3829 LEU A CD1   1 
ATOM   16659 C  CD2   . LEU A 1 3829 ? 217.746 251.116 195.095 1.00 44.23  ? 3829 LEU A CD2   1 
ATOM   16660 N  N     . GLN A 1 3830 ? 215.832 251.461 199.761 1.00 33.73  ? 3830 GLN A N     1 
ATOM   16661 C  CA    . GLN A 1 3830 ? 214.718 252.342 200.092 1.00 33.98  ? 3830 GLN A CA    1 
ATOM   16662 C  C     . GLN A 1 3830 ? 215.037 253.226 201.288 1.00 38.11  ? 3830 GLN A C     1 
ATOM   16663 O  O     . GLN A 1 3830 ? 214.547 254.355 201.368 1.00 48.16  ? 3830 GLN A O     1 
ATOM   16664 C  CB    . GLN A 1 3830 ? 213.457 251.521 200.355 1.00 36.58  ? 3830 GLN A CB    1 
ATOM   16665 C  CG    . GLN A 1 3830 ? 212.172 252.336 200.348 1.00 44.44  ? 3830 GLN A CG    1 
ATOM   16666 C  CD    . GLN A 1 3830 ? 212.172 253.427 199.295 1.00 49.03  ? 3830 GLN A CD    1 
ATOM   16667 O  OE1   . GLN A 1 3830 ? 212.253 253.153 198.099 1.00 49.69  ? 3830 GLN A OE1   1 
ATOM   16668 N  NE2   . GLN A 1 3830 ? 212.077 254.674 199.738 1.00 43.46  ? 3830 GLN A NE2   1 
ATOM   16669 N  N     . PHE A 1 3831 ? 215.856 252.741 202.221 1.00 34.88  ? 3831 PHE A N     1 
ATOM   16670 C  CA    . PHE A 1 3831 ? 216.280 253.574 203.343 1.00 36.78  ? 3831 PHE A CA    1 
ATOM   16671 C  C     . PHE A 1 3831 ? 217.089 254.774 202.858 1.00 41.22  ? 3831 PHE A C     1 
ATOM   16672 O  O     . PHE A 1 3831 ? 216.827 255.920 203.253 1.00 46.73  ? 3831 PHE A O     1 
ATOM   16673 C  CB    . PHE A 1 3831 ? 217.086 252.723 204.325 1.00 39.81  ? 3831 PHE A CB    1 
ATOM   16674 C  CG    . PHE A 1 3831 ? 217.490 253.443 205.577 1.00 44.22  ? 3831 PHE A CG    1 
ATOM   16675 C  CD1   . PHE A 1 3831 ? 216.541 254.023 206.398 1.00 42.42  ? 3831 PHE A CD1   1 
ATOM   16676 C  CD2   . PHE A 1 3831 ? 218.818 253.509 205.951 1.00 38.73  ? 3831 PHE A CD2   1 
ATOM   16677 C  CE1   . PHE A 1 3831 ? 216.915 254.675 207.554 1.00 42.97  ? 3831 PHE A CE1   1 
ATOM   16678 C  CE2   . PHE A 1 3831 ? 219.196 254.159 207.104 1.00 37.39  ? 3831 PHE A CE2   1 
ATOM   16679 C  CZ    . PHE A 1 3831 ? 218.243 254.741 207.907 1.00 40.46  ? 3831 PHE A CZ    1 
ATOM   16680 N  N     . PHE A 1 3832 ? 218.058 254.535 201.974 1.00 37.42  ? 3832 PHE A N     1 
ATOM   16681 C  CA    . PHE A 1 3832 ? 218.840 255.640 201.436 1.00 37.00  ? 3832 PHE A CA    1 
ATOM   16682 C  C     . PHE A 1 3832 ? 217.987 256.552 200.568 1.00 34.51  ? 3832 PHE A C     1 
ATOM   16683 O  O     . PHE A 1 3832 ? 218.204 257.766 200.538 1.00 45.93  ? 3832 PHE A O     1 
ATOM   16684 C  CB    . PHE A 1 3832 ? 220.030 255.121 200.637 1.00 32.09  ? 3832 PHE A CB    1 
ATOM   16685 C  CG    . PHE A 1 3832 ? 220.761 256.199 199.905 1.00 34.41  ? 3832 PHE A CG    1 
ATOM   16686 C  CD1   . PHE A 1 3832 ? 221.617 257.046 200.582 1.00 36.00  ? 3832 PHE A CD1   1 
ATOM   16687 C  CD2   . PHE A 1 3832 ? 220.569 256.390 198.550 1.00 37.34  ? 3832 PHE A CD2   1 
ATOM   16688 C  CE1   . PHE A 1 3832 ? 222.280 258.051 199.919 1.00 39.79  ? 3832 PHE A CE1   1 
ATOM   16689 C  CE2   . PHE A 1 3832 ? 221.227 257.393 197.884 1.00 42.83  ? 3832 PHE A CE2   1 
ATOM   16690 C  CZ    . PHE A 1 3832 ? 222.084 258.224 198.570 1.00 45.13  ? 3832 PHE A CZ    1 
ATOM   16691 N  N     . LEU A 1 3833 ? 217.027 255.987 199.833 1.00 32.11  ? 3833 LEU A N     1 
ATOM   16692 C  CA    . LEU A 1 3833 ? 216.149 256.824 199.026 1.00 29.16  ? 3833 LEU A CA    1 
ATOM   16693 C  C     . LEU A 1 3833 ? 215.263 257.700 199.899 1.00 35.14  ? 3833 LEU A C     1 
ATOM   16694 O  O     . LEU A 1 3833 ? 214.972 258.842 199.533 1.00 49.08  ? 3833 LEU A O     1 
ATOM   16695 C  CB    . LEU A 1 3833 ? 215.303 255.960 198.094 1.00 33.06  ? 3833 LEU A CB    1 
ATOM   16696 C  CG    . LEU A 1 3833 ? 216.074 255.272 196.967 1.00 42.06  ? 3833 LEU A CG    1 
ATOM   16697 C  CD1   . LEU A 1 3833 ? 215.118 254.588 196.006 1.00 44.04  ? 3833 LEU A CD1   1 
ATOM   16698 C  CD2   . LEU A 1 3833 ? 216.961 256.264 196.236 1.00 40.23  ? 3833 LEU A CD2   1 
ATOM   16699 N  N     . ASP A 1 3834 ? 214.827 257.187 201.050 1.00 36.38  ? 3834 ASP A N     1 
ATOM   16700 C  CA    . ASP A 1 3834 ? 214.105 258.019 202.007 1.00 34.99  ? 3834 ASP A CA    1 
ATOM   16701 C  C     . ASP A 1 3834 ? 214.990 259.138 202.534 1.00 39.14  ? 3834 ASP A C     1 
ATOM   16702 O  O     . ASP A 1 3834 ? 214.534 260.276 202.689 1.00 43.62  ? 3834 ASP A O     1 
ATOM   16703 C  CB    . ASP A 1 3834 ? 213.581 257.164 203.159 1.00 38.83  ? 3834 ASP A CB    1 
ATOM   16704 C  CG    . ASP A 1 3834 ? 212.477 256.223 202.729 1.00 54.36  ? 3834 ASP A CG    1 
ATOM   16705 O  OD1   . ASP A 1 3834 ? 212.131 256.226 201.529 1.00 52.55  ? 3834 ASP A OD1   1 
ATOM   16706 O  OD2   . ASP A 1 3834 ? 211.953 255.485 203.589 1.00 51.62  ? 3834 ASP A OD2   1 
ATOM   16707 N  N     . ILE A 1 3835 ? 216.257 258.833 202.819 1.00 39.66  ? 3835 ILE A N     1 
ATOM   16708 C  CA    . ILE A 1 3835 ? 217.197 259.876 203.237 1.00 31.70  ? 3835 ILE A CA    1 
ATOM   16709 C  C     . ILE A 1 3835 ? 217.315 260.948 202.157 1.00 41.38  ? 3835 ILE A C     1 
ATOM   16710 O  O     . ILE A 1 3835 ? 217.257 262.153 202.433 1.00 49.33  ? 3835 ILE A O     1 
ATOM   16711 C  CB    . ILE A 1 3835 ? 218.569 259.259 203.564 1.00 33.79  ? 3835 ILE A CB    1 
ATOM   16712 C  CG1   . ILE A 1 3835 ? 218.495 258.413 204.835 1.00 43.75  ? 3835 ILE A CG1   1 
ATOM   16713 C  CG2   . ILE A 1 3835 ? 219.625 260.340 203.692 1.00 37.35  ? 3835 ILE A CG2   1 
ATOM   16714 C  CD1   . ILE A 1 3835 ? 219.748 257.619 205.100 1.00 35.71  ? 3835 ILE A CD1   1 
ATOM   16715 N  N     . TYR A 1 3836 ? 217.474 260.515 200.907 1.00 43.03  ? 3836 TYR A N     1 
ATOM   16716 C  CA    . TYR A 1 3836 ? 217.635 261.442 199.792 1.00 32.12  ? 3836 TYR A CA    1 
ATOM   16717 C  C     . TYR A 1 3836 ? 216.393 262.301 199.597 1.00 36.42  ? 3836 TYR A C     1 
ATOM   16718 O  O     . TYR A 1 3836 ? 216.494 263.505 199.337 1.00 50.59  ? 3836 TYR A O     1 
ATOM   16719 C  CB    . TYR A 1 3836 ? 217.955 260.653 198.525 1.00 39.65  ? 3836 TYR A CB    1 
ATOM   16720 C  CG    . TYR A 1 3836 ? 218.407 261.486 197.355 1.00 48.65  ? 3836 TYR A CG    1 
ATOM   16721 C  CD1   . TYR A 1 3836 ? 219.328 262.507 197.521 1.00 51.89  ? 3836 TYR A CD1   1 
ATOM   16722 C  CD2   . TYR A 1 3836 ? 217.934 261.232 196.077 1.00 46.19  ? 3836 TYR A CD2   1 
ATOM   16723 C  CE1   . TYR A 1 3836 ? 219.748 263.263 196.452 1.00 42.51  ? 3836 TYR A CE1   1 
ATOM   16724 C  CE2   . TYR A 1 3836 ? 218.352 261.980 195.004 1.00 44.38  ? 3836 TYR A CE2   1 
ATOM   16725 C  CZ    . TYR A 1 3836 ? 219.260 262.993 195.198 1.00 43.21  ? 3836 TYR A CZ    1 
ATOM   16726 O  OH    . TYR A 1 3836 ? 219.683 263.743 194.131 1.00 52.86  ? 3836 TYR A OH    1 
ATOM   16727 N  N     . HIS A 1 3837 ? 215.210 261.694 199.703 1.00 41.38  ? 3837 HIS A N     1 
ATOM   16728 C  CA    . HIS A 1 3837 ? 213.964 262.441 199.582 1.00 40.73  ? 3837 HIS A CA    1 
ATOM   16729 C  C     . HIS A 1 3837 ? 213.812 263.445 200.717 1.00 48.42  ? 3837 HIS A C     1 
ATOM   16730 O  O     . HIS A 1 3837 ? 213.411 264.591 200.488 1.00 55.00  ? 3837 HIS A O     1 
ATOM   16731 C  CB    . HIS A 1 3837 ? 212.787 261.464 199.547 1.00 45.30  ? 3837 HIS A CB    1 
ATOM   16732 C  CG    . HIS A 1 3837 ? 211.441 262.120 199.542 1.00 53.98  ? 3837 HIS A CG    1 
ATOM   16733 N  ND1   . HIS A 1 3837 ? 210.903 262.736 200.651 1.00 55.02  ? 3837 HIS A ND1   1 
ATOM   16734 C  CD2   . HIS A 1 3837 ? 210.514 262.239 198.562 1.00 55.30  ? 3837 HIS A CD2   1 
ATOM   16735 C  CE1   . HIS A 1 3837 ? 209.709 263.215 200.353 1.00 55.24  ? 3837 HIS A CE1   1 
ATOM   16736 N  NE2   . HIS A 1 3837 ? 209.449 262.926 199.090 1.00 57.97  ? 3837 HIS A NE2   1 
ATOM   16737 N  N     . ASN A 1 3838 ? 214.129 263.036 201.947 1.00 48.88  ? 3838 ASN A N     1 
ATOM   16738 C  CA    . ASN A 1 3838 ? 214.084 263.943 203.086 1.00 45.62  ? 3838 ASN A CA    1 
ATOM   16739 C  C     . ASN A 1 3838 ? 215.102 265.067 202.978 1.00 48.52  ? 3838 ASN A C     1 
ATOM   16740 O  O     . ASN A 1 3838 ? 214.930 266.102 203.629 1.00 59.79  ? 3838 ASN A O     1 
ATOM   16741 C  CB    . ASN A 1 3838 ? 214.313 263.163 204.380 1.00 47.27  ? 3838 ASN A CB    1 
ATOM   16742 C  CG    . ASN A 1 3838 ? 214.088 264.006 205.615 1.00 49.92  ? 3838 ASN A CG    1 
ATOM   16743 O  OD1   . ASN A 1 3838 ? 215.037 264.486 206.234 1.00 49.94  ? 3838 ASN A OD1   1 
ATOM   16744 N  ND2   . ASN A 1 3838 ? 212.827 264.188 205.985 1.00 52.07  ? 3838 ASN A ND2   1 
ATOM   16745 N  N     . VAL A 1 3839 ? 216.162 264.882 202.201 1.00 46.71  ? 3839 VAL A N     1 
ATOM   16746 C  CA    . VAL A 1 3839 ? 217.085 265.981 201.939 1.00 40.81  ? 3839 VAL A CA    1 
ATOM   16747 C  C     . VAL A 1 3839 ? 216.552 266.910 200.852 1.00 45.39  ? 3839 VAL A C     1 
ATOM   16748 O  O     . VAL A 1 3839 ? 216.567 268.132 201.011 1.00 48.52  ? 3839 VAL A O     1 
ATOM   16749 C  CB    . VAL A 1 3839 ? 218.473 265.421 201.579 1.00 44.63  ? 3839 VAL A CB    1 
ATOM   16750 C  CG1   . VAL A 1 3839 ? 219.352 266.511 201.007 1.00 48.27  ? 3839 VAL A CG1   1 
ATOM   16751 C  CG2   . VAL A 1 3839 ? 219.117 264.810 202.803 1.00 50.58  ? 3839 VAL A CG2   1 
ATOM   16752 N  N     . LEU A 1 3840 ? 216.077 266.353 199.735 1.00 50.98  ? 3840 LEU A N     1 
ATOM   16753 C  CA    . LEU A 1 3840 ? 215.554 267.185 198.653 1.00 45.87  ? 3840 LEU A CA    1 
ATOM   16754 C  C     . LEU A 1 3840 ? 214.254 267.870 199.054 1.00 48.09  ? 3840 LEU A C     1 
ATOM   16755 O  O     . LEU A 1 3840 ? 214.110 269.088 198.906 1.00 53.58  ? 3840 LEU A O     1 
ATOM   16756 C  CB    . LEU A 1 3840 ? 215.344 266.339 197.398 1.00 44.58  ? 3840 LEU A CB    1 
ATOM   16757 C  CG    . LEU A 1 3840 ? 216.603 265.775 196.747 1.00 43.05  ? 3840 LEU A CG    1 
ATOM   16758 C  CD1   . LEU A 1 3840 ? 216.225 264.890 195.582 1.00 50.18  ? 3840 LEU A CD1   1 
ATOM   16759 C  CD2   . LEU A 1 3840 ? 217.510 266.899 196.294 1.00 44.13  ? 3840 LEU A CD2   1 
ATOM   16760 N  N     . TYR A 1 3841 ? 213.295 267.102 199.558 1.00 53.52  ? 3841 TYR A N     1 
ATOM   16761 C  CA    . TYR A 1 3841 ? 212.036 267.625 200.061 1.00 49.60  ? 3841 TYR A CA    1 
ATOM   16762 C  C     . TYR A 1 3841 ? 212.042 267.572 201.582 1.00 58.96  ? 3841 TYR A C     1 
ATOM   16763 O  O     . TYR A 1 3841 ? 212.797 266.811 202.189 1.00 65.48  ? 3841 TYR A O     1 
ATOM   16764 C  CB    . TYR A 1 3841 ? 210.845 266.828 199.517 1.00 50.60  ? 3841 TYR A CB    1 
ATOM   16765 C  CG    . TYR A 1 3841 ? 210.864 266.631 198.020 1.00 51.00  ? 3841 TYR A CG    1 
ATOM   16766 C  CD1   . TYR A 1 3841 ? 210.864 267.715 197.157 1.00 53.98  ? 3841 TYR A CD1   1 
ATOM   16767 C  CD2   . TYR A 1 3841 ? 210.887 265.358 197.471 1.00 50.77  ? 3841 TYR A CD2   1 
ATOM   16768 C  CE1   . TYR A 1 3841 ? 210.882 267.537 195.789 1.00 56.80  ? 3841 TYR A CE1   1 
ATOM   16769 C  CE2   . TYR A 1 3841 ? 210.906 265.170 196.105 1.00 54.03  ? 3841 TYR A CE2   1 
ATOM   16770 C  CZ    . TYR A 1 3841 ? 210.904 266.262 195.269 1.00 58.75  ? 3841 TYR A CZ    1 
ATOM   16771 O  OH    . TYR A 1 3841 ? 210.922 266.079 193.907 1.00 59.43  ? 3841 TYR A OH    1 
ATOM   16772 N  N     . GLU A 1 3842 ? 211.185 268.387 202.192 1.00 62.90  ? 3842 GLU A N     1 
ATOM   16773 C  CA    . GLU A 1 3842 ? 211.081 268.459 203.651 1.00 66.57  ? 3842 GLU A CA    1 
ATOM   16774 C  C     . GLU A 1 3842 ? 212.414 268.850 204.285 1.00 64.98  ? 3842 GLU A C     1 
ATOM   16775 O  O     . GLU A 1 3842 ? 212.796 268.338 205.338 1.00 65.22  ? 3842 GLU A O     1 
ATOM   16776 C  CB    . GLU A 1 3842 ? 210.571 267.140 204.236 1.00 63.76  ? 3842 GLU A CB    1 
ATOM   16777 C  CG    . GLU A 1 3842 ? 209.137 266.807 203.870 1.00 68.81  ? 3842 GLU A CG    1 
ATOM   16778 C  CD    . GLU A 1 3842 ? 208.681 265.485 204.453 1.00 74.01  ? 3842 GLU A CD    1 
ATOM   16779 O  OE1   . GLU A 1 3842 ? 209.521 264.768 205.036 1.00 69.24  ? 3842 GLU A OE1   1 
ATOM   16780 O  OE2   . GLU A 1 3842 ? 207.481 265.162 204.331 1.00 73.60  ? 3842 GLU A OE2   1 
ATOM   16781 N  N     . ASN A 1 3843 ? 213.132 269.765 203.635 1.00 58.79  ? 3843 ASN A N     1 
ATOM   16782 C  CA    . ASN A 1 3843 ? 214.370 270.292 204.183 1.00 58.64  ? 3843 ASN A CA    1 
ATOM   16783 C  C     . ASN A 1 3843 ? 214.098 271.658 204.791 1.00 63.83  ? 3843 ASN A C     1 
ATOM   16784 O  O     . ASN A 1 3843 ? 213.793 272.604 204.049 1.00 65.66  ? 3843 ASN A O     1 
ATOM   16785 C  CB    . ASN A 1 3843 ? 215.442 270.396 203.101 1.00 53.60  ? 3843 ASN A CB    1 
ATOM   16786 C  CG    . ASN A 1 3843 ? 216.844 270.400 203.671 1.00 55.41  ? 3843 ASN A CG    1 
ATOM   16787 O  OD1   . ASN A 1 3843 ? 217.040 270.206 204.868 1.00 59.98  ? 3843 ASN A OD1   1 
ATOM   16788 N  ND2   . ASN A 1 3843 ? 217.829 270.626 202.812 1.00 59.25  ? 3843 ASN A ND2   1 
ATOM   16789 N  N     . PRO A 1 3844 ? 214.178 271.814 206.114 1.00 66.48  ? 3844 PRO A N     1 
ATOM   16790 C  CA    . PRO A 1 3844 ? 213.926 273.134 206.715 1.00 65.01  ? 3844 PRO A CA    1 
ATOM   16791 C  C     . PRO A 1 3844 ? 214.891 274.209 206.252 1.00 64.32  ? 3844 PRO A C     1 
ATOM   16792 O  O     . PRO A 1 3844 ? 214.538 275.394 206.290 1.00 65.97  ? 3844 PRO A O     1 
ATOM   16793 C  CB    . PRO A 1 3844 ? 214.068 272.868 208.220 1.00 63.45  ? 3844 PRO A CB    1 
ATOM   16794 C  CG    . PRO A 1 3844 ? 213.855 271.399 208.372 1.00 60.55  ? 3844 PRO A CG    1 
ATOM   16795 C  CD    . PRO A 1 3844 ? 214.412 270.778 207.132 1.00 66.15  ? 3844 PRO A CD    1 
ATOM   16796 N  N     . ASN A 1 3845 ? 216.094 273.839 205.814 1.00 56.21  ? 3845 ASN A N     1 
ATOM   16797 C  CA    . ASN A 1 3845 ? 217.087 274.817 205.392 1.00 61.44  ? 3845 ASN A CA    1 
ATOM   16798 C  C     . ASN A 1 3845 ? 216.838 275.353 203.990 1.00 62.65  ? 3845 ASN A C     1 
ATOM   16799 O  O     . ASN A 1 3845 ? 217.559 276.257 203.555 1.00 63.53  ? 3845 ASN A O     1 
ATOM   16800 C  CB    . ASN A 1 3845 ? 218.485 274.203 205.465 1.00 62.71  ? 3845 ASN A CB    1 
ATOM   16801 C  CG    . ASN A 1 3845 ? 218.856 273.769 206.867 1.00 64.23  ? 3845 ASN A CG    1 
ATOM   16802 O  OD1   . ASN A 1 3845 ? 219.027 272.581 207.136 1.00 63.25  ? 3845 ASN A OD1   1 
ATOM   16803 N  ND2   . ASN A 1 3845 ? 218.981 274.733 207.771 1.00 63.72  ? 3845 ASN A ND2   1 
ATOM   16804 N  N     . LEU A 1 3846 ? 215.850 274.819 203.274 1.00 61.76  ? 3846 LEU A N     1 
ATOM   16805 C  CA    . LEU A 1 3846 ? 215.526 275.258 201.924 1.00 61.10  ? 3846 LEU A CA    1 
ATOM   16806 C  C     . LEU A 1 3846 ? 214.221 276.039 201.861 1.00 66.10  ? 3846 LEU A C     1 
ATOM   16807 O  O     . LEU A 1 3846 ? 213.676 276.228 200.769 1.00 71.42  ? 3846 LEU A O     1 
ATOM   16808 C  CB    . LEU A 1 3846 ? 215.452 274.055 200.982 1.00 61.83  ? 3846 LEU A CB    1 
ATOM   16809 C  CG    . LEU A 1 3846 ? 216.742 273.282 200.714 1.00 56.45  ? 3846 LEU A CG    1 
ATOM   16810 C  CD1   . LEU A 1 3846 ? 216.441 272.030 199.918 1.00 59.24  ? 3846 LEU A CD1   1 
ATOM   16811 C  CD2   . LEU A 1 3846 ? 217.738 274.154 199.983 1.00 60.00  ? 3846 LEU A CD2   1 
ATOM   16812 N  N     . LYS A 1 3847 ? 213.703 276.491 203.005 1.00 67.65  ? 3847 LYS A N     1 
ATOM   16813 C  CA    . LYS A 1 3847 ? 212.382 277.110 203.028 1.00 69.44  ? 3847 LYS A CA    1 
ATOM   16814 C  C     . LYS A 1 3847 ? 212.374 278.437 202.277 1.00 70.21  ? 3847 LYS A C     1 
ATOM   16815 O  O     . LYS A 1 3847 ? 211.494 278.686 201.446 1.00 67.78  ? 3847 LYS A O     1 
ATOM   16816 C  CB    . LYS A 1 3847 ? 211.922 277.304 204.473 1.00 66.34  ? 3847 LYS A CB    1 
ATOM   16817 C  CG    . LYS A 1 3847 ? 210.552 277.941 204.602 1.00 69.84  ? 3847 LYS A CG    1 
ATOM   16818 C  CD    . LYS A 1 3847 ? 209.467 277.009 204.089 1.00 73.43  ? 3847 LYS A CD    1 
ATOM   16819 C  CE    . LYS A 1 3847 ? 208.081 277.572 204.357 1.00 73.84  ? 3847 LYS A CE    1 
ATOM   16820 N  NZ    . LYS A 1 3847 ? 207.831 278.814 203.576 1.00 69.90  ? 3847 LYS A NZ    1 
ATOM   16821 N  N     . GLY A 1 3848 ? 213.347 279.303 202.555 1.00 66.07  ? 3848 GLY A N     1 
ATOM   16822 C  CA    . GLY A 1 3848 ? 213.397 280.620 201.952 1.00 67.64  ? 3848 GLY A CA    1 
ATOM   16823 C  C     . GLY A 1 3848 ? 214.514 280.868 200.966 1.00 70.19  ? 3848 GLY A C     1 
ATOM   16824 O  O     . GLY A 1 3848 ? 214.747 282.029 200.603 1.00 68.76  ? 3848 GLY A O     1 
ATOM   16825 N  N     . VAL A 1 3849 ? 215.213 279.837 200.510 1.00 71.34  ? 3849 VAL A N     1 
ATOM   16826 C  CA    . VAL A 1 3849 ? 216.340 280.000 199.599 1.00 68.79  ? 3849 VAL A CA    1 
ATOM   16827 C  C     . VAL A 1 3849 ? 215.852 279.793 198.173 1.00 71.48  ? 3849 VAL A C     1 
ATOM   16828 O  O     . VAL A 1 3849 ? 215.127 278.833 197.884 1.00 71.54  ? 3849 VAL A O     1 
ATOM   16829 C  CB    . VAL A 1 3849 ? 217.475 279.021 199.952 1.00 68.51  ? 3849 VAL A CB    1 
ATOM   16830 C  CG1   . VAL A 1 3849 ? 218.636 279.186 198.989 1.00 70.62  ? 3849 VAL A CG1   1 
ATOM   16831 C  CG2   . VAL A 1 3849 ? 217.929 279.230 201.384 1.00 67.99  ? 3849 VAL A CG2   1 
ATOM   16832 N  N     . THR A 1 3850 ? 216.243 280.698 197.276 1.00 74.82  ? 3850 THR A N     1 
ATOM   16833 C  CA    . THR A 1 3850 ? 215.775 280.648 195.896 1.00 76.66  ? 3850 THR A CA    1 
ATOM   16834 C  C     . THR A 1 3850 ? 216.922 280.424 194.918 1.00 75.57  ? 3850 THR A C     1 
ATOM   16835 O  O     . THR A 1 3850 ? 216.710 279.903 193.819 1.00 75.22  ? 3850 THR A O     1 
ATOM   16836 C  CB    . THR A 1 3850 ? 215.029 281.934 195.536 1.00 75.77  ? 3850 THR A CB    1 
ATOM   16837 O  OG1   . THR A 1 3850 ? 215.905 283.057 195.695 1.00 75.77  ? 3850 THR A OG1   1 
ATOM   16838 C  CG2   . THR A 1 3850 ? 213.814 282.114 196.433 1.00 74.22  ? 3850 THR A CG2   1 
ATOM   16839 N  N     . ASP A 1 3851 ? 218.133 280.822 195.300 1.00 73.53  ? 3851 ASP A N     1 
ATOM   16840 C  CA    . ASP A 1 3851 ? 219.291 280.624 194.438 1.00 70.48  ? 3851 ASP A CA    1 
ATOM   16841 C  C     . ASP A 1 3851 ? 219.513 279.139 194.190 1.00 76.04  ? 3851 ASP A C     1 
ATOM   16842 O  O     . ASP A 1 3851 ? 219.306 278.312 195.081 1.00 82.60  ? 3851 ASP A O     1 
ATOM   16843 C  CB    . ASP A 1 3851 ? 220.533 281.249 195.071 1.00 74.32  ? 3851 ASP A CB    1 
ATOM   16844 C  CG    . ASP A 1 3851 ? 221.705 281.314 194.113 1.00 75.45  ? 3851 ASP A CG    1 
ATOM   16845 O  OD1   . ASP A 1 3851 ? 221.495 281.119 192.898 1.00 74.24  ? 3851 ASP A OD1   1 
ATOM   16846 O  OD2   . ASP A 1 3851 ? 222.839 281.561 194.575 1.00 77.10  ? 3851 ASP A OD2   1 
ATOM   16847 N  N     . HIS A 1 3852 ? 219.924 278.799 192.968 1.00 74.03  ? 3852 HIS A N     1 
ATOM   16848 C  CA    . HIS A 1 3852 ? 220.088 277.392 192.619 1.00 70.64  ? 3852 HIS A CA    1 
ATOM   16849 C  C     . HIS A 1 3852 ? 221.385 276.820 193.179 1.00 66.93  ? 3852 HIS A C     1 
ATOM   16850 O  O     . HIS A 1 3852 ? 221.389 275.716 193.735 1.00 76.70  ? 3852 HIS A O     1 
ATOM   16851 C  CB    . HIS A 1 3852 ? 220.028 277.218 191.103 1.00 68.07  ? 3852 HIS A CB    1 
ATOM   16852 C  CG    . HIS A 1 3852 ? 218.635 277.222 190.555 1.00 72.84  ? 3852 HIS A CG    1 
ATOM   16853 N  ND1   . HIS A 1 3852 ? 218.263 277.985 189.470 1.00 69.66  ? 3852 HIS A ND1   1 
ATOM   16854 C  CD2   . HIS A 1 3852 ? 217.521 276.563 190.951 1.00 72.00  ? 3852 HIS A CD2   1 
ATOM   16855 C  CE1   . HIS A 1 3852 ? 216.981 277.790 189.216 1.00 69.41  ? 3852 HIS A CE1   1 
ATOM   16856 N  NE2   . HIS A 1 3852 ? 216.507 276.932 190.101 1.00 70.03  ? 3852 HIS A NE2   1 
ATOM   16857 N  N     . THR A 1 3853 ? 222.494 277.549 193.041 1.00 60.70  ? 3853 THR A N     1 
ATOM   16858 C  CA    . THR A 1 3853 ? 223.776 277.038 193.520 1.00 65.96  ? 3853 THR A CA    1 
ATOM   16859 C  C     . THR A 1 3853 ? 223.792 276.920 195.039 1.00 67.79  ? 3853 THR A C     1 
ATOM   16860 O  O     . THR A 1 3853 ? 224.306 275.939 195.591 1.00 70.27  ? 3853 THR A O     1 
ATOM   16861 C  CB    . THR A 1 3853 ? 224.914 277.936 193.038 1.00 65.22  ? 3853 THR A CB    1 
ATOM   16862 O  OG1   . THR A 1 3853 ? 224.890 278.013 191.608 1.00 66.45  ? 3853 THR A OG1   1 
ATOM   16863 C  CG2   . THR A 1 3853 ? 226.255 277.376 193.477 1.00 64.56  ? 3853 THR A CG2   1 
ATOM   16864 N  N     . GLN A 1 3854 ? 223.232 277.911 195.735 1.00 62.17  ? 3854 GLN A N     1 
ATOM   16865 C  CA    . GLN A 1 3854 ? 223.162 277.835 197.188 1.00 63.89  ? 3854 GLN A CA    1 
ATOM   16866 C  C     . GLN A 1 3854 ? 222.260 276.699 197.649 1.00 66.35  ? 3854 GLN A C     1 
ATOM   16867 O  O     . GLN A 1 3854 ? 222.588 276.012 198.624 1.00 73.47  ? 3854 GLN A O     1 
ATOM   16868 C  CB    . GLN A 1 3854 ? 222.675 279.163 197.767 1.00 63.70  ? 3854 GLN A CB    1 
ATOM   16869 C  CG    . GLN A 1 3854 ? 222.855 279.273 199.271 1.00 68.25  ? 3854 GLN A CG    1 
ATOM   16870 C  CD    . GLN A 1 3854 ? 222.512 280.648 199.801 1.00 72.00  ? 3854 GLN A CD    1 
ATOM   16871 O  OE1   . GLN A 1 3854 ? 222.097 281.530 199.050 1.00 70.84  ? 3854 GLN A OE1   1 
ATOM   16872 N  NE2   . GLN A 1 3854 ? 222.686 280.839 201.104 1.00 67.06  ? 3854 GLN A NE2   1 
ATOM   16873 N  N     . ARG A 1 3855 ? 221.133 276.483 196.967 1.00 57.17  ? 3855 ARG A N     1 
ATOM   16874 C  CA    . ARG A 1 3855 ? 220.280 275.347 197.295 1.00 53.78  ? 3855 ARG A CA    1 
ATOM   16875 C  C     . ARG A 1 3855 ? 221.011 274.031 197.068 1.00 53.91  ? 3855 ARG A C     1 
ATOM   16876 O  O     . ARG A 1 3855 ? 220.864 273.092 197.856 1.00 63.49  ? 3855 ARG A O     1 
ATOM   16877 C  CB    . ARG A 1 3855 ? 218.994 275.394 196.472 1.00 56.12  ? 3855 ARG A CB    1 
ATOM   16878 C  CG    . ARG A 1 3855 ? 217.922 276.288 197.055 1.00 56.26  ? 3855 ARG A CG    1 
ATOM   16879 C  CD    . ARG A 1 3855 ? 216.676 276.303 196.196 1.00 55.10  ? 3855 ARG A CD    1 
ATOM   16880 N  NE    . ARG A 1 3855 ? 216.007 275.009 196.192 1.00 56.04  ? 3855 ARG A NE    1 
ATOM   16881 C  CZ    . ARG A 1 3855 ? 214.871 274.752 196.824 1.00 57.49  ? 3855 ARG A CZ    1 
ATOM   16882 N  NH1   . ARG A 1 3855 ? 214.249 275.680 197.533 1.00 54.29  ? 3855 ARG A NH1   1 
ATOM   16883 N  NH2   . ARG A 1 3855 ? 214.347 273.533 196.747 1.00 58.93  ? 3855 ARG A NH2   1 
ATOM   16884 N  N     . LEU A 1 3856 ? 221.800 273.944 195.996 1.00 52.27  ? 3856 LEU A N     1 
ATOM   16885 C  CA    . LEU A 1 3856 ? 222.584 272.738 195.751 1.00 54.12  ? 3856 LEU A CA    1 
ATOM   16886 C  C     . LEU A 1 3856 ? 223.597 272.500 196.862 1.00 50.78  ? 3856 LEU A C     1 
ATOM   16887 O  O     . LEU A 1 3856 ? 223.779 271.364 197.313 1.00 51.04  ? 3856 LEU A O     1 
ATOM   16888 C  CB    . LEU A 1 3856 ? 223.291 272.836 194.401 1.00 55.69  ? 3856 LEU A CB    1 
ATOM   16889 C  CG    . LEU A 1 3856 ? 224.164 271.638 194.033 1.00 56.15  ? 3856 LEU A CG    1 
ATOM   16890 C  CD1   . LEU A 1 3856 ? 223.365 270.346 194.079 1.00 52.34  ? 3856 LEU A CD1   1 
ATOM   16891 C  CD2   . LEU A 1 3856 ? 224.788 271.841 192.672 1.00 54.33  ? 3856 LEU A CD2   1 
ATOM   16892 N  N     . SER A 1 3857 ? 224.273 273.559 197.311 1.00 46.22  ? 3857 SER A N     1 
ATOM   16893 C  CA    . SER A 1 3857 ? 225.227 273.415 198.408 1.00 49.92  ? 3857 SER A CA    1 
ATOM   16894 C  C     . SER A 1 3857 ? 224.533 272.972 199.692 1.00 53.10  ? 3857 SER A C     1 
ATOM   16895 O  O     . SER A 1 3857 ? 225.045 272.112 200.423 1.00 58.08  ? 3857 SER A O     1 
ATOM   16896 C  CB    . SER A 1 3857 ? 225.973 274.729 198.627 1.00 50.35  ? 3857 SER A CB    1 
ATOM   16897 O  OG    . SER A 1 3857 ? 225.088 275.745 199.064 1.00 59.90  ? 3857 SER A OG    1 
ATOM   16898 N  N     . ILE A 1 3858 ? 223.366 273.551 199.982 1.00 47.42  ? 3858 ILE A N     1 
ATOM   16899 C  CA    . ILE A 1 3858 ? 222.608 273.164 201.170 1.00 38.62  ? 3858 ILE A CA    1 
ATOM   16900 C  C     . ILE A 1 3858 ? 222.210 271.696 201.089 1.00 46.36  ? 3858 ILE A C     1 
ATOM   16901 O  O     . ILE A 1 3858 ? 222.321 270.947 202.067 1.00 59.27  ? 3858 ILE A O     1 
ATOM   16902 C  CB    . ILE A 1 3858 ? 221.376 274.072 201.335 1.00 47.66  ? 3858 ILE A CB    1 
ATOM   16903 C  CG1   . ILE A 1 3858 ? 221.803 275.499 201.679 1.00 49.86  ? 3858 ILE A CG1   1 
ATOM   16904 C  CG2   . ILE A 1 3858 ? 220.445 273.529 202.401 1.00 47.81  ? 3858 ILE A CG2   1 
ATOM   16905 C  CD1   . ILE A 1 3858 ? 220.673 276.497 201.621 1.00 52.10  ? 3858 ILE A CD1   1 
ATOM   16906 N  N     . ILE A 1 3859 ? 221.733 271.267 199.919 1.00 49.18  ? 3859 ILE A N     1 
ATOM   16907 C  CA    . ILE A 1 3859 ? 221.331 269.876 199.739 1.00 43.67  ? 3859 ILE A CA    1 
ATOM   16908 C  C     . ILE A 1 3859 ? 222.525 268.950 199.916 1.00 45.07  ? 3859 ILE A C     1 
ATOM   16909 O  O     . ILE A 1 3859 ? 222.419 267.894 200.547 1.00 47.92  ? 3859 ILE A O     1 
ATOM   16910 C  CB    . ILE A 1 3859 ? 220.663 269.689 198.364 1.00 44.86  ? 3859 ILE A CB    1 
ATOM   16911 C  CG1   . ILE A 1 3859 ? 219.294 270.368 198.341 1.00 46.05  ? 3859 ILE A CG1   1 
ATOM   16912 C  CG2   . ILE A 1 3859 ? 220.516 268.220 198.033 1.00 43.30  ? 3859 ILE A CG2   1 
ATOM   16913 C  CD1   . ILE A 1 3859 ? 218.682 270.455 196.966 1.00 45.05  ? 3859 ILE A CD1   1 
ATOM   16914 N  N     . THR A 1 3860 ? 223.683 269.333 199.374 1.00 37.85  ? 3860 THR A N     1 
ATOM   16915 C  CA    . THR A 1 3860 ? 224.874 268.501 199.513 1.00 32.75  ? 3860 THR A CA    1 
ATOM   16916 C  C     . THR A 1 3860 ? 225.294 268.370 200.972 1.00 38.90  ? 3860 THR A C     1 
ATOM   16917 O  O     . THR A 1 3860 ? 225.672 267.281 201.420 1.00 51.89  ? 3860 THR A O     1 
ATOM   16918 C  CB    . THR A 1 3860 ? 226.016 269.078 198.678 1.00 44.27  ? 3860 THR A CB    1 
ATOM   16919 O  OG1   . THR A 1 3860 ? 225.598 269.192 197.313 1.00 49.99  ? 3860 THR A OG1   1 
ATOM   16920 C  CG2   . THR A 1 3860 ? 227.232 268.174 198.747 1.00 43.65  ? 3860 THR A CG2   1 
ATOM   16921 N  N     . LYS A 1 3861 ? 225.241 269.467 201.730 1.00 36.67  ? 3861 LYS A N     1 
ATOM   16922 C  CA    . LYS A 1 3861 ? 225.607 269.410 203.144 1.00 35.96  ? 3861 LYS A CA    1 
ATOM   16923 C  C     . LYS A 1 3861 ? 224.634 268.543 203.939 1.00 41.70  ? 3861 LYS A C     1 
ATOM   16924 O  O     . LYS A 1 3861 ? 225.043 267.630 204.677 1.00 42.90  ? 3861 LYS A O     1 
ATOM   16925 C  CB    . LYS A 1 3861 ? 225.657 270.826 203.717 1.00 38.08  ? 3861 LYS A CB    1 
ATOM   16926 C  CG    . LYS A 1 3861 ? 226.071 270.901 205.172 1.00 47.53  ? 3861 LYS A CG    1 
ATOM   16927 C  CD    . LYS A 1 3861 ? 226.165 272.343 205.639 1.00 42.90  ? 3861 LYS A CD    1 
ATOM   16928 C  CE    . LYS A 1 3861 ? 226.584 272.421 207.096 1.00 42.51  ? 3861 LYS A CE    1 
ATOM   16929 N  NZ    . LYS A 1 3861 ? 226.698 273.828 207.567 1.00 43.16  ? 3861 LYS A NZ    1 
ATOM   16930 N  N     . ASP A 1 3862 ? 223.335 268.809 203.802 1.00 45.42  ? 3862 ASP A N     1 
ATOM   16931 C  CA    . ASP A 1 3862 ? 222.365 268.029 204.554 1.00 40.61  ? 3862 ASP A CA    1 
ATOM   16932 C  C     . ASP A 1 3862 ? 222.251 266.591 204.076 1.00 41.55  ? 3862 ASP A C     1 
ATOM   16933 O  O     . ASP A 1 3862 ? 221.752 265.761 204.831 1.00 47.12  ? 3862 ASP A O     1 
ATOM   16934 C  CB    . ASP A 1 3862 ? 220.989 268.697 204.538 1.00 38.47  ? 3862 ASP A CB    1 
ATOM   16935 C  CG    . ASP A 1 3862 ? 221.018 270.097 205.117 1.00 55.08  ? 3862 ASP A CG    1 
ATOM   16936 O  OD1   . ASP A 1 3862 ? 221.011 271.075 204.347 1.00 56.88  ? 3862 ASP A OD1   1 
ATOM   16937 O  OD2   . ASP A 1 3862 ? 221.056 270.219 206.360 1.00 56.85  ? 3862 ASP A OD2   1 
ATOM   16938 N  N     . LEU A 1 3863 ? 222.735 266.257 202.880 1.00 34.80  ? 3863 LEU A N     1 
ATOM   16939 C  CA    . LEU A 1 3863 ? 222.780 264.853 202.494 1.00 34.68  ? 3863 LEU A CA    1 
ATOM   16940 C  C     . LEU A 1 3863 ? 223.662 264.058 203.445 1.00 41.71  ? 3863 LEU A C     1 
ATOM   16941 O  O     . LEU A 1 3863 ? 223.216 263.068 204.038 1.00 45.68  ? 3863 LEU A O     1 
ATOM   16942 C  CB    . LEU A 1 3863 ? 223.279 264.721 201.056 1.00 41.47  ? 3863 LEU A CB    1 
ATOM   16943 C  CG    . LEU A 1 3863 ? 223.582 263.308 200.563 1.00 38.59  ? 3863 LEU A CG    1 
ATOM   16944 C  CD1   . LEU A 1 3863 ? 222.297 262.580 200.219 1.00 40.97  ? 3863 LEU A CD1   1 
ATOM   16945 C  CD2   . LEU A 1 3863 ? 224.513 263.361 199.367 1.00 31.84  ? 3863 LEU A CD2   1 
ATOM   16946 N  N     . PHE A 1 3864 ? 224.904 264.505 203.640 1.00 39.57  ? 3864 PHE A N     1 
ATOM   16947 C  CA    . PHE A 1 3864 ? 225.789 263.864 204.604 1.00 33.30  ? 3864 PHE A CA    1 
ATOM   16948 C  C     . PHE A 1 3864 ? 225.250 263.964 206.021 1.00 36.62  ? 3864 PHE A C     1 
ATOM   16949 O  O     . PHE A 1 3864 ? 225.304 262.978 206.770 1.00 43.67  ? 3864 PHE A O     1 
ATOM   16950 C  CB    . PHE A 1 3864 ? 227.184 264.486 204.539 1.00 33.55  ? 3864 PHE A CB    1 
ATOM   16951 C  CG    . PHE A 1 3864 ? 227.903 264.228 203.250 1.00 41.08  ? 3864 PHE A CG    1 
ATOM   16952 C  CD1   . PHE A 1 3864 ? 228.688 263.101 203.093 1.00 37.50  ? 3864 PHE A CD1   1 
ATOM   16953 C  CD2   . PHE A 1 3864 ? 227.795 265.115 202.195 1.00 38.36  ? 3864 PHE A CD2   1 
ATOM   16954 C  CE1   . PHE A 1 3864 ? 229.347 262.864 201.908 1.00 34.28  ? 3864 PHE A CE1   1 
ATOM   16955 C  CE2   . PHE A 1 3864 ? 228.453 264.882 201.009 1.00 37.30  ? 3864 PHE A CE2   1 
ATOM   16956 C  CZ    . PHE A 1 3864 ? 229.230 263.756 200.865 1.00 36.78  ? 3864 PHE A CZ    1 
ATOM   16957 N  N     . GLN A 1 3865 ? 224.722 265.131 206.405 1.00 35.30  ? 3865 GLN A N     1 
ATOM   16958 C  CA    . GLN A 1 3865 ? 224.227 265.282 207.771 1.00 30.26  ? 3865 GLN A CA    1 
ATOM   16959 C  C     . GLN A 1 3865 ? 223.095 264.302 208.067 1.00 32.73  ? 3865 GLN A C     1 
ATOM   16960 O  O     . GLN A 1 3865 ? 223.123 263.593 209.080 1.00 37.23  ? 3865 GLN A O     1 
ATOM   16961 C  CB    . GLN A 1 3865 ? 223.771 266.719 208.011 1.00 37.15  ? 3865 GLN A CB    1 
ATOM   16962 C  CG    . GLN A 1 3865 ? 223.357 266.995 209.443 1.00 39.17  ? 3865 GLN A CG    1 
ATOM   16963 C  CD    . GLN A 1 3865 ? 224.497 266.808 210.423 1.00 40.42  ? 3865 GLN A CD    1 
ATOM   16964 O  OE1   . GLN A 1 3865 ? 225.343 267.685 210.581 1.00 42.62  ? 3865 GLN A OE1   1 
ATOM   16965 N  NE2   . GLN A 1 3865 ? 224.523 265.661 211.087 1.00 36.46  ? 3865 GLN A NE2   1 
ATOM   16966 N  N     . VAL A 1 3866 ? 222.095 264.237 207.186 1.00 35.77  ? 3866 VAL A N     1 
ATOM   16967 C  CA    . VAL A 1 3866 ? 220.943 263.371 207.404 1.00 28.73  ? 3866 VAL A CA    1 
ATOM   16968 C  C     . VAL A 1 3866 ? 221.342 261.907 207.291 1.00 31.21  ? 3866 VAL A C     1 
ATOM   16969 O  O     . VAL A 1 3866 ? 220.835 261.059 208.032 1.00 40.90  ? 3866 VAL A O     1 
ATOM   16970 C  CB    . VAL A 1 3866 ? 219.815 263.736 206.423 1.00 32.96  ? 3866 VAL A CB    1 
ATOM   16971 C  CG1   . VAL A 1 3866 ? 218.701 262.710 206.476 1.00 36.13  ? 3866 VAL A CG1   1 
ATOM   16972 C  CG2   . VAL A 1 3866 ? 219.276 265.118 206.737 1.00 34.01  ? 3866 VAL A CG2   1 
ATOM   16973 N  N     . ALA A 1 3867 ? 222.253 261.580 206.369 1.00 36.55  ? 3867 ALA A N     1 
ATOM   16974 C  CA    . ALA A 1 3867 ? 222.711 260.201 206.266 1.00 24.36  ? 3867 ALA A CA    1 
ATOM   16975 C  C     . ALA A 1 3867 ? 223.365 259.746 207.562 1.00 31.46  ? 3867 ALA A C     1 
ATOM   16976 O  O     . ALA A 1 3867 ? 223.071 258.655 208.063 1.00 44.17  ? 3867 ALA A O     1 
ATOM   16977 C  CB    . ALA A 1 3867 ? 223.678 260.053 205.093 1.00 22.70  ? 3867 ALA A CB    1 
ATOM   16978 N  N     . PHE A 1 3868 ? 224.235 260.581 208.137 1.00 34.78  ? 3868 PHE A N     1 
ATOM   16979 C  CA    . PHE A 1 3868 ? 224.855 260.216 209.407 1.00 19.08  ? 3868 PHE A CA    1 
ATOM   16980 C  C     . PHE A 1 3868 ? 223.821 260.126 210.522 1.00 28.86  ? 3868 PHE A C     1 
ATOM   16981 O  O     . PHE A 1 3868 ? 223.841 259.185 211.320 1.00 34.78  ? 3868 PHE A O     1 
ATOM   16982 C  CB    . PHE A 1 3868 ? 225.950 261.212 209.778 1.00 19.84  ? 3868 PHE A CB    1 
ATOM   16983 C  CG    . PHE A 1 3868 ? 226.620 260.902 211.084 1.00 34.07  ? 3868 PHE A CG    1 
ATOM   16984 C  CD1   . PHE A 1 3868 ? 227.605 259.935 211.156 1.00 39.49  ? 3868 PHE A CD1   1 
ATOM   16985 C  CD2   . PHE A 1 3868 ? 226.250 261.560 212.242 1.00 31.85  ? 3868 PHE A CD2   1 
ATOM   16986 C  CE1   . PHE A 1 3868 ? 228.213 259.638 212.354 1.00 23.73  ? 3868 PHE A CE1   1 
ATOM   16987 C  CE2   . PHE A 1 3868 ? 226.854 261.266 213.442 1.00 27.56  ? 3868 PHE A CE2   1 
ATOM   16988 C  CZ    . PHE A 1 3868 ? 227.836 260.304 213.497 1.00 27.08  ? 3868 PHE A CZ    1 
ATOM   16989 N  N     . ASN A 1 3869 ? 222.905 261.096 210.592 1.00 33.84  ? 3869 ASN A N     1 
ATOM   16990 C  CA    . ASN A 1 3869 ? 221.930 261.105 211.679 1.00 26.66  ? 3869 ASN A CA    1 
ATOM   16991 C  C     . ASN A 1 3869 ? 221.037 259.872 211.637 1.00 36.66  ? 3869 ASN A C     1 
ATOM   16992 O  O     . ASN A 1 3869 ? 220.737 259.278 212.678 1.00 44.36  ? 3869 ASN A O     1 
ATOM   16993 C  CB    . ASN A 1 3869 ? 221.083 262.373 211.616 1.00 28.60  ? 3869 ASN A CB    1 
ATOM   16994 C  CG    . ASN A 1 3869 ? 221.865 263.613 211.975 1.00 44.01  ? 3869 ASN A CG    1 
ATOM   16995 O  OD1   . ASN A 1 3869 ? 223.012 263.532 212.411 1.00 50.25  ? 3869 ASN A OD1   1 
ATOM   16996 N  ND2   . ASN A 1 3869 ? 221.248 264.773 211.796 1.00 43.49  ? 3869 ASN A ND2   1 
ATOM   16997 N  N     . ARG A 1 3870 ? 220.596 259.475 210.443 1.00 35.43  ? 3870 ARG A N     1 
ATOM   16998 C  CA    . ARG A 1 3870 ? 219.709 258.324 210.330 1.00 31.35  ? 3870 ARG A CA    1 
ATOM   16999 C  C     . ARG A 1 3870 ? 220.462 257.015 210.522 1.00 37.93  ? 3870 ARG A C     1 
ATOM   17000 O  O     . ARG A 1 3870 ? 219.959 256.095 211.177 1.00 36.68  ? 3870 ARG A O     1 
ATOM   17001 C  CB    . ARG A 1 3870 ? 219.004 258.341 208.977 1.00 29.87  ? 3870 ARG A CB    1 
ATOM   17002 C  CG    . ARG A 1 3870 ? 218.060 259.510 208.791 1.00 33.23  ? 3870 ARG A CG    1 
ATOM   17003 C  CD    . ARG A 1 3870 ? 216.796 259.077 208.082 1.00 37.09  ? 3870 ARG A CD    1 
ATOM   17004 N  NE    . ARG A 1 3870 ? 215.919 260.203 207.793 1.00 43.45  ? 3870 ARG A NE    1 
ATOM   17005 C  CZ    . ARG A 1 3870 ? 214.741 260.094 207.195 1.00 45.94  ? 3870 ARG A CZ    1 
ATOM   17006 N  NH1   . ARG A 1 3870 ? 214.273 258.923 206.800 1.00 45.64  ? 3870 ARG A NH1   1 
ATOM   17007 N  NH2   . ARG A 1 3870 ? 214.013 261.187 206.993 1.00 40.14  ? 3870 ARG A NH2   1 
ATOM   17008 N  N     . VAL A 1 3871 ? 221.662 256.904 209.951 1.00 39.06  ? 3871 VAL A N     1 
ATOM   17009 C  CA    . VAL A 1 3871 ? 222.387 255.638 210.004 1.00 27.65  ? 3871 VAL A CA    1 
ATOM   17010 C  C     . VAL A 1 3871 ? 222.971 255.408 211.392 1.00 38.06  ? 3871 VAL A C     1 
ATOM   17011 O  O     . VAL A 1 3871 ? 222.888 254.304 211.940 1.00 43.98  ? 3871 VAL A O     1 
ATOM   17012 C  CB    . VAL A 1 3871 ? 223.475 255.602 208.919 1.00 25.92  ? 3871 VAL A CB    1 
ATOM   17013 C  CG1   . VAL A 1 3871 ? 224.438 254.464 209.171 1.00 28.67  ? 3871 VAL A CG1   1 
ATOM   17014 C  CG2   . VAL A 1 3871 ? 222.843 255.470 207.560 1.00 31.09  ? 3871 VAL A CG2   1 
ATOM   17015 N  N     . ALA A 1 3872 ? 223.567 256.445 211.984 1.00 34.99  ? 3872 ALA A N     1 
ATOM   17016 C  CA    . ALA A 1 3872 ? 224.241 256.275 213.266 1.00 25.16  ? 3872 ALA A CA    1 
ATOM   17017 C  C     . ALA A 1 3872 ? 223.270 256.039 214.412 1.00 34.23  ? 3872 ALA A C     1 
ATOM   17018 O  O     . ALA A 1 3872 ? 223.699 255.613 215.489 1.00 46.42  ? 3872 ALA A O     1 
ATOM   17019 C  CB    . ALA A 1 3872 ? 225.114 257.489 213.576 1.00 27.45  ? 3872 ALA A CB    1 
ATOM   17020 N  N     . ARG A 1 3873 ? 221.979 256.312 214.217 1.00 39.50  ? 3873 ARG A N     1 
ATOM   17021 C  CA    . ARG A 1 3873 ? 221.008 256.021 215.264 1.00 36.17  ? 3873 ARG A CA    1 
ATOM   17022 C  C     . ARG A 1 3873 ? 220.832 254.522 215.457 1.00 33.81  ? 3873 ARG A C     1 
ATOM   17023 O  O     . ARG A 1 3873 ? 220.461 254.077 216.547 1.00 38.85  ? 3873 ARG A O     1 
ATOM   17024 C  CB    . ARG A 1 3873 ? 219.667 256.674 214.938 1.00 43.53  ? 3873 ARG A CB    1 
ATOM   17025 C  CG    . ARG A 1 3873 ? 219.515 258.084 215.474 1.00 42.77  ? 3873 ARG A CG    1 
ATOM   17026 C  CD    . ARG A 1 3873 ? 219.914 258.171 216.936 1.00 46.03  ? 3873 ARG A CD    1 
ATOM   17027 N  NE    . ARG A 1 3873 ? 219.676 259.501 217.484 1.00 47.04  ? 3873 ARG A NE    1 
ATOM   17028 C  CZ    . ARG A 1 3873 ? 220.184 259.945 218.625 1.00 50.94  ? 3873 ARG A CZ    1 
ATOM   17029 N  NH1   . ARG A 1 3873 ? 220.968 259.187 219.374 1.00 44.04  ? 3873 ARG A NH1   1 
ATOM   17030 N  NH2   . ARG A 1 3873 ? 219.899 261.180 219.026 1.00 44.43  ? 3873 ARG A NH2   1 
ATOM   17031 N  N     . GLY A 1 3874 ? 221.090 253.735 214.417 1.00 32.81  ? 3874 GLY A N     1 
ATOM   17032 C  CA    . GLY A 1 3874 ? 221.012 252.294 214.515 1.00 32.19  ? 3874 GLY A CA    1 
ATOM   17033 C  C     . GLY A 1 3874 ? 222.376 251.640 214.508 1.00 36.79  ? 3874 GLY A C     1 
ATOM   17034 O  O     . GLY A 1 3874 ? 222.562 250.577 213.910 1.00 47.43  ? 3874 GLY A O     1 
ATOM   17035 N  N     . MET A 1 3875 ? 223.340 252.272 215.172 1.00 33.73  ? 3875 MET A N     1 
ATOM   17036 C  CA    . MET A 1 3875 ? 224.695 251.754 215.265 1.00 27.51  ? 3875 MET A CA    1 
ATOM   17037 C  C     . MET A 1 3875 ? 225.178 251.885 216.700 1.00 34.79  ? 3875 MET A C     1 
ATOM   17038 O  O     . MET A 1 3875 ? 224.729 252.760 217.443 1.00 42.23  ? 3875 MET A O     1 
ATOM   17039 C  CB    . MET A 1 3875 ? 225.652 252.503 214.328 1.00 25.95  ? 3875 MET A CB    1 
ATOM   17040 C  CG    . MET A 1 3875 ? 225.374 252.298 212.853 1.00 40.42  ? 3875 MET A CG    1 
ATOM   17041 S  SD    . MET A 1 3875 ? 226.466 253.261 211.794 1.00 45.14  ? 3875 MET A SD    1 
ATOM   17042 C  CE    . MET A 1 3875 ? 228.016 252.413 212.032 1.00 36.45  ? 3875 MET A CE    1 
ATOM   17043 N  N     . LEU A 1 3876 ? 226.095 251.003 217.087 1.00 36.08  ? 3876 LEU A N     1 
ATOM   17044 C  CA    . LEU A 1 3876 ? 226.757 251.143 218.374 1.00 31.81  ? 3876 LEU A CA    1 
ATOM   17045 C  C     . LEU A 1 3876 ? 227.669 252.363 218.355 1.00 37.97  ? 3876 LEU A C     1 
ATOM   17046 O  O     . LEU A 1 3876 ? 228.237 252.722 217.322 1.00 51.06  ? 3876 LEU A O     1 
ATOM   17047 C  CB    . LEU A 1 3876 ? 227.557 249.885 218.708 1.00 32.32  ? 3876 LEU A CB    1 
ATOM   17048 C  CG    . LEU A 1 3876 ? 226.781 248.567 218.709 1.00 35.11  ? 3876 LEU A CG    1 
ATOM   17049 C  CD1   . LEU A 1 3876 ? 227.734 247.390 218.728 1.00 40.62  ? 3876 LEU A CD1   1 
ATOM   17050 C  CD2   . LEU A 1 3876 ? 225.834 248.504 219.891 1.00 34.67  ? 3876 LEU A CD2   1 
ATOM   17051 N  N     . HIS A 1 3877 ? 227.799 253.009 219.517 1.00 32.03  ? 3877 HIS A N     1 
ATOM   17052 C  CA    . HIS A 1 3877 ? 228.525 254.274 219.578 1.00 30.34  ? 3877 HIS A CA    1 
ATOM   17053 C  C     . HIS A 1 3877 ? 229.984 254.115 219.172 1.00 37.17  ? 3877 HIS A C     1 
ATOM   17054 O  O     . HIS A 1 3877 ? 230.601 255.074 218.694 1.00 42.11  ? 3877 HIS A O     1 
ATOM   17055 C  CB    . HIS A 1 3877 ? 228.433 254.873 220.979 1.00 29.44  ? 3877 HIS A CB    1 
ATOM   17056 C  CG    . HIS A 1 3877 ? 228.877 256.299 221.051 1.00 34.49  ? 3877 HIS A CG    1 
ATOM   17057 N  ND1   . HIS A 1 3877 ? 230.181 256.661 221.309 1.00 36.78  ? 3877 HIS A ND1   1 
ATOM   17058 C  CD2   . HIS A 1 3877 ? 228.193 257.455 220.886 1.00 33.64  ? 3877 HIS A CD2   1 
ATOM   17059 C  CE1   . HIS A 1 3877 ? 230.280 257.977 221.306 1.00 39.42  ? 3877 HIS A CE1   1 
ATOM   17060 N  NE2   . HIS A 1 3877 ? 229.088 258.483 221.051 1.00 44.07  ? 3877 HIS A NE2   1 
ATOM   17061 N  N     . GLN A 1 3878 ? 230.554 252.925 219.353 1.00 37.14  ? 3878 GLN A N     1 
ATOM   17062 C  CA    . GLN A 1 3878 ? 231.930 252.696 218.933 1.00 36.47  ? 3878 GLN A CA    1 
ATOM   17063 C  C     . GLN A 1 3878 ? 232.085 252.721 217.419 1.00 44.80  ? 3878 GLN A C     1 
ATOM   17064 O  O     . GLN A 1 3878 ? 233.212 252.841 216.927 1.00 53.98  ? 3878 GLN A O     1 
ATOM   17065 C  CB    . GLN A 1 3878 ? 232.431 251.363 219.486 1.00 36.37  ? 3878 GLN A CB    1 
ATOM   17066 C  CG    . GLN A 1 3878 ? 231.650 250.161 218.996 1.00 38.93  ? 3878 GLN A CG    1 
ATOM   17067 C  CD    . GLN A 1 3878 ? 232.118 248.870 219.629 1.00 43.06  ? 3878 GLN A CD    1 
ATOM   17068 O  OE1   . GLN A 1 3878 ? 233.076 248.856 220.399 1.00 44.42  ? 3878 GLN A OE1   1 
ATOM   17069 N  NE2   . GLN A 1 3878 ? 231.442 247.775 219.308 1.00 44.98  ? 3878 GLN A NE2   1 
ATOM   17070 N  N     . ASP A 1 3879 ? 230.989 252.608 216.673 1.00 37.42  ? 3879 ASP A N     1 
ATOM   17071 C  CA    . ASP A 1 3879 ? 231.032 252.593 215.218 1.00 28.77  ? 3879 ASP A CA    1 
ATOM   17072 C  C     . ASP A 1 3879 ? 230.599 253.909 214.586 1.00 35.90  ? 3879 ASP A C     1 
ATOM   17073 O  O     . ASP A 1 3879 ? 230.598 254.014 213.357 1.00 46.49  ? 3879 ASP A O     1 
ATOM   17074 C  CB    . ASP A 1 3879 ? 230.158 251.458 214.681 1.00 28.87  ? 3879 ASP A CB    1 
ATOM   17075 C  CG    . ASP A 1 3879 ? 230.627 250.095 215.137 1.00 43.70  ? 3879 ASP A CG    1 
ATOM   17076 O  OD1   . ASP A 1 3879 ? 231.851 249.908 215.282 1.00 47.28  ? 3879 ASP A OD1   1 
ATOM   17077 O  OD2   . ASP A 1 3879 ? 229.774 249.209 215.343 1.00 47.66  ? 3879 ASP A OD2   1 
ATOM   17078 N  N     . HIS A 1 3880 ? 230.224 254.909 215.387 1.00 39.55  ? 3880 HIS A N     1 
ATOM   17079 C  CA    . HIS A 1 3880 ? 229.865 256.208 214.824 1.00 30.11  ? 3880 HIS A CA    1 
ATOM   17080 C  C     . HIS A 1 3880 ? 231.063 256.863 214.150 1.00 34.25  ? 3880 HIS A C     1 
ATOM   17081 O  O     . HIS A 1 3880 ? 230.935 257.456 213.072 1.00 44.17  ? 3880 HIS A O     1 
ATOM   17082 C  CB    . HIS A 1 3880 ? 229.314 257.120 215.919 1.00 27.69  ? 3880 HIS A CB    1 
ATOM   17083 C  CG    . HIS A 1 3880 ? 227.964 256.718 216.423 1.00 27.16  ? 3880 HIS A CG    1 
ATOM   17084 N  ND1   . HIS A 1 3880 ? 227.242 257.491 217.306 1.00 37.33  ? 3880 HIS A ND1   1 
ATOM   17085 C  CD2   . HIS A 1 3880 ? 227.205 255.626 216.173 1.00 28.31  ? 3880 HIS A CD2   1 
ATOM   17086 C  CE1   . HIS A 1 3880 ? 226.097 256.892 217.578 1.00 38.31  ? 3880 HIS A CE1   1 
ATOM   17087 N  NE2   . HIS A 1 3880 ? 226.049 255.759 216.902 1.00 35.28  ? 3880 HIS A NE2   1 
ATOM   17088 N  N     . ILE A 1 3881 ? 232.237 256.765 214.776 1.00 40.49  ? 3881 ILE A N     1 
ATOM   17089 C  CA    . ILE A 1 3881 ? 233.421 257.439 214.258 1.00 37.72  ? 3881 ILE A CA    1 
ATOM   17090 C  C     . ILE A 1 3881 ? 233.871 256.823 212.941 1.00 39.27  ? 3881 ILE A C     1 
ATOM   17091 O  O     . ILE A 1 3881 ? 234.363 257.534 212.062 1.00 44.32  ? 3881 ILE A O     1 
ATOM   17092 C  CB    . ILE A 1 3881 ? 234.545 257.430 215.311 1.00 42.22  ? 3881 ILE A CB    1 
ATOM   17093 C  CG1   . ILE A 1 3881 ? 235.760 258.206 214.803 1.00 36.31  ? 3881 ILE A CG1   1 
ATOM   17094 C  CG2   . ILE A 1 3881 ? 234.919 256.008 215.696 1.00 43.11  ? 3881 ILE A CG2   1 
ATOM   17095 C  CD1   . ILE A 1 3881 ? 235.442 259.619 214.377 1.00 31.42  ? 3881 ILE A CD1   1 
ATOM   17096 N  N     . THR A 1 3882 ? 233.717 255.509 212.771 1.00 33.77  ? 3882 THR A N     1 
ATOM   17097 C  CA    . THR A 1 3882 ? 234.088 254.885 211.504 1.00 30.21  ? 3882 THR A CA    1 
ATOM   17098 C  C     . THR A 1 3882 ? 233.238 255.416 210.355 1.00 38.14  ? 3882 THR A C     1 
ATOM   17099 O  O     . THR A 1 3882 ? 233.764 255.796 209.299 1.00 54.54  ? 3882 THR A O     1 
ATOM   17100 C  CB    . THR A 1 3882 ? 233.951 253.367 211.612 1.00 33.75  ? 3882 THR A CB    1 
ATOM   17101 O  OG1   . THR A 1 3882 ? 234.714 252.895 212.728 1.00 49.38  ? 3882 THR A OG1   1 
ATOM   17102 C  CG2   . THR A 1 3882 ? 234.448 252.694 210.348 1.00 36.19  ? 3882 THR A CG2   1 
ATOM   17103 N  N     . PHE A 1 3883 ? 231.919 255.453 210.547 1.00 29.03  ? 3883 PHE A N     1 
ATOM   17104 C  CA    . PHE A 1 3883 ? 231.037 255.973 209.511 1.00 27.75  ? 3883 PHE A CA    1 
ATOM   17105 C  C     . PHE A 1 3883 ? 231.307 257.448 209.249 1.00 34.70  ? 3883 PHE A C     1 
ATOM   17106 O  O     . PHE A 1 3883 ? 231.286 257.891 208.096 1.00 49.35  ? 3883 PHE A O     1 
ATOM   17107 C  CB    . PHE A 1 3883 ? 229.577 255.753 209.903 1.00 24.22  ? 3883 PHE A CB    1 
ATOM   17108 C  CG    . PHE A 1 3883 ? 228.607 256.016 208.791 1.00 29.04  ? 3883 PHE A CG    1 
ATOM   17109 C  CD1   . PHE A 1 3883 ? 228.841 255.520 207.522 1.00 31.33  ? 3883 PHE A CD1   1 
ATOM   17110 C  CD2   . PHE A 1 3883 ? 227.466 256.762 209.012 1.00 30.00  ? 3883 PHE A CD2   1 
ATOM   17111 C  CE1   . PHE A 1 3883 ? 227.954 255.761 206.496 1.00 29.90  ? 3883 PHE A CE1   1 
ATOM   17112 C  CE2   . PHE A 1 3883 ? 226.577 257.006 207.989 1.00 29.68  ? 3883 PHE A CE2   1 
ATOM   17113 C  CZ    . PHE A 1 3883 ? 226.820 256.504 206.730 1.00 29.04  ? 3883 PHE A CZ    1 
ATOM   17114 N  N     . ALA A 1 3884 ? 231.562 258.225 210.305 1.00 35.50  ? 3884 ALA A N     1 
ATOM   17115 C  CA    . ALA A 1 3884 ? 231.879 259.636 210.113 1.00 32.10  ? 3884 ALA A CA    1 
ATOM   17116 C  C     . ALA A 1 3884 ? 233.184 259.825 209.352 1.00 28.40  ? 3884 ALA A C     1 
ATOM   17117 O  O     . ALA A 1 3884 ? 233.278 260.711 208.499 1.00 38.21  ? 3884 ALA A O     1 
ATOM   17118 C  CB    . ALA A 1 3884 ? 231.941 260.351 211.459 1.00 34.19  ? 3884 ALA A CB    1 
ATOM   17119 N  N     . MET A 1 3885 ? 234.196 259.006 209.641 1.00 24.69  ? 3885 MET A N     1 
ATOM   17120 C  CA    . MET A 1 3885 ? 235.459 259.090 208.916 1.00 30.69  ? 3885 MET A CA    1 
ATOM   17121 C  C     . MET A 1 3885 ? 235.268 258.766 207.442 1.00 40.13  ? 3885 MET A C     1 
ATOM   17122 O  O     . MET A 1 3885 ? 235.831 259.442 206.573 1.00 52.90  ? 3885 MET A O     1 
ATOM   17123 C  CB    . MET A 1 3885 ? 236.485 258.142 209.537 1.00 30.10  ? 3885 MET A CB    1 
ATOM   17124 C  CG    . MET A 1 3885 ? 237.082 258.627 210.844 1.00 37.95  ? 3885 MET A CG    1 
ATOM   17125 S  SD    . MET A 1 3885 ? 238.406 259.824 210.634 1.00 56.81  ? 3885 MET A SD    1 
ATOM   17126 C  CE    . MET A 1 3885 ? 239.467 258.963 209.482 1.00 40.57  ? 3885 MET A CE    1 
ATOM   17127 N  N     . LEU A 1 3886 ? 234.479 257.735 207.139 1.00 40.27  ? 3886 LEU A N     1 
ATOM   17128 C  CA    . LEU A 1 3886 ? 234.270 257.393 205.735 1.00 34.87  ? 3886 LEU A CA    1 
ATOM   17129 C  C     . LEU A 1 3886 ? 233.424 258.436 205.014 1.00 29.87  ? 3886 LEU A C     1 
ATOM   17130 O  O     . LEU A 1 3886 ? 233.666 258.715 203.835 1.00 46.08  ? 3886 LEU A O     1 
ATOM   17131 C  CB    . LEU A 1 3886 ? 233.649 256.007 205.611 1.00 32.85  ? 3886 LEU A CB    1 
ATOM   17132 C  CG    . LEU A 1 3886 ? 234.632 254.898 205.983 1.00 36.20  ? 3886 LEU A CG    1 
ATOM   17133 C  CD1   . LEU A 1 3886 ? 234.045 253.560 205.649 1.00 33.57  ? 3886 LEU A CD1   1 
ATOM   17134 C  CD2   . LEU A 1 3886 ? 235.962 255.090 205.273 1.00 41.53  ? 3886 LEU A CD2   1 
ATOM   17135 N  N     . LEU A 1 3887 ? 232.444 259.032 205.696 1.00 27.04  ? 3887 LEU A N     1 
ATOM   17136 C  CA    . LEU A 1 3887 ? 231.712 260.146 205.101 1.00 31.59  ? 3887 LEU A CA    1 
ATOM   17137 C  C     . LEU A 1 3887 ? 232.627 261.336 204.844 1.00 33.11  ? 3887 LEU A C     1 
ATOM   17138 O  O     . LEU A 1 3887 ? 232.501 262.009 203.813 1.00 45.13  ? 3887 LEU A O     1 
ATOM   17139 C  CB    . LEU A 1 3887 ? 230.551 260.559 206.004 1.00 34.24  ? 3887 LEU A CB    1 
ATOM   17140 C  CG    . LEU A 1 3887 ? 229.355 259.614 206.093 1.00 27.96  ? 3887 LEU A CG    1 
ATOM   17141 C  CD1   . LEU A 1 3887 ? 228.278 260.220 206.970 1.00 28.21  ? 3887 LEU A CD1   1 
ATOM   17142 C  CD2   . LEU A 1 3887 ? 228.812 259.302 204.714 1.00 35.52  ? 3887 LEU A CD2   1 
ATOM   17143 N  N     . ALA A 1 3888 ? 233.546 261.612 205.770 1.00 35.23  ? 3888 ALA A N     1 
ATOM   17144 C  CA    . ALA A 1 3888 ? 234.510 262.685 205.565 1.00 37.78  ? 3888 ALA A CA    1 
ATOM   17145 C  C     . ALA A 1 3888 ? 235.398 262.402 204.363 1.00 35.44  ? 3888 ALA A C     1 
ATOM   17146 O  O     . ALA A 1 3888 ? 235.701 263.310 203.585 1.00 42.12  ? 3888 ALA A O     1 
ATOM   17147 C  CB    . ALA A 1 3888 ? 235.353 262.878 206.825 1.00 33.57  ? 3888 ALA A CB    1 
ATOM   17148 N  N     . ARG A 1 3889 ? 235.825 261.149 204.196 1.00 37.14  ? 3889 ARG A N     1 
ATOM   17149 C  CA    . ARG A 1 3889 ? 236.605 260.783 203.016 1.00 37.31  ? 3889 ARG A CA    1 
ATOM   17150 C  C     . ARG A 1 3889 ? 235.798 260.963 201.735 1.00 39.12  ? 3889 ARG A C     1 
ATOM   17151 O  O     . ARG A 1 3889 ? 236.322 261.454 200.726 1.00 44.25  ? 3889 ARG A O     1 
ATOM   17152 C  CB    . ARG A 1 3889 ? 237.098 259.343 203.139 1.00 42.36  ? 3889 ARG A CB    1 
ATOM   17153 C  CG    . ARG A 1 3889 ? 238.126 259.129 204.229 1.00 46.43  ? 3889 ARG A CG    1 
ATOM   17154 C  CD    . ARG A 1 3889 ? 238.980 257.912 203.934 1.00 45.45  ? 3889 ARG A CD    1 
ATOM   17155 N  NE    . ARG A 1 3889 ? 239.631 258.011 202.635 1.00 47.03  ? 3889 ARG A NE    1 
ATOM   17156 C  CZ    . ARG A 1 3889 ? 240.346 257.042 202.080 1.00 49.86  ? 3889 ARG A CZ    1 
ATOM   17157 N  NH1   . ARG A 1 3889 ? 240.518 255.878 202.684 1.00 46.45  ? 3889 ARG A NH1   1 
ATOM   17158 N  NH2   . ARG A 1 3889 ? 240.903 257.246 200.891 1.00 45.95  ? 3889 ARG A NH2   1 
ATOM   17159 N  N     . ILE A 1 3890 ? 234.523 260.565 201.754 1.00 42.67  ? 3890 ILE A N     1 
ATOM   17160 C  CA    . ILE A 1 3890 ? 233.664 260.743 200.586 1.00 38.75  ? 3890 ILE A CA    1 
ATOM   17161 C  C     . ILE A 1 3890 ? 233.565 262.216 200.217 1.00 42.22  ? 3890 ILE A C     1 
ATOM   17162 O  O     . ILE A 1 3890 ? 233.686 262.587 199.043 1.00 49.08  ? 3890 ILE A O     1 
ATOM   17163 C  CB    . ILE A 1 3890 ? 232.272 260.136 200.843 1.00 35.55  ? 3890 ILE A CB    1 
ATOM   17164 C  CG1   . ILE A 1 3890 ? 232.345 258.613 200.892 1.00 40.77  ? 3890 ILE A CG1   1 
ATOM   17165 C  CG2   . ILE A 1 3890 ? 231.287 260.580 199.778 1.00 34.49  ? 3890 ILE A CG2   1 
ATOM   17166 C  CD1   . ILE A 1 3890 ? 231.078 257.975 201.389 1.00 33.54  ? 3890 ILE A CD1   1 
ATOM   17167 N  N     . LYS A 1 3891 ? 233.341 263.080 201.210 1.00 45.20  ? 3891 LYS A N     1 
ATOM   17168 C  CA    . LYS A 1 3891 ? 233.269 264.511 200.927 1.00 39.76  ? 3891 LYS A CA    1 
ATOM   17169 C  C     . LYS A 1 3891 ? 234.611 265.048 200.447 1.00 47.71  ? 3891 LYS A C     1 
ATOM   17170 O  O     . LYS A 1 3891 ? 234.659 265.932 199.585 1.00 53.93  ? 3891 LYS A O     1 
ATOM   17171 C  CB    . LYS A 1 3891 ? 232.799 265.280 202.159 1.00 35.22  ? 3891 LYS A CB    1 
ATOM   17172 C  CG    . LYS A 1 3891 ? 232.326 266.684 201.833 1.00 41.55  ? 3891 LYS A CG    1 
ATOM   17173 C  CD    . LYS A 1 3891 ? 231.890 267.437 203.070 1.00 46.72  ? 3891 LYS A CD    1 
ATOM   17174 C  CE    . LYS A 1 3891 ? 231.146 268.710 202.705 1.00 51.61  ? 3891 LYS A CE    1 
ATOM   17175 N  NZ    . LYS A 1 3891 ? 229.988 268.440 201.809 1.00 47.83  ? 3891 LYS A NZ    1 
ATOM   17176 N  N     . LEU A 1 3892 ? 235.710 264.533 201.001 1.00 50.35  ? 3892 LEU A N     1 
ATOM   17177 C  CA    . LEU A 1 3892 ? 237.039 264.970 200.590 1.00 48.09  ? 3892 LEU A CA    1 
ATOM   17178 C  C     . LEU A 1 3892 ? 237.284 264.671 199.118 1.00 56.21  ? 3892 LEU A C     1 
ATOM   17179 O  O     . LEU A 1 3892 ? 237.838 265.505 198.392 1.00 56.12  ? 3892 LEU A O     1 
ATOM   17180 C  CB    . LEU A 1 3892 ? 238.093 264.290 201.467 1.00 50.57  ? 3892 LEU A CB    1 
ATOM   17181 C  CG    . LEU A 1 3892 ? 239.569 264.681 201.385 1.00 51.73  ? 3892 LEU A CG    1 
ATOM   17182 C  CD1   . LEU A 1 3892 ? 240.232 264.388 202.712 1.00 49.53  ? 3892 LEU A CD1   1 
ATOM   17183 C  CD2   . LEU A 1 3892 ? 240.285 263.931 200.278 1.00 56.71  ? 3892 LEU A CD2   1 
ATOM   17184 N  N     . LYS A 1 3893 ? 236.887 263.481 198.658 1.00 55.12  ? 3893 LYS A N     1 
ATOM   17185 C  CA    . LYS A 1 3893 ? 237.036 263.168 197.240 1.00 51.80  ? 3893 LYS A CA    1 
ATOM   17186 C  C     . LYS A 1 3893 ? 236.172 264.071 196.370 1.00 59.44  ? 3893 LYS A C     1 
ATOM   17187 O  O     . LYS A 1 3893 ? 236.539 264.362 195.226 1.00 63.77  ? 3893 LYS A O     1 
ATOM   17188 C  CB    . LYS A 1 3893 ? 236.697 261.703 196.975 1.00 52.06  ? 3893 LYS A CB    1 
ATOM   17189 C  CG    . LYS A 1 3893 ? 237.700 260.720 197.544 1.00 57.38  ? 3893 LYS A CG    1 
ATOM   17190 C  CD    . LYS A 1 3893 ? 237.223 259.292 197.360 1.00 59.34  ? 3893 LYS A CD    1 
ATOM   17191 C  CE    . LYS A 1 3893 ? 237.278 258.885 195.896 1.00 57.28  ? 3893 LYS A CE    1 
ATOM   17192 N  NZ    . LYS A 1 3893 ? 236.925 257.452 195.697 1.00 62.66  ? 3893 LYS A NZ    1 
ATOM   17193 N  N     . GLY A 1 3894 ? 235.032 264.522 196.885 1.00 65.28  ? 3894 GLY A N     1 
ATOM   17194 C  CA    . GLY A 1 3894 ? 234.134 265.373 196.134 1.00 65.00  ? 3894 GLY A CA    1 
ATOM   17195 C  C     . GLY A 1 3894 ? 234.496 266.837 196.094 1.00 67.41  ? 3894 GLY A C     1 
ATOM   17196 O  O     . GLY A 1 3894 ? 233.795 267.618 195.446 1.00 70.12  ? 3894 GLY A O     1 
ATOM   17197 N  N     . THR A 1 3895 ? 235.571 267.238 196.765 1.00 68.57  ? 3895 THR A N     1 
ATOM   17198 C  CA    . THR A 1 3895 ? 236.020 268.623 196.778 1.00 72.91  ? 3895 THR A CA    1 
ATOM   17199 C  C     . THR A 1 3895 ? 237.061 268.827 195.685 1.00 71.59  ? 3895 THR A C     1 
ATOM   17200 O  O     . THR A 1 3895 ? 238.065 268.109 195.636 1.00 66.57  ? 3895 THR A O     1 
ATOM   17201 C  CB    . THR A 1 3895 ? 236.601 269.000 198.141 1.00 73.04  ? 3895 THR A CB    1 
ATOM   17202 O  OG1   . THR A 1 3895 ? 235.599 268.835 199.151 1.00 67.42  ? 3895 THR A OG1   1 
ATOM   17203 C  CG2   . THR A 1 3895 ? 237.070 270.443 198.137 1.00 69.35  ? 3895 THR A CG2   1 
ATOM   17204 N  N     . VAL A 1 3896 ? 236.813 269.804 194.810 1.00 79.69  ? 3896 VAL A N     1 
ATOM   17205 C  CA    . VAL A 1 3896 ? 237.708 270.038 193.681 1.00 81.25  ? 3896 VAL A CA    1 
ATOM   17206 C  C     . VAL A 1 3896 ? 239.035 270.618 194.153 1.00 79.85  ? 3896 VAL A C     1 
ATOM   17207 O  O     . VAL A 1 3896 ? 240.104 270.239 193.659 1.00 77.60  ? 3896 VAL A O     1 
ATOM   17208 C  CB    . VAL A 1 3896 ? 237.027 270.950 192.645 1.00 81.33  ? 3896 VAL A CB    1 
ATOM   17209 C  CG1   . VAL A 1 3896 ? 237.859 271.026 191.375 1.00 79.41  ? 3896 VAL A CG1   1 
ATOM   17210 C  CG2   . VAL A 1 3896 ? 235.623 270.451 192.341 1.00 77.61  ? 3896 VAL A CG2   1 
ATOM   17211 N  N     . GLY A 1 3897 ? 238.993 271.543 195.107 1.00 76.38  ? 3897 GLY A N     1 
ATOM   17212 C  CA    . GLY A 1 3897 ? 240.202 272.194 195.571 1.00 75.87  ? 3897 GLY A CA    1 
ATOM   17213 C  C     . GLY A 1 3897 ? 240.917 271.453 196.681 1.00 79.42  ? 3897 GLY A C     1 
ATOM   17214 O  O     . GLY A 1 3897 ? 241.370 272.069 197.650 1.00 79.04  ? 3897 GLY A O     1 
ATOM   17215 N  N     . GLU A 1 3898 ? 241.028 270.130 196.554 1.00 75.04  ? 3898 GLU A N     1 
ATOM   17216 C  CA    . GLU A 1 3898 ? 241.701 269.311 197.548 1.00 70.27  ? 3898 GLU A CA    1 
ATOM   17217 C  C     . GLU A 1 3898 ? 242.551 268.255 196.856 1.00 69.14  ? 3898 GLU A C     1 
ATOM   17218 O  O     . GLU A 1 3898 ? 242.148 267.718 195.813 1.00 69.83  ? 3898 GLU A O     1 
ATOM   17219 C  CB    . GLU A 1 3898 ? 240.699 268.622 198.484 1.00 68.63  ? 3898 GLU A CB    1 
ATOM   17220 C  CG    . GLU A 1 3898 ? 240.241 269.476 199.651 1.00 68.31  ? 3898 GLU A CG    1 
ATOM   17221 C  CD    . GLU A 1 3898 ? 241.380 269.888 200.556 1.00 71.94  ? 3898 GLU A CD    1 
ATOM   17222 O  OE1   . GLU A 1 3898 ? 242.189 269.016 200.935 1.00 71.64  ? 3898 GLU A OE1   1 
ATOM   17223 O  OE2   . GLU A 1 3898 ? 241.465 271.087 200.890 1.00 72.35  ? 3898 GLU A OE2   1 
ATOM   17224 N  N     . PRO A 1 3899 ? 243.720 267.937 197.405 1.00 67.98  ? 3899 PRO A N     1 
ATOM   17225 C  CA    . PRO A 1 3899 ? 244.496 266.808 196.885 1.00 62.94  ? 3899 PRO A CA    1 
ATOM   17226 C  C     . PRO A 1 3899 ? 243.815 265.486 197.198 1.00 66.72  ? 3899 PRO A C     1 
ATOM   17227 O  O     . PRO A 1 3899 ? 242.891 265.403 198.010 1.00 72.26  ? 3899 PRO A O     1 
ATOM   17228 C  CB    . PRO A 1 3899 ? 245.838 266.927 197.614 1.00 61.64  ? 3899 PRO A CB    1 
ATOM   17229 C  CG    . PRO A 1 3899 ? 245.892 268.340 198.098 1.00 65.58  ? 3899 PRO A CG    1 
ATOM   17230 C  CD    . PRO A 1 3899 ? 244.478 268.720 198.393 1.00 67.21  ? 3899 PRO A CD    1 
ATOM   17231 N  N     . THR A 1 3900 ? 244.283 264.436 196.522 1.00 64.03  ? 3900 THR A N     1 
ATOM   17232 C  CA    . THR A 1 3900 ? 243.704 263.112 196.729 1.00 65.35  ? 3900 THR A CA    1 
ATOM   17233 C  C     . THR A 1 3900 ? 244.031 262.571 198.116 1.00 66.46  ? 3900 THR A C     1 
ATOM   17234 O  O     . THR A 1 3900 ? 243.184 261.934 198.753 1.00 64.17  ? 3900 THR A O     1 
ATOM   17235 C  CB    . THR A 1 3900 ? 244.195 262.147 195.650 1.00 65.92  ? 3900 THR A CB    1 
ATOM   17236 O  OG1   . THR A 1 3900 ? 245.567 261.814 195.891 1.00 70.32  ? 3900 THR A OG1   1 
ATOM   17237 C  CG2   . THR A 1 3900 ? 244.066 262.781 194.275 1.00 65.79  ? 3900 THR A CG2   1 
ATOM   17238 N  N     . TYR A 1 3901 ? 245.252 262.818 198.598 1.00 65.14  ? 3901 TYR A N     1 
ATOM   17239 C  CA    . TYR A 1 3901 ? 245.730 262.297 199.881 1.00 63.09  ? 3901 TYR A CA    1 
ATOM   17240 C  C     . TYR A 1 3901 ? 245.645 260.775 199.937 1.00 63.31  ? 3901 TYR A C     1 
ATOM   17241 O  O     . TYR A 1 3901 ? 245.333 260.198 200.980 1.00 65.12  ? 3901 TYR A O     1 
ATOM   17242 C  CB    . TYR A 1 3901 ? 244.971 262.918 201.058 1.00 56.18  ? 3901 TYR A CB    1 
ATOM   17243 C  CG    . TYR A 1 3901 ? 245.200 264.402 201.208 1.00 59.61  ? 3901 TYR A CG    1 
ATOM   17244 C  CD1   . TYR A 1 3901 ? 246.483 264.916 201.309 1.00 62.58  ? 3901 TYR A CD1   1 
ATOM   17245 C  CD2   . TYR A 1 3901 ? 244.134 265.289 201.241 1.00 59.23  ? 3901 TYR A CD2   1 
ATOM   17246 C  CE1   . TYR A 1 3901 ? 246.699 266.269 201.439 1.00 61.18  ? 3901 TYR A CE1   1 
ATOM   17247 C  CE2   . TYR A 1 3901 ? 244.339 266.644 201.376 1.00 58.68  ? 3901 TYR A CE2   1 
ATOM   17248 C  CZ    . TYR A 1 3901 ? 245.624 267.129 201.472 1.00 63.94  ? 3901 TYR A CZ    1 
ATOM   17249 O  OH    . TYR A 1 3901 ? 245.838 268.480 201.602 1.00 68.19  ? 3901 TYR A OH    1 
ATOM   17250 N  N     . ASP A 1 3902 ? 245.924 260.115 198.811 1.00 64.07  ? 3902 ASP A N     1 
ATOM   17251 C  CA    . ASP A 1 3902 ? 245.815 258.661 198.763 1.00 64.96  ? 3902 ASP A CA    1 
ATOM   17252 C  C     . ASP A 1 3902 ? 246.958 257.989 199.512 1.00 61.06  ? 3902 ASP A C     1 
ATOM   17253 O  O     . ASP A 1 3902 ? 246.750 256.973 200.182 1.00 60.47  ? 3902 ASP A O     1 
ATOM   17254 C  CB    . ASP A 1 3902 ? 245.770 258.186 197.312 1.00 68.37  ? 3902 ASP A CB    1 
ATOM   17255 C  CG    . ASP A 1 3902 ? 244.359 258.114 196.766 1.00 70.80  ? 3902 ASP A CG    1 
ATOM   17256 O  OD1   . ASP A 1 3902 ? 243.408 258.090 197.576 1.00 67.49  ? 3902 ASP A OD1   1 
ATOM   17257 O  OD2   . ASP A 1 3902 ? 244.199 258.080 195.528 1.00 69.88  ? 3902 ASP A OD2   1 
ATOM   17258 N  N     . ALA A 1 3903 ? 248.173 258.529 199.400 1.00 63.80  ? 3903 ALA A N     1 
ATOM   17259 C  CA    . ALA A 1 3903 ? 249.306 257.943 200.110 1.00 63.72  ? 3903 ALA A CA    1 
ATOM   17260 C  C     . ALA A 1 3903 ? 249.138 258.068 201.618 1.00 68.19  ? 3903 ALA A C     1 
ATOM   17261 O  O     . ALA A 1 3903 ? 249.419 257.122 202.366 1.00 68.65  ? 3903 ALA A O     1 
ATOM   17262 C  CB    . ALA A 1 3903 ? 250.607 258.604 199.658 1.00 63.04  ? 3903 ALA A CB    1 
ATOM   17263 N  N     . GLU A 1 3904 ? 248.678 259.233 202.083 1.00 65.87  ? 3904 GLU A N     1 
ATOM   17264 C  CA    . GLU A 1 3904 ? 248.491 259.441 203.513 1.00 54.77  ? 3904 GLU A CA    1 
ATOM   17265 C  C     . GLU A 1 3904 ? 247.473 258.465 204.085 1.00 56.37  ? 3904 GLU A C     1 
ATOM   17266 O  O     . GLU A 1 3904 ? 247.705 257.860 205.135 1.00 63.04  ? 3904 GLU A O     1 
ATOM   17267 C  CB    . GLU A 1 3904 ? 248.058 260.881 203.778 1.00 53.93  ? 3904 GLU A CB    1 
ATOM   17268 C  CG    . GLU A 1 3904 ? 249.205 261.869 203.869 1.00 56.56  ? 3904 GLU A CG    1 
ATOM   17269 C  CD    . GLU A 1 3904 ? 249.636 262.384 202.513 1.00 66.13  ? 3904 GLU A CD    1 
ATOM   17270 O  OE1   . GLU A 1 3904 ? 248.889 262.179 201.535 1.00 68.47  ? 3904 GLU A OE1   1 
ATOM   17271 O  OE2   . GLU A 1 3904 ? 250.721 262.994 202.424 1.00 64.81  ? 3904 GLU A OE2   1 
ATOM   17272 N  N     . PHE A 1 3905 ? 246.345 258.280 203.397 1.00 53.44  ? 3905 PHE A N     1 
ATOM   17273 C  CA    . PHE A 1 3905 ? 245.325 257.364 203.896 1.00 53.97  ? 3905 PHE A CA    1 
ATOM   17274 C  C     . PHE A 1 3905 ? 245.745 255.911 203.738 1.00 57.35  ? 3905 PHE A C     1 
ATOM   17275 O  O     . PHE A 1 3905 ? 245.380 255.068 204.565 1.00 61.40  ? 3905 PHE A O     1 
ATOM   17276 C  CB    . PHE A 1 3905 ? 244.004 257.621 203.182 1.00 53.30  ? 3905 PHE A CB    1 
ATOM   17277 C  CG    . PHE A 1 3905 ? 243.190 258.705 203.810 1.00 60.04  ? 3905 PHE A CG    1 
ATOM   17278 C  CD1   . PHE A 1 3905 ? 242.632 258.529 205.063 1.00 55.78  ? 3905 PHE A CD1   1 
ATOM   17279 C  CD2   . PHE A 1 3905 ? 242.999 259.909 203.159 1.00 58.42  ? 3905 PHE A CD2   1 
ATOM   17280 C  CE1   . PHE A 1 3905 ? 241.887 259.527 205.647 1.00 54.76  ? 3905 PHE A CE1   1 
ATOM   17281 C  CE2   . PHE A 1 3905 ? 242.255 260.909 203.738 1.00 57.31  ? 3905 PHE A CE2   1 
ATOM   17282 C  CZ    . PHE A 1 3905 ? 241.700 260.718 204.983 1.00 59.55  ? 3905 PHE A CZ    1 
ATOM   17283 N  N     . GLN A 1 3906 ? 246.507 255.600 202.689 1.00 63.89  ? 3906 GLN A N     1 
ATOM   17284 C  CA    . GLN A 1 3906 ? 247.040 254.253 202.531 1.00 59.80  ? 3906 GLN A CA    1 
ATOM   17285 C  C     . GLN A 1 3906 ? 247.960 253.895 203.688 1.00 60.25  ? 3906 GLN A C     1 
ATOM   17286 O  O     . GLN A 1 3906 ? 247.919 252.771 204.200 1.00 63.70  ? 3906 GLN A O     1 
ATOM   17287 C  CB    . GLN A 1 3906 ? 247.776 254.143 201.195 1.00 63.41  ? 3906 GLN A CB    1 
ATOM   17288 C  CG    . GLN A 1 3906 ? 247.820 252.747 200.604 1.00 64.88  ? 3906 GLN A CG    1 
ATOM   17289 C  CD    . GLN A 1 3906 ? 248.956 251.917 201.165 1.00 69.64  ? 3906 GLN A CD    1 
ATOM   17290 O  OE1   . GLN A 1 3906 ? 248.818 250.711 201.365 1.00 67.75  ? 3906 GLN A OE1   1 
ATOM   17291 N  NE2   . GLN A 1 3906 ? 250.085 252.561 201.430 1.00 64.67  ? 3906 GLN A NE2   1 
ATOM   17292 N  N     . HIS A 1 3907 ? 248.796 254.843 204.117 1.00 62.16  ? 3907 HIS A N     1 
ATOM   17293 C  CA    . HIS A 1 3907 ? 249.636 254.594 205.283 1.00 62.74  ? 3907 HIS A CA    1 
ATOM   17294 C  C     . HIS A 1 3907 ? 248.829 254.608 206.575 1.00 60.75  ? 3907 HIS A C     1 
ATOM   17295 O  O     . HIS A 1 3907 ? 249.162 253.887 207.519 1.00 61.08  ? 3907 HIS A O     1 
ATOM   17296 C  CB    . HIS A 1 3907 ? 250.762 255.621 205.358 1.00 62.95  ? 3907 HIS A CB    1 
ATOM   17297 C  CG    . HIS A 1 3907 ? 251.722 255.371 206.478 1.00 68.72  ? 3907 HIS A CG    1 
ATOM   17298 N  ND1   . HIS A 1 3907 ? 251.748 256.136 207.623 1.00 66.38  ? 3907 HIS A ND1   1 
ATOM   17299 C  CD2   . HIS A 1 3907 ? 252.680 254.427 206.635 1.00 68.94  ? 3907 HIS A CD2   1 
ATOM   17300 C  CE1   . HIS A 1 3907 ? 252.684 255.680 208.434 1.00 65.67  ? 3907 HIS A CE1   1 
ATOM   17301 N  NE2   . HIS A 1 3907 ? 253.266 254.644 207.858 1.00 68.20  ? 3907 HIS A NE2   1 
ATOM   17302 N  N     . PHE A 1 3908 ? 247.779 255.427 206.643 1.00 59.34  ? 3908 PHE A N     1 
ATOM   17303 C  CA    . PHE A 1 3908 ? 246.956 255.477 207.845 1.00 55.31  ? 3908 PHE A CA    1 
ATOM   17304 C  C     . PHE A 1 3908 ? 246.246 254.151 208.084 1.00 56.03  ? 3908 PHE A C     1 
ATOM   17305 O  O     . PHE A 1 3908 ? 246.181 253.671 209.221 1.00 61.03  ? 3908 PHE A O     1 
ATOM   17306 C  CB    . PHE A 1 3908 ? 245.949 256.620 207.729 1.00 52.76  ? 3908 PHE A CB    1 
ATOM   17307 C  CG    . PHE A 1 3908 ? 245.069 256.783 208.931 1.00 55.73  ? 3908 PHE A CG    1 
ATOM   17308 C  CD1   . PHE A 1 3908 ? 245.617 256.968 210.187 1.00 56.64  ? 3908 PHE A CD1   1 
ATOM   17309 C  CD2   . PHE A 1 3908 ? 243.692 256.764 208.804 1.00 55.55  ? 3908 PHE A CD2   1 
ATOM   17310 C  CE1   . PHE A 1 3908 ? 244.808 257.124 211.292 1.00 54.01  ? 3908 PHE A CE1   1 
ATOM   17311 C  CE2   . PHE A 1 3908 ? 242.880 256.920 209.905 1.00 54.23  ? 3908 PHE A CE2   1 
ATOM   17312 C  CZ    . PHE A 1 3908 ? 243.440 257.102 211.150 1.00 56.07  ? 3908 PHE A CZ    1 
ATOM   17313 N  N     . LEU A 1 3909 ? 245.720 253.540 207.024 1.00 55.99  ? 3909 LEU A N     1 
ATOM   17314 C  CA    . LEU A 1 3909 ? 244.958 252.305 207.157 1.00 56.91  ? 3909 LEU A CA    1 
ATOM   17315 C  C     . LEU A 1 3909 ? 245.839 251.060 207.152 1.00 64.96  ? 3909 LEU A C     1 
ATOM   17316 O  O     . LEU A 1 3909 ? 245.568 250.114 207.898 1.00 67.36  ? 3909 LEU A O     1 
ATOM   17317 C  CB    . LEU A 1 3909 ? 243.919 252.217 206.037 1.00 56.49  ? 3909 LEU A CB    1 
ATOM   17318 C  CG    . LEU A 1 3909 ? 242.828 253.289 206.082 1.00 60.66  ? 3909 LEU A CG    1 
ATOM   17319 C  CD1   . LEU A 1 3909 ? 241.890 253.161 204.900 1.00 59.75  ? 3909 LEU A CD1   1 
ATOM   17320 C  CD2   . LEU A 1 3909 ? 242.055 253.208 207.385 1.00 61.14  ? 3909 LEU A CD2   1 
ATOM   17321 N  N     . ARG A 1 3910 ? 246.889 251.037 206.333 1.00 72.04  ? 3910 ARG A N     1 
ATOM   17322 C  CA    . ARG A 1 3910 ? 247.773 249.883 206.204 1.00 66.63  ? 3910 ARG A CA    1 
ATOM   17323 C  C     . ARG A 1 3910 ? 249.227 250.256 206.474 1.00 70.25  ? 3910 ARG A C     1 
ATOM   17324 O  O     . ARG A 1 3910 ? 250.132 249.866 205.735 1.00 69.51  ? 3910 ARG A O     1 
ATOM   17325 C  CB    . ARG A 1 3910 ? 247.652 249.245 204.822 1.00 66.35  ? 3910 ARG A CB    1 
ATOM   17326 C  CG    . ARG A 1 3910 ? 246.319 249.437 204.130 1.00 68.32  ? 3910 ARG A CG    1 
ATOM   17327 C  CD    . ARG A 1 3910 ? 246.360 248.824 202.740 1.00 66.96  ? 3910 ARG A CD    1 
ATOM   17328 N  NE    . ARG A 1 3910 ? 246.321 247.367 202.771 1.00 72.58  ? 3910 ARG A NE    1 
ATOM   17329 C  CZ    . ARG A 1 3910 ? 245.236 246.640 202.538 1.00 75.17  ? 3910 ARG A CZ    1 
ATOM   17330 N  NH1   . ARG A 1 3910 ? 244.083 247.202 202.216 1.00 73.09  ? 3910 ARG A NH1   1 
ATOM   17331 N  NH2   . ARG A 1 3910 ? 245.315 245.315 202.618 1.00 71.42  ? 3910 ARG A NH2   1 
ATOM   17332 N  N     . GLY A 1 3911 ? 249.474 251.024 207.537 1.00 80.23  ? 3911 GLY A N     1 
ATOM   17333 C  CA    . GLY A 1 3911 ? 250.839 251.387 207.875 1.00 76.16  ? 3911 GLY A CA    1 
ATOM   17334 C  C     . GLY A 1 3911 ? 251.569 250.375 208.726 1.00 76.62  ? 3911 GLY A C     1 
ATOM   17335 O  O     . GLY A 1 3911 ? 252.800 250.421 208.805 1.00 76.78  ? 3911 GLY A O     1 
ATOM   17336 N  N     . ASN A 1 3912 ? 250.841 249.464 209.365 1.00 84.03  ? 3912 ASN A N     1 
ATOM   17337 C  CA    . ASN A 1 3912 ? 251.437 248.415 210.178 1.00 83.42  ? 3912 ASN A CA    1 
ATOM   17338 C  C     . ASN A 1 3912 ? 251.877 247.213 209.355 1.00 85.44  ? 3912 ASN A C     1 
ATOM   17339 O  O     . ASN A 1 3912 ? 252.419 246.258 209.920 1.00 86.15  ? 3912 ASN A O     1 
ATOM   17340 C  CB    . ASN A 1 3912 ? 250.450 247.972 211.261 1.00 81.67  ? 3912 ASN A CB    1 
ATOM   17341 C  CG    . ASN A 1 3912 ? 249.046 247.786 210.725 1.00 83.63  ? 3912 ASN A CG    1 
ATOM   17342 O  OD1   . ASN A 1 3912 ? 248.364 248.755 210.395 1.00 83.35  ? 3912 ASN A OD1   1 
ATOM   17343 N  ND2   . ASN A 1 3912 ? 248.606 246.537 210.635 1.00 82.87  ? 3912 ASN A ND2   1 
ATOM   17344 N  N     . GLU A 1 3913 ? 251.656 247.237 208.045 1.00 85.28  ? 3913 GLU A N     1 
ATOM   17345 C  CA    . GLU A 1 3913 ? 252.062 246.158 207.158 1.00 86.57  ? 3913 GLU A CA    1 
ATOM   17346 C  C     . GLU A 1 3913 ? 253.442 246.375 206.552 1.00 86.85  ? 3913 GLU A C     1 
ATOM   17347 O  O     . GLU A 1 3913 ? 253.871 245.570 205.720 1.00 86.74  ? 3913 GLU A O     1 
ATOM   17348 C  CB    . GLU A 1 3913 ? 251.032 245.983 206.039 1.00 86.12  ? 3913 GLU A CB    1 
ATOM   17349 C  CG    . GLU A 1 3913 ? 249.622 245.715 206.533 1.00 86.91  ? 3913 GLU A CG    1 
ATOM   17350 C  CD    . GLU A 1 3913 ? 248.651 245.442 205.403 1.00 89.02  ? 3913 GLU A CD    1 
ATOM   17351 O  OE1   . GLU A 1 3913 ? 249.066 245.524 204.228 1.00 84.25  ? 3913 GLU A OE1   1 
ATOM   17352 O  OE2   . GLU A 1 3913 ? 247.472 245.147 205.689 1.00 89.66  ? 3913 GLU A OE2   1 
ATOM   17353 N  N     . ILE A 1 3914 ? 254.141 247.436 206.942 1.00 83.15  ? 3914 ILE A N     1 
ATOM   17354 C  CA    . ILE A 1 3914 ? 255.478 247.704 206.425 1.00 82.16  ? 3914 ILE A CA    1 
ATOM   17355 C  C     . ILE A 1 3914 ? 256.480 246.838 207.175 1.00 86.81  ? 3914 ILE A C     1 
ATOM   17356 O  O     . ILE A 1 3914 ? 256.524 246.845 208.411 1.00 86.45  ? 3914 ILE A O     1 
ATOM   17357 C  CB    . ILE A 1 3914 ? 255.821 249.196 206.551 1.00 80.75  ? 3914 ILE A CB    1 
ATOM   17358 C  CG1   . ILE A 1 3914 ? 255.025 250.009 205.529 1.00 82.16  ? 3914 ILE A CG1   1 
ATOM   17359 C  CG2   . ILE A 1 3914 ? 257.311 249.420 206.365 1.00 82.51  ? 3914 ILE A CG2   1 
ATOM   17360 C  CD1   . ILE A 1 3914 ? 255.201 251.502 205.666 1.00 81.34  ? 3914 ILE A CD1   1 
ATOM   17361 N  N     . VAL A 1 3915 ? 257.288 246.086 206.427 1.00 89.16  ? 3915 VAL A N     1 
ATOM   17362 C  CA    . VAL A 1 3915 ? 258.249 245.175 207.034 1.00 90.40  ? 3915 VAL A CA    1 
ATOM   17363 C  C     . VAL A 1 3915 ? 259.440 245.964 207.559 1.00 91.18  ? 3915 VAL A C     1 
ATOM   17364 O  O     . VAL A 1 3915 ? 259.983 246.836 206.868 1.00 86.95  ? 3915 VAL A O     1 
ATOM   17365 C  CB    . VAL A 1 3915 ? 258.690 244.107 206.022 1.00 89.56  ? 3915 VAL A CB    1 
ATOM   17366 C  CG1   . VAL A 1 3915 ? 259.561 243.060 206.699 1.00 87.92  ? 3915 VAL A CG1   1 
ATOM   17367 C  CG2   . VAL A 1 3915 ? 257.476 243.460 205.375 1.00 87.54  ? 3915 VAL A CG2   1 
ATOM   17368 N  N     . LEU A 1 3916 ? 259.852 245.660 208.785 1.00 89.41  ? 3916 LEU A N     1 
ATOM   17369 C  CA    . LEU A 1 3916 ? 260.971 246.321 209.440 1.00 89.98  ? 3916 LEU A CA    1 
ATOM   17370 C  C     . LEU A 1 3916 ? 262.023 245.287 209.841 1.00 90.58  ? 3916 LEU A C     1 
ATOM   17371 O  O     . LEU A 1 3916 ? 261.908 244.097 209.538 1.00 86.72  ? 3916 LEU A O     1 
ATOM   17372 C  CB    . LEU A 1 3916 ? 260.487 247.113 210.656 1.00 87.70  ? 3916 LEU A CB    1 
ATOM   17373 C  CG    . LEU A 1 3916 ? 259.555 248.297 210.408 1.00 88.21  ? 3916 LEU A CG    1 
ATOM   17374 C  CD1   . LEU A 1 3916 ? 259.325 249.047 211.706 1.00 87.48  ? 3916 LEU A CD1   1 
ATOM   17375 C  CD2   . LEU A 1 3916 ? 260.134 249.218 209.348 1.00 85.49  ? 3916 LEU A CD2   1 
ATOM   17376 N  N     . SER A 1 3917 ? 263.058 245.761 210.532 1.00 93.44  ? 3917 SER A N     1 
ATOM   17377 C  CA    . SER A 1 3917 ? 264.101 244.900 211.068 1.00 92.57  ? 3917 SER A CA    1 
ATOM   17378 C  C     . SER A 1 3917 ? 264.603 245.498 212.374 1.00 91.88  ? 3917 SER A C     1 
ATOM   17379 O  O     . SER A 1 3917 ? 264.492 246.706 212.601 1.00 88.03  ? 3917 SER A O     1 
ATOM   17380 C  CB    . SER A 1 3917 ? 265.261 244.726 210.079 1.00 90.59  ? 3917 SER A CB    1 
ATOM   17381 O  OG    . SER A 1 3917 ? 264.821 244.122 208.875 1.00 89.89  ? 3917 SER A OG    1 
ATOM   17382 N  N     . ALA A 1 3918 ? 265.150 244.636 213.234 1.00 92.11  ? 3918 ALA A N     1 
ATOM   17383 C  CA    . ALA A 1 3918 ? 265.646 245.095 214.528 1.00 92.48  ? 3918 ALA A CA    1 
ATOM   17384 C  C     . ALA A 1 3918 ? 266.829 246.041 214.363 1.00 92.96  ? 3918 ALA A C     1 
ATOM   17385 O  O     . ALA A 1 3918 ? 266.914 247.073 215.038 1.00 89.70  ? 3918 ALA A O     1 
ATOM   17386 C  CB    . ALA A 1 3918 ? 266.028 243.896 215.397 1.00 87.69  ? 3918 ALA A CB    1 
ATOM   17387 N  N     . GLY A 1 3919 ? 267.755 245.705 213.464 1.00 86.44  ? 3919 GLY A N     1 
ATOM   17388 C  CA    . GLY A 1 3919 ? 268.919 246.553 213.266 1.00 83.72  ? 3919 GLY A CA    1 
ATOM   17389 C  C     . GLY A 1 3919 ? 268.597 247.824 212.505 1.00 85.57  ? 3919 GLY A C     1 
ATOM   17390 O  O     . GLY A 1 3919 ? 269.403 248.757 212.462 1.00 83.03  ? 3919 GLY A O     1 
ATOM   17391 N  N     . SER A 1 3920 ? 267.417 247.875 211.883 1.00 89.17  ? 3920 SER A N     1 
ATOM   17392 C  CA    . SER A 1 3920 ? 267.040 249.051 211.108 1.00 88.61  ? 3920 SER A CA    1 
ATOM   17393 C  C     . SER A 1 3920 ? 266.465 250.147 211.998 1.00 87.57  ? 3920 SER A C     1 
ATOM   17394 O  O     . SER A 1 3920 ? 266.249 251.274 211.539 1.00 84.29  ? 3920 SER A O     1 
ATOM   17395 C  CB    . SER A 1 3920 ? 266.038 248.663 210.021 1.00 86.64  ? 3920 SER A CB    1 
ATOM   17396 O  OG    . SER A 1 3920 ? 266.561 247.648 209.183 1.00 84.61  ? 3920 SER A OG    1 
ATOM   17397 N  N     . THR A 1 3921 ? 266.200 249.836 213.262 1.00 90.28  ? 3921 THR A N     1 
ATOM   17398 C  CA    . THR A 1 3921 ? 265.551 250.782 214.165 1.00 93.20  ? 3921 THR A CA    1 
ATOM   17399 C  C     . THR A 1 3921 ? 266.578 251.680 214.852 1.00 91.99  ? 3921 THR A C     1 
ATOM   17400 O  O     . THR A 1 3921 ? 267.462 251.170 215.556 1.00 88.96  ? 3921 THR A O     1 
ATOM   17401 C  CB    . THR A 1 3921 ? 264.729 250.033 215.210 1.00 91.21  ? 3921 THR A CB    1 
ATOM   17402 O  OG1   . THR A 1 3921 ? 263.844 249.116 214.555 1.00 88.61  ? 3921 THR A OG1   1 
ATOM   17403 C  CG2   . THR A 1 3921 ? 263.912 251.010 216.040 1.00 90.38  ? 3921 THR A CG2   1 
ATOM   17404 N  N     . PRO A 1 3922 ? 266.502 253.000 214.679 1.00 94.77  ? 3922 PRO A N     1 
ATOM   17405 C  CA    . PRO A 1 3922 ? 267.465 253.911 215.314 1.00 93.62  ? 3922 PRO A CA    1 
ATOM   17406 C  C     . PRO A 1 3922 ? 267.505 253.869 216.835 1.00 94.88  ? 3922 PRO A C     1 
ATOM   17407 O  O     . PRO A 1 3922 ? 268.523 254.278 217.406 1.00 94.94  ? 3922 PRO A O     1 
ATOM   17408 C  CB    . PRO A 1 3922 ? 266.976 255.294 214.851 1.00 93.40  ? 3922 PRO A CB    1 
ATOM   17409 C  CG    . PRO A 1 3922 ? 266.063 255.063 213.693 1.00 94.77  ? 3922 PRO A CG    1 
ATOM   17410 C  CD    . PRO A 1 3922 ? 265.902 253.597 213.477 1.00 94.97  ? 3922 PRO A CD    1 
ATOM   17411 N  N     . ARG A 1 3923 ? 266.444 253.410 217.498 1.00 96.63  ? 3923 ARG A N     1 
ATOM   17412 C  CA    . ARG A 1 3923 ? 266.291 253.535 218.949 1.00 99.23  ? 3923 ARG A CA    1 
ATOM   17413 C  C     . ARG A 1 3923 ? 266.327 255.010 219.362 1.00 98.22  ? 3923 ARG A C     1 
ATOM   17414 O  O     . ARG A 1 3923 ? 267.238 255.491 220.036 1.00 95.86  ? 3923 ARG A O     1 
ATOM   17415 C  CB    . ARG A 1 3923 ? 267.345 252.704 219.692 1.00 96.68  ? 3923 ARG A CB    1 
ATOM   17416 C  CG    . ARG A 1 3923 ? 267.128 252.611 221.198 1.00 96.06  ? 3923 ARG A CG    1 
ATOM   17417 C  CD    . ARG A 1 3923 ? 265.670 252.362 221.539 1.00 97.33  ? 3923 ARG A CD    1 
ATOM   17418 N  NE    . ARG A 1 3923 ? 265.440 252.363 222.979 1.00 99.42  ? 3923 ARG A NE    1 
ATOM   17419 C  CZ    . ARG A 1 3923 ? 264.251 252.214 223.546 1.00 99.98  ? 3923 ARG A CZ    1 
ATOM   17420 N  NH1   . ARG A 1 3923 ? 263.153 252.077 222.822 1.00 100.11 ? 3923 ARG A NH1   1 
ATOM   17421 N  NH2   . ARG A 1 3923 ? 264.161 252.209 224.873 1.00 96.01  ? 3923 ARG A NH2   1 
ATOM   17422 N  N     . ILE A 1 3924 ? 265.295 255.720 218.900 1.00 91.81  ? 3924 ILE A N     1 
ATOM   17423 C  CA    . ILE A 1 3924 ? 265.188 257.150 219.149 1.00 90.33  ? 3924 ILE A CA    1 
ATOM   17424 C  C     . ILE A 1 3924 ? 265.045 257.411 220.647 1.00 90.15  ? 3924 ILE A C     1 
ATOM   17425 O  O     . ILE A 1 3924 ? 264.316 256.710 221.361 1.00 90.58  ? 3924 ILE A O     1 
ATOM   17426 C  CB    . ILE A 1 3924 ? 264.004 257.750 218.369 1.00 91.15  ? 3924 ILE A CB    1 
ATOM   17427 C  CG1   . ILE A 1 3924 ? 264.208 257.600 216.858 1.00 91.37  ? 3924 ILE A CG1   1 
ATOM   17428 C  CG2   . ILE A 1 3924 ? 263.809 259.216 218.720 1.00 88.48  ? 3924 ILE A CG2   1 
ATOM   17429 C  CD1   . ILE A 1 3924 ? 263.674 256.305 216.272 1.00 91.27  ? 3924 ILE A CD1   1 
ATOM   17430 N  N     . GLN A 1 3925 ? 265.753 258.429 221.127 1.00 84.35  ? 3925 GLN A N     1 
ATOM   17431 C  CA    . GLN A 1 3925 ? 265.705 258.801 222.532 1.00 85.91  ? 3925 GLN A CA    1 
ATOM   17432 C  C     . GLN A 1 3925 ? 264.361 259.427 222.885 1.00 88.39  ? 3925 GLN A C     1 
ATOM   17433 O  O     . GLN A 1 3925 ? 263.788 260.202 222.116 1.00 86.49  ? 3925 GLN A O     1 
ATOM   17434 C  CB    . GLN A 1 3925 ? 266.838 259.772 222.865 1.00 86.24  ? 3925 GLN A CB    1 
ATOM   17435 C  CG    . GLN A 1 3925 ? 266.962 260.113 224.342 1.00 85.81  ? 3925 GLN A CG    1 
ATOM   17436 C  CD    . GLN A 1 3925 ? 266.216 261.381 224.707 1.00 88.72  ? 3925 GLN A CD    1 
ATOM   17437 O  OE1   . GLN A 1 3925 ? 265.660 262.057 223.841 1.00 88.43  ? 3925 GLN A OE1   1 
ATOM   17438 N  NE2   . GLN A 1 3925 ? 266.194 261.707 225.994 1.00 86.91  ? 3925 GLN A NE2   1 
ATOM   17439 N  N     . GLY A 1 3926 ? 263.862 259.080 224.070 1.00 84.06  ? 3926 GLY A N     1 
ATOM   17440 C  CA    . GLY A 1 3926 ? 262.614 259.629 224.564 1.00 80.60  ? 3926 GLY A CA    1 
ATOM   17441 C  C     . GLY A 1 3926 ? 261.392 258.957 223.975 1.00 82.26  ? 3926 GLY A C     1 
ATOM   17442 O  O     . GLY A 1 3926 ? 260.258 259.359 224.250 1.00 82.11  ? 3926 GLY A O     1 
ATOM   17443 N  N     . LEU A 1 3927 ? 261.614 257.927 223.165 1.00 77.29  ? 3927 LEU A N     1 
ATOM   17444 C  CA    . LEU A 1 3927 ? 260.548 257.209 222.485 1.00 75.51  ? 3927 LEU A CA    1 
ATOM   17445 C  C     . LEU A 1 3927 ? 260.635 255.730 222.828 1.00 78.02  ? 3927 LEU A C     1 
ATOM   17446 O  O     . LEU A 1 3927 ? 261.728 255.160 222.882 1.00 81.10  ? 3927 LEU A O     1 
ATOM   17447 C  CB    . LEU A 1 3927 ? 260.637 257.395 220.967 1.00 77.01  ? 3927 LEU A CB    1 
ATOM   17448 C  CG    . LEU A 1 3927 ? 259.853 258.543 220.331 1.00 78.78  ? 3927 LEU A CG    1 
ATOM   17449 C  CD1   . LEU A 1 3927 ? 260.360 259.890 220.814 1.00 75.78  ? 3927 LEU A CD1   1 
ATOM   17450 C  CD2   . LEU A 1 3927 ? 259.943 258.454 218.822 1.00 79.70  ? 3927 LEU A CD2   1 
ATOM   17451 N  N     . THR A 1 3928 ? 259.481 255.112 223.062 1.00 78.97  ? 3928 THR A N     1 
ATOM   17452 C  CA    . THR A 1 3928 ? 259.455 253.688 223.345 1.00 78.70  ? 3928 THR A CA    1 
ATOM   17453 C  C     . THR A 1 3928 ? 259.786 252.895 222.082 1.00 80.07  ? 3928 THR A C     1 
ATOM   17454 O  O     . THR A 1 3928 ? 259.970 253.448 220.994 1.00 81.22  ? 3928 THR A O     1 
ATOM   17455 C  CB    . THR A 1 3928 ? 258.092 253.270 223.895 1.00 78.70  ? 3928 THR A CB    1 
ATOM   17456 O  OG1   . THR A 1 3928 ? 257.104 253.377 222.865 1.00 82.00  ? 3928 THR A OG1   1 
ATOM   17457 C  CG2   . THR A 1 3928 ? 257.696 254.165 225.056 1.00 77.01  ? 3928 THR A CG2   1 
ATOM   17458 N  N     . VAL A 1 3929 ? 259.865 251.573 222.240 1.00 83.19  ? 3929 VAL A N     1 
ATOM   17459 C  CA    . VAL A 1 3929 ? 260.227 250.710 221.119 1.00 84.87  ? 3929 VAL A CA    1 
ATOM   17460 C  C     . VAL A 1 3929 ? 259.160 250.780 220.030 1.00 86.80  ? 3929 VAL A C     1 
ATOM   17461 O  O     . VAL A 1 3929 ? 259.463 250.962 218.843 1.00 85.42  ? 3929 VAL A O     1 
ATOM   17462 C  CB    . VAL A 1 3929 ? 260.444 249.267 221.610 1.00 85.09  ? 3929 VAL A CB    1 
ATOM   17463 C  CG1   . VAL A 1 3929 ? 260.721 248.339 220.445 1.00 84.07  ? 3929 VAL A CG1   1 
ATOM   17464 C  CG2   . VAL A 1 3929 ? 261.578 249.212 222.622 1.00 83.72  ? 3929 VAL A CG2   1 
ATOM   17465 N  N     . GLU A 1 3930 ? 257.890 250.656 220.425 1.00 84.29  ? 3930 GLU A N     1 
ATOM   17466 C  CA    . GLU A 1 3930 ? 256.801 250.704 219.455 1.00 83.38  ? 3930 GLU A CA    1 
ATOM   17467 C  C     . GLU A 1 3930 ? 256.680 252.084 218.822 1.00 81.35  ? 3930 GLU A C     1 
ATOM   17468 O  O     . GLU A 1 3930 ? 256.387 252.201 217.626 1.00 85.00  ? 3930 GLU A O     1 
ATOM   17469 C  CB    . GLU A 1 3930 ? 255.486 250.303 220.122 1.00 82.58  ? 3930 GLU A CB    1 
ATOM   17470 C  CG    . GLU A 1 3930 ? 255.605 249.133 221.087 1.00 85.51  ? 3930 GLU A CG    1 
ATOM   17471 C  CD    . GLU A 1 3930 ? 255.718 247.790 220.385 1.00 88.68  ? 3930 GLU A CD    1 
ATOM   17472 O  OE1   . GLU A 1 3930 ? 255.736 247.760 219.136 1.00 85.62  ? 3930 GLU A OE1   1 
ATOM   17473 O  OE2   . GLU A 1 3930 ? 255.787 246.760 221.088 1.00 86.36  ? 3930 GLU A OE2   1 
ATOM   17474 N  N     . GLN A 1 3931 ? 256.892 253.142 219.608 1.00 74.78  ? 3931 GLN A N     1 
ATOM   17475 C  CA    . GLN A 1 3931 ? 256.881 254.486 219.043 1.00 74.45  ? 3931 GLN A CA    1 
ATOM   17476 C  C     . GLN A 1 3931 ? 257.991 254.651 218.016 1.00 78.88  ? 3931 GLN A C     1 
ATOM   17477 O  O     . GLN A 1 3931 ? 257.793 255.283 216.973 1.00 82.16  ? 3931 GLN A O     1 
ATOM   17478 C  CB    . GLN A 1 3931 ? 257.011 255.528 220.153 1.00 70.92  ? 3931 GLN A CB    1 
ATOM   17479 C  CG    . GLN A 1 3931 ? 255.788 255.641 221.044 1.00 73.95  ? 3931 GLN A CG    1 
ATOM   17480 C  CD    . GLN A 1 3931 ? 255.835 256.855 221.946 1.00 75.35  ? 3931 GLN A CD    1 
ATOM   17481 O  OE1   . GLN A 1 3931 ? 256.775 257.646 221.892 1.00 76.79  ? 3931 GLN A OE1   1 
ATOM   17482 N  NE2   . GLN A 1 3931 ? 254.822 257.005 222.790 1.00 73.37  ? 3931 GLN A NE2   1 
ATOM   17483 N  N     . ALA A 1 3932 ? 259.169 254.087 218.293 1.00 81.71  ? 3932 ALA A N     1 
ATOM   17484 C  CA    . ALA A 1 3932 ? 260.260 254.139 217.325 1.00 81.15  ? 3932 ALA A CA    1 
ATOM   17485 C  C     . ALA A 1 3932 ? 259.903 253.390 216.047 1.00 81.36  ? 3932 ALA A C     1 
ATOM   17486 O  O     . ALA A 1 3932 ? 260.190 253.865 214.940 1.00 81.90  ? 3932 ALA A O     1 
ATOM   17487 C  CB    . ALA A 1 3932 ? 261.537 253.572 217.943 1.00 81.96  ? 3932 ALA A CB    1 
ATOM   17488 N  N     . GLU A 1 3933 ? 259.279 252.213 216.176 1.00 78.06  ? 3933 GLU A N     1 
ATOM   17489 C  CA    . GLU A 1 3933 ? 258.859 251.487 214.980 1.00 79.39  ? 3933 GLU A CA    1 
ATOM   17490 C  C     . GLU A 1 3933 ? 257.851 252.293 214.175 1.00 83.17  ? 3933 GLU A C     1 
ATOM   17491 O  O     . GLU A 1 3933 ? 257.923 252.339 212.942 1.00 86.77  ? 3933 GLU A O     1 
ATOM   17492 C  CB    . GLU A 1 3933 ? 258.257 250.129 215.338 1.00 79.87  ? 3933 GLU A CB    1 
ATOM   17493 C  CG    . GLU A 1 3933 ? 259.211 249.113 215.922 1.00 81.74  ? 3933 GLU A CG    1 
ATOM   17494 C  CD    . GLU A 1 3933 ? 258.497 248.118 216.811 1.00 85.12  ? 3933 GLU A CD    1 
ATOM   17495 O  OE1   . GLU A 1 3933 ? 257.459 247.577 216.377 1.00 84.49  ? 3933 GLU A OE1   1 
ATOM   17496 O  OE2   . GLU A 1 3933 ? 258.970 247.870 217.935 1.00 83.39  ? 3933 GLU A OE2   1 
ATOM   17497 N  N     . ALA A 1 3934 ? 256.892 252.923 214.855 1.00 76.73  ? 3934 ALA A N     1 
ATOM   17498 C  CA    . ALA A 1 3934 ? 255.910 253.744 214.156 1.00 75.26  ? 3934 ALA A CA    1 
ATOM   17499 C  C     . ALA A 1 3934 ? 256.563 254.932 213.463 1.00 77.90  ? 3934 ALA A C     1 
ATOM   17500 O  O     . ALA A 1 3934 ? 256.167 255.292 212.350 1.00 77.96  ? 3934 ALA A O     1 
ATOM   17501 C  CB    . ALA A 1 3934 ? 254.835 254.220 215.130 1.00 71.19  ? 3934 ALA A CB    1 
ATOM   17502 N  N     . VAL A 1 3935 ? 257.554 255.555 214.105 1.00 75.86  ? 3935 VAL A N     1 
ATOM   17503 C  CA    . VAL A 1 3935 ? 258.246 256.687 213.497 1.00 75.76  ? 3935 VAL A CA    1 
ATOM   17504 C  C     . VAL A 1 3935 ? 258.987 256.253 212.241 1.00 78.78  ? 3935 VAL A C     1 
ATOM   17505 O  O     . VAL A 1 3935 ? 258.906 256.910 211.196 1.00 78.22  ? 3935 VAL A O     1 
ATOM   17506 C  CB    . VAL A 1 3935 ? 259.198 257.341 214.512 1.00 75.17  ? 3935 VAL A CB    1 
ATOM   17507 C  CG1   . VAL A 1 3935 ? 260.125 258.318 213.815 1.00 74.54  ? 3935 VAL A CG1   1 
ATOM   17508 C  CG2   . VAL A 1 3935 ? 258.404 258.052 215.575 1.00 75.72  ? 3935 VAL A CG2   1 
ATOM   17509 N  N     . VAL A 1 3936 ? 259.726 255.144 212.320 1.00 79.39  ? 3936 VAL A N     1 
ATOM   17510 C  CA    . VAL A 1 3936 ? 260.474 254.707 211.144 1.00 75.89  ? 3936 VAL A CA    1 
ATOM   17511 C  C     . VAL A 1 3936 ? 259.530 254.224 210.049 1.00 77.87  ? 3936 VAL A C     1 
ATOM   17512 O  O     . VAL A 1 3936 ? 259.838 254.349 208.858 1.00 78.50  ? 3936 VAL A O     1 
ATOM   17513 C  CB    . VAL A 1 3936 ? 261.524 253.643 211.520 1.00 76.52  ? 3936 VAL A CB    1 
ATOM   17514 C  CG1   . VAL A 1 3936 ? 262.368 254.125 212.688 1.00 77.35  ? 3936 VAL A CG1   1 
ATOM   17515 C  CG2   . VAL A 1 3936 ? 260.868 252.318 211.846 1.00 76.50  ? 3936 VAL A CG2   1 
ATOM   17516 N  N     . ARG A 1 3937 ? 258.373 253.668 210.420 1.00 76.98  ? 3937 ARG A N     1 
ATOM   17517 C  CA    . ARG A 1 3937 ? 257.360 253.340 209.421 1.00 76.27  ? 3937 ARG A CA    1 
ATOM   17518 C  C     . ARG A 1 3937 ? 256.750 254.601 208.823 1.00 76.50  ? 3937 ARG A C     1 
ATOM   17519 O  O     . ARG A 1 3937 ? 256.546 254.684 207.607 1.00 77.78  ? 3937 ARG A O     1 
ATOM   17520 C  CB    . ARG A 1 3937 ? 256.273 252.465 210.041 1.00 74.63  ? 3937 ARG A CB    1 
ATOM   17521 C  CG    . ARG A 1 3937 ? 256.664 251.012 210.212 1.00 74.13  ? 3937 ARG A CG    1 
ATOM   17522 C  CD    . ARG A 1 3937 ? 255.483 250.182 210.677 1.00 75.11  ? 3937 ARG A CD    1 
ATOM   17523 N  NE    . ARG A 1 3937 ? 255.744 248.752 210.577 1.00 79.54  ? 3937 ARG A NE    1 
ATOM   17524 C  CZ    . ARG A 1 3937 ? 255.862 247.938 211.616 1.00 82.03  ? 3937 ARG A CZ    1 
ATOM   17525 N  NH1   . ARG A 1 3937 ? 255.745 248.380 212.857 1.00 80.30  ? 3937 ARG A NH1   1 
ATOM   17526 N  NH2   . ARG A 1 3937 ? 256.102 246.647 211.405 1.00 78.77  ? 3937 ARG A NH2   1 
ATOM   17527 N  N     . LEU A 1 3938 ? 256.449 255.592 209.667 1.00 73.15  ? 3938 LEU A N     1 
ATOM   17528 C  CA    . LEU A 1 3938 ? 255.888 256.847 209.180 1.00 73.57  ? 3938 LEU A CA    1 
ATOM   17529 C  C     . LEU A 1 3938 ? 256.879 257.607 208.309 1.00 74.09  ? 3938 LEU A C     1 
ATOM   17530 O  O     . LEU A 1 3938 ? 256.469 258.394 207.448 1.00 74.48  ? 3938 LEU A O     1 
ATOM   17531 C  CB    . LEU A 1 3938 ? 255.446 257.710 210.363 1.00 71.82  ? 3938 LEU A CB    1 
ATOM   17532 C  CG    . LEU A 1 3938 ? 254.785 259.062 210.088 1.00 70.29  ? 3938 LEU A CG    1 
ATOM   17533 C  CD1   . LEU A 1 3938 ? 253.467 258.889 209.358 1.00 71.01  ? 3938 LEU A CD1   1 
ATOM   17534 C  CD2   . LEU A 1 3938 ? 254.585 259.821 211.385 1.00 72.23  ? 3938 LEU A CD2   1 
ATOM   17535 N  N     . SER A 1 3939 ? 258.178 257.382 208.507 1.00 78.41  ? 3939 SER A N     1 
ATOM   17536 C  CA    . SER A 1 3939 ? 259.199 258.075 207.733 1.00 81.76  ? 3939 SER A CA    1 
ATOM   17537 C  C     . SER A 1 3939 ? 259.219 257.660 206.269 1.00 82.31  ? 3939 SER A C     1 
ATOM   17538 O  O     . SER A 1 3939 ? 259.846 258.351 205.459 1.00 82.04  ? 3939 SER A O     1 
ATOM   17539 C  CB    . SER A 1 3939 ? 260.576 257.836 208.352 1.00 80.53  ? 3939 SER A CB    1 
ATOM   17540 O  OG    . SER A 1 3939 ? 261.001 256.501 208.143 1.00 80.06  ? 3939 SER A OG    1 
ATOM   17541 N  N     . CYS A 1 3940 ? 258.557 256.556 205.911 1.00 79.19  ? 3940 CYS A N     1 
ATOM   17542 C  CA    . CYS A 1 3940 ? 258.535 256.126 204.517 1.00 78.32  ? 3940 CYS A CA    1 
ATOM   17543 C  C     . CYS A 1 3940 ? 257.850 257.152 203.624 1.00 81.37  ? 3940 CYS A C     1 
ATOM   17544 O  O     . CYS A 1 3940 ? 258.174 257.252 202.435 1.00 81.53  ? 3940 CYS A O     1 
ATOM   17545 C  CB    . CYS A 1 3940 ? 257.840 254.770 204.396 1.00 79.50  ? 3940 CYS A CB    1 
ATOM   17546 S  SG    . CYS A 1 3940 ? 258.647 253.433 205.306 1.00 89.96  ? 3940 CYS A SG    1 
ATOM   17547 N  N     . LEU A 1 3941 ? 256.906 257.910 204.169 1.00 81.74  ? 3941 LEU A N     1 
ATOM   17548 C  CA    . LEU A 1 3941 ? 256.247 258.946 203.391 1.00 81.11  ? 3941 LEU A CA    1 
ATOM   17549 C  C     . LEU A 1 3941 ? 257.238 260.057 203.052 1.00 79.52  ? 3941 LEU A C     1 
ATOM   17550 O  O     . LEU A 1 3941 ? 258.063 260.431 203.891 1.00 76.23  ? 3941 LEU A O     1 
ATOM   17551 C  CB    . LEU A 1 3941 ? 255.060 259.524 204.161 1.00 77.45  ? 3941 LEU A CB    1 
ATOM   17552 C  CG    . LEU A 1 3941 ? 253.679 258.957 203.832 1.00 77.74  ? 3941 LEU A CG    1 
ATOM   17553 C  CD1   . LEU A 1 3941 ? 253.642 257.460 204.084 1.00 77.43  ? 3941 LEU A CD1   1 
ATOM   17554 C  CD2   . LEU A 1 3941 ? 252.607 259.663 204.642 1.00 75.79  ? 3941 LEU A CD2   1 
ATOM   17555 N  N     . PRO A 1 3942 ? 257.204 260.581 201.825 1.00 77.67  ? 3942 PRO A N     1 
ATOM   17556 C  CA    . PRO A 1 3942 ? 258.073 261.721 201.491 1.00 75.84  ? 3942 PRO A CA    1 
ATOM   17557 C  C     . PRO A 1 3942 ? 257.910 262.907 202.427 1.00 74.33  ? 3942 PRO A C     1 
ATOM   17558 O  O     . PRO A 1 3942 ? 258.899 263.578 202.747 1.00 72.51  ? 3942 PRO A O     1 
ATOM   17559 C  CB    . PRO A 1 3942 ? 257.637 262.078 200.062 1.00 73.73  ? 3942 PRO A CB    1 
ATOM   17560 C  CG    . PRO A 1 3942 ? 256.853 260.882 199.550 1.00 72.30  ? 3942 PRO A CG    1 
ATOM   17561 C  CD    . PRO A 1 3942 ? 256.820 259.833 200.619 1.00 74.83  ? 3942 PRO A CD    1 
ATOM   17562 N  N     . ALA A 1 3943 ? 256.684 263.187 202.873 1.00 75.23  ? 3943 ALA A N     1 
ATOM   17563 C  CA    . ALA A 1 3943 ? 256.447 264.335 203.740 1.00 75.32  ? 3943 ALA A CA    1 
ATOM   17564 C  C     . ALA A 1 3943 ? 257.018 264.140 205.137 1.00 77.66  ? 3943 ALA A C     1 
ATOM   17565 O  O     . ALA A 1 3943 ? 257.204 265.125 205.859 1.00 76.00  ? 3943 ALA A O     1 
ATOM   17566 C  CB    . ALA A 1 3943 ? 254.949 264.626 203.829 1.00 71.10  ? 3943 ALA A CB    1 
ATOM   17567 N  N     . PHE A 1 3944 ? 257.299 262.900 205.535 1.00 75.49  ? 3944 PHE A N     1 
ATOM   17568 C  CA    . PHE A 1 3944 ? 257.851 262.599 206.849 1.00 71.99  ? 3944 PHE A CA    1 
ATOM   17569 C  C     . PHE A 1 3944 ? 259.263 262.030 206.755 1.00 74.26  ? 3944 PHE A C     1 
ATOM   17570 O  O     . PHE A 1 3944 ? 259.711 261.320 207.657 1.00 76.84  ? 3944 PHE A O     1 
ATOM   17571 C  CB    . PHE A 1 3944 ? 256.938 261.636 207.606 1.00 74.78  ? 3944 PHE A CB    1 
ATOM   17572 C  CG    . PHE A 1 3944 ? 255.639 262.249 208.043 1.00 72.63  ? 3944 PHE A CG    1 
ATOM   17573 C  CD1   . PHE A 1 3944 ? 255.591 263.092 209.138 1.00 70.45  ? 3944 PHE A CD1   1 
ATOM   17574 C  CD2   . PHE A 1 3944 ? 254.468 261.983 207.358 1.00 71.15  ? 3944 PHE A CD2   1 
ATOM   17575 C  CE1   . PHE A 1 3944 ? 254.401 263.659 209.539 1.00 70.37  ? 3944 PHE A CE1   1 
ATOM   17576 C  CE2   . PHE A 1 3944 ? 253.275 262.547 207.757 1.00 68.64  ? 3944 PHE A CE2   1 
ATOM   17577 C  CZ    . PHE A 1 3944 ? 253.242 263.385 208.848 1.00 71.11  ? 3944 PHE A CZ    1 
ATOM   17578 N  N     . LYS A 1 3945 ? 259.970 262.328 205.662 1.00 84.42  ? 3945 LYS A N     1 
ATOM   17579 C  CA    . LYS A 1 3945 ? 261.335 261.834 205.506 1.00 83.77  ? 3945 LYS A CA    1 
ATOM   17580 C  C     . LYS A 1 3945 ? 262.251 262.392 206.586 1.00 84.29  ? 3945 LYS A C     1 
ATOM   17581 O  O     . LYS A 1 3945 ? 263.043 261.653 207.184 1.00 83.33  ? 3945 LYS A O     1 
ATOM   17582 C  CB    . LYS A 1 3945 ? 261.869 262.194 204.120 1.00 81.31  ? 3945 LYS A CB    1 
ATOM   17583 C  CG    . LYS A 1 3945 ? 261.501 261.209 203.027 1.00 83.91  ? 3945 LYS A CG    1 
ATOM   17584 C  CD    . LYS A 1 3945 ? 262.256 261.513 201.743 1.00 84.32  ? 3945 LYS A CD    1 
ATOM   17585 C  CE    . LYS A 1 3945 ? 261.646 262.694 201.006 1.00 81.41  ? 3945 LYS A CE    1 
ATOM   17586 N  NZ    . LYS A 1 3945 ? 261.557 262.449 199.540 1.00 78.83  ? 3945 LYS A NZ    1 
ATOM   17587 N  N     . ASP A 1 3946 ? 262.154 263.693 206.855 1.00 80.49  ? 3946 ASP A N     1 
ATOM   17588 C  CA    . ASP A 1 3946 ? 262.967 264.345 207.878 1.00 81.89  ? 3946 ASP A CA    1 
ATOM   17589 C  C     . ASP A 1 3946 ? 262.108 264.430 209.139 1.00 81.95  ? 3946 ASP A C     1 
ATOM   17590 O  O     . ASP A 1 3946 ? 261.515 265.459 209.463 1.00 84.63  ? 3946 ASP A O     1 
ATOM   17591 C  CB    . ASP A 1 3946 ? 263.444 265.713 207.386 1.00 81.90  ? 3946 ASP A CB    1 
ATOM   17592 C  CG    . ASP A 1 3946 ? 263.984 266.596 208.499 1.00 84.81  ? 3946 ASP A CG    1 
ATOM   17593 O  OD1   . ASP A 1 3946 ? 264.487 266.058 209.507 1.00 85.56  ? 3946 ASP A OD1   1 
ATOM   17594 O  OD2   . ASP A 1 3946 ? 263.902 267.834 208.363 1.00 82.08  ? 3946 ASP A OD2   1 
ATOM   17595 N  N     . LEU A 1 3947 ? 262.029 263.305 209.846 1.00 72.29  ? 3947 LEU A N     1 
ATOM   17596 C  CA    . LEU A 1 3947 ? 261.216 263.194 211.050 1.00 75.36  ? 3947 LEU A CA    1 
ATOM   17597 C  C     . LEU A 1 3947 ? 262.043 262.907 212.291 1.00 75.17  ? 3947 LEU A C     1 
ATOM   17598 O  O     . LEU A 1 3947 ? 261.903 263.611 213.298 1.00 75.28  ? 3947 LEU A O     1 
ATOM   17599 C  CB    . LEU A 1 3947 ? 260.151 262.100 210.867 1.00 73.69  ? 3947 LEU A CB    1 
ATOM   17600 C  CG    . LEU A 1 3947 ? 259.242 261.834 212.067 1.00 71.05  ? 3947 LEU A CG    1 
ATOM   17601 C  CD1   . LEU A 1 3947 ? 258.528 263.105 212.493 1.00 73.27  ? 3947 LEU A CD1   1 
ATOM   17602 C  CD2   . LEU A 1 3947 ? 258.241 260.742 211.745 1.00 72.43  ? 3947 LEU A CD2   1 
ATOM   17603 N  N     . ILE A 1 3948 ? 262.905 261.888 212.249 1.00 77.22  ? 3948 ILE A N     1 
ATOM   17604 C  CA    . ILE A 1 3948 ? 263.722 261.553 213.413 1.00 78.23  ? 3948 ILE A CA    1 
ATOM   17605 C  C     . ILE A 1 3948 ? 264.629 262.722 213.774 1.00 79.11  ? 3948 ILE A C     1 
ATOM   17606 O  O     . ILE A 1 3948 ? 264.810 263.046 214.954 1.00 79.67  ? 3948 ILE A O     1 
ATOM   17607 C  CB    . ILE A 1 3948 ? 264.530 260.267 213.157 1.00 75.24  ? 3948 ILE A CB    1 
ATOM   17608 C  CG1   . ILE A 1 3948 ? 263.603 259.068 212.938 1.00 75.68  ? 3948 ILE A CG1   1 
ATOM   17609 C  CG2   . ILE A 1 3948 ? 265.466 259.989 214.317 1.00 75.13  ? 3948 ILE A CG2   1 
ATOM   17610 C  CD1   . ILE A 1 3948 ? 263.184 258.850 211.497 1.00 76.86  ? 3948 ILE A CD1   1 
ATOM   17611 N  N     . ALA A 1 3949 ? 265.209 263.374 212.765 1.00 77.98  ? 3949 ALA A N     1 
ATOM   17612 C  CA    . ALA A 1 3949 ? 265.977 264.587 213.019 1.00 76.68  ? 3949 ALA A CA    1 
ATOM   17613 C  C     . ALA A 1 3949 ? 265.096 265.675 213.617 1.00 81.88  ? 3949 ALA A C     1 
ATOM   17614 O  O     . ALA A 1 3949 ? 265.518 266.393 214.530 1.00 84.99  ? 3949 ALA A O     1 
ATOM   17615 C  CB    . ALA A 1 3949 ? 266.634 265.074 211.729 1.00 76.31  ? 3949 ALA A CB    1 
ATOM   17616 N  N     . LYS A 1 3950 ? 263.867 265.812 213.114 1.00 79.70  ? 3950 LYS A N     1 
ATOM   17617 C  CA    . LYS A 1 3950 ? 262.947 266.801 213.668 1.00 77.09  ? 3950 LYS A CA    1 
ATOM   17618 C  C     . LYS A 1 3950 ? 262.583 266.471 215.111 1.00 79.81  ? 3950 LYS A C     1 
ATOM   17619 O  O     . LYS A 1 3950 ? 262.512 267.367 215.960 1.00 79.47  ? 3950 LYS A O     1 
ATOM   17620 C  CB    . LYS A 1 3950 ? 261.689 266.888 212.804 1.00 74.88  ? 3950 LYS A CB    1 
ATOM   17621 C  CG    . LYS A 1 3950 ? 261.780 267.904 211.679 1.00 75.61  ? 3950 LYS A CG    1 
ATOM   17622 C  CD    . LYS A 1 3950 ? 260.401 268.302 211.185 1.00 78.41  ? 3950 LYS A CD    1 
ATOM   17623 C  CE    . LYS A 1 3950 ? 260.485 269.223 209.980 1.00 76.00  ? 3950 LYS A CE    1 
ATOM   17624 N  NZ    . LYS A 1 3950 ? 261.040 268.522 208.791 1.00 75.05  ? 3950 LYS A NZ    1 
ATOM   17625 N  N     . VAL A 1 3951 ? 262.344 265.191 215.406 1.00 79.36  ? 3951 VAL A N     1 
ATOM   17626 C  CA    . VAL A 1 3951 ? 262.002 264.788 216.768 1.00 76.92  ? 3951 VAL A CA    1 
ATOM   17627 C  C     . VAL A 1 3951 ? 263.165 265.066 217.713 1.00 78.14  ? 3951 VAL A C     1 
ATOM   17628 O  O     . VAL A 1 3951 ? 262.981 265.597 218.815 1.00 80.81  ? 3951 VAL A O     1 
ATOM   17629 C  CB    . VAL A 1 3951 ? 261.586 263.306 216.804 1.00 73.63  ? 3951 VAL A CB    1 
ATOM   17630 C  CG1   . VAL A 1 3951 ? 261.432 262.833 218.236 1.00 74.83  ? 3951 VAL A CG1   1 
ATOM   17631 C  CG2   . VAL A 1 3951 ? 260.290 263.102 216.044 1.00 74.11  ? 3951 VAL A CG2   1 
ATOM   17632 N  N     . GLN A 1 3952 ? 264.381 264.709 217.295 1.00 78.12  ? 3952 GLN A N     1 
ATOM   17633 C  CA    . GLN A 1 3952 ? 265.548 264.917 218.147 1.00 79.52  ? 3952 GLN A CA    1 
ATOM   17634 C  C     . GLN A 1 3952 ? 265.833 266.400 218.355 1.00 79.30  ? 3952 GLN A C     1 
ATOM   17635 O  O     . GLN A 1 3952 ? 266.187 266.819 219.463 1.00 77.97  ? 3952 GLN A O     1 
ATOM   17636 C  CB    . GLN A 1 3952 ? 266.766 264.216 217.548 1.00 80.15  ? 3952 GLN A CB    1 
ATOM   17637 C  CG    . GLN A 1 3952 ? 266.742 262.702 217.675 1.00 80.21  ? 3952 GLN A CG    1 
ATOM   17638 C  CD    . GLN A 1 3952 ? 267.677 262.023 216.695 1.00 82.73  ? 3952 GLN A CD    1 
ATOM   17639 O  OE1   . GLN A 1 3952 ? 268.369 262.684 215.921 1.00 84.52  ? 3952 GLN A OE1   1 
ATOM   17640 N  NE2   . GLN A 1 3952 ? 267.706 260.697 216.725 1.00 80.75  ? 3952 GLN A NE2   1 
ATOM   17641 N  N     . ALA A 1 3953 ? 265.693 267.207 217.301 1.00 82.63  ? 3953 ALA A N     1 
ATOM   17642 C  CA    . ALA A 1 3953 ? 266.003 268.629 217.407 1.00 84.44  ? 3953 ALA A CA    1 
ATOM   17643 C  C     . ALA A 1 3953 ? 265.053 269.341 218.362 1.00 86.11  ? 3953 ALA A C     1 
ATOM   17644 O  O     . ALA A 1 3953 ? 265.477 270.199 219.145 1.00 85.59  ? 3953 ALA A O     1 
ATOM   17645 C  CB    . ALA A 1 3953 ? 265.959 269.279 216.024 1.00 80.80  ? 3953 ALA A CB    1 
ATOM   17646 N  N     . ASP A 1 3954 ? 263.767 269.004 218.310 1.00 89.60  ? 3954 ASP A N     1 
ATOM   17647 C  CA    . ASP A 1 3954 ? 262.788 269.674 219.155 1.00 89.50  ? 3954 ASP A CA    1 
ATOM   17648 C  C     . ASP A 1 3954 ? 262.948 269.234 220.605 1.00 90.13  ? 3954 ASP A C     1 
ATOM   17649 O  O     . ASP A 1 3954 ? 262.885 268.040 220.915 1.00 86.12  ? 3954 ASP A O     1 
ATOM   17650 C  CB    . ASP A 1 3954 ? 261.372 269.375 218.663 1.00 89.52  ? 3954 ASP A CB    1 
ATOM   17651 C  CG    . ASP A 1 3954 ? 260.350 270.364 219.191 1.00 90.62  ? 3954 ASP A CG    1 
ATOM   17652 O  OD1   . ASP A 1 3954 ? 260.743 271.299 219.919 1.00 87.26  ? 3954 ASP A OD1   1 
ATOM   17653 O  OD2   . ASP A 1 3954 ? 259.152 270.208 218.872 1.00 86.56  ? 3954 ASP A OD2   1 
ATOM   17654 N  N     . GLU A 1 3955 ? 263.155 270.204 221.495 1.00 96.52  ? 3955 GLU A N     1 
ATOM   17655 C  CA    . GLU A 1 3955 ? 263.278 269.925 222.919 1.00 96.98  ? 3955 GLU A CA    1 
ATOM   17656 C  C     . GLU A 1 3955 ? 261.938 269.919 223.638 1.00 97.49  ? 3955 GLU A C     1 
ATOM   17657 O  O     . GLU A 1 3955 ? 261.817 269.285 224.692 1.00 93.80  ? 3955 GLU A O     1 
ATOM   17658 C  CB    . GLU A 1 3955 ? 264.205 270.949 223.583 1.00 95.91  ? 3955 GLU A CB    1 
ATOM   17659 C  CG    . GLU A 1 3955 ? 263.728 272.390 223.474 1.00 97.46  ? 3955 GLU A CG    1 
ATOM   17660 C  CD    . GLU A 1 3955 ? 264.342 273.121 222.296 1.00 97.28  ? 3955 GLU A CD    1 
ATOM   17661 O  OE1   . GLU A 1 3955 ? 265.112 272.492 221.540 1.00 98.13  ? 3955 GLU A OE1   1 
ATOM   17662 O  OE2   . GLU A 1 3955 ? 264.060 274.326 222.129 1.00 93.37  ? 3955 GLU A OE2   1 
ATOM   17663 N  N     . GLN A 1 3956 ? 260.935 270.605 223.095 1.00 90.61  ? 3956 GLN A N     1 
ATOM   17664 C  CA    . GLN A 1 3956 ? 259.596 270.616 223.666 1.00 91.09  ? 3956 GLN A CA    1 
ATOM   17665 C  C     . GLN A 1 3956 ? 258.811 269.354 223.327 1.00 90.29  ? 3956 GLN A C     1 
ATOM   17666 O  O     . GLN A 1 3956 ? 257.713 269.160 223.860 1.00 89.43  ? 3956 GLN A O     1 
ATOM   17667 C  CB    . GLN A 1 3956 ? 258.842 271.861 223.180 1.00 89.24  ? 3956 GLN A CB    1 
ATOM   17668 C  CG    . GLN A 1 3956 ? 257.561 272.184 223.935 1.00 88.36  ? 3956 GLN A CG    1 
ATOM   17669 C  CD    . GLN A 1 3956 ? 256.911 273.467 223.453 1.00 90.11  ? 3956 GLN A CD    1 
ATOM   17670 O  OE1   . GLN A 1 3956 ? 257.402 274.115 222.529 1.00 88.16  ? 3956 GLN A OE1   1 
ATOM   17671 N  NE2   . GLN A 1 3956 ? 255.800 273.839 224.078 1.00 91.63  ? 3956 GLN A NE2   1 
ATOM   17672 N  N     . PHE A 1 3957 ? 259.355 268.487 222.469 1.00 76.45  ? 3957 PHE A N     1 
ATOM   17673 C  CA    . PHE A 1 3957 ? 258.630 267.288 222.064 1.00 75.41  ? 3957 PHE A CA    1 
ATOM   17674 C  C     . PHE A 1 3957 ? 258.360 266.370 223.249 1.00 78.82  ? 3957 PHE A C     1 
ATOM   17675 O  O     . PHE A 1 3957 ? 257.332 265.684 223.288 1.00 82.52  ? 3957 PHE A O     1 
ATOM   17676 C  CB    . PHE A 1 3957 ? 259.408 266.543 220.981 1.00 76.05  ? 3957 PHE A CB    1 
ATOM   17677 C  CG    . PHE A 1 3957 ? 258.685 265.350 220.438 1.00 74.58  ? 3957 PHE A CG    1 
ATOM   17678 C  CD1   . PHE A 1 3957 ? 257.763 265.492 219.417 1.00 74.18  ? 3957 PHE A CD1   1 
ATOM   17679 C  CD2   . PHE A 1 3957 ? 258.918 264.088 220.954 1.00 72.48  ? 3957 PHE A CD2   1 
ATOM   17680 C  CE1   . PHE A 1 3957 ? 257.092 264.400 218.918 1.00 75.48  ? 3957 PHE A CE1   1 
ATOM   17681 C  CE2   . PHE A 1 3957 ? 258.249 262.992 220.459 1.00 75.68  ? 3957 PHE A CE2   1 
ATOM   17682 C  CZ    . PHE A 1 3957 ? 257.334 263.149 219.441 1.00 78.16  ? 3957 PHE A CZ    1 
ATOM   17683 N  N     . GLY A 1 3958 ? 259.280 266.324 224.213 1.00 76.51  ? 3958 GLY A N     1 
ATOM   17684 C  CA    . GLY A 1 3958 ? 259.037 265.529 225.406 1.00 73.00  ? 3958 GLY A CA    1 
ATOM   17685 C  C     . GLY A 1 3958 ? 257.827 266.010 226.182 1.00 76.77  ? 3958 GLY A C     1 
ATOM   17686 O  O     . GLY A 1 3958 ? 257.083 265.208 226.752 1.00 74.99  ? 3958 GLY A O     1 
ATOM   17687 N  N     . ILE A 1 3959 ? 257.615 267.326 226.215 1.00 76.59  ? 3959 ILE A N     1 
ATOM   17688 C  CA    . ILE A 1 3959 ? 256.442 267.877 226.885 1.00 74.46  ? 3959 ILE A CA    1 
ATOM   17689 C  C     . ILE A 1 3959 ? 255.173 267.486 226.139 1.00 77.01  ? 3959 ILE A C     1 
ATOM   17690 O  O     . ILE A 1 3959 ? 254.152 267.149 226.752 1.00 78.60  ? 3959 ILE A O     1 
ATOM   17691 C  CB    . ILE A 1 3959 ? 256.573 269.405 227.019 1.00 77.54  ? 3959 ILE A CB    1 
ATOM   17692 C  CG1   . ILE A 1 3959 ? 257.831 269.761 227.814 1.00 79.42  ? 3959 ILE A CG1   1 
ATOM   17693 C  CG2   . ILE A 1 3959 ? 255.342 269.991 227.685 1.00 75.69  ? 3959 ILE A CG2   1 
ATOM   17694 C  CD1   . ILE A 1 3959 ? 257.836 269.219 229.223 1.00 77.26  ? 3959 ILE A CD1   1 
ATOM   17695 N  N     . TRP A 1 3960 ? 255.214 267.530 224.805 1.00 69.22  ? 3960 TRP A N     1 
ATOM   17696 C  CA    . TRP A 1 3960 ? 254.040 267.172 224.015 1.00 67.50  ? 3960 TRP A CA    1 
ATOM   17697 C  C     . TRP A 1 3960 ? 253.698 265.695 224.162 1.00 65.96  ? 3960 TRP A C     1 
ATOM   17698 O  O     . TRP A 1 3960 ? 252.520 265.330 224.252 1.00 65.15  ? 3960 TRP A O     1 
ATOM   17699 C  CB    . TRP A 1 3960 ? 254.265 267.513 222.543 1.00 68.28  ? 3960 TRP A CB    1 
ATOM   17700 C  CG    . TRP A 1 3960 ? 253.125 267.089 221.674 1.00 68.76  ? 3960 TRP A CG    1 
ATOM   17701 C  CD1   . TRP A 1 3960 ? 251.930 267.726 221.523 1.00 66.06  ? 3960 TRP A CD1   1 
ATOM   17702 C  CD2   . TRP A 1 3960 ? 253.058 265.916 220.856 1.00 63.49  ? 3960 TRP A CD2   1 
ATOM   17703 N  NE1   . TRP A 1 3960 ? 251.129 267.032 220.652 1.00 64.59  ? 3960 TRP A NE1   1 
ATOM   17704 C  CE2   . TRP A 1 3960 ? 251.798 265.914 220.231 1.00 62.79  ? 3960 TRP A CE2   1 
ATOM   17705 C  CE3   . TRP A 1 3960 ? 253.945 264.870 220.587 1.00 64.73  ? 3960 TRP A CE3   1 
ATOM   17706 C  CZ2   . TRP A 1 3960 ? 251.403 264.910 219.352 1.00 62.54  ? 3960 TRP A CZ2   1 
ATOM   17707 C  CZ3   . TRP A 1 3960 ? 253.550 263.874 219.717 1.00 65.24  ? 3960 TRP A CZ3   1 
ATOM   17708 C  CH2   . TRP A 1 3960 ? 252.291 263.901 219.109 1.00 64.26  ? 3960 TRP A CH2   1 
ATOM   17709 N  N     . LEU A 1 3961 ? 254.715 264.831 224.182 1.00 64.04  ? 3961 LEU A N     1 
ATOM   17710 C  CA    . LEU A 1 3961 ? 254.472 263.392 224.186 1.00 66.94  ? 3961 LEU A CA    1 
ATOM   17711 C  C     . LEU A 1 3961 ? 253.695 262.960 225.423 1.00 72.57  ? 3961 LEU A C     1 
ATOM   17712 O  O     . LEU A 1 3961 ? 252.803 262.108 225.338 1.00 72.60  ? 3961 LEU A O     1 
ATOM   17713 C  CB    . LEU A 1 3961 ? 255.797 262.639 224.095 1.00 67.92  ? 3961 LEU A CB    1 
ATOM   17714 C  CG    . LEU A 1 3961 ? 255.771 261.318 223.327 1.00 67.98  ? 3961 LEU A CG    1 
ATOM   17715 C  CD1   . LEU A 1 3961 ? 255.229 261.529 221.926 1.00 70.02  ? 3961 LEU A CD1   1 
ATOM   17716 C  CD2   . LEU A 1 3961 ? 257.156 260.701 223.281 1.00 70.34  ? 3961 LEU A CD2   1 
ATOM   17717 N  N     . ASP A 1 3962 ? 254.018 263.534 226.581 1.00 74.86  ? 3962 ASP A N     1 
ATOM   17718 C  CA    . ASP A 1 3962 ? 253.356 263.196 227.833 1.00 72.47  ? 3962 ASP A CA    1 
ATOM   17719 C  C     . ASP A 1 3962 ? 252.180 264.117 228.140 1.00 74.86  ? 3962 ASP A C     1 
ATOM   17720 O  O     . ASP A 1 3962 ? 251.690 264.127 229.274 1.00 76.63  ? 3962 ASP A O     1 
ATOM   17721 C  CB    . ASP A 1 3962 ? 254.362 263.219 228.983 1.00 74.60  ? 3962 ASP A CB    1 
ATOM   17722 C  CG    . ASP A 1 3962 ? 255.375 262.094 228.894 1.00 80.43  ? 3962 ASP A CG    1 
ATOM   17723 O  OD1   . ASP A 1 3962 ? 255.034 261.026 228.343 1.00 79.62  ? 3962 ASP A OD1   1 
ATOM   17724 O  OD2   . ASP A 1 3962 ? 256.512 262.276 229.376 1.00 80.50  ? 3962 ASP A OD2   1 
ATOM   17725 N  N     . SER A 1 3963 ? 251.723 264.891 227.160 1.00 72.44  ? 3963 SER A N     1 
ATOM   17726 C  CA    . SER A 1 3963 ? 250.573 265.759 227.363 1.00 68.75  ? 3963 SER A CA    1 
ATOM   17727 C  C     . SER A 1 3963 ? 249.300 264.936 227.521 1.00 68.43  ? 3963 SER A C     1 
ATOM   17728 O  O     . SER A 1 3963 ? 249.191 263.815 227.019 1.00 67.40  ? 3963 SER A O     1 
ATOM   17729 C  CB    . SER A 1 3963 ? 250.420 266.731 226.194 1.00 67.62  ? 3963 SER A CB    1 
ATOM   17730 O  OG    . SER A 1 3963 ? 251.558 267.563 226.068 1.00 75.06  ? 3963 SER A OG    1 
ATOM   17731 N  N     . SER A 1 3964 ? 248.331 265.507 228.238 1.00 64.09  ? 3964 SER A N     1 
ATOM   17732 C  CA    . SER A 1 3964 ? 247.062 264.816 228.438 1.00 68.83  ? 3964 SER A CA    1 
ATOM   17733 C  C     . SER A 1 3964 ? 246.278 264.707 227.135 1.00 69.22  ? 3964 SER A C     1 
ATOM   17734 O  O     . SER A 1 3964 ? 245.702 263.655 226.837 1.00 67.05  ? 3964 SER A O     1 
ATOM   17735 C  CB    . SER A 1 3964 ? 246.235 265.532 229.505 1.00 67.51  ? 3964 SER A CB    1 
ATOM   17736 O  OG    . SER A 1 3964 ? 245.806 266.804 229.054 1.00 67.15  ? 3964 SER A OG    1 
ATOM   17737 N  N     . SER A 1 3965 ? 246.247 265.781 226.348 1.00 63.09  ? 3965 SER A N     1 
ATOM   17738 C  CA    . SER A 1 3965 ? 245.533 265.817 225.072 1.00 60.20  ? 3965 SER A CA    1 
ATOM   17739 C  C     . SER A 1 3965 ? 246.479 266.352 224.006 1.00 60.46  ? 3965 SER A C     1 
ATOM   17740 O  O     . SER A 1 3965 ? 246.383 267.518 223.600 1.00 61.55  ? 3965 SER A O     1 
ATOM   17741 C  CB    . SER A 1 3965 ? 244.268 266.669 225.171 1.00 58.65  ? 3965 SER A CB    1 
ATOM   17742 O  OG    . SER A 1 3965 ? 244.578 267.980 225.603 1.00 63.74  ? 3965 SER A OG    1 
ATOM   17743 N  N     . PRO A 1 3966 ? 247.414 265.524 223.532 1.00 54.07  ? 3966 PRO A N     1 
ATOM   17744 C  CA    . PRO A 1 3966 ? 248.363 265.995 222.515 1.00 53.08  ? 3966 PRO A CA    1 
ATOM   17745 C  C     . PRO A 1 3966 ? 247.726 266.269 221.167 1.00 57.84  ? 3966 PRO A C     1 
ATOM   17746 O  O     . PRO A 1 3966 ? 248.332 266.973 220.351 1.00 61.50  ? 3966 PRO A O     1 
ATOM   17747 C  CB    . PRO A 1 3966 ? 249.372 264.847 222.426 1.00 59.64  ? 3966 PRO A CB    1 
ATOM   17748 C  CG    . PRO A 1 3966 ? 248.586 263.651 222.806 1.00 57.12  ? 3966 PRO A CG    1 
ATOM   17749 C  CD    . PRO A 1 3966 ? 247.629 264.108 223.868 1.00 56.30  ? 3966 PRO A CD    1 
ATOM   17750 N  N     . GLU A 1 3967 ? 246.531 265.735 220.906 1.00 61.09  ? 3967 GLU A N     1 
ATOM   17751 C  CA    . GLU A 1 3967 ? 245.903 265.915 219.602 1.00 54.60  ? 3967 GLU A CA    1 
ATOM   17752 C  C     . GLU A 1 3967 ? 245.553 267.372 219.336 1.00 53.35  ? 3967 GLU A C     1 
ATOM   17753 O  O     . GLU A 1 3967 ? 245.411 267.773 218.176 1.00 60.06  ? 3967 GLU A O     1 
ATOM   17754 C  CB    . GLU A 1 3967 ? 244.655 265.037 219.501 1.00 48.26  ? 3967 GLU A CB    1 
ATOM   17755 C  CG    . GLU A 1 3967 ? 243.456 265.583 220.243 1.00 49.04  ? 3967 GLU A CG    1 
ATOM   17756 C  CD    . GLU A 1 3967 ? 243.297 264.972 221.617 1.00 59.11  ? 3967 GLU A CD    1 
ATOM   17757 O  OE1   . GLU A 1 3967 ? 242.338 265.340 222.326 1.00 60.47  ? 3967 GLU A OE1   1 
ATOM   17758 O  OE2   . GLU A 1 3967 ? 244.128 264.119 221.989 1.00 59.52  ? 3967 GLU A OE2   1 
ATOM   17759 N  N     . GLN A 1 3968 ? 245.412 268.179 220.388 1.00 60.16  ? 3968 GLN A N     1 
ATOM   17760 C  CA    . GLN A 1 3968 ? 245.079 269.585 220.208 1.00 61.87  ? 3968 GLN A CA    1 
ATOM   17761 C  C     . GLN A 1 3968 ? 246.271 270.418 219.756 1.00 63.61  ? 3968 GLN A C     1 
ATOM   17762 O  O     . GLN A 1 3968 ? 246.077 271.454 219.113 1.00 64.38  ? 3968 GLN A O     1 
ATOM   17763 C  CB    . GLN A 1 3968 ? 244.511 270.156 221.507 1.00 58.85  ? 3968 GLN A CB    1 
ATOM   17764 C  CG    . GLN A 1 3968 ? 243.117 269.663 221.843 1.00 59.62  ? 3968 GLN A CG    1 
ATOM   17765 C  CD    . GLN A 1 3968 ? 242.624 270.186 223.175 1.00 66.73  ? 3968 GLN A CD    1 
ATOM   17766 O  OE1   . GLN A 1 3968 ? 243.043 271.250 223.630 1.00 65.82  ? 3968 GLN A OE1   1 
ATOM   17767 N  NE2   . GLN A 1 3968 ? 241.730 269.439 223.811 1.00 67.00  ? 3968 GLN A NE2   1 
ATOM   17768 N  N     . THR A 1 3969 ? 247.495 269.998 220.080 1.00 65.21  ? 3969 THR A N     1 
ATOM   17769 C  CA    . THR A 1 3969 ? 248.694 270.789 219.817 1.00 66.66  ? 3969 THR A CA    1 
ATOM   17770 C  C     . THR A 1 3969 ? 249.779 269.915 219.184 1.00 69.09  ? 3969 THR A C     1 
ATOM   17771 O  O     . THR A 1 3969 ? 250.931 269.904 219.606 1.00 73.32  ? 3969 THR A O     1 
ATOM   17772 C  CB    . THR A 1 3969 ? 249.214 271.444 221.097 1.00 68.84  ? 3969 THR A CB    1 
ATOM   17773 O  OG1   . THR A 1 3969 ? 249.520 270.432 222.063 1.00 72.11  ? 3969 THR A OG1   1 
ATOM   17774 C  CG2   . THR A 1 3969 ? 248.181 272.401 221.677 1.00 65.73  ? 3969 THR A CG2   1 
ATOM   17775 N  N     . VAL A 1 3970 ? 249.408 269.162 218.156 1.00 65.45  ? 3970 VAL A N     1 
ATOM   17776 C  CA    . VAL A 1 3970 ? 250.374 268.287 217.479 1.00 58.88  ? 3970 VAL A CA    1 
ATOM   17777 C  C     . VAL A 1 3970 ? 251.470 269.142 216.851 1.00 59.34  ? 3970 VAL A C     1 
ATOM   17778 O  O     . VAL A 1 3970 ? 251.162 270.125 216.155 1.00 61.11  ? 3970 VAL A O     1 
ATOM   17779 C  CB    . VAL A 1 3970 ? 249.671 267.433 216.423 1.00 57.21  ? 3970 VAL A CB    1 
ATOM   17780 C  CG1   . VAL A 1 3970 ? 250.647 266.467 215.780 1.00 59.85  ? 3970 VAL A CG1   1 
ATOM   17781 C  CG2   . VAL A 1 3970 ? 248.505 266.683 217.040 1.00 62.04  ? 3970 VAL A CG2   1 
ATOM   17782 N  N     . PRO A 1 3971 ? 252.745 268.826 217.067 1.00 68.71  ? 3971 PRO A N     1 
ATOM   17783 C  CA    . PRO A 1 3971 ? 253.814 269.660 216.512 1.00 70.77  ? 3971 PRO A CA    1 
ATOM   17784 C  C     . PRO A 1 3971 ? 253.909 269.532 215.001 1.00 75.50  ? 3971 PRO A C     1 
ATOM   17785 O  O     . PRO A 1 3971 ? 253.476 268.544 214.403 1.00 78.97  ? 3971 PRO A O     1 
ATOM   17786 C  CB    . PRO A 1 3971 ? 255.074 269.122 217.196 1.00 68.16  ? 3971 PRO A CB    1 
ATOM   17787 C  CG    . PRO A 1 3971 ? 254.743 267.714 217.517 1.00 69.32  ? 3971 PRO A CG    1 
ATOM   17788 C  CD    . PRO A 1 3971 ? 253.280 267.699 217.849 1.00 72.39  ? 3971 PRO A CD    1 
ATOM   17789 N  N     . TYR A 1 3972 ? 254.491 270.561 214.386 1.00 75.75  ? 3972 TYR A N     1 
ATOM   17790 C  CA    . TYR A 1 3972 ? 254.693 270.611 212.939 1.00 74.10  ? 3972 TYR A CA    1 
ATOM   17791 C  C     . TYR A 1 3972 ? 255.955 269.822 212.584 1.00 75.27  ? 3972 TYR A C     1 
ATOM   17792 O  O     . TYR A 1 3972 ? 257.036 270.366 212.351 1.00 81.24  ? 3972 TYR A O     1 
ATOM   17793 C  CB    . TYR A 1 3972 ? 254.774 272.060 212.481 1.00 73.35  ? 3972 TYR A CB    1 
ATOM   17794 C  CG    . TYR A 1 3972 ? 254.944 272.256 210.995 1.00 78.19  ? 3972 TYR A CG    1 
ATOM   17795 C  CD1   . TYR A 1 3972 ? 253.879 272.083 210.122 1.00 77.77  ? 3972 TYR A CD1   1 
ATOM   17796 C  CD2   . TYR A 1 3972 ? 256.171 272.635 210.467 1.00 80.03  ? 3972 TYR A CD2   1 
ATOM   17797 C  CE1   . TYR A 1 3972 ? 254.037 272.271 208.763 1.00 78.81  ? 3972 TYR A CE1   1 
ATOM   17798 C  CE2   . TYR A 1 3972 ? 256.339 272.822 209.114 1.00 79.07  ? 3972 TYR A CE2   1 
ATOM   17799 C  CZ    . TYR A 1 3972 ? 255.271 272.641 208.266 1.00 80.91  ? 3972 TYR A CZ    1 
ATOM   17800 O  OH    . TYR A 1 3972 ? 255.447 272.833 206.917 1.00 79.36  ? 3972 TYR A OH    1 
ATOM   17801 N  N     . LEU A 1 3973 ? 255.799 268.500 212.553 1.00 70.57  ? 3973 LEU A N     1 
ATOM   17802 C  CA    . LEU A 1 3973 ? 256.910 267.584 212.336 1.00 71.41  ? 3973 LEU A CA    1 
ATOM   17803 C  C     . LEU A 1 3973 ? 257.062 267.153 210.882 1.00 72.90  ? 3973 LEU A C     1 
ATOM   17804 O  O     . LEU A 1 3973 ? 257.906 266.299 210.591 1.00 72.18  ? 3973 LEU A O     1 
ATOM   17805 C  CB    . LEU A 1 3973 ? 256.756 266.347 213.224 1.00 72.88  ? 3973 LEU A CB    1 
ATOM   17806 C  CG    . LEU A 1 3973 ? 256.868 266.561 214.732 1.00 72.81  ? 3973 LEU A CG    1 
ATOM   17807 C  CD1   . LEU A 1 3973 ? 256.887 265.228 215.452 1.00 73.98  ? 3973 LEU A CD1   1 
ATOM   17808 C  CD2   . LEU A 1 3973 ? 258.114 267.362 215.063 1.00 73.20  ? 3973 LEU A CD2   1 
ATOM   17809 N  N     . TRP A 1 3974 ? 256.271 267.707 209.969 1.00 74.04  ? 3974 TRP A N     1 
ATOM   17810 C  CA    . TRP A 1 3974 ? 256.379 267.395 208.551 1.00 73.13  ? 3974 TRP A CA    1 
ATOM   17811 C  C     . TRP A 1 3974 ? 256.746 268.651 207.776 1.00 74.59  ? 3974 TRP A C     1 
ATOM   17812 O  O     . TRP A 1 3974 ? 256.375 269.763 208.164 1.00 70.52  ? 3974 TRP A O     1 
ATOM   17813 C  CB    . TRP A 1 3974 ? 255.076 266.804 208.000 1.00 71.72  ? 3974 TRP A CB    1 
ATOM   17814 C  CG    . TRP A 1 3974 ? 253.921 267.749 208.030 1.00 71.86  ? 3974 TRP A CG    1 
ATOM   17815 C  CD1   . TRP A 1 3974 ? 253.458 268.508 206.998 1.00 71.01  ? 3974 TRP A CD1   1 
ATOM   17816 C  CD2   . TRP A 1 3974 ? 253.068 268.025 209.145 1.00 71.83  ? 3974 TRP A CD2   1 
ATOM   17817 N  NE1   . TRP A 1 3974 ? 252.376 269.250 207.403 1.00 72.47  ? 3974 TRP A NE1   1 
ATOM   17818 C  CE2   . TRP A 1 3974 ? 252.116 268.970 208.718 1.00 72.37  ? 3974 TRP A CE2   1 
ATOM   17819 C  CE3   . TRP A 1 3974 ? 253.020 267.569 210.465 1.00 69.56  ? 3974 TRP A CE3   1 
ATOM   17820 C  CZ2   . TRP A 1 3974 ? 251.128 269.465 209.562 1.00 71.32  ? 3974 TRP A CZ2   1 
ATOM   17821 C  CZ3   . TRP A 1 3974 ? 252.040 268.062 211.300 1.00 69.02  ? 3974 TRP A CZ3   1 
ATOM   17822 C  CH2   . TRP A 1 3974 ? 251.107 269.000 210.847 1.00 74.09  ? 3974 TRP A CH2   1 
ATOM   17823 N  N     . SER A 1 3975 ? 257.486 268.467 206.687 1.00 86.03  ? 3975 SER A N     1 
ATOM   17824 C  CA    . SER A 1 3975 ? 257.909 269.556 205.818 1.00 85.92  ? 3975 SER A CA    1 
ATOM   17825 C  C     . SER A 1 3975 ? 257.290 269.369 204.441 1.00 86.74  ? 3975 SER A C     1 
ATOM   17826 O  O     . SER A 1 3975 ? 257.360 268.277 203.868 1.00 87.17  ? 3975 SER A O     1 
ATOM   17827 C  CB    . SER A 1 3975 ? 259.433 269.611 205.712 1.00 85.75  ? 3975 SER A CB    1 
ATOM   17828 O  OG    . SER A 1 3975 ? 259.950 268.390 205.212 1.00 86.92  ? 3975 SER A OG    1 
ATOM   17829 N  N     . GLU A 1 3976 ? 256.686 270.431 203.916 1.00 93.44  ? 3976 GLU A N     1 
ATOM   17830 C  CA    . GLU A 1 3976 ? 256.036 270.409 202.614 1.00 93.83  ? 3976 GLU A CA    1 
ATOM   17831 C  C     . GLU A 1 3976 ? 256.414 271.663 201.838 1.00 94.24  ? 3976 GLU A C     1 
ATOM   17832 O  O     . GLU A 1 3976 ? 256.763 272.686 202.435 1.00 93.49  ? 3976 GLU A O     1 
ATOM   17833 C  CB    . GLU A 1 3976 ? 254.517 270.295 202.767 1.00 92.53  ? 3976 GLU A CB    1 
ATOM   17834 C  CG    . GLU A 1 3976 ? 253.813 271.607 203.043 1.00 93.55  ? 3976 GLU A CG    1 
ATOM   17835 C  CD    . GLU A 1 3976 ? 253.795 271.969 204.513 1.00 94.23  ? 3976 GLU A CD    1 
ATOM   17836 O  OE1   . GLU A 1 3976 ? 254.817 271.756 205.194 1.00 94.43  ? 3976 GLU A OE1   1 
ATOM   17837 O  OE2   . GLU A 1 3976 ? 252.757 272.475 204.988 1.00 94.61  ? 3976 GLU A OE2   1 
ATOM   17838 N  N     . GLU A 1 3977 ? 256.355 271.574 200.507 1.00 100.23 ? 3977 GLU A N     1 
ATOM   17839 C  CA    . GLU A 1 3977 ? 256.789 272.679 199.657 1.00 100.89 ? 3977 GLU A CA    1 
ATOM   17840 C  C     . GLU A 1 3977 ? 255.843 273.870 199.759 1.00 101.35 ? 3977 GLU A C     1 
ATOM   17841 O  O     . GLU A 1 3977 ? 256.274 275.013 199.945 1.00 100.02 ? 3977 GLU A O     1 
ATOM   17842 C  CB    . GLU A 1 3977 ? 256.907 272.206 198.206 1.00 98.81  ? 3977 GLU A CB    1 
ATOM   17843 C  CG    . GLU A 1 3977 ? 257.909 271.080 197.986 1.00 100.31 ? 3977 GLU A CG    1 
ATOM   17844 C  CD    . GLU A 1 3977 ? 257.332 269.711 198.287 1.00 103.83 ? 3977 GLU A CD    1 
ATOM   17845 O  OE1   . GLU A 1 3977 ? 256.127 269.630 198.602 1.00 103.45 ? 3977 GLU A OE1   1 
ATOM   17846 O  OE2   . GLU A 1 3977 ? 258.084 268.716 198.208 1.00 104.24 ? 3977 GLU A OE2   1 
ATOM   17847 N  N     . THR A 1 3978 ? 254.542 273.619 199.639 1.00 95.06  ? 3978 THR A N     1 
ATOM   17848 C  CA    . THR A 1 3978 ? 253.561 274.690 199.659 1.00 95.93  ? 3978 THR A CA    1 
ATOM   17849 C  C     . THR A 1 3978 ? 252.606 274.514 200.835 1.00 95.41  ? 3978 THR A C     1 
ATOM   17850 O  O     . THR A 1 3978 ? 252.235 273.385 201.169 1.00 93.17  ? 3978 THR A O     1 
ATOM   17851 C  CB    . THR A 1 3978 ? 252.754 274.731 198.356 1.00 96.64  ? 3978 THR A CB    1 
ATOM   17852 O  OG1   . THR A 1 3978 ? 252.010 273.515 198.212 1.00 95.02  ? 3978 THR A OG1   1 
ATOM   17853 C  CG2   . THR A 1 3978 ? 253.680 274.897 197.161 1.00 91.57  ? 3978 THR A CG2   1 
ATOM   17854 N  N     . PRO A 1 3979 ? 252.178 275.609 201.467 1.00 90.90  ? 3979 PRO A N     1 
ATOM   17855 C  CA    . PRO A 1 3979 ? 251.388 275.492 202.702 1.00 88.55  ? 3979 PRO A CA    1 
ATOM   17856 C  C     . PRO A 1 3979 ? 250.156 274.620 202.509 1.00 89.76  ? 3979 PRO A C     1 
ATOM   17857 O  O     . PRO A 1 3979 ? 249.462 274.701 201.494 1.00 87.83  ? 3979 PRO A O     1 
ATOM   17858 C  CB    . PRO A 1 3979 ? 251.000 276.939 203.025 1.00 86.67  ? 3979 PRO A CB    1 
ATOM   17859 C  CG    . PRO A 1 3979 ? 251.900 277.804 202.222 1.00 87.89  ? 3979 PRO A CG    1 
ATOM   17860 C  CD    . PRO A 1 3979 ? 252.587 276.993 201.173 1.00 87.52  ? 3979 PRO A CD    1 
ATOM   17861 N  N     . ALA A 1 3980 ? 249.894 273.779 203.504 1.00 82.81  ? 3980 ALA A N     1 
ATOM   17862 C  CA    . ALA A 1 3980 ? 248.853 272.769 203.415 1.00 79.57  ? 3980 ALA A CA    1 
ATOM   17863 C  C     . ALA A 1 3980 ? 247.498 273.332 203.821 1.00 76.41  ? 3980 ALA A C     1 
ATOM   17864 O  O     . ALA A 1 3980 ? 247.397 274.222 204.670 1.00 74.09  ? 3980 ALA A O     1 
ATOM   17865 C  CB    . ALA A 1 3980 ? 249.197 271.564 204.292 1.00 73.67  ? 3980 ALA A CB    1 
ATOM   17866 N  N     . THR A 1 3981 ? 246.454 272.798 203.197 1.00 62.32  ? 3981 THR A N     1 
ATOM   17867 C  CA    . THR A 1 3981 ? 245.095 273.135 203.575 1.00 66.07  ? 3981 THR A CA    1 
ATOM   17868 C  C     . THR A 1 3981 ? 244.792 272.565 204.962 1.00 64.72  ? 3981 THR A C     1 
ATOM   17869 O  O     . THR A 1 3981 ? 245.453 271.623 205.407 1.00 62.95  ? 3981 THR A O     1 
ATOM   17870 C  CB    . THR A 1 3981 ? 244.117 272.581 202.538 1.00 66.08  ? 3981 THR A CB    1 
ATOM   17871 O  OG1   . THR A 1 3981 ? 242.778 272.981 202.852 1.00 62.13  ? 3981 THR A OG1   1 
ATOM   17872 C  CG2   . THR A 1 3981 ? 244.192 271.068 202.497 1.00 61.22  ? 3981 THR A CG2   1 
ATOM   17873 N  N     . PRO A 1 3982 ? 243.819 273.137 205.679 1.00 62.48  ? 3982 PRO A N     1 
ATOM   17874 C  CA    . PRO A 1 3982 ? 243.489 272.595 207.008 1.00 57.42  ? 3982 PRO A CA    1 
ATOM   17875 C  C     . PRO A 1 3982 ? 243.139 271.118 207.000 1.00 56.70  ? 3982 PRO A C     1 
ATOM   17876 O  O     . PRO A 1 3982 ? 243.428 270.423 207.980 1.00 59.67  ? 3982 PRO A O     1 
ATOM   17877 C  CB    . PRO A 1 3982 ? 242.297 273.458 207.456 1.00 51.89  ? 3982 PRO A CB    1 
ATOM   17878 C  CG    . PRO A 1 3982 ? 241.920 274.297 206.262 1.00 55.94  ? 3982 PRO A CG    1 
ATOM   17879 C  CD    . PRO A 1 3982 ? 243.162 274.432 205.456 1.00 56.85  ? 3982 PRO A CD    1 
ATOM   17880 N  N     . ILE A 1 3983 ? 242.529 270.612 205.927 1.00 51.14  ? 3983 ILE A N     1 
ATOM   17881 C  CA    . ILE A 1 3983 ? 242.248 269.182 205.842 1.00 48.47  ? 3983 ILE A CA    1 
ATOM   17882 C  C     . ILE A 1 3983 ? 243.542 268.383 205.727 1.00 53.24  ? 3983 ILE A C     1 
ATOM   17883 O  O     . ILE A 1 3983 ? 243.703 267.340 206.372 1.00 62.97  ? 3983 ILE A O     1 
ATOM   17884 C  CB    . ILE A 1 3983 ? 241.299 268.899 204.666 1.00 50.62  ? 3983 ILE A CB    1 
ATOM   17885 C  CG1   . ILE A 1 3983 ? 240.002 269.691 204.834 1.00 54.21  ? 3983 ILE A CG1   1 
ATOM   17886 C  CG2   . ILE A 1 3983 ? 241.017 267.415 204.563 1.00 44.96  ? 3983 ILE A CG2   1 
ATOM   17887 C  CD1   . ILE A 1 3983 ? 239.036 269.535 203.684 1.00 49.22  ? 3983 ILE A CD1   1 
ATOM   17888 N  N     . GLY A 1 3984 ? 244.480 268.846 204.898 1.00 49.58  ? 3984 GLY A N     1 
ATOM   17889 C  CA    . GLY A 1 3984 ? 245.766 268.178 204.805 1.00 49.24  ? 3984 GLY A CA    1 
ATOM   17890 C  C     . GLY A 1 3984 ? 246.553 268.242 206.095 1.00 52.26  ? 3984 GLY A C     1 
ATOM   17891 O  O     . GLY A 1 3984 ? 247.205 267.265 206.482 1.00 57.44  ? 3984 GLY A O     1 
ATOM   17892 N  N     . GLN A 1 3985 ? 246.500 269.385 206.782 1.00 58.87  ? 3985 GLN A N     1 
ATOM   17893 C  CA    . GLN A 1 3985 ? 247.086 269.474 208.112 1.00 53.26  ? 3985 GLN A CA    1 
ATOM   17894 C  C     . GLN A 1 3985 ? 246.449 268.462 209.051 1.00 57.48  ? 3985 GLN A C     1 
ATOM   17895 O  O     . GLN A 1 3985 ? 247.147 267.806 209.827 1.00 65.78  ? 3985 GLN A O     1 
ATOM   17896 C  CB    . GLN A 1 3985 ? 246.923 270.887 208.669 1.00 53.51  ? 3985 GLN A CB    1 
ATOM   17897 C  CG    . GLN A 1 3985 ? 248.035 271.844 208.291 1.00 62.08  ? 3985 GLN A CG    1 
ATOM   17898 C  CD    . GLN A 1 3985 ? 247.938 273.158 209.038 1.00 64.81  ? 3985 GLN A CD    1 
ATOM   17899 O  OE1   . GLN A 1 3985 ? 246.847 273.604 209.391 1.00 63.14  ? 3985 GLN A OE1   1 
ATOM   17900 N  NE2   . GLN A 1 3985 ? 249.083 273.783 209.287 1.00 60.19  ? 3985 GLN A NE2   1 
ATOM   17901 N  N     . ALA A 1 3986 ? 245.123 268.320 208.990 1.00 50.12  ? 3986 ALA A N     1 
ATOM   17902 C  CA    . ALA A 1 3986 ? 244.438 267.360 209.848 1.00 38.32  ? 3986 ALA A CA    1 
ATOM   17903 C  C     . ALA A 1 3986 ? 244.896 265.939 209.559 1.00 43.28  ? 3986 ALA A C     1 
ATOM   17904 O  O     . ALA A 1 3986 ? 245.099 265.148 210.484 1.00 57.92  ? 3986 ALA A O     1 
ATOM   17905 C  CB    . ALA A 1 3986 ? 242.926 267.482 209.672 1.00 46.16  ? 3986 ALA A CB    1 
ATOM   17906 N  N     . ILE A 1 3987 ? 245.067 265.596 208.282 1.00 45.10  ? 3987 ILE A N     1 
ATOM   17907 C  CA    . ILE A 1 3987 ? 245.530 264.254 207.931 1.00 51.23  ? 3987 ILE A CA    1 
ATOM   17908 C  C     . ILE A 1 3987 ? 246.944 264.020 208.450 1.00 54.06  ? 3987 ILE A C     1 
ATOM   17909 O  O     . ILE A 1 3987 ? 247.262 262.945 208.976 1.00 57.99  ? 3987 ILE A O     1 
ATOM   17910 C  CB    . ILE A 1 3987 ? 245.445 264.030 206.411 1.00 47.78  ? 3987 ILE A CB    1 
ATOM   17911 C  CG1   . ILE A 1 3987 ? 244.020 264.253 205.921 1.00 53.40  ? 3987 ILE A CG1   1 
ATOM   17912 C  CG2   . ILE A 1 3987 ? 245.890 262.628 206.059 1.00 48.16  ? 3987 ILE A CG2   1 
ATOM   17913 C  CD1   . ILE A 1 3987 ? 243.843 264.007 204.454 1.00 57.23  ? 3987 ILE A CD1   1 
ATOM   17914 N  N     . HIS A 1 3988 ? 247.820 265.016 208.299 1.00 52.00  ? 3988 HIS A N     1 
ATOM   17915 C  CA    . HIS A 1 3988 ? 249.192 264.857 208.774 1.00 49.02  ? 3988 HIS A CA    1 
ATOM   17916 C  C     . HIS A 1 3988 ? 249.246 264.720 210.293 1.00 56.27  ? 3988 HIS A C     1 
ATOM   17917 O  O     . HIS A 1 3988 ? 249.991 263.885 210.822 1.00 62.13  ? 3988 HIS A O     1 
ATOM   17918 C  CB    . HIS A 1 3988 ? 250.044 266.027 208.294 1.00 52.68  ? 3988 HIS A CB    1 
ATOM   17919 C  CG    . HIS A 1 3988 ? 250.404 265.949 206.844 1.00 57.59  ? 3988 HIS A CG    1 
ATOM   17920 N  ND1   . HIS A 1 3988 ? 249.886 266.809 205.901 1.00 59.28  ? 3988 HIS A ND1   1 
ATOM   17921 C  CD2   . HIS A 1 3988 ? 251.224 265.105 206.173 1.00 57.76  ? 3988 HIS A CD2   1 
ATOM   17922 C  CE1   . HIS A 1 3988 ? 250.375 266.502 204.713 1.00 57.17  ? 3988 HIS A CE1   1 
ATOM   17923 N  NE2   . HIS A 1 3988 ? 251.189 265.472 204.850 1.00 57.39  ? 3988 HIS A NE2   1 
ATOM   17924 N  N     . ARG A 1 3989 ? 248.456 265.522 211.012 1.00 51.91  ? 3989 ARG A N     1 
ATOM   17925 C  CA    . ARG A 1 3989 ? 248.388 265.383 212.463 1.00 45.09  ? 3989 ARG A CA    1 
ATOM   17926 C  C     . ARG A 1 3989 ? 247.789 264.042 212.861 1.00 48.28  ? 3989 ARG A C     1 
ATOM   17927 O  O     . ARG A 1 3989 ? 248.168 263.468 213.884 1.00 55.08  ? 3989 ARG A O     1 
ATOM   17928 C  CB    . ARG A 1 3989 ? 247.581 266.527 213.075 1.00 47.45  ? 3989 ARG A CB    1 
ATOM   17929 C  CG    . ARG A 1 3989 ? 248.006 267.913 212.647 1.00 46.18  ? 3989 ARG A CG    1 
ATOM   17930 C  CD    . ARG A 1 3989 ? 247.820 268.924 213.755 1.00 51.63  ? 3989 ARG A CD    1 
ATOM   17931 N  NE    . ARG A 1 3989 ? 247.746 270.284 213.236 1.00 54.20  ? 3989 ARG A NE    1 
ATOM   17932 C  CZ    . ARG A 1 3989 ? 246.615 270.947 213.042 1.00 61.33  ? 3989 ARG A CZ    1 
ATOM   17933 N  NH1   . ARG A 1 3989 ? 245.440 270.403 213.313 1.00 59.00  ? 3989 ARG A NH1   1 
ATOM   17934 N  NH2   . ARG A 1 3989 ? 246.663 272.187 212.563 1.00 55.98  ? 3989 ARG A NH2   1 
ATOM   17935 N  N     . LEU A 1 3990 ? 246.839 263.533 212.074 1.00 44.57  ? 3990 LEU A N     1 
ATOM   17936 C  CA    . LEU A 1 3990 ? 246.277 262.215 212.345 1.00 44.50  ? 3990 LEU A CA    1 
ATOM   17937 C  C     . LEU A 1 3990 ? 247.341 261.135 212.222 1.00 46.23  ? 3990 LEU A C     1 
ATOM   17938 O  O     . LEU A 1 3990 ? 247.426 260.234 213.066 1.00 54.52  ? 3990 LEU A O     1 
ATOM   17939 C  CB    . LEU A 1 3990 ? 245.113 261.947 211.390 1.00 47.22  ? 3990 LEU A CB    1 
ATOM   17940 C  CG    . LEU A 1 3990 ? 244.242 260.707 211.587 1.00 48.82  ? 3990 LEU A CG    1 
ATOM   17941 C  CD1   . LEU A 1 3990 ? 243.847 260.544 213.037 1.00 51.01  ? 3990 LEU A CD1   1 
ATOM   17942 C  CD2   . LEU A 1 3990 ? 243.010 260.803 210.708 1.00 42.50  ? 3990 LEU A CD2   1 
ATOM   17943 N  N     . LEU A 1 3991 ? 248.172 261.219 211.184 1.00 53.32  ? 3991 LEU A N     1 
ATOM   17944 C  CA    . LEU A 1 3991 ? 249.274 260.272 211.039 1.00 53.01  ? 3991 LEU A CA    1 
ATOM   17945 C  C     . LEU A 1 3991 ? 250.259 260.387 212.198 1.00 52.77  ? 3991 LEU A C     1 
ATOM   17946 O  O     . LEU A 1 3991 ? 250.719 259.371 212.736 1.00 52.90  ? 3991 LEU A O     1 
ATOM   17947 C  CB    . LEU A 1 3991 ? 249.987 260.500 209.707 1.00 51.66  ? 3991 LEU A CB    1 
ATOM   17948 C  CG    . LEU A 1 3991 ? 249.211 260.144 208.441 1.00 50.10  ? 3991 LEU A CG    1 
ATOM   17949 C  CD1   . LEU A 1 3991 ? 249.984 260.584 207.216 1.00 53.82  ? 3991 LEU A CD1   1 
ATOM   17950 C  CD2   . LEU A 1 3991 ? 248.931 258.657 208.390 1.00 49.74  ? 3991 LEU A CD2   1 
ATOM   17951 N  N     . LEU A 1 3992 ? 250.589 261.617 212.597 1.00 48.95  ? 3992 LEU A N     1 
ATOM   17952 C  CA    . LEU A 1 3992 ? 251.512 261.811 213.711 1.00 48.58  ? 3992 LEU A CA    1 
ATOM   17953 C  C     . LEU A 1 3992 ? 250.944 261.254 215.013 1.00 49.63  ? 3992 LEU A C     1 
ATOM   17954 O  O     . LEU A 1 3992 ? 251.670 260.631 215.794 1.00 54.80  ? 3992 LEU A O     1 
ATOM   17955 C  CB    . LEU A 1 3992 ? 251.845 263.293 213.864 1.00 54.29  ? 3992 LEU A CB    1 
ATOM   17956 C  CG    . LEU A 1 3992 ? 252.950 263.834 212.957 1.00 51.58  ? 3992 LEU A CG    1 
ATOM   17957 C  CD1   . LEU A 1 3992 ? 253.186 265.302 213.239 1.00 51.53  ? 3992 LEU A CD1   1 
ATOM   17958 C  CD2   . LEU A 1 3992 ? 254.228 263.041 213.143 1.00 55.31  ? 3992 LEU A CD2   1 
ATOM   17959 N  N     . ILE A 1 3993 ? 249.653 261.478 215.266 1.00 49.24  ? 3993 ILE A N     1 
ATOM   17960 C  CA    . ILE A 1 3993 ? 249.014 260.955 216.471 1.00 45.93  ? 3993 ILE A CA    1 
ATOM   17961 C  C     . ILE A 1 3993 ? 248.995 259.434 216.446 1.00 41.05  ? 3993 ILE A C     1 
ATOM   17962 O  O     . ILE A 1 3993 ? 249.229 258.780 217.468 1.00 55.51  ? 3993 ILE A O     1 
ATOM   17963 C  CB    . ILE A 1 3993 ? 247.598 261.540 216.622 1.00 53.61  ? 3993 ILE A CB    1 
ATOM   17964 C  CG1   . ILE A 1 3993 ? 247.661 262.979 217.137 1.00 53.03  ? 3993 ILE A CG1   1 
ATOM   17965 C  CG2   . ILE A 1 3993 ? 246.760 260.690 217.557 1.00 51.04  ? 3993 ILE A CG2   1 
ATOM   17966 C  CD1   . ILE A 1 3993 ? 248.113 263.091 218.572 1.00 47.77  ? 3993 ILE A CD1   1 
ATOM   17967 N  N     . GLN A 1 3994 ? 248.717 258.845 215.281 1.00 45.66  ? 3994 GLN A N     1 
ATOM   17968 C  CA    . GLN A 1 3994 ? 248.754 257.392 215.169 1.00 46.01  ? 3994 GLN A CA    1 
ATOM   17969 C  C     . GLN A 1 3994 ? 250.141 256.854 215.482 1.00 49.00  ? 3994 GLN A C     1 
ATOM   17970 O  O     . GLN A 1 3994 ? 250.282 255.830 216.160 1.00 51.09  ? 3994 GLN A O     1 
ATOM   17971 C  CB    . GLN A 1 3994 ? 248.322 256.962 213.769 1.00 46.47  ? 3994 GLN A CB    1 
ATOM   17972 C  CG    . GLN A 1 3994 ? 248.023 255.483 213.641 1.00 48.23  ? 3994 GLN A CG    1 
ATOM   17973 C  CD    . GLN A 1 3994 ? 248.059 255.013 212.205 1.00 54.78  ? 3994 GLN A CD    1 
ATOM   17974 O  OE1   . GLN A 1 3994 ? 248.654 255.659 211.346 1.00 57.93  ? 3994 GLN A OE1   1 
ATOM   17975 N  NE2   . GLN A 1 3994 ? 247.417 253.883 211.935 1.00 49.50  ? 3994 GLN A NE2   1 
ATOM   17976 N  N     . ALA A 1 3995 ? 251.181 257.532 214.994 1.00 58.36  ? 3995 ALA A N     1 
ATOM   17977 C  CA    . ALA A 1 3995 ? 252.541 257.064 215.236 1.00 56.92  ? 3995 ALA A CA    1 
ATOM   17978 C  C     . ALA A 1 3995 ? 252.941 257.222 216.699 1.00 56.91  ? 3995 ALA A C     1 
ATOM   17979 O  O     . ALA A 1 3995 ? 253.542 256.314 217.285 1.00 59.83  ? 3995 ALA A O     1 
ATOM   17980 C  CB    . ALA A 1 3995 ? 253.520 257.809 214.331 1.00 55.16  ? 3995 ALA A CB    1 
ATOM   17981 N  N     . PHE A 1 3996 ? 252.611 258.359 217.310 1.00 58.28  ? 3996 PHE A N     1 
ATOM   17982 C  CA    . PHE A 1 3996 ? 253.140 258.706 218.624 1.00 53.65  ? 3996 PHE A CA    1 
ATOM   17983 C  C     . PHE A 1 3996 ? 252.196 258.335 219.763 1.00 57.64  ? 3996 PHE A C     1 
ATOM   17984 O  O     . PHE A 1 3996 ? 252.603 257.657 220.711 1.00 65.12  ? 3996 PHE A O     1 
ATOM   17985 C  CB    . PHE A 1 3996 ? 253.453 260.203 218.673 1.00 53.46  ? 3996 PHE A CB    1 
ATOM   17986 C  CG    . PHE A 1 3996 ? 254.692 260.584 217.924 1.00 59.15  ? 3996 PHE A CG    1 
ATOM   17987 C  CD1   . PHE A 1 3996 ? 255.918 260.052 218.275 1.00 61.85  ? 3996 PHE A CD1   1 
ATOM   17988 C  CD2   . PHE A 1 3996 ? 254.631 261.467 216.861 1.00 62.86  ? 3996 PHE A CD2   1 
ATOM   17989 C  CE1   . PHE A 1 3996 ? 257.057 260.399 217.588 1.00 61.47  ? 3996 PHE A CE1   1 
ATOM   17990 C  CE2   . PHE A 1 3996 ? 255.770 261.815 216.168 1.00 60.14  ? 3996 PHE A CE2   1 
ATOM   17991 C  CZ    . PHE A 1 3996 ? 256.985 261.280 216.532 1.00 60.56  ? 3996 PHE A CZ    1 
ATOM   17992 N  N     . ARG A 1 3997 ? 250.941 258.771 219.692 1.00 57.26  ? 3997 ARG A N     1 
ATOM   17993 C  CA    . ARG A 1 3997 ? 249.982 258.615 220.785 1.00 53.14  ? 3997 ARG A CA    1 
ATOM   17994 C  C     . ARG A 1 3997 ? 248.739 257.912 220.259 1.00 52.97  ? 3997 ARG A C     1 
ATOM   17995 O  O     . ARG A 1 3997 ? 247.718 258.554 219.982 1.00 58.93  ? 3997 ARG A O     1 
ATOM   17996 C  CB    . ARG A 1 3997 ? 249.627 259.969 221.400 1.00 53.82  ? 3997 ARG A CB    1 
ATOM   17997 C  CG    . ARG A 1 3997 ? 250.792 260.678 222.072 1.00 53.26  ? 3997 ARG A CG    1 
ATOM   17998 C  CD    . ARG A 1 3997 ? 251.141 260.026 223.397 1.00 56.05  ? 3997 ARG A CD    1 
ATOM   17999 N  NE    . ARG A 1 3997 ? 249.974 259.888 224.259 1.00 57.55  ? 3997 ARG A NE    1 
ATOM   18000 C  CZ    . ARG A 1 3997 ? 249.527 260.831 225.077 1.00 56.51  ? 3997 ARG A CZ    1 
ATOM   18001 N  NH1   . ARG A 1 3997 ? 250.141 261.997 225.188 1.00 54.58  ? 3997 ARG A NH1   1 
ATOM   18002 N  NH2   . ARG A 1 3997 ? 248.439 260.598 225.803 1.00 57.51  ? 3997 ARG A NH2   1 
ATOM   18003 N  N     . PRO A 1 3998 ? 248.792 256.587 220.103 1.00 45.46  ? 3998 PRO A N     1 
ATOM   18004 C  CA    . PRO A 1 3998 ? 247.615 255.861 219.599 1.00 47.98  ? 3998 PRO A CA    1 
ATOM   18005 C  C     . PRO A 1 3998 ? 246.400 255.956 220.504 1.00 55.79  ? 3998 PRO A C     1 
ATOM   18006 O  O     . PRO A 1 3998 ? 245.277 255.769 220.023 1.00 56.93  ? 3998 PRO A O     1 
ATOM   18007 C  CB    . PRO A 1 3998 ? 248.116 254.415 219.484 1.00 46.98  ? 3998 PRO A CB    1 
ATOM   18008 C  CG    . PRO A 1 3998 ? 249.298 254.342 220.381 1.00 51.43  ? 3998 PRO A CG    1 
ATOM   18009 C  CD    . PRO A 1 3998 ? 249.934 255.692 220.344 1.00 55.04  ? 3998 PRO A CD    1 
ATOM   18010 N  N     . ASP A 1 3999 ? 246.580 256.236 221.797 1.00 53.21  ? 3999 ASP A N     1 
ATOM   18011 C  CA    . ASP A 1 3999 ? 245.432 256.389 222.683 1.00 50.48  ? 3999 ASP A CA    1 
ATOM   18012 C  C     . ASP A 1 3999 ? 244.623 257.640 222.369 1.00 54.75  ? 3999 ASP A C     1 
ATOM   18013 O  O     . ASP A 1 3999 ? 243.461 257.728 222.775 1.00 59.08  ? 3999 ASP A O     1 
ATOM   18014 C  CB    . ASP A 1 3999 ? 245.887 256.411 224.143 1.00 50.36  ? 3999 ASP A CB    1 
ATOM   18015 C  CG    . ASP A 1 3999 ? 247.040 257.362 224.381 1.00 56.89  ? 3999 ASP A CG    1 
ATOM   18016 O  OD1   . ASP A 1 3999 ? 248.181 257.016 224.012 1.00 60.73  ? 3999 ASP A OD1   1 
ATOM   18017 O  OD2   . ASP A 1 3999 ? 246.808 258.453 224.941 1.00 50.89  ? 3999 ASP A OD2   1 
ATOM   18018 N  N     . ARG A 1 4000 ? 245.206 258.603 221.661 1.00 49.06  ? 4000 ARG A N     1 
ATOM   18019 C  CA    . ARG A 1 4000 ? 244.495 259.795 221.224 1.00 47.58  ? 4000 ARG A CA    1 
ATOM   18020 C  C     . ARG A 1 4000 ? 244.086 259.724 219.760 1.00 50.37  ? 4000 ARG A C     1 
ATOM   18021 O  O     . ARG A 1 4000 ? 243.739 260.752 219.173 1.00 58.18  ? 4000 ARG A O     1 
ATOM   18022 C  CB    . ARG A 1 4000 ? 245.347 261.040 221.470 1.00 44.02  ? 4000 ARG A CB    1 
ATOM   18023 C  CG    . ARG A 1 4000 ? 245.927 261.122 222.865 1.00 46.50  ? 4000 ARG A CG    1 
ATOM   18024 C  CD    . ARG A 1 4000 ? 244.845 261.028 223.923 1.00 51.72  ? 4000 ARG A CD    1 
ATOM   18025 N  NE    . ARG A 1 4000 ? 243.885 262.121 223.829 1.00 53.85  ? 4000 ARG A NE    1 
ATOM   18026 C  CZ    . ARG A 1 4000 ? 242.729 262.157 224.477 1.00 55.35  ? 4000 ARG A CZ    1 
ATOM   18027 N  NH1   . ARG A 1 4000 ? 242.354 261.171 225.275 1.00 52.99  ? 4000 ARG A NH1   1 
ATOM   18028 N  NH2   . ARG A 1 4000 ? 241.930 263.207 224.321 1.00 48.67  ? 4000 ARG A NH2   1 
ATOM   18029 N  N     . LEU A 1 4001 ? 244.130 258.534 219.156 1.00 45.85  ? 4001 LEU A N     1 
ATOM   18030 C  CA    . LEU A 1 4001 ? 243.757 258.400 217.752 1.00 42.25  ? 4001 LEU A CA    1 
ATOM   18031 C  C     . LEU A 1 4001 ? 242.281 258.705 217.536 1.00 44.75  ? 4001 LEU A C     1 
ATOM   18032 O  O     . LEU A 1 4001 ? 241.907 259.290 216.515 1.00 63.98  ? 4001 LEU A O     1 
ATOM   18033 C  CB    . LEU A 1 4001 ? 244.090 256.996 217.251 1.00 44.66  ? 4001 LEU A CB    1 
ATOM   18034 C  CG    . LEU A 1 4001 ? 244.105 256.827 215.733 1.00 40.26  ? 4001 LEU A CG    1 
ATOM   18035 C  CD1   . LEU A 1 4001 ? 245.059 257.823 215.111 1.00 43.17  ? 4001 LEU A CD1   1 
ATOM   18036 C  CD2   . LEU A 1 4001 ? 244.489 255.411 215.354 1.00 50.16  ? 4001 LEU A CD2   1 
ATOM   18037 N  N     . LEU A 1 4002 ? 241.425 258.301 218.477 1.00 36.94  ? 4002 LEU A N     1 
ATOM   18038 C  CA    . LEU A 1 4002 ? 239.994 258.549 218.326 1.00 38.01  ? 4002 LEU A CA    1 
ATOM   18039 C  C     . LEU A 1 4002 ? 239.679 260.040 218.373 1.00 42.63  ? 4002 LEU A C     1 
ATOM   18040 O  O     . LEU A 1 4002 ? 238.863 260.535 217.587 1.00 49.02  ? 4002 LEU A O     1 
ATOM   18041 C  CB    . LEU A 1 4002 ? 239.218 257.803 219.408 1.00 43.36  ? 4002 LEU A CB    1 
ATOM   18042 C  CG    . LEU A 1 4002 ? 239.023 256.302 219.196 1.00 44.04  ? 4002 LEU A CG    1 
ATOM   18043 C  CD1   . LEU A 1 4002 ? 238.004 255.765 220.182 1.00 44.98  ? 4002 LEU A CD1   1 
ATOM   18044 C  CD2   . LEU A 1 4002 ? 238.600 256.005 217.769 1.00 38.93  ? 4002 LEU A CD2   1 
ATOM   18045 N  N     . ALA A 1 4003 ? 240.319 260.773 219.285 1.00 33.66  ? 4003 ALA A N     1 
ATOM   18046 C  CA    . ALA A 1 4003 ? 240.084 262.210 219.372 1.00 31.52  ? 4003 ALA A CA    1 
ATOM   18047 C  C     . ALA A 1 4003 ? 240.582 262.929 218.126 1.00 40.09  ? 4003 ALA A C     1 
ATOM   18048 O  O     . ALA A 1 4003 ? 239.934 263.863 217.637 1.00 45.57  ? 4003 ALA A O     1 
ATOM   18049 C  CB    . ALA A 1 4003 ? 240.750 262.774 220.624 1.00 40.46  ? 4003 ALA A CB    1 
ATOM   18050 N  N     . MET A 1 4004 ? 241.727 262.507 217.590 1.00 41.78  ? 4004 MET A N     1 
ATOM   18051 C  CA    . MET A 1 4004 ? 242.220 263.127 216.367 1.00 35.59  ? 4004 MET A CA    1 
ATOM   18052 C  C     . MET A 1 4004 ? 241.349 262.771 215.169 1.00 43.94  ? 4004 MET A C     1 
ATOM   18053 O  O     . MET A 1 4004 ? 241.186 263.591 214.260 1.00 57.76  ? 4004 MET A O     1 
ATOM   18054 C  CB    . MET A 1 4004 ? 243.670 262.727 216.115 1.00 34.93  ? 4004 MET A CB    1 
ATOM   18055 C  CG    . MET A 1 4004 ? 244.318 263.549 215.024 1.00 47.90  ? 4004 MET A CG    1 
ATOM   18056 S  SD    . MET A 1 4004 ? 244.104 265.313 215.312 1.00 58.24  ? 4004 MET A SD    1 
ATOM   18057 C  CE    . MET A 1 4004 ? 244.090 265.934 213.636 1.00 43.76  ? 4004 MET A CE    1 
ATOM   18058 N  N     . ALA A 1 4005 ? 240.777 261.565 215.146 1.00 32.88  ? 4005 ALA A N     1 
ATOM   18059 C  CA    . ALA A 1 4005 ? 239.807 261.234 214.107 1.00 24.27  ? 4005 ALA A CA    1 
ATOM   18060 C  C     . ALA A 1 4005 ? 238.561 262.099 214.221 1.00 38.28  ? 4005 ALA A C     1 
ATOM   18061 O  O     . ALA A 1 4005 ? 237.999 262.521 213.204 1.00 54.09  ? 4005 ALA A O     1 
ATOM   18062 C  CB    . ALA A 1 4005 ? 239.440 259.754 214.180 1.00 26.34  ? 4005 ALA A CB    1 
ATOM   18063 N  N     . HIS A 1 4006 ? 238.115 262.368 215.449 1.00 35.56  ? 4006 HIS A N     1 
ATOM   18064 C  CA    . HIS A 1 4006 ? 236.998 263.286 215.648 1.00 33.80  ? 4006 HIS A CA    1 
ATOM   18065 C  C     . HIS A 1 4006 ? 237.336 264.677 215.128 1.00 40.54  ? 4006 HIS A C     1 
ATOM   18066 O  O     . HIS A 1 4006 ? 236.500 265.336 214.500 1.00 43.39  ? 4006 HIS A O     1 
ATOM   18067 C  CB    . HIS A 1 4006 ? 236.630 263.345 217.128 1.00 33.62  ? 4006 HIS A CB    1 
ATOM   18068 C  CG    . HIS A 1 4006 ? 235.754 262.220 217.579 1.00 42.10  ? 4006 HIS A CG    1 
ATOM   18069 N  ND1   . HIS A 1 4006 ? 236.172 260.907 217.579 1.00 45.01  ? 4006 HIS A ND1   1 
ATOM   18070 C  CD2   . HIS A 1 4006 ? 234.487 262.211 218.053 1.00 46.12  ? 4006 HIS A CD2   1 
ATOM   18071 C  CE1   . HIS A 1 4006 ? 235.197 260.137 218.026 1.00 42.81  ? 4006 HIS A CE1   1 
ATOM   18072 N  NE2   . HIS A 1 4006 ? 234.163 260.903 218.321 1.00 50.04  ? 4006 HIS A NE2   1 
ATOM   18073 N  N     . MET A 1 4007 ? 238.561 265.139 215.383 1.00 48.04  ? 4007 MET A N     1 
ATOM   18074 C  CA    . MET A 1 4007 ? 238.985 266.440 214.871 1.00 43.59  ? 4007 MET A CA    1 
ATOM   18075 C  C     . MET A 1 4007 ? 239.040 266.450 213.347 1.00 42.22  ? 4007 MET A C     1 
ATOM   18076 O  O     . MET A 1 4007 ? 238.700 267.455 212.717 1.00 47.47  ? 4007 MET A O     1 
ATOM   18077 C  CB    . MET A 1 4007 ? 240.341 266.825 215.456 1.00 43.22  ? 4007 MET A CB    1 
ATOM   18078 C  CG    . MET A 1 4007 ? 240.277 267.341 216.880 1.00 45.05  ? 4007 MET A CG    1 
ATOM   18079 S  SD    . MET A 1 4007 ? 241.906 267.455 217.634 1.00 63.48  ? 4007 MET A SD    1 
ATOM   18080 C  CE    . MET A 1 4007 ? 242.741 268.521 216.462 1.00 44.06  ? 4007 MET A CE    1 
ATOM   18081 N  N     . PHE A 1 4008 ? 239.486 265.349 212.739 1.00 38.00  ? 4008 PHE A N     1 
ATOM   18082 C  CA    . PHE A 1 4008 ? 239.494 265.244 211.282 1.00 39.82  ? 4008 PHE A CA    1 
ATOM   18083 C  C     . PHE A 1 4008 ? 238.079 265.320 210.716 1.00 44.08  ? 4008 PHE A C     1 
ATOM   18084 O  O     . PHE A 1 4008 ? 237.826 266.032 209.732 1.00 49.88  ? 4008 PHE A O     1 
ATOM   18085 C  CB    . PHE A 1 4008 ? 240.179 263.938 210.880 1.00 35.97  ? 4008 PHE A CB    1 
ATOM   18086 C  CG    . PHE A 1 4008 ? 240.138 263.642 209.410 1.00 41.98  ? 4008 PHE A CG    1 
ATOM   18087 C  CD1   . PHE A 1 4008 ? 240.897 264.375 208.518 1.00 45.71  ? 4008 PHE A CD1   1 
ATOM   18088 C  CD2   . PHE A 1 4008 ? 239.365 262.603 208.925 1.00 41.39  ? 4008 PHE A CD2   1 
ATOM   18089 C  CE1   . PHE A 1 4008 ? 240.867 264.089 207.170 1.00 37.78  ? 4008 PHE A CE1   1 
ATOM   18090 C  CE2   . PHE A 1 4008 ? 239.334 262.313 207.578 1.00 40.59  ? 4008 PHE A CE2   1 
ATOM   18091 C  CZ    . PHE A 1 4008 ? 240.089 263.055 206.701 1.00 40.20  ? 4008 PHE A CZ    1 
ATOM   18092 N  N     . VAL A 1 4009 ? 237.140 264.607 211.342 1.00 41.86  ? 4009 VAL A N     1 
ATOM   18093 C  CA    . VAL A 1 4009 ? 235.741 264.675 210.931 1.00 34.60  ? 4009 VAL A CA    1 
ATOM   18094 C  C     . VAL A 1 4009 ? 235.221 266.101 211.050 1.00 40.01  ? 4009 VAL A C     1 
ATOM   18095 O  O     . VAL A 1 4009 ? 234.530 266.604 210.156 1.00 46.46  ? 4009 VAL A O     1 
ATOM   18096 C  CB    . VAL A 1 4009 ? 234.894 263.693 211.762 1.00 33.34  ? 4009 VAL A CB    1 
ATOM   18097 C  CG1   . VAL A 1 4009 ? 233.415 263.927 211.523 1.00 32.11  ? 4009 VAL A CG1   1 
ATOM   18098 C  CG2   . VAL A 1 4009 ? 235.267 262.263 211.431 1.00 41.45  ? 4009 VAL A CG2   1 
ATOM   18099 N  N     . SER A 1 4010 ? 235.549 266.777 212.154 1.00 38.12  ? 4010 SER A N     1 
ATOM   18100 C  CA    . SER A 1 4010 ? 235.121 268.160 212.334 1.00 34.08  ? 4010 SER A CA    1 
ATOM   18101 C  C     . SER A 1 4010 ? 235.713 269.075 211.271 1.00 41.45  ? 4010 SER A C     1 
ATOM   18102 O  O     . SER A 1 4010 ? 235.031 269.984 210.785 1.00 47.11  ? 4010 SER A O     1 
ATOM   18103 C  CB    . SER A 1 4010 ? 235.506 268.650 213.728 1.00 42.34  ? 4010 SER A CB    1 
ATOM   18104 O  OG    . SER A 1 4010 ? 234.938 267.826 214.729 1.00 46.14  ? 4010 SER A OG    1 
ATOM   18105 N  N     . THR A 1 4011 ? 236.977 268.858 210.907 1.00 46.34  ? 4011 THR A N     1 
ATOM   18106 C  CA    . THR A 1 4011 ? 237.599 269.650 209.853 1.00 43.10  ? 4011 THR A CA    1 
ATOM   18107 C  C     . THR A 1 4011 ? 236.895 269.454 208.519 1.00 47.76  ? 4011 THR A C     1 
ATOM   18108 O  O     . THR A 1 4011 ? 236.715 270.418 207.767 1.00 49.85  ? 4011 THR A O     1 
ATOM   18109 C  CB    . THR A 1 4011 ? 239.079 269.292 209.723 1.00 42.60  ? 4011 THR A CB    1 
ATOM   18110 O  OG1   . THR A 1 4011 ? 239.726 269.456 210.990 1.00 54.17  ? 4011 THR A OG1   1 
ATOM   18111 C  CG2   . THR A 1 4011 ? 239.755 270.183 208.699 1.00 46.16  ? 4011 THR A CG2   1 
ATOM   18112 N  N     . ASN A 1 4012 ? 236.487 268.224 208.207 1.00 48.71  ? 4012 ASN A N     1 
ATOM   18113 C  CA    . ASN A 1 4012 ? 235.789 267.978 206.948 1.00 40.11  ? 4012 ASN A CA    1 
ATOM   18114 C  C     . ASN A 1 4012 ? 234.305 268.326 207.028 1.00 45.35  ? 4012 ASN A C     1 
ATOM   18115 O  O     . ASN A 1 4012 ? 233.802 269.120 206.227 1.00 51.78  ? 4012 ASN A O     1 
ATOM   18116 C  CB    . ASN A 1 4012 ? 235.960 266.517 206.527 1.00 38.59  ? 4012 ASN A CB    1 
ATOM   18117 C  CG    . ASN A 1 4012 ? 237.348 266.219 206.033 1.00 43.92  ? 4012 ASN A CG    1 
ATOM   18118 O  OD1   . ASN A 1 4012 ? 237.932 266.996 205.287 1.00 55.63  ? 4012 ASN A OD1   1 
ATOM   18119 N  ND2   . ASN A 1 4012 ? 237.887 265.089 206.448 1.00 44.98  ? 4012 ASN A ND2   1 
ATOM   18120 N  N     . LEU A 1 4013 ? 233.596 267.738 207.987 1.00 40.05  ? 4013 LEU A N     1 
ATOM   18121 C  CA    . LEU A 1 4013 ? 232.140 267.752 208.007 1.00 33.21  ? 4013 LEU A CA    1 
ATOM   18122 C  C     . LEU A 1 4013 ? 231.550 268.767 208.977 1.00 38.55  ? 4013 LEU A C     1 
ATOM   18123 O  O     . LEU A 1 4013 ? 230.331 268.779 209.168 1.00 47.61  ? 4013 LEU A O     1 
ATOM   18124 C  CB    . LEU A 1 4013 ? 231.628 266.349 208.340 1.00 44.88  ? 4013 LEU A CB    1 
ATOM   18125 C  CG    . LEU A 1 4013 ? 231.943 265.305 207.265 1.00 42.90  ? 4013 LEU A CG    1 
ATOM   18126 C  CD1   . LEU A 1 4013 ? 231.583 263.914 207.726 1.00 39.75  ? 4013 LEU A CD1   1 
ATOM   18127 C  CD2   . LEU A 1 4013 ? 231.182 265.637 206.003 1.00 40.44  ? 4013 LEU A CD2   1 
ATOM   18128 N  N     . GLY A 1 4014 ? 232.367 269.617 209.584 1.00 48.80  ? 4014 GLY A N     1 
ATOM   18129 C  CA    . GLY A 1 4014 ? 231.876 270.601 210.523 1.00 46.46  ? 4014 GLY A CA    1 
ATOM   18130 C  C     . GLY A 1 4014 ? 231.964 270.117 211.962 1.00 51.00  ? 4014 GLY A C     1 
ATOM   18131 O  O     . GLY A 1 4014 ? 232.000 268.920 212.252 1.00 56.56  ? 4014 GLY A O     1 
ATOM   18132 N  N     . GLU A 1 4015 ? 231.982 271.082 212.885 1.00 56.68  ? 4015 GLU A N     1 
ATOM   18133 C  CA    . GLU A 1 4015 ? 232.203 270.752 214.290 1.00 58.36  ? 4015 GLU A CA    1 
ATOM   18134 C  C     . GLU A 1 4015 ? 230.985 270.092 214.924 1.00 58.09  ? 4015 GLU A C     1 
ATOM   18135 O  O     . GLU A 1 4015 ? 231.134 269.285 215.848 1.00 59.84  ? 4015 GLU A O     1 
ATOM   18136 C  CB    . GLU A 1 4015 ? 232.589 272.006 215.074 1.00 55.13  ? 4015 GLU A CB    1 
ATOM   18137 C  CG    . GLU A 1 4015 ? 233.941 272.592 214.696 1.00 58.68  ? 4015 GLU A CG    1 
ATOM   18138 C  CD    . GLU A 1 4015 ? 233.877 273.478 213.467 1.00 67.89  ? 4015 GLU A CD    1 
ATOM   18139 O  OE1   . GLU A 1 4015 ? 232.765 273.691 212.939 1.00 65.12  ? 4015 GLU A OE1   1 
ATOM   18140 O  OE2   . GLU A 1 4015 ? 234.941 273.963 213.028 1.00 67.28  ? 4015 GLU A OE2   1 
ATOM   18141 N  N     . SER A 1 4016 ? 229.782 270.416 214.453 1.00 52.56  ? 4016 SER A N     1 
ATOM   18142 C  CA    . SER A 1 4016 ? 228.555 269.868 215.013 1.00 56.91  ? 4016 SER A CA    1 
ATOM   18143 C  C     . SER A 1 4016 ? 227.986 268.732 214.170 1.00 57.62  ? 4016 SER A C     1 
ATOM   18144 O  O     . SER A 1 4016 ? 226.778 268.479 214.218 1.00 58.96  ? 4016 SER A O     1 
ATOM   18145 C  CB    . SER A 1 4016 ? 227.512 270.973 215.181 1.00 59.51  ? 4016 SER A CB    1 
ATOM   18146 O  OG    . SER A 1 4016 ? 227.265 271.632 213.952 1.00 62.40  ? 4016 SER A OG    1 
ATOM   18147 N  N     . PHE A 1 4017 ? 228.830 268.051 213.393 1.00 46.73  ? 4017 PHE A N     1 
ATOM   18148 C  CA    . PHE A 1 4017 ? 228.346 266.949 212.570 1.00 42.73  ? 4017 PHE A CA    1 
ATOM   18149 C  C     . PHE A 1 4017 ? 227.844 265.796 213.429 1.00 51.14  ? 4017 PHE A C     1 
ATOM   18150 O  O     . PHE A 1 4017 ? 226.766 265.246 213.176 1.00 56.59  ? 4017 PHE A O     1 
ATOM   18151 C  CB    . PHE A 1 4017 ? 229.454 266.468 211.636 1.00 36.95  ? 4017 PHE A CB    1 
ATOM   18152 C  CG    . PHE A 1 4017 ? 228.987 265.493 210.600 1.00 39.46  ? 4017 PHE A CG    1 
ATOM   18153 C  CD1   . PHE A 1 4017 ? 228.178 265.908 209.560 1.00 44.71  ? 4017 PHE A CD1   1 
ATOM   18154 C  CD2   . PHE A 1 4017 ? 229.342 264.160 210.673 1.00 40.58  ? 4017 PHE A CD2   1 
ATOM   18155 C  CE1   . PHE A 1 4017 ? 227.745 265.017 208.607 1.00 47.90  ? 4017 PHE A CE1   1 
ATOM   18156 C  CE2   . PHE A 1 4017 ? 228.905 263.264 209.726 1.00 42.55  ? 4017 PHE A CE2   1 
ATOM   18157 C  CZ    . PHE A 1 4017 ? 228.109 263.695 208.690 1.00 44.27  ? 4017 PHE A CZ    1 
ATOM   18158 N  N     . MET A 1 4018 ? 228.608 265.424 214.455 1.00 46.69  ? 4018 MET A N     1 
ATOM   18159 C  CA    . MET A 1 4018 ? 228.292 264.287 215.308 1.00 41.34  ? 4018 MET A CA    1 
ATOM   18160 C  C     . MET A 1 4018 ? 227.665 264.704 216.633 1.00 45.99  ? 4018 MET A C     1 
ATOM   18161 O  O     . MET A 1 4018 ? 227.575 263.885 217.553 1.00 48.74  ? 4018 MET A O     1 
ATOM   18162 C  CB    . MET A 1 4018 ? 229.552 263.459 215.556 1.00 38.00  ? 4018 MET A CB    1 
ATOM   18163 C  CG    . MET A 1 4018 ? 230.091 262.770 214.320 1.00 40.35  ? 4018 MET A CG    1 
ATOM   18164 S  SD    . MET A 1 4018 ? 231.405 261.603 214.703 1.00 48.21  ? 4018 MET A SD    1 
ATOM   18165 C  CE    . MET A 1 4018 ? 232.671 262.728 215.264 1.00 48.33  ? 4018 MET A CE    1 
ATOM   18166 N  N     . SER A 1 4019 ? 227.228 265.959 216.750 1.00 51.24  ? 4019 SER A N     1 
ATOM   18167 C  CA    . SER A 1 4019 ? 226.681 266.454 218.006 1.00 51.16  ? 4019 SER A CA    1 
ATOM   18168 C  C     . SER A 1 4019 ? 225.262 265.969 218.273 1.00 55.48  ? 4019 SER A C     1 
ATOM   18169 O  O     . SER A 1 4019 ? 224.784 266.094 219.404 1.00 61.71  ? 4019 SER A O     1 
ATOM   18170 C  CB    . SER A 1 4019 ? 226.706 267.983 218.024 1.00 55.99  ? 4019 SER A CB    1 
ATOM   18171 O  OG    . SER A 1 4019 ? 225.829 268.516 217.048 1.00 61.03  ? 4019 SER A OG    1 
ATOM   18172 N  N     . ILE A 1 4020 ? 224.573 265.439 217.264 1.00 49.25  ? 4020 ILE A N     1 
ATOM   18173 C  CA    . ILE A 1 4020 ? 223.230 264.915 217.488 1.00 50.34  ? 4020 ILE A CA    1 
ATOM   18174 C  C     . ILE A 1 4020 ? 223.289 263.605 218.263 1.00 51.37  ? 4020 ILE A C     1 
ATOM   18175 O  O     . ILE A 1 4020 ? 222.403 263.304 219.071 1.00 55.01  ? 4020 ILE A O     1 
ATOM   18176 C  CB    . ILE A 1 4020 ? 222.491 264.753 216.148 1.00 53.60  ? 4020 ILE A CB    1 
ATOM   18177 C  CG1   . ILE A 1 4020 ? 222.402 266.098 215.427 1.00 59.03  ? 4020 ILE A CG1   1 
ATOM   18178 C  CG2   . ILE A 1 4020 ? 221.097 264.193 216.369 1.00 51.31  ? 4020 ILE A CG2   1 
ATOM   18179 C  CD1   . ILE A 1 4020 ? 221.641 267.151 216.199 1.00 55.86  ? 4020 ILE A CD1   1 
ATOM   18180 N  N     . MET A 1 4021 ? 224.336 262.809 218.038 1.00 51.52  ? 4021 MET A N     1 
ATOM   18181 C  CA    . MET A 1 4021 ? 224.416 261.489 218.651 1.00 54.81  ? 4021 MET A CA    1 
ATOM   18182 C  C     . MET A 1 4021 ? 224.673 261.552 220.150 1.00 56.49  ? 4021 MET A C     1 
ATOM   18183 O  O     . MET A 1 4021 ? 224.537 260.531 220.832 1.00 59.97  ? 4021 MET A O     1 
ATOM   18184 C  CB    . MET A 1 4021 ? 225.502 260.663 217.965 1.00 48.31  ? 4021 MET A CB    1 
ATOM   18185 C  CG    . MET A 1 4021 ? 225.147 260.254 216.547 1.00 49.49  ? 4021 MET A CG    1 
ATOM   18186 S  SD    . MET A 1 4021 ? 223.521 259.484 216.448 1.00 66.22  ? 4021 MET A SD    1 
ATOM   18187 C  CE    . MET A 1 4021 ? 222.708 260.560 215.273 1.00 48.84  ? 4021 MET A CE    1 
ATOM   18188 N  N     . GLU A 1 4022 ? 225.042 262.716 220.679 1.00 58.46  ? 4022 GLU A N     1 
ATOM   18189 C  CA    . GLU A 1 4022 ? 225.272 262.881 222.107 1.00 58.88  ? 4022 GLU A CA    1 
ATOM   18190 C  C     . GLU A 1 4022 ? 224.061 263.455 222.833 1.00 54.50  ? 4022 GLU A C     1 
ATOM   18191 O  O     . GLU A 1 4022 ? 224.159 263.774 224.022 1.00 54.78  ? 4022 GLU A O     1 
ATOM   18192 C  CB    . GLU A 1 4022 ? 226.499 263.766 222.344 1.00 59.14  ? 4022 GLU A CB    1 
ATOM   18193 C  CG    . GLU A 1 4022 ? 226.277 265.239 222.064 1.00 62.72  ? 4022 GLU A CG    1 
ATOM   18194 C  CD    . GLU A 1 4022 ? 227.570 265.981 221.796 1.00 65.37  ? 4022 GLU A CD    1 
ATOM   18195 O  OE1   . GLU A 1 4022 ? 228.478 265.387 221.178 1.00 65.47  ? 4022 GLU A OE1   1 
ATOM   18196 O  OE2   . GLU A 1 4022 ? 227.679 267.157 222.203 1.00 63.04  ? 4022 GLU A OE2   1 
ATOM   18197 N  N     . GLN A 1 4023 ? 222.933 263.593 222.149 1.00 57.72  ? 4023 GLN A N     1 
ATOM   18198 C  CA    . GLN A 1 4023 ? 221.656 264.051 222.666 1.00 58.47  ? 4023 GLN A CA    1 
ATOM   18199 C  C     . GLN A 1 4023 ? 220.685 262.883 222.788 1.00 62.38  ? 4023 GLN A C     1 
ATOM   18200 O  O     . GLN A 1 4023 ? 220.784 261.907 222.039 1.00 67.39  ? 4023 GLN A O     1 
ATOM   18201 C  CB    . GLN A 1 4023 ? 221.055 265.120 221.748 1.00 57.42  ? 4023 GLN A CB    1 
ATOM   18202 C  CG    . GLN A 1 4023 ? 221.809 266.439 221.749 1.00 57.68  ? 4023 GLN A CG    1 
ATOM   18203 C  CD    . GLN A 1 4023 ? 221.407 267.339 222.901 1.00 69.14  ? 4023 GLN A CD    1 
ATOM   18204 O  OE1   . GLN A 1 4023 ? 220.270 267.296 223.368 1.00 67.27  ? 4023 GLN A OE1   1 
ATOM   18205 N  NE2   . GLN A 1 4023 ? 222.342 268.159 223.365 1.00 67.37  ? 4023 GLN A NE2   1 
ATOM   18206 N  N     . PRO A 1 4024 ? 219.746 262.944 223.733 1.00 60.92  ? 4024 PRO A N     1 
ATOM   18207 C  CA    . PRO A 1 4024 ? 218.777 261.851 223.875 1.00 60.33  ? 4024 PRO A CA    1 
ATOM   18208 C  C     . PRO A 1 4024 ? 217.945 261.676 222.614 1.00 63.06  ? 4024 PRO A C     1 
ATOM   18209 O  O     . PRO A 1 4024 ? 217.593 262.645 221.939 1.00 61.93  ? 4024 PRO A O     1 
ATOM   18210 C  CB    . PRO A 1 4024 ? 217.916 262.290 225.065 1.00 54.06  ? 4024 PRO A CB    1 
ATOM   18211 C  CG    . PRO A 1 4024 ? 218.168 263.755 225.217 1.00 56.72  ? 4024 PRO A CG    1 
ATOM   18212 C  CD    . PRO A 1 4024 ? 219.570 263.976 224.765 1.00 58.51  ? 4024 PRO A CD    1 
ATOM   18213 N  N     . LEU A 1 4025 ? 217.636 260.419 222.300 1.00 57.99  ? 4025 LEU A N     1 
ATOM   18214 C  CA    . LEU A 1 4025 ? 216.877 260.112 221.096 1.00 55.86  ? 4025 LEU A CA    1 
ATOM   18215 C  C     . LEU A 1 4025 ? 215.469 260.682 221.193 1.00 59.30  ? 4025 LEU A C     1 
ATOM   18216 O  O     . LEU A 1 4025 ? 214.771 260.483 222.191 1.00 61.79  ? 4025 LEU A O     1 
ATOM   18217 C  CB    . LEU A 1 4025 ? 216.822 258.599 220.883 1.00 55.87  ? 4025 LEU A CB    1 
ATOM   18218 C  CG    . LEU A 1 4025 ? 215.935 258.103 219.741 1.00 54.22  ? 4025 LEU A CG    1 
ATOM   18219 C  CD1   . LEU A 1 4025 ? 216.604 258.350 218.408 1.00 53.18  ? 4025 LEU A CD1   1 
ATOM   18220 C  CD2   . LEU A 1 4025 ? 215.614 256.632 219.907 1.00 50.16  ? 4025 LEU A CD2   1 
ATOM   18221 N  N     . ASP A 1 4026 ? 215.051 261.392 220.148 1.00 59.09  ? 4026 ASP A N     1 
ATOM   18222 C  CA    . ASP A 1 4026 ? 213.730 262.014 220.095 1.00 62.74  ? 4026 ASP A CA    1 
ATOM   18223 C  C     . ASP A 1 4026 ? 212.826 261.109 219.267 1.00 64.14  ? 4026 ASP A C     1 
ATOM   18224 O  O     . ASP A 1 4026 ? 212.676 261.286 218.059 1.00 66.28  ? 4026 ASP A O     1 
ATOM   18225 C  CB    . ASP A 1 4026 ? 213.813 263.419 219.511 1.00 63.10  ? 4026 ASP A CB    1 
ATOM   18226 C  CG    . ASP A 1 4026 ? 212.493 264.158 219.584 1.00 64.48  ? 4026 ASP A CG    1 
ATOM   18227 O  OD1   . ASP A 1 4026 ? 211.972 264.332 220.705 1.00 65.78  ? 4026 ASP A OD1   1 
ATOM   18228 O  OD2   . ASP A 1 4026 ? 211.976 264.564 218.523 1.00 60.32  ? 4026 ASP A OD2   1 
ATOM   18229 N  N     . LEU A 1 4027 ? 212.213 260.129 219.933 1.00 59.44  ? 4027 LEU A N     1 
ATOM   18230 C  CA    . LEU A 1 4027 ? 211.379 259.159 219.235 1.00 56.19  ? 4027 LEU A CA    1 
ATOM   18231 C  C     . LEU A 1 4027 ? 210.101 259.771 218.680 1.00 59.26  ? 4027 LEU A C     1 
ATOM   18232 O  O     . LEU A 1 4027 ? 209.534 259.222 217.731 1.00 64.38  ? 4027 LEU A O     1 
ATOM   18233 C  CB    . LEU A 1 4027 ? 211.027 258.001 220.166 1.00 59.27  ? 4027 LEU A CB    1 
ATOM   18234 C  CG    . LEU A 1 4027 ? 211.896 256.749 220.069 1.00 58.90  ? 4027 LEU A CG    1 
ATOM   18235 C  CD1   . LEU A 1 4027 ? 211.443 255.718 221.086 1.00 62.88  ? 4027 LEU A CD1   1 
ATOM   18236 C  CD2   . LEU A 1 4027 ? 211.856 256.174 218.665 1.00 57.18  ? 4027 LEU A CD2   1 
ATOM   18237 N  N     . THR A 1 4028 ? 209.634 260.886 219.244 1.00 65.90  ? 4028 THR A N     1 
ATOM   18238 C  CA    . THR A 1 4028 ? 208.379 261.478 218.789 1.00 68.28  ? 4028 THR A CA    1 
ATOM   18239 C  C     . THR A 1 4028 ? 208.461 261.887 217.324 1.00 67.48  ? 4028 THR A C     1 
ATOM   18240 O  O     . THR A 1 4028 ? 207.616 261.499 216.508 1.00 70.11  ? 4028 THR A O     1 
ATOM   18241 C  CB    . THR A 1 4028 ? 208.025 262.683 219.661 1.00 69.13  ? 4028 THR A CB    1 
ATOM   18242 O  OG1   . THR A 1 4028 ? 207.904 262.267 221.026 1.00 69.61  ? 4028 THR A OG1   1 
ATOM   18243 C  CG2   . THR A 1 4028 ? 206.714 263.300 219.206 1.00 67.72  ? 4028 THR A CG2   1 
ATOM   18244 N  N     . HIS A 1 4029 ? 209.487 262.660 216.971 1.00 64.86  ? 4029 HIS A N     1 
ATOM   18245 C  CA    . HIS A 1 4029 ? 209.639 263.132 215.601 1.00 66.23  ? 4029 HIS A CA    1 
ATOM   18246 C  C     . HIS A 1 4029 ? 209.990 262.002 214.641 1.00 69.75  ? 4029 HIS A C     1 
ATOM   18247 O  O     . HIS A 1 4029 ? 209.542 262.013 213.490 1.00 70.26  ? 4029 HIS A O     1 
ATOM   18248 C  CB    . HIS A 1 4029 ? 210.706 264.226 215.547 1.00 67.45  ? 4029 HIS A CB    1 
ATOM   18249 C  CG    . HIS A 1 4029 ? 210.944 264.774 214.176 1.00 72.82  ? 4029 HIS A CG    1 
ATOM   18250 N  ND1   . HIS A 1 4029 ? 209.941 265.328 213.411 1.00 72.55  ? 4029 HIS A ND1   1 
ATOM   18251 C  CD2   . HIS A 1 4029 ? 212.073 264.858 213.433 1.00 69.99  ? 4029 HIS A CD2   1 
ATOM   18252 C  CE1   . HIS A 1 4029 ? 210.440 265.727 212.255 1.00 71.29  ? 4029 HIS A CE1   1 
ATOM   18253 N  NE2   . HIS A 1 4029 ? 211.732 265.453 212.243 1.00 73.44  ? 4029 HIS A NE2   1 
ATOM   18254 N  N     . ILE A 1 4030 ? 210.779 261.023 215.091 1.00 63.16  ? 4030 ILE A N     1 
ATOM   18255 C  CA    . ILE A 1 4030 ? 211.210 259.936 214.214 1.00 57.63  ? 4030 ILE A CA    1 
ATOM   18256 C  C     . ILE A 1 4030 ? 210.154 258.855 214.050 1.00 57.19  ? 4030 ILE A C     1 
ATOM   18257 O  O     . ILE A 1 4030 ? 210.262 258.034 213.134 1.00 64.22  ? 4030 ILE A O     1 
ATOM   18258 C  CB    . ILE A 1 4030 ? 212.526 259.331 214.739 1.00 53.10  ? 4030 ILE A CB    1 
ATOM   18259 C  CG1   . ILE A 1 4030 ? 213.483 260.445 215.150 1.00 58.60  ? 4030 ILE A CG1   1 
ATOM   18260 C  CG2   . ILE A 1 4030 ? 213.198 258.485 213.679 1.00 55.95  ? 4030 ILE A CG2   1 
ATOM   18261 C  CD1   . ILE A 1 4030 ? 214.755 259.949 215.779 1.00 55.67  ? 4030 ILE A CD1   1 
ATOM   18262 N  N     . VAL A 1 4031 ? 209.131 258.832 214.895 1.00 54.47  ? 4031 VAL A N     1 
ATOM   18263 C  CA    . VAL A 1 4031 ? 208.030 257.885 214.756 1.00 50.67  ? 4031 VAL A CA    1 
ATOM   18264 C  C     . VAL A 1 4031 ? 206.829 258.524 214.072 1.00 55.24  ? 4031 VAL A C     1 
ATOM   18265 O  O     . VAL A 1 4031 ? 206.227 257.927 213.180 1.00 57.62  ? 4031 VAL A O     1 
ATOM   18266 C  CB    . VAL A 1 4031 ? 207.650 257.295 216.133 1.00 52.62  ? 4031 VAL A CB    1 
ATOM   18267 C  CG1   . VAL A 1 4031 ? 206.315 256.580 216.056 1.00 52.72  ? 4031 VAL A CG1   1 
ATOM   18268 C  CG2   . VAL A 1 4031 ? 208.727 256.334 216.598 1.00 52.51  ? 4031 VAL A CG2   1 
ATOM   18269 N  N     . GLY A 1 4032 ? 206.467 259.745 214.473 1.00 61.25  ? 4032 GLY A N     1 
ATOM   18270 C  CA    . GLY A 1 4032 ? 205.380 260.435 213.798 1.00 64.35  ? 4032 GLY A CA    1 
ATOM   18271 C  C     . GLY A 1 4032 ? 205.669 260.669 212.328 1.00 65.21  ? 4032 GLY A C     1 
ATOM   18272 O  O     . GLY A 1 4032 ? 204.799 260.483 211.475 1.00 66.31  ? 4032 GLY A O     1 
ATOM   18273 N  N     . THR A 1 4033 ? 206.893 261.077 212.015 1.00 65.87  ? 4033 THR A N     1 
ATOM   18274 C  CA    . THR A 1 4033 ? 207.372 261.220 210.650 1.00 63.98  ? 4033 THR A CA    1 
ATOM   18275 C  C     . THR A 1 4033 ? 208.597 260.336 210.459 1.00 67.68  ? 4033 THR A C     1 
ATOM   18276 O  O     . THR A 1 4033 ? 209.125 259.760 211.410 1.00 71.94  ? 4033 THR A O     1 
ATOM   18277 C  CB    . THR A 1 4033 ? 207.711 262.681 210.332 1.00 67.10  ? 4033 THR A CB    1 
ATOM   18278 O  OG1   . THR A 1 4033 ? 208.492 263.232 211.399 1.00 62.85  ? 4033 THR A OG1   1 
ATOM   18279 C  CG2   . THR A 1 4033 ? 206.441 263.498 210.172 1.00 66.58  ? 4033 THR A CG2   1 
ATOM   18280 N  N     . GLU A 1 4034 ? 209.038 260.221 209.207 1.00 62.05  ? 4034 GLU A N     1 
ATOM   18281 C  CA    . GLU A 1 4034 ? 210.216 259.469 208.775 1.00 60.01  ? 4034 GLU A CA    1 
ATOM   18282 C  C     . GLU A 1 4034 ? 210.059 257.959 208.900 1.00 61.09  ? 4034 GLU A C     1 
ATOM   18283 O  O     . GLU A 1 4034 ? 210.974 257.229 208.503 1.00 64.51  ? 4034 GLU A O     1 
ATOM   18284 C  CB    . GLU A 1 4034 ? 211.492 259.875 209.529 1.00 57.00  ? 4034 GLU A CB    1 
ATOM   18285 C  CG    . GLU A 1 4034 ? 211.745 261.366 209.600 1.00 62.79  ? 4034 GLU A CG    1 
ATOM   18286 C  CD    . GLU A 1 4034 ? 213.009 261.696 210.366 1.00 67.09  ? 4034 GLU A CD    1 
ATOM   18287 O  OE1   . GLU A 1 4034 ? 213.663 260.756 210.864 1.00 62.03  ? 4034 GLU A OE1   1 
ATOM   18288 O  OE2   . GLU A 1 4034 ? 213.349 262.892 210.471 1.00 69.68  ? 4034 GLU A OE2   1 
ATOM   18289 N  N     . VAL A 1 4035 ? 208.947 257.460 209.433 1.00 58.46  ? 4035 VAL A N     1 
ATOM   18290 C  CA    . VAL A 1 4035 ? 208.701 256.026 209.536 1.00 55.93  ? 4035 VAL A CA    1 
ATOM   18291 C  C     . VAL A 1 4035 ? 207.355 255.728 208.899 1.00 58.20  ? 4035 VAL A C     1 
ATOM   18292 O  O     . VAL A 1 4035 ? 206.330 256.280 209.317 1.00 60.01  ? 4035 VAL A O     1 
ATOM   18293 C  CB    . VAL A 1 4035 ? 208.736 255.530 210.991 1.00 52.18  ? 4035 VAL A CB    1 
ATOM   18294 C  CG1   . VAL A 1 4035 ? 208.050 254.182 211.105 1.00 49.34  ? 4035 VAL A CG1   1 
ATOM   18295 C  CG2   . VAL A 1 4035 ? 210.171 255.413 211.467 1.00 56.46  ? 4035 VAL A CG2   1 
ATOM   18296 N  N     . LYS A 1 4036 ? 207.358 254.864 207.893 1.00 57.73  ? 4036 LYS A N     1 
ATOM   18297 C  CA    . LYS A 1 4036 ? 206.132 254.456 207.231 1.00 55.52  ? 4036 LYS A CA    1 
ATOM   18298 C  C     . LYS A 1 4036 ? 205.373 253.452 208.095 1.00 54.58  ? 4036 LYS A C     1 
ATOM   18299 O  O     . LYS A 1 4036 ? 205.974 252.735 208.897 1.00 61.06  ? 4036 LYS A O     1 
ATOM   18300 C  CB    . LYS A 1 4036 ? 206.445 253.840 205.873 1.00 56.61  ? 4036 LYS A CB    1 
ATOM   18301 C  CG    . LYS A 1 4036 ? 207.444 254.635 205.054 1.00 55.72  ? 4036 LYS A CG    1 
ATOM   18302 C  CD    . LYS A 1 4036 ? 206.768 255.775 204.315 1.00 55.44  ? 4036 LYS A CD    1 
ATOM   18303 C  CE    . LYS A 1 4036 ? 207.785 256.789 203.819 1.00 58.42  ? 4036 LYS A CE    1 
ATOM   18304 N  NZ    . LYS A 1 4036 ? 208.237 257.701 204.906 1.00 63.26  ? 4036 LYS A NZ    1 
ATOM   18305 N  N     . PRO A 1 4037 ? 204.047 253.391 207.957 1.00 52.59  ? 4037 PRO A N     1 
ATOM   18306 C  CA    . PRO A 1 4037 ? 203.278 252.417 208.748 1.00 52.44  ? 4037 PRO A CA    1 
ATOM   18307 C  C     . PRO A 1 4037 ? 203.679 250.973 208.502 1.00 55.03  ? 4037 PRO A C     1 
ATOM   18308 O  O     . PRO A 1 4037 ? 203.591 250.153 209.423 1.00 58.82  ? 4037 PRO A O     1 
ATOM   18309 C  CB    . PRO A 1 4037 ? 201.828 252.682 208.320 1.00 49.62  ? 4037 PRO A CB    1 
ATOM   18310 C  CG    . PRO A 1 4037 ? 201.923 253.459 207.049 1.00 57.13  ? 4037 PRO A CG    1 
ATOM   18311 C  CD    . PRO A 1 4037 ? 203.173 254.263 207.158 1.00 55.17  ? 4037 PRO A CD    1 
ATOM   18312 N  N     . ASN A 1 4038 ? 204.118 250.632 207.294 1.00 53.07  ? 4038 ASN A N     1 
ATOM   18313 C  CA    . ASN A 1 4038 ? 204.526 249.270 206.981 1.00 50.01  ? 4038 ASN A CA    1 
ATOM   18314 C  C     . ASN A 1 4038 ? 205.983 248.990 207.329 1.00 55.06  ? 4038 ASN A C     1 
ATOM   18315 O  O     . ASN A 1 4038 ? 206.450 247.868 207.111 1.00 56.67  ? 4038 ASN A O     1 
ATOM   18316 C  CB    . ASN A 1 4038 ? 204.284 248.971 205.498 1.00 50.19  ? 4038 ASN A CB    1 
ATOM   18317 C  CG    . ASN A 1 4038 ? 204.914 250.001 204.586 1.00 62.69  ? 4038 ASN A CG    1 
ATOM   18318 O  OD1   . ASN A 1 4038 ? 204.847 251.201 204.848 1.00 58.76  ? 4038 ASN A OD1   1 
ATOM   18319 N  ND2   . ASN A 1 4038 ? 205.535 249.537 203.509 1.00 61.56  ? 4038 ASN A ND2   1 
ATOM   18320 N  N     . THR A 1 4039 ? 206.707 249.974 207.865 1.00 50.77  ? 4039 THR A N     1 
ATOM   18321 C  CA    . THR A 1 4039 ? 208.088 249.779 208.278 1.00 40.03  ? 4039 THR A CA    1 
ATOM   18322 C  C     . THR A 1 4039 ? 208.131 249.547 209.780 1.00 43.31  ? 4039 THR A C     1 
ATOM   18323 O  O     . THR A 1 4039 ? 207.807 250.466 210.547 1.00 52.93  ? 4039 THR A O     1 
ATOM   18324 C  CB    . THR A 1 4039 ? 208.939 250.991 207.903 1.00 45.66  ? 4039 THR A CB    1 
ATOM   18325 O  OG1   . THR A 1 4039 ? 209.106 251.042 206.481 1.00 53.49  ? 4039 THR A OG1   1 
ATOM   18326 C  CG2   . THR A 1 4039 ? 210.303 250.904 208.554 1.00 43.24  ? 4039 THR A CG2   1 
ATOM   18327 N  N     . PRO A 1 4040 ? 208.498 248.355 210.247 1.00 30.55  ? 4040 PRO A N     1 
ATOM   18328 C  CA    . PRO A 1 4040 ? 208.576 248.121 211.692 1.00 36.88  ? 4040 PRO A CA    1 
ATOM   18329 C  C     . PRO A 1 4040 ? 209.693 248.925 212.340 1.00 38.84  ? 4040 PRO A C     1 
ATOM   18330 O  O     . PRO A 1 4040 ? 210.697 249.265 211.712 1.00 42.68  ? 4040 PRO A O     1 
ATOM   18331 C  CB    . PRO A 1 4040 ? 208.839 246.614 211.792 1.00 32.34  ? 4040 PRO A CB    1 
ATOM   18332 C  CG    . PRO A 1 4040 ? 209.444 246.248 210.480 1.00 34.12  ? 4040 PRO A CG    1 
ATOM   18333 C  CD    . PRO A 1 4040 ? 208.792 247.140 209.471 1.00 39.50  ? 4040 PRO A CD    1 
ATOM   18334 N  N     . VAL A 1 4041 ? 209.500 249.250 213.611 1.00 34.65  ? 4041 VAL A N     1 
ATOM   18335 C  CA    . VAL A 1 4041 ? 210.491 249.992 214.377 1.00 30.57  ? 4041 VAL A CA    1 
ATOM   18336 C  C     . VAL A 1 4041 ? 211.243 248.988 215.235 1.00 36.82  ? 4041 VAL A C     1 
ATOM   18337 O  O     . VAL A 1 4041 ? 210.700 248.448 216.204 1.00 46.16  ? 4041 VAL A O     1 
ATOM   18338 C  CB    . VAL A 1 4041 ? 209.844 251.097 215.219 1.00 36.42  ? 4041 VAL A CB    1 
ATOM   18339 C  CG1   . VAL A 1 4041 ? 210.896 251.856 215.987 1.00 37.79  ? 4041 VAL A CG1   1 
ATOM   18340 C  CG2   . VAL A 1 4041 ? 209.087 252.048 214.325 1.00 35.08  ? 4041 VAL A CG2   1 
ATOM   18341 N  N     . LEU A 1 4042 ? 212.496 248.732 214.881 1.00 35.23  ? 4042 LEU A N     1 
ATOM   18342 C  CA    . LEU A 1 4042 ? 213.290 247.712 215.555 1.00 31.94  ? 4042 LEU A CA    1 
ATOM   18343 C  C     . LEU A 1 4042 ? 213.998 248.358 216.739 1.00 37.85  ? 4042 LEU A C     1 
ATOM   18344 O  O     . LEU A 1 4042 ? 214.892 249.191 216.558 1.00 48.59  ? 4042 LEU A O     1 
ATOM   18345 C  CB    . LEU A 1 4042 ? 214.277 247.074 214.581 1.00 32.70  ? 4042 LEU A CB    1 
ATOM   18346 C  CG    . LEU A 1 4042 ? 213.711 246.613 213.237 1.00 39.28  ? 4042 LEU A CG    1 
ATOM   18347 C  CD1   . LEU A 1 4042 ? 214.785 245.874 212.485 1.00 38.38  ? 4042 LEU A CD1   1 
ATOM   18348 C  CD2   . LEU A 1 4042 ? 212.484 245.733 213.404 1.00 36.63  ? 4042 LEU A CD2   1 
ATOM   18349 N  N     . MET A 1 4043 ? 213.601 247.966 217.947 1.00 36.85  ? 4043 MET A N     1 
ATOM   18350 C  CA    . MET A 1 4043 ? 214.050 248.621 219.177 1.00 31.92  ? 4043 MET A CA    1 
ATOM   18351 C  C     . MET A 1 4043 ? 215.213 247.828 219.774 1.00 41.09  ? 4043 MET A C     1 
ATOM   18352 O  O     . MET A 1 4043 ? 215.146 247.307 220.889 1.00 45.71  ? 4043 MET A O     1 
ATOM   18353 C  CB    . MET A 1 4043 ? 212.888 248.707 220.164 1.00 38.53  ? 4043 MET A CB    1 
ATOM   18354 C  CG    . MET A 1 4043 ? 211.728 249.590 219.711 1.00 37.24  ? 4043 MET A CG    1 
ATOM   18355 S  SD    . MET A 1 4043 ? 212.013 251.346 219.414 1.00 69.58  ? 4043 MET A SD    1 
ATOM   18356 C  CE    . MET A 1 4043 ? 212.286 251.939 221.075 1.00 45.07  ? 4043 MET A CE    1 
ATOM   18357 N  N     . CYS A 1 4044 ? 216.298 247.753 219.008 1.00 36.71  ? 4044 CYS A N     1 
ATOM   18358 C  CA    . CYS A 1 4044 ? 217.410 246.876 219.362 1.00 27.05  ? 4044 CYS A CA    1 
ATOM   18359 C  C     . CYS A 1 4044 ? 218.208 247.442 220.530 1.00 34.23  ? 4044 CYS A C     1 
ATOM   18360 O  O     . CYS A 1 4044 ? 218.466 248.643 220.599 1.00 49.34  ? 4044 CYS A O     1 
ATOM   18361 C  CB    . CYS A 1 4044 ? 218.326 246.666 218.161 1.00 38.02  ? 4044 CYS A CB    1 
ATOM   18362 S  SG    . CYS A 1 4044 ? 217.477 246.379 216.596 1.00 54.91  ? 4044 CYS A SG    1 
ATOM   18363 N  N     . SER A 1 4045 ? 218.624 246.562 221.440 1.00 40.18  ? 4045 SER A N     1 
ATOM   18364 C  CA    . SER A 1 4045 ? 219.300 246.991 222.651 1.00 44.09  ? 4045 SER A CA    1 
ATOM   18365 C  C     . SER A 1 4045 ? 220.413 246.021 223.021 1.00 42.55  ? 4045 SER A C     1 
ATOM   18366 O  O     . SER A 1 4045 ? 220.329 244.821 222.755 1.00 51.07  ? 4045 SER A O     1 
ATOM   18367 C  CB    . SER A 1 4045 ? 218.317 247.114 223.815 1.00 46.54  ? 4045 SER A CB    1 
ATOM   18368 O  OG    . SER A 1 4045 ? 217.712 245.864 224.085 1.00 44.85  ? 4045 SER A OG    1 
ATOM   18369 N  N     . VAL A 1 4046 ? 221.458 246.559 223.644 1.00 46.16  ? 4046 VAL A N     1 
ATOM   18370 C  CA    . VAL A 1 4046 ? 222.554 245.757 224.181 1.00 46.11  ? 4046 VAL A CA    1 
ATOM   18371 C  C     . VAL A 1 4046 ? 222.039 245.029 225.416 1.00 53.29  ? 4046 VAL A C     1 
ATOM   18372 O  O     . VAL A 1 4046 ? 221.008 245.430 225.973 1.00 56.56  ? 4046 VAL A O     1 
ATOM   18373 C  CB    . VAL A 1 4046 ? 223.772 246.633 224.506 1.00 47.46  ? 4046 VAL A CB    1 
ATOM   18374 C  CG1   . VAL A 1 4046 ? 224.278 247.319 223.251 1.00 48.89  ? 4046 VAL A CG1   1 
ATOM   18375 C  CG2   . VAL A 1 4046 ? 223.415 247.650 225.567 1.00 45.41  ? 4046 VAL A CG2   1 
ATOM   18376 N  N     . PRO A 1 4047 ? 222.692 243.956 225.869 1.00 64.44  ? 4047 PRO A N     1 
ATOM   18377 C  CA    . PRO A 1 4047 ? 222.211 243.262 227.070 1.00 56.65  ? 4047 PRO A CA    1 
ATOM   18378 C  C     . PRO A 1 4047 ? 222.138 244.198 228.267 1.00 55.26  ? 4047 PRO A C     1 
ATOM   18379 O  O     . PRO A 1 4047 ? 223.033 245.012 228.503 1.00 60.63  ? 4047 PRO A O     1 
ATOM   18380 C  CB    . PRO A 1 4047 ? 223.250 242.154 227.284 1.00 56.65  ? 4047 PRO A CB    1 
ATOM   18381 C  CG    . PRO A 1 4047 ? 224.433 242.559 226.465 1.00 52.49  ? 4047 PRO A CG    1 
ATOM   18382 C  CD    . PRO A 1 4047 ? 223.864 243.278 225.290 1.00 57.04  ? 4047 PRO A CD    1 
ATOM   18383 N  N     . GLY A 1 4048 ? 221.056 244.068 229.030 1.00 54.00  ? 4048 GLY A N     1 
ATOM   18384 C  CA    . GLY A 1 4048 ? 220.810 244.919 230.170 1.00 56.02  ? 4048 GLY A CA    1 
ATOM   18385 C  C     . GLY A 1 4048 ? 219.981 246.152 229.892 1.00 54.06  ? 4048 GLY A C     1 
ATOM   18386 O  O     . GLY A 1 4048 ? 219.618 246.858 230.840 1.00 52.62  ? 4048 GLY A O     1 
ATOM   18387 N  N     . TYR A 1 4049 ? 219.670 246.436 228.633 1.00 55.07  ? 4049 TYR A N     1 
ATOM   18388 C  CA    . TYR A 1 4049 ? 218.832 247.567 228.269 1.00 53.68  ? 4049 TYR A CA    1 
ATOM   18389 C  C     . TYR A 1 4049 ? 217.569 247.063 227.592 1.00 55.59  ? 4049 TYR A C     1 
ATOM   18390 O  O     . TYR A 1 4049 ? 217.621 246.162 226.749 1.00 59.84  ? 4049 TYR A O     1 
ATOM   18391 C  CB    . TYR A 1 4049 ? 219.577 248.543 227.350 1.00 46.01  ? 4049 TYR A CB    1 
ATOM   18392 C  CG    . TYR A 1 4049 ? 220.445 249.515 228.109 1.00 53.28  ? 4049 TYR A CG    1 
ATOM   18393 C  CD1   . TYR A 1 4049 ? 221.466 249.061 228.931 1.00 56.32  ? 4049 TYR A CD1   1 
ATOM   18394 C  CD2   . TYR A 1 4049 ? 220.229 250.882 228.027 1.00 48.94  ? 4049 TYR A CD2   1 
ATOM   18395 C  CE1   . TYR A 1 4049 ? 222.256 249.939 229.639 1.00 56.63  ? 4049 TYR A CE1   1 
ATOM   18396 C  CE2   . TYR A 1 4049 ? 221.017 251.770 228.733 1.00 53.28  ? 4049 TYR A CE2   1 
ATOM   18397 C  CZ    . TYR A 1 4049 ? 222.029 251.292 229.537 1.00 58.76  ? 4049 TYR A CZ    1 
ATOM   18398 O  OH    . TYR A 1 4049 ? 222.818 252.166 230.247 1.00 58.29  ? 4049 TYR A OH    1 
ATOM   18399 N  N     . ASP A 1 4050 ? 216.433 247.635 227.979 1.00 54.47  ? 4050 ASP A N     1 
ATOM   18400 C  CA    . ASP A 1 4050 ? 215.147 247.301 227.387 1.00 51.58  ? 4050 ASP A CA    1 
ATOM   18401 C  C     . ASP A 1 4050 ? 214.485 248.586 226.918 1.00 58.50  ? 4050 ASP A C     1 
ATOM   18402 O  O     . ASP A 1 4050 ? 214.380 249.549 227.684 1.00 56.59  ? 4050 ASP A O     1 
ATOM   18403 C  CB    . ASP A 1 4050 ? 214.252 246.568 228.389 1.00 48.85  ? 4050 ASP A CB    1 
ATOM   18404 C  CG    . ASP A 1 4050 ? 212.928 246.153 227.789 1.00 58.27  ? 4050 ASP A CG    1 
ATOM   18405 O  OD1   . ASP A 1 4050 ? 212.936 245.471 226.744 1.00 57.04  ? 4050 ASP A OD1   1 
ATOM   18406 O  OD2   . ASP A 1 4050 ? 211.879 246.509 228.362 1.00 53.39  ? 4050 ASP A OD2   1 
ATOM   18407 N  N     . ALA A 1 4051 ? 214.046 248.602 225.662 1.00 51.69  ? 4051 ALA A N     1 
ATOM   18408 C  CA    . ALA A 1 4051 ? 213.436 249.781 225.065 1.00 44.30  ? 4051 ALA A CA    1 
ATOM   18409 C  C     . ALA A 1 4051 ? 211.915 249.749 225.099 1.00 47.84  ? 4051 ALA A C     1 
ATOM   18410 O  O     . ALA A 1 4051 ? 211.280 250.611 224.488 1.00 56.75  ? 4051 ALA A O     1 
ATOM   18411 C  CB    . ALA A 1 4051 ? 213.914 249.946 223.621 1.00 53.51  ? 4051 ALA A CB    1 
ATOM   18412 N  N     . SER A 1 4052 ? 211.318 248.773 225.786 1.00 50.52  ? 4052 SER A N     1 
ATOM   18413 C  CA    . SER A 1 4052 ? 209.864 248.727 225.905 1.00 41.60  ? 4052 SER A CA    1 
ATOM   18414 C  C     . SER A 1 4052 ? 209.323 249.925 226.674 1.00 49.17  ? 4052 SER A C     1 
ATOM   18415 O  O     . SER A 1 4052 ? 208.268 250.465 226.319 1.00 53.54  ? 4052 SER A O     1 
ATOM   18416 C  CB    . SER A 1 4052 ? 209.437 247.430 226.586 1.00 43.38  ? 4052 SER A CB    1 
ATOM   18417 O  OG    . SER A 1 4052 ? 209.782 246.307 225.798 1.00 58.50  ? 4052 SER A OG    1 
ATOM   18418 N  N     . GLY A 1 4053 ? 210.018 250.341 227.735 1.00 54.38  ? 4053 GLY A N     1 
ATOM   18419 C  CA    . GLY A 1 4053 ? 209.577 251.500 228.489 1.00 52.56  ? 4053 GLY A CA    1 
ATOM   18420 C  C     . GLY A 1 4053 ? 209.559 252.766 227.660 1.00 52.41  ? 4053 GLY A C     1 
ATOM   18421 O  O     . GLY A 1 4053 ? 208.677 253.612 227.831 1.00 54.16  ? 4053 GLY A O     1 
ATOM   18422 N  N     . HIS A 1 4054 ? 210.521 252.911 226.747 1.00 53.83  ? 4054 HIS A N     1 
ATOM   18423 C  CA    . HIS A 1 4054 ? 210.510 254.049 225.837 1.00 53.23  ? 4054 HIS A CA    1 
ATOM   18424 C  C     . HIS A 1 4054 ? 209.247 254.058 224.990 1.00 55.84  ? 4054 HIS A C     1 
ATOM   18425 O  O     . HIS A 1 4054 ? 208.627 255.109 224.801 1.00 58.20  ? 4054 HIS A O     1 
ATOM   18426 C  CB    . HIS A 1 4054 ? 211.748 254.019 224.942 1.00 51.64  ? 4054 HIS A CB    1 
ATOM   18427 C  CG    . HIS A 1 4054 ? 213.040 254.101 225.692 1.00 55.16  ? 4054 HIS A CG    1 
ATOM   18428 N  ND1   . HIS A 1 4054 ? 213.215 254.923 226.783 1.00 61.67  ? 4054 HIS A ND1   1 
ATOM   18429 C  CD2   . HIS A 1 4054 ? 214.217 253.459 225.511 1.00 58.79  ? 4054 HIS A CD2   1 
ATOM   18430 C  CE1   . HIS A 1 4054 ? 214.447 254.787 227.240 1.00 58.59  ? 4054 HIS A CE1   1 
ATOM   18431 N  NE2   . HIS A 1 4054 ? 215.076 253.904 226.487 1.00 60.30  ? 4054 HIS A NE2   1 
ATOM   18432 N  N     . VAL A 1 4055 ? 208.849 252.894 224.477 1.00 56.11  ? 4055 VAL A N     1 
ATOM   18433 C  CA    . VAL A 1 4055 ? 207.663 252.823 223.630 1.00 47.12  ? 4055 VAL A CA    1 
ATOM   18434 C  C     . VAL A 1 4055 ? 206.404 253.102 224.440 1.00 52.17  ? 4055 VAL A C     1 
ATOM   18435 O  O     . VAL A 1 4055 ? 205.496 253.797 223.972 1.00 61.35  ? 4055 VAL A O     1 
ATOM   18436 C  CB    . VAL A 1 4055 ? 207.595 251.461 222.921 1.00 47.00  ? 4055 VAL A CB    1 
ATOM   18437 C  CG1   . VAL A 1 4055 ? 206.522 251.481 221.858 1.00 47.46  ? 4055 VAL A CG1   1 
ATOM   18438 C  CG2   . VAL A 1 4055 ? 208.939 251.121 222.312 1.00 48.73  ? 4055 VAL A CG2   1 
ATOM   18439 N  N     . GLU A 1 4056 ? 206.319 252.564 225.661 1.00 52.68  ? 4056 GLU A N     1 
ATOM   18440 C  CA    . GLU A 1 4056 ? 205.168 252.868 226.509 1.00 49.60  ? 4056 GLU A CA    1 
ATOM   18441 C  C     . GLU A 1 4056 ? 205.073 254.357 226.816 1.00 60.96  ? 4056 GLU A C     1 
ATOM   18442 O  O     . GLU A 1 4056 ? 203.987 254.942 226.740 1.00 67.79  ? 4056 GLU A O     1 
ATOM   18443 C  CB    . GLU A 1 4056 ? 205.218 252.060 227.806 1.00 52.87  ? 4056 GLU A CB    1 
ATOM   18444 C  CG    . GLU A 1 4056 ? 205.297 250.556 227.635 1.00 59.02  ? 4056 GLU A CG    1 
ATOM   18445 C  CD    . GLU A 1 4056 ? 204.048 249.988 226.980 1.00 68.41  ? 4056 GLU A CD    1 
ATOM   18446 O  OE1   . GLU A 1 4056 ? 204.107 248.860 226.453 1.00 65.49  ? 4056 GLU A OE1   1 
ATOM   18447 O  OE2   . GLU A 1 4056 ? 202.999 250.668 226.994 1.00 68.97  ? 4056 GLU A OE2   1 
ATOM   18448 N  N     . ASP A 1 4057 ? 206.196 254.990 227.161 1.00 64.36  ? 4057 ASP A N     1 
ATOM   18449 C  CA    . ASP A 1 4057 ? 206.170 256.418 227.459 1.00 61.58  ? 4057 ASP A CA    1 
ATOM   18450 C  C     . ASP A 1 4057 ? 205.815 257.238 226.224 1.00 61.72  ? 4057 ASP A C     1 
ATOM   18451 O  O     . ASP A 1 4057 ? 205.049 258.206 226.311 1.00 67.73  ? 4057 ASP A O     1 
ATOM   18452 C  CB    . ASP A 1 4057 ? 207.518 256.850 228.031 1.00 64.21  ? 4057 ASP A CB    1 
ATOM   18453 C  CG    . ASP A 1 4057 ? 207.734 256.350 229.446 1.00 70.01  ? 4057 ASP A CG    1 
ATOM   18454 O  OD1   . ASP A 1 4057 ? 207.245 255.246 229.765 1.00 66.68  ? 4057 ASP A OD1   1 
ATOM   18455 O  OD2   . ASP A 1 4057 ? 208.395 257.054 230.236 1.00 68.98  ? 4057 ASP A OD2   1 
ATOM   18456 N  N     . LEU A 1 4058 ? 206.362 256.866 225.064 1.00 58.51  ? 4058 LEU A N     1 
ATOM   18457 C  CA    . LEU A 1 4058 ? 206.055 257.578 223.829 1.00 59.44  ? 4058 LEU A CA    1 
ATOM   18458 C  C     . LEU A 1 4058 ? 204.582 257.451 223.469 1.00 61.81  ? 4058 LEU A C     1 
ATOM   18459 O  O     . LEU A 1 4058 ? 203.958 258.426 223.036 1.00 69.61  ? 4058 LEU A O     1 
ATOM   18460 C  CB    . LEU A 1 4058 ? 206.934 257.051 222.695 1.00 61.53  ? 4058 LEU A CB    1 
ATOM   18461 C  CG    . LEU A 1 4058 ? 206.611 257.550 221.289 1.00 62.04  ? 4058 LEU A CG    1 
ATOM   18462 C  CD1   . LEU A 1 4058 ? 207.159 258.948 221.095 1.00 62.05  ? 4058 LEU A CD1   1 
ATOM   18463 C  CD2   . LEU A 1 4058 ? 207.172 256.604 220.244 1.00 61.65  ? 4058 LEU A CD2   1 
ATOM   18464 N  N     . ALA A 1 4059 ? 204.009 256.259 223.637 1.00 62.17  ? 4059 ALA A N     1 
ATOM   18465 C  CA    . ALA A 1 4059 ? 202.589 256.080 223.362 1.00 63.79  ? 4059 ALA A CA    1 
ATOM   18466 C  C     . ALA A 1 4059 ? 201.732 256.854 224.355 1.00 65.79  ? 4059 ALA A C     1 
ATOM   18467 O  O     . ALA A 1 4059 ? 200.694 257.412 223.983 1.00 68.76  ? 4059 ALA A O     1 
ATOM   18468 C  CB    . ALA A 1 4059 ? 202.234 254.595 223.384 1.00 58.78  ? 4059 ALA A CB    1 
ATOM   18469 N  N     . ALA A 1 4060 ? 202.146 256.894 225.623 1.00 68.90  ? 4060 ALA A N     1 
ATOM   18470 C  CA    . ALA A 1 4060 ? 201.375 257.611 226.633 1.00 69.41  ? 4060 ALA A CA    1 
ATOM   18471 C  C     . ALA A 1 4060 ? 201.381 259.113 226.376 1.00 73.65  ? 4060 ALA A C     1 
ATOM   18472 O  O     . ALA A 1 4060 ? 200.350 259.780 226.518 1.00 74.56  ? 4060 ALA A O     1 
ATOM   18473 C  CB    . ALA A 1 4060 ? 201.922 257.299 228.026 1.00 69.47  ? 4060 ALA A CB    1 
ATOM   18474 N  N     . GLU A 1 4061 ? 202.537 259.667 226.002 1.00 73.17  ? 4061 GLU A N     1 
ATOM   18475 C  CA    . GLU A 1 4061 ? 202.617 261.112 225.810 1.00 72.01  ? 4061 GLU A CA    1 
ATOM   18476 C  C     . GLU A 1 4061 ? 201.838 261.550 224.575 1.00 73.87  ? 4061 GLU A C     1 
ATOM   18477 O  O     . GLU A 1 4061 ? 201.275 262.650 224.545 1.00 74.88  ? 4061 GLU A O     1 
ATOM   18478 C  CB    . GLU A 1 4061 ? 204.077 261.561 225.726 1.00 69.97  ? 4061 GLU A CB    1 
ATOM   18479 C  CG    . GLU A 1 4061 ? 204.792 261.205 224.437 1.00 76.00  ? 4061 GLU A CG    1 
ATOM   18480 C  CD    . GLU A 1 4061 ? 206.239 261.656 224.432 1.00 80.54  ? 4061 GLU A CD    1 
ATOM   18481 O  OE1   . GLU A 1 4061 ? 206.707 262.165 225.472 1.00 76.79  ? 4061 GLU A OE1   1 
ATOM   18482 O  OE2   . GLU A 1 4061 ? 206.907 261.506 223.388 1.00 81.30  ? 4061 GLU A OE2   1 
ATOM   18483 N  N     . GLN A 1 4062 ? 201.787 260.703 223.548 1.00 71.65  ? 4062 GLN A N     1 
ATOM   18484 C  CA    . GLN A 1 4062 ? 201.007 260.999 222.354 1.00 72.09  ? 4062 GLN A CA    1 
ATOM   18485 C  C     . GLN A 1 4062 ? 199.552 260.575 222.483 1.00 73.89  ? 4062 GLN A C     1 
ATOM   18486 O  O     . GLN A 1 4062 ? 198.781 260.780 221.539 1.00 74.84  ? 4062 GLN A O     1 
ATOM   18487 C  CB    . GLN A 1 4062 ? 201.630 260.322 221.130 1.00 70.14  ? 4062 GLN A CB    1 
ATOM   18488 C  CG    . GLN A 1 4062 ? 203.077 260.700 220.870 1.00 71.05  ? 4062 GLN A CG    1 
ATOM   18489 C  CD    . GLN A 1 4062 ? 203.556 260.242 219.507 1.00 75.29  ? 4062 GLN A CD    1 
ATOM   18490 O  OE1   . GLN A 1 4062 ? 202.790 259.680 218.725 1.00 73.95  ? 4062 GLN A OE1   1 
ATOM   18491 N  NE2   . GLN A 1 4062 ? 204.829 260.478 219.216 1.00 76.23  ? 4062 GLN A NE2   1 
ATOM   18492 N  N     . ASN A 1 4063 ? 199.167 259.992 223.619 1.00 76.90  ? 4063 ASN A N     1 
ATOM   18493 C  CA    . ASN A 1 4063 ? 197.814 259.479 223.833 1.00 74.07  ? 4063 ASN A CA    1 
ATOM   18494 C  C     . ASN A 1 4063 ? 197.433 258.476 222.750 1.00 72.54  ? 4063 ASN A C     1 
ATOM   18495 O  O     . ASN A 1 4063 ? 196.289 258.416 222.297 1.00 73.38  ? 4063 ASN A O     1 
ATOM   18496 C  CB    . ASN A 1 4063 ? 196.795 260.616 223.913 1.00 73.02  ? 4063 ASN A CB    1 
ATOM   18497 C  CG    . ASN A 1 4063 ? 196.721 261.229 225.294 1.00 78.17  ? 4063 ASN A CG    1 
ATOM   18498 O  OD1   . ASN A 1 4063 ? 196.714 260.519 226.299 1.00 78.94  ? 4063 ASN A OD1   1 
ATOM   18499 N  ND2   . ASN A 1 4063 ? 196.667 262.554 225.353 1.00 76.77  ? 4063 ASN A ND2   1 
ATOM   18500 N  N     . THR A 1 4064 ? 198.410 257.681 222.329 1.00 66.07  ? 4064 THR A N     1 
ATOM   18501 C  CA    . THR A 1 4064 ? 198.200 256.634 221.341 1.00 64.05  ? 4064 THR A CA    1 
ATOM   18502 C  C     . THR A 1 4064 ? 198.092 255.301 222.065 1.00 65.51  ? 4064 THR A C     1 
ATOM   18503 O  O     . THR A 1 4064 ? 199.040 254.872 222.732 1.00 67.86  ? 4064 THR A O     1 
ATOM   18504 C  CB    . THR A 1 4064 ? 199.336 256.599 220.320 1.00 68.14  ? 4064 THR A CB    1 
ATOM   18505 O  OG1   . THR A 1 4064 ? 199.666 257.934 219.919 1.00 74.91  ? 4064 THR A OG1   1 
ATOM   18506 C  CG2   . THR A 1 4064 ? 198.923 255.800 219.097 1.00 64.48  ? 4064 THR A CG2   1 
ATOM   18507 N  N     . GLN A 1 4065 ? 196.937 254.656 221.939 1.00 64.23  ? 4065 GLN A N     1 
ATOM   18508 C  CA    . GLN A 1 4065 ? 196.740 253.342 222.530 1.00 62.19  ? 4065 GLN A CA    1 
ATOM   18509 C  C     . GLN A 1 4065 ? 197.666 252.316 221.884 1.00 62.04  ? 4065 GLN A C     1 
ATOM   18510 O  O     . GLN A 1 4065 ? 197.893 252.338 220.671 1.00 61.67  ? 4065 GLN A O     1 
ATOM   18511 C  CB    . GLN A 1 4065 ? 195.272 252.938 222.393 1.00 58.11  ? 4065 GLN A CB    1 
ATOM   18512 C  CG    . GLN A 1 4065 ? 194.829 252.647 220.970 1.00 66.44  ? 4065 GLN A CG    1 
ATOM   18513 C  CD    . GLN A 1 4065 ? 194.431 253.907 220.219 1.00 72.41  ? 4065 GLN A CD    1 
ATOM   18514 O  OE1   . GLN A 1 4065 ? 194.760 255.019 220.631 1.00 67.96  ? 4065 GLN A OE1   1 
ATOM   18515 N  NE2   . GLN A 1 4065 ? 193.720 253.737 219.111 1.00 68.68  ? 4065 GLN A NE2   1 
ATOM   18516 N  N     . ILE A 1 4066 ? 198.225 251.434 222.709 1.00 55.96  ? 4066 ILE A N     1 
ATOM   18517 C  CA    . ILE A 1 4066 ? 199.236 250.476 222.283 1.00 50.65  ? 4066 ILE A CA    1 
ATOM   18518 C  C     . ILE A 1 4066 ? 198.951 249.123 222.919 1.00 56.45  ? 4066 ILE A C     1 
ATOM   18519 O  O     . ILE A 1 4066 ? 198.458 249.035 224.048 1.00 58.91  ? 4066 ILE A O     1 
ATOM   18520 C  CB    . ILE A 1 4066 ? 200.662 250.961 222.638 1.00 48.08  ? 4066 ILE A CB    1 
ATOM   18521 C  CG1   . ILE A 1 4066 ? 201.719 249.990 222.114 1.00 46.48  ? 4066 ILE A CG1   1 
ATOM   18522 C  CG2   . ILE A 1 4066 ? 200.808 251.164 224.134 1.00 52.09  ? 4066 ILE A CG2   1 
ATOM   18523 C  CD1   . ILE A 1 4066 ? 203.121 250.520 222.201 1.00 52.09  ? 4066 ILE A CD1   1 
ATOM   18524 N  N     . THR A 1 4067 ? 199.256 248.062 222.176 1.00 48.56  ? 4067 THR A N     1 
ATOM   18525 C  CA    . THR A 1 4067 ? 199.154 246.689 222.656 1.00 45.50  ? 4067 THR A CA    1 
ATOM   18526 C  C     . THR A 1 4067 ? 200.564 246.120 222.753 1.00 42.83  ? 4067 THR A C     1 
ATOM   18527 O  O     . THR A 1 4067 ? 201.270 246.026 221.744 1.00 50.26  ? 4067 THR A O     1 
ATOM   18528 C  CB    . THR A 1 4067 ? 198.284 245.848 221.724 1.00 47.95  ? 4067 THR A CB    1 
ATOM   18529 O  OG1   . THR A 1 4067 ? 196.971 246.416 221.654 1.00 51.81  ? 4067 THR A OG1   1 
ATOM   18530 C  CG2   . THR A 1 4067 ? 198.186 244.420 222.227 1.00 45.33  ? 4067 THR A CG2   1 
ATOM   18531 N  N     . SER A 1 4068 ? 200.972 245.745 223.961 1.00 38.31  ? 4068 SER A N     1 
ATOM   18532 C  CA    . SER A 1 4068 ? 202.296 245.182 224.193 1.00 42.39  ? 4068 SER A CA    1 
ATOM   18533 C  C     . SER A 1 4068 ? 202.173 243.676 224.388 1.00 42.00  ? 4068 SER A C     1 
ATOM   18534 O  O     . SER A 1 4068 ? 201.416 243.216 225.250 1.00 49.36  ? 4068 SER A O     1 
ATOM   18535 C  CB    . SER A 1 4068 ? 202.955 245.834 225.406 1.00 46.23  ? 4068 SER A CB    1 
ATOM   18536 O  OG    . SER A 1 4068 ? 202.900 247.246 225.317 1.00 51.12  ? 4068 SER A OG    1 
ATOM   18537 N  N     . ILE A 1 4069 ? 202.909 242.913 223.585 1.00 31.33  ? 4069 ILE A N     1 
ATOM   18538 C  CA    . ILE A 1 4069 ? 202.842 241.457 223.589 1.00 38.95  ? 4069 ILE A CA    1 
ATOM   18539 C  C     . ILE A 1 4069 ? 204.259 240.919 223.708 1.00 40.72  ? 4069 ILE A C     1 
ATOM   18540 O  O     . ILE A 1 4069 ? 205.160 241.365 222.989 1.00 45.38  ? 4069 ILE A O     1 
ATOM   18541 C  CB    . ILE A 1 4069 ? 202.150 240.919 222.327 1.00 40.59  ? 4069 ILE A CB    1 
ATOM   18542 C  CG1   . ILE A 1 4069 ? 200.742 241.501 222.222 1.00 44.72  ? 4069 ILE A CG1   1 
ATOM   18543 C  CG2   . ILE A 1 4069 ? 202.106 239.402 222.343 1.00 36.01  ? 4069 ILE A CG2   1 
ATOM   18544 C  CD1   . ILE A 1 4069 ? 200.012 241.109 220.980 1.00 42.29  ? 4069 ILE A CD1   1 
ATOM   18545 N  N     . ALA A 1 4070 ? 204.456 239.968 224.617 1.00 40.37  ? 4070 ALA A N     1 
ATOM   18546 C  CA    . ALA A 1 4070 ? 205.768 239.370 224.826 1.00 36.14  ? 4070 ALA A CA    1 
ATOM   18547 C  C     . ALA A 1 4070 ? 205.855 238.052 224.067 1.00 39.05  ? 4070 ALA A C     1 
ATOM   18548 O  O     . ALA A 1 4070 ? 205.045 237.145 224.287 1.00 45.12  ? 4070 ALA A O     1 
ATOM   18549 C  CB    . ALA A 1 4070 ? 206.024 239.161 226.315 1.00 25.88  ? 4070 ALA A CB    1 
ATOM   18550 N  N     . ILE A 1 4071 ? 206.836 237.948 223.181 1.00 36.53  ? 4071 ILE A N     1 
ATOM   18551 C  CA    . ILE A 1 4071 ? 206.967 236.799 222.293 1.00 39.90  ? 4071 ILE A CA    1 
ATOM   18552 C  C     . ILE A 1 4071 ? 207.589 235.633 223.050 1.00 44.36  ? 4071 ILE A C     1 
ATOM   18553 O  O     . ILE A 1 4071 ? 208.384 235.818 223.977 1.00 47.19  ? 4071 ILE A O     1 
ATOM   18554 C  CB    . ILE A 1 4071 ? 207.795 237.194 221.052 1.00 32.72  ? 4071 ILE A CB    1 
ATOM   18555 C  CG1   . ILE A 1 4071 ? 207.099 238.324 220.296 1.00 35.67  ? 4071 ILE A CG1   1 
ATOM   18556 C  CG2   . ILE A 1 4071 ? 208.011 236.015 220.122 1.00 42.30  ? 4071 ILE A CG2   1 
ATOM   18557 C  CD1   . ILE A 1 4071 ? 205.682 238.002 219.892 1.00 38.11  ? 4071 ILE A CD1   1 
ATOM   18558 N  N     . GLY A 1 4072 ? 207.228 234.414 222.650 1.00 47.13  ? 4072 GLY A N     1 
ATOM   18559 C  CA    . GLY A 1 4072 ? 207.785 233.223 223.257 1.00 43.42  ? 4072 GLY A CA    1 
ATOM   18560 C  C     . GLY A 1 4072 ? 206.828 232.053 223.365 1.00 46.02  ? 4072 GLY A C     1 
ATOM   18561 O  O     . GLY A 1 4072 ? 207.263 230.899 223.410 1.00 53.46  ? 4072 GLY A O     1 
ATOM   18562 N  N     . SER A 1 4073 ? 205.529 232.326 223.398 1.00 51.96  ? 4073 SER A N     1 
ATOM   18563 C  CA    . SER A 1 4073 ? 204.517 231.287 223.505 1.00 47.29  ? 4073 SER A CA    1 
ATOM   18564 C  C     . SER A 1 4073 ? 203.613 231.297 222.278 1.00 54.95  ? 4073 SER A C     1 
ATOM   18565 O  O     . SER A 1 4073 ? 203.521 232.292 221.555 1.00 68.39  ? 4073 SER A O     1 
ATOM   18566 C  CB    . SER A 1 4073 ? 203.682 231.466 224.775 1.00 46.95  ? 4073 SER A CB    1 
ATOM   18567 O  OG    . SER A 1 4073 ? 203.062 232.739 224.803 1.00 55.11  ? 4073 SER A OG    1 
ATOM   18568 N  N     . ALA A 1 4074 ? 202.950 230.161 222.045 1.00 54.78  ? 4074 ALA A N     1 
ATOM   18569 C  CA    . ALA A 1 4074 ? 202.020 230.062 220.924 1.00 54.87  ? 4074 ALA A CA    1 
ATOM   18570 C  C     . ALA A 1 4074 ? 200.852 231.025 221.090 1.00 55.14  ? 4074 ALA A C     1 
ATOM   18571 O  O     . ALA A 1 4074 ? 200.419 231.667 220.123 1.00 61.76  ? 4074 ALA A O     1 
ATOM   18572 C  CB    . ALA A 1 4074 ? 201.516 228.626 220.787 1.00 55.68  ? 4074 ALA A CB    1 
ATOM   18573 N  N     . GLU A 1 4075 ? 200.324 231.132 222.311 1.00 51.00  ? 4075 GLU A N     1 
ATOM   18574 C  CA    . GLU A 1 4075 ? 199.330 232.159 222.593 1.00 53.67  ? 4075 GLU A CA    1 
ATOM   18575 C  C     . GLU A 1 4075 ? 199.878 233.543 222.288 1.00 59.97  ? 4075 GLU A C     1 
ATOM   18576 O  O     . GLU A 1 4075 ? 199.133 234.421 221.840 1.00 67.30  ? 4075 GLU A O     1 
ATOM   18577 C  CB    . GLU A 1 4075 ? 198.880 232.076 224.052 1.00 54.76  ? 4075 GLU A CB    1 
ATOM   18578 C  CG    . GLU A 1 4075 ? 198.396 230.700 224.480 1.00 59.17  ? 4075 GLU A CG    1 
ATOM   18579 C  CD    . GLU A 1 4075 ? 199.487 229.869 225.126 1.00 62.01  ? 4075 GLU A CD    1 
ATOM   18580 O  OE1   . GLU A 1 4075 ? 200.606 230.390 225.311 1.00 66.83  ? 4075 GLU A OE1   1 
ATOM   18581 O  OE2   . GLU A 1 4075 ? 199.225 228.693 225.453 1.00 55.46  ? 4075 GLU A OE2   1 
ATOM   18582 N  N     . GLY A 1 4076 ? 201.177 233.750 222.508 1.00 54.77  ? 4076 GLY A N     1 
ATOM   18583 C  CA    . GLY A 1 4076 ? 201.784 235.018 222.148 1.00 50.77  ? 4076 GLY A CA    1 
ATOM   18584 C  C     . GLY A 1 4076 ? 201.728 235.288 220.657 1.00 52.01  ? 4076 GLY A C     1 
ATOM   18585 O  O     . GLY A 1 4076 ? 201.423 236.404 220.236 1.00 60.23  ? 4076 GLY A O     1 
ATOM   18586 N  N     . PHE A 1 4077 ? 202.017 234.272 219.839 1.00 48.84  ? 4077 PHE A N     1 
ATOM   18587 C  CA    . PHE A 1 4077 ? 201.943 234.446 218.391 1.00 48.45  ? 4077 PHE A CA    1 
ATOM   18588 C  C     . PHE A 1 4077 ? 200.514 234.715 217.938 1.00 48.51  ? 4077 PHE A C     1 
ATOM   18589 O  O     . PHE A 1 4077 ? 200.280 235.566 217.070 1.00 54.32  ? 4077 PHE A O     1 
ATOM   18590 C  CB    . PHE A 1 4077 ? 202.505 233.216 217.683 1.00 48.23  ? 4077 PHE A CB    1 
ATOM   18591 C  CG    . PHE A 1 4077 ? 203.945 232.946 217.993 1.00 51.68  ? 4077 PHE A CG    1 
ATOM   18592 C  CD1   . PHE A 1 4077 ? 204.899 233.930 217.814 1.00 52.83  ? 4077 PHE A CD1   1 
ATOM   18593 C  CD2   . PHE A 1 4077 ? 204.347 231.711 218.466 1.00 53.73  ? 4077 PHE A CD2   1 
ATOM   18594 C  CE1   . PHE A 1 4077 ? 206.224 233.687 218.099 1.00 53.69  ? 4077 PHE A CE1   1 
ATOM   18595 C  CE2   . PHE A 1 4077 ? 205.671 231.464 218.753 1.00 51.21  ? 4077 PHE A CE2   1 
ATOM   18596 C  CZ    . PHE A 1 4077 ? 206.610 232.454 218.570 1.00 52.10  ? 4077 PHE A CZ    1 
ATOM   18597 N  N     . ASN A 1 4078 ? 199.543 233.996 218.507 1.00 46.90  ? 4078 ASN A N     1 
ATOM   18598 C  CA    . ASN A 1 4078 ? 198.150 234.237 218.142 1.00 51.55  ? 4078 ASN A CA    1 
ATOM   18599 C  C     . ASN A 1 4078 ? 197.716 235.648 218.521 1.00 52.83  ? 4078 ASN A C     1 
ATOM   18600 O  O     . ASN A 1 4078 ? 197.056 236.340 217.732 1.00 56.60  ? 4078 ASN A O     1 
ATOM   18601 C  CB    . ASN A 1 4078 ? 197.247 233.199 218.808 1.00 53.81  ? 4078 ASN A CB    1 
ATOM   18602 C  CG    . ASN A 1 4078 ? 197.656 231.778 218.482 1.00 60.23  ? 4078 ASN A CG    1 
ATOM   18603 O  OD1   . ASN A 1 4078 ? 198.480 231.545 217.599 1.00 62.54  ? 4078 ASN A OD1   1 
ATOM   18604 N  ND2   . ASN A 1 4078 ? 197.080 230.819 219.195 1.00 53.11  ? 4078 ASN A ND2   1 
ATOM   18605 N  N     . GLN A 1 4079 ? 198.088 236.095 219.721 1.00 49.70  ? 4079 GLN A N     1 
ATOM   18606 C  CA    . GLN A 1 4079 ? 197.752 237.446 220.152 1.00 45.96  ? 4079 GLN A CA    1 
ATOM   18607 C  C     . GLN A 1 4079 ? 198.432 238.490 219.279 1.00 45.74  ? 4079 GLN A C     1 
ATOM   18608 O  O     . GLN A 1 4079 ? 197.830 239.518 218.957 1.00 52.70  ? 4079 GLN A O     1 
ATOM   18609 C  CB    . GLN A 1 4079 ? 198.138 237.632 221.618 1.00 51.21  ? 4079 GLN A CB    1 
ATOM   18610 C  CG    . GLN A 1 4079 ? 197.365 238.718 222.339 1.00 57.21  ? 4079 GLN A CG    1 
ATOM   18611 C  CD    . GLN A 1 4079 ? 197.872 238.946 223.748 1.00 60.46  ? 4079 GLN A CD    1 
ATOM   18612 O  OE1   . GLN A 1 4079 ? 198.263 238.004 224.437 1.00 51.92  ? 4079 GLN A OE1   1 
ATOM   18613 N  NE2   . GLN A 1 4079 ? 197.869 240.200 224.183 1.00 56.27  ? 4079 GLN A NE2   1 
ATOM   18614 N  N     . ALA A 1 4080 ? 199.686 238.249 218.891 1.00 42.65  ? 4080 ALA A N     1 
ATOM   18615 C  CA    . ALA A 1 4080 ? 200.387 239.181 218.016 1.00 39.57  ? 4080 ALA A CA    1 
ATOM   18616 C  C     . ALA A 1 4080 ? 199.701 239.287 216.665 1.00 42.82  ? 4080 ALA A C     1 
ATOM   18617 O  O     . ALA A 1 4080 ? 199.526 240.389 216.133 1.00 47.40  ? 4080 ALA A O     1 
ATOM   18618 C  CB    . ALA A 1 4080 ? 201.842 238.746 217.843 1.00 42.55  ? 4080 ALA A CB    1 
ATOM   18619 N  N     . ASP A 1 4081 ? 199.306 238.148 216.093 1.00 51.62  ? 4081 ASP A N     1 
ATOM   18620 C  CA    . ASP A 1 4081 ? 198.620 238.169 214.807 1.00 43.66  ? 4081 ASP A CA    1 
ATOM   18621 C  C     . ASP A 1 4081 ? 197.306 238.932 214.909 1.00 46.64  ? 4081 ASP A C     1 
ATOM   18622 O  O     . ASP A 1 4081 ? 197.009 239.787 214.065 1.00 52.81  ? 4081 ASP A O     1 
ATOM   18623 C  CB    . ASP A 1 4081 ? 198.386 236.737 214.322 1.00 42.73  ? 4081 ASP A CB    1 
ATOM   18624 C  CG    . ASP A 1 4081 ? 197.869 236.672 212.895 1.00 59.08  ? 4081 ASP A CG    1 
ATOM   18625 O  OD1   . ASP A 1 4081 ? 197.656 237.733 212.274 1.00 59.99  ? 4081 ASP A OD1   1 
ATOM   18626 O  OD2   . ASP A 1 4081 ? 197.678 235.546 212.390 1.00 59.17  ? 4081 ASP A OD2   1 
ATOM   18627 N  N     . LYS A 1 4082 ? 196.516 238.655 215.952 1.00 47.08  ? 4082 LYS A N     1 
ATOM   18628 C  CA    . LYS A 1 4082 ? 195.245 239.357 216.117 1.00 43.71  ? 4082 LYS A CA    1 
ATOM   18629 C  C     . LYS A 1 4082 ? 195.456 240.854 216.306 1.00 45.61  ? 4082 LYS A C     1 
ATOM   18630 O  O     . LYS A 1 4082 ? 194.745 241.670 215.706 1.00 53.48  ? 4082 LYS A O     1 
ATOM   18631 C  CB    . LYS A 1 4082 ? 194.472 238.778 217.302 1.00 47.40  ? 4082 LYS A CB    1 
ATOM   18632 C  CG    . LYS A 1 4082 ? 194.013 237.344 217.115 1.00 55.48  ? 4082 LYS A CG    1 
ATOM   18633 C  CD    . LYS A 1 4082 ? 193.243 236.856 218.331 1.00 52.67  ? 4082 LYS A CD    1 
ATOM   18634 C  CE    . LYS A 1 4082 ? 192.701 235.452 218.118 1.00 52.22  ? 4082 LYS A CE    1 
ATOM   18635 N  NZ    . LYS A 1 4082 ? 193.794 234.444 218.023 1.00 52.88  ? 4082 LYS A NZ    1 
ATOM   18636 N  N     . ALA A 1 4083 ? 196.432 241.235 217.135 1.00 46.94  ? 4083 ALA A N     1 
ATOM   18637 C  CA    . ALA A 1 4083 ? 196.677 242.646 217.405 1.00 43.09  ? 4083 ALA A CA    1 
ATOM   18638 C  C     . ALA A 1 4083 ? 197.135 243.379 216.155 1.00 46.72  ? 4083 ALA A C     1 
ATOM   18639 O  O     . ALA A 1 4083 ? 196.683 244.497 215.889 1.00 52.08  ? 4083 ALA A O     1 
ATOM   18640 C  CB    . ALA A 1 4083 ? 197.707 242.794 218.523 1.00 45.00  ? 4083 ALA A CB    1 
ATOM   18641 N  N     . ILE A 1 4084 ? 198.032 242.773 215.376 1.00 39.70  ? 4084 ILE A N     1 
ATOM   18642 C  CA    . ILE A 1 4084 ? 198.489 243.411 214.146 1.00 40.16  ? 4084 ILE A CA    1 
ATOM   18643 C  C     . ILE A 1 4084 ? 197.342 243.543 213.154 1.00 43.80  ? 4084 ILE A C     1 
ATOM   18644 O  O     . ILE A 1 4084 ? 197.168 244.593 212.523 1.00 46.58  ? 4084 ILE A O     1 
ATOM   18645 C  CB    . ILE A 1 4084 ? 199.675 242.632 213.550 1.00 43.74  ? 4084 ILE A CB    1 
ATOM   18646 C  CG1   . ILE A 1 4084 ? 200.926 242.842 214.401 1.00 44.72  ? 4084 ILE A CG1   1 
ATOM   18647 C  CG2   . ILE A 1 4084 ? 199.935 243.057 212.118 1.00 42.88  ? 4084 ILE A CG2   1 
ATOM   18648 C  CD1   . ILE A 1 4084 ? 202.040 241.883 214.087 1.00 39.86  ? 4084 ILE A CD1   1 
ATOM   18649 N  N     . ASN A 1 4085 ? 196.534 242.488 213.005 1.00 46.75  ? 4085 ASN A N     1 
ATOM   18650 C  CA    . ASN A 1 4085 ? 195.419 242.542 212.066 1.00 42.19  ? 4085 ASN A CA    1 
ATOM   18651 C  C     . ASN A 1 4085 ? 194.416 243.618 212.458 1.00 45.59  ? 4085 ASN A C     1 
ATOM   18652 O  O     . ASN A 1 4085 ? 193.857 244.300 211.592 1.00 51.81  ? 4085 ASN A O     1 
ATOM   18653 C  CB    . ASN A 1 4085 ? 194.739 241.176 211.986 1.00 43.85  ? 4085 ASN A CB    1 
ATOM   18654 C  CG    . ASN A 1 4085 ? 195.557 240.167 211.213 1.00 50.54  ? 4085 ASN A CG    1 
ATOM   18655 O  OD1   . ASN A 1 4085 ? 196.492 240.528 210.503 1.00 53.36  ? 4085 ASN A OD1   1 
ATOM   18656 N  ND2   . ASN A 1 4085 ? 195.214 238.894 211.350 1.00 46.68  ? 4085 ASN A ND2   1 
ATOM   18657 N  N     . THR A 1 4086 ? 194.166 243.779 213.758 1.00 46.36  ? 4086 THR A N     1 
ATOM   18658 C  CA    . THR A 1 4086 ? 193.244 244.818 214.204 1.00 40.76  ? 4086 THR A CA    1 
ATOM   18659 C  C     . THR A 1 4086 ? 193.847 246.210 214.041 1.00 48.77  ? 4086 THR A C     1 
ATOM   18660 O  O     . THR A 1 4086 ? 193.151 247.151 213.640 1.00 52.85  ? 4086 THR A O     1 
ATOM   18661 C  CB    . THR A 1 4086 ? 192.846 244.572 215.658 1.00 47.98  ? 4086 THR A CB    1 
ATOM   18662 O  OG1   . THR A 1 4086 ? 192.227 243.285 215.773 1.00 48.77  ? 4086 THR A OG1   1 
ATOM   18663 C  CG2   . THR A 1 4086 ? 191.872 245.636 216.136 1.00 50.99  ? 4086 THR A CG2   1 
ATOM   18664 N  N     . ALA A 1 4087 ? 195.141 246.359 214.335 1.00 49.90  ? 4087 ALA A N     1 
ATOM   18665 C  CA    . ALA A 1 4087 ? 195.748 247.683 214.361 1.00 43.02  ? 4087 ALA A CA    1 
ATOM   18666 C  C     . ALA A 1 4087 ? 196.021 248.223 212.964 1.00 49.38  ? 4087 ALA A C     1 
ATOM   18667 O  O     . ALA A 1 4087 ? 195.974 249.441 212.760 1.00 54.42  ? 4087 ALA A O     1 
ATOM   18668 C  CB    . ALA A 1 4087 ? 197.039 247.652 215.175 1.00 44.75  ? 4087 ALA A CB    1 
ATOM   18669 N  N     . VAL A 1 4088 ? 196.313 247.353 211.992 1.00 44.94  ? 4088 VAL A N     1 
ATOM   18670 C  CA    . VAL A 1 4088 ? 196.541 247.847 210.637 1.00 42.65  ? 4088 VAL A CA    1 
ATOM   18671 C  C     . VAL A 1 4088 ? 195.289 248.489 210.060 1.00 55.33  ? 4088 VAL A C     1 
ATOM   18672 O  O     . VAL A 1 4088 ? 195.378 249.246 209.087 1.00 60.94  ? 4088 VAL A O     1 
ATOM   18673 C  CB    . VAL A 1 4088 ? 197.043 246.730 209.704 1.00 39.31  ? 4088 VAL A CB    1 
ATOM   18674 C  CG1   . VAL A 1 4088 ? 198.404 246.243 210.152 1.00 48.45  ? 4088 VAL A CG1   1 
ATOM   18675 C  CG2   . VAL A 1 4088 ? 196.047 245.592 209.649 1.00 48.94  ? 4088 VAL A CG2   1 
ATOM   18676 N  N     . LYS A 1 4089 ? 194.120 248.205 210.630 1.00 58.80  ? 4089 LYS A N     1 
ATOM   18677 C  CA    . LYS A 1 4089 ? 192.875 248.843 210.227 1.00 52.25  ? 4089 LYS A CA    1 
ATOM   18678 C  C     . LYS A 1 4089 ? 192.464 249.976 211.156 1.00 53.92  ? 4089 LYS A C     1 
ATOM   18679 O  O     . LYS A 1 4089 ? 192.113 251.060 210.683 1.00 58.47  ? 4089 LYS A O     1 
ATOM   18680 C  CB    . LYS A 1 4089 ? 191.748 247.808 210.159 1.00 47.30  ? 4089 LYS A CB    1 
ATOM   18681 C  CG    . LYS A 1 4089 ? 191.958 246.735 209.106 1.00 51.71  ? 4089 LYS A CG    1 
ATOM   18682 C  CD    . LYS A 1 4089 ? 190.776 245.783 209.043 1.00 55.94  ? 4089 LYS A CD    1 
ATOM   18683 C  CE    . LYS A 1 4089 ? 190.707 244.897 210.274 1.00 59.54  ? 4089 LYS A CE    1 
ATOM   18684 N  NZ    . LYS A 1 4089 ? 191.864 243.964 210.347 1.00 61.74  ? 4089 LYS A NZ    1 
ATOM   18685 N  N     . SER A 1 4090 ? 192.504 249.752 212.470 1.00 52.48  ? 4090 SER A N     1 
ATOM   18686 C  CA    . SER A 1 4090 ? 192.063 250.771 213.415 1.00 49.00  ? 4090 SER A CA    1 
ATOM   18687 C  C     . SER A 1 4090 ? 193.081 251.891 213.589 1.00 54.38  ? 4090 SER A C     1 
ATOM   18688 O  O     . SER A 1 4090 ? 192.694 253.031 213.868 1.00 58.89  ? 4090 SER A O     1 
ATOM   18689 C  CB    . SER A 1 4090 ? 191.757 250.127 214.765 1.00 55.97  ? 4090 SER A CB    1 
ATOM   18690 O  OG    . SER A 1 4090 ? 192.923 249.546 215.315 1.00 61.86  ? 4090 SER A OG    1 
ATOM   18691 N  N     . GLY A 1 4091 ? 194.367 251.600 213.434 1.00 58.14  ? 4091 GLY A N     1 
ATOM   18692 C  CA    . GLY A 1 4091 ? 195.403 252.591 213.630 1.00 53.67  ? 4091 GLY A CA    1 
ATOM   18693 C  C     . GLY A 1 4091 ? 196.071 252.578 214.986 1.00 60.14  ? 4091 GLY A C     1 
ATOM   18694 O  O     . GLY A 1 4091 ? 196.814 253.515 215.296 1.00 62.47  ? 4091 GLY A O     1 
ATOM   18695 N  N     . ARG A 1 4092 ? 195.830 251.555 215.801 1.00 60.71  ? 4092 ARG A N     1 
ATOM   18696 C  CA    . ARG A 1 4092 ? 196.484 251.432 217.093 1.00 52.22  ? 4092 ARG A CA    1 
ATOM   18697 C  C     . ARG A 1 4092 ? 197.977 251.172 216.903 1.00 55.55  ? 4092 ARG A C     1 
ATOM   18698 O  O     . ARG A 1 4092 ? 198.459 250.904 215.799 1.00 54.75  ? 4092 ARG A O     1 
ATOM   18699 C  CB    . ARG A 1 4092 ? 195.842 250.304 217.897 1.00 55.35  ? 4092 ARG A CB    1 
ATOM   18700 C  CG    . ARG A 1 4092 ? 194.324 250.345 217.935 1.00 54.31  ? 4092 ARG A CG    1 
ATOM   18701 C  CD    . ARG A 1 4092 ? 193.750 249.263 218.840 1.00 61.04  ? 4092 ARG A CD    1 
ATOM   18702 N  NE    . ARG A 1 4092 ? 193.744 249.635 220.249 1.00 68.44  ? 4092 ARG A NE    1 
ATOM   18703 C  CZ    . ARG A 1 4092 ? 194.654 249.240 221.129 1.00 65.78  ? 4092 ARG A CZ    1 
ATOM   18704 N  NH1   . ARG A 1 4092 ? 195.662 248.461 220.776 1.00 59.52  ? 4092 ARG A NH1   1 
ATOM   18705 N  NH2   . ARG A 1 4092 ? 194.548 249.637 222.394 1.00 57.84  ? 4092 ARG A NH2   1 
ATOM   18706 N  N     . TRP A 1 4093 ? 198.720 251.256 217.999 1.00 54.13  ? 4093 TRP A N     1 
ATOM   18707 C  CA    . TRP A 1 4093 ? 200.118 250.859 218.028 1.00 45.19  ? 4093 TRP A CA    1 
ATOM   18708 C  C     . TRP A 1 4093 ? 200.240 249.452 218.593 1.00 50.10  ? 4093 TRP A C     1 
ATOM   18709 O  O     . TRP A 1 4093 ? 199.428 249.020 219.414 1.00 54.37  ? 4093 TRP A O     1 
ATOM   18710 C  CB    . TRP A 1 4093 ? 200.959 251.823 218.866 1.00 48.01  ? 4093 TRP A CB    1 
ATOM   18711 C  CG    . TRP A 1 4093 ? 201.283 253.109 218.187 1.00 47.94  ? 4093 TRP A CG    1 
ATOM   18712 C  CD1   . TRP A 1 4093 ? 200.796 253.552 216.996 1.00 51.37  ? 4093 TRP A CD1   1 
ATOM   18713 C  CD2   . TRP A 1 4093 ? 202.188 254.114 218.650 1.00 50.07  ? 4093 TRP A CD2   1 
ATOM   18714 N  NE1   . TRP A 1 4093 ? 201.334 254.778 216.692 1.00 49.30  ? 4093 TRP A NE1   1 
ATOM   18715 C  CE2   . TRP A 1 4093 ? 202.193 255.145 217.693 1.00 50.18  ? 4093 TRP A CE2   1 
ATOM   18716 C  CE3   . TRP A 1 4093 ? 202.993 254.246 219.786 1.00 50.49  ? 4093 TRP A CE3   1 
ATOM   18717 C  CZ2   . TRP A 1 4093 ? 202.969 256.290 217.835 1.00 51.10  ? 4093 TRP A CZ2   1 
ATOM   18718 C  CZ3   . TRP A 1 4093 ? 203.762 255.382 219.924 1.00 50.15  ? 4093 TRP A CZ3   1 
ATOM   18719 C  CH2   . TRP A 1 4093 ? 203.745 256.389 218.955 1.00 49.69  ? 4093 TRP A CH2   1 
ATOM   18720 N  N     . VAL A 1 4094 ? 201.256 248.733 218.130 1.00 44.36  ? 4094 VAL A N     1 
ATOM   18721 C  CA    . VAL A 1 4094 ? 201.528 247.376 218.586 1.00 42.14  ? 4094 VAL A CA    1 
ATOM   18722 C  C     . VAL A 1 4094 ? 203.025 247.236 218.804 1.00 41.50  ? 4094 VAL A C     1 
ATOM   18723 O  O     . VAL A 1 4094 ? 203.820 247.588 217.926 1.00 47.10  ? 4094 VAL A O     1 
ATOM   18724 C  CB    . VAL A 1 4094 ? 201.027 246.319 217.583 1.00 38.75  ? 4094 VAL A CB    1 
ATOM   18725 C  CG1   . VAL A 1 4094 ? 201.523 244.943 217.969 1.00 39.46  ? 4094 VAL A CG1   1 
ATOM   18726 C  CG2   . VAL A 1 4094 ? 199.516 246.325 217.528 1.00 47.94  ? 4094 VAL A CG2   1 
ATOM   18727 N  N     . MET A 1 4095 ? 203.412 246.734 219.972 1.00 36.65  ? 4095 MET A N     1 
ATOM   18728 C  CA    . MET A 1 4095 ? 204.800 246.410 220.257 1.00 38.44  ? 4095 MET A CA    1 
ATOM   18729 C  C     . MET A 1 4095 ? 204.901 244.940 220.628 1.00 38.28  ? 4095 MET A C     1 
ATOM   18730 O  O     . MET A 1 4095 ? 204.138 244.454 221.468 1.00 43.30  ? 4095 MET A O     1 
ATOM   18731 C  CB    . MET A 1 4095 ? 205.372 247.280 221.377 1.00 41.32  ? 4095 MET A CB    1 
ATOM   18732 C  CG    . MET A 1 4095 ? 206.553 246.636 222.080 1.00 44.62  ? 4095 MET A CG    1 
ATOM   18733 S  SD    . MET A 1 4095 ? 207.463 247.743 223.159 1.00 54.50  ? 4095 MET A SD    1 
ATOM   18734 C  CE    . MET A 1 4095 ? 206.222 248.094 224.383 1.00 41.84  ? 4095 MET A CE    1 
ATOM   18735 N  N     . LEU A 1 4096 ? 205.834 244.236 219.994 1.00 31.31  ? 4096 LEU A N     1 
ATOM   18736 C  CA    . LEU A 1 4096 ? 206.131 242.846 220.310 1.00 30.91  ? 4096 LEU A CA    1 
ATOM   18737 C  C     . LEU A 1 4096 ? 207.526 242.792 220.911 1.00 32.11  ? 4096 LEU A C     1 
ATOM   18738 O  O     . LEU A 1 4096 ? 208.484 243.280 220.304 1.00 41.15  ? 4096 LEU A O     1 
ATOM   18739 C  CB    . LEU A 1 4096 ? 206.033 241.965 219.064 1.00 33.03  ? 4096 LEU A CB    1 
ATOM   18740 C  CG    . LEU A 1 4096 ? 204.813 242.231 218.183 1.00 31.58  ? 4096 LEU A CG    1 
ATOM   18741 C  CD1   . LEU A 1 4096 ? 204.910 241.459 216.890 1.00 31.70  ? 4096 LEU A CD1   1 
ATOM   18742 C  CD2   . LEU A 1 4096 ? 203.533 241.879 218.915 1.00 34.08  ? 4096 LEU A CD2   1 
ATOM   18743 N  N     . LYS A 1 4097 ? 207.638 242.207 222.097 1.00 36.08  ? 4097 LYS A N     1 
ATOM   18744 C  CA    . LYS A 1 4097 ? 208.884 242.214 222.846 1.00 35.42  ? 4097 LYS A CA    1 
ATOM   18745 C  C     . LYS A 1 4097 ? 209.602 240.877 222.727 1.00 32.82  ? 4097 LYS A C     1 
ATOM   18746 O  O     . LYS A 1 4097 ? 208.978 239.825 222.578 1.00 42.81  ? 4097 LYS A O     1 
ATOM   18747 C  CB    . LYS A 1 4097 ? 208.634 242.532 224.320 1.00 31.38  ? 4097 LYS A CB    1 
ATOM   18748 C  CG    . LYS A 1 4097 ? 207.610 243.620 224.563 1.00 33.70  ? 4097 LYS A CG    1 
ATOM   18749 C  CD    . LYS A 1 4097 ? 207.440 243.868 226.045 1.00 32.38  ? 4097 LYS A CD    1 
ATOM   18750 C  CE    . LYS A 1 4097 ? 206.007 244.197 226.390 1.00 39.99  ? 4097 LYS A CE    1 
ATOM   18751 N  NZ    . LYS A 1 4097 ? 205.723 243.934 227.826 1.00 45.12  ? 4097 LYS A NZ    1 
ATOM   18752 N  N     . ASN A 1 4098 ? 210.933 240.938 222.806 1.00 31.56  ? 4098 ASN A N     1 
ATOM   18753 C  CA    . ASN A 1 4098 ? 211.792 239.755 222.747 1.00 31.66  ? 4098 ASN A CA    1 
ATOM   18754 C  C     . ASN A 1 4098 ? 211.529 238.935 221.487 1.00 40.00  ? 4098 ASN A C     1 
ATOM   18755 O  O     . ASN A 1 4098 ? 211.460 237.706 221.529 1.00 49.56  ? 4098 ASN A O     1 
ATOM   18756 C  CB    . ASN A 1 4098 ? 211.632 238.891 223.999 1.00 37.00  ? 4098 ASN A CB    1 
ATOM   18757 C  CG    . ASN A 1 4098 ? 211.792 239.684 225.278 1.00 38.59  ? 4098 ASN A CG    1 
ATOM   18758 O  OD1   . ASN A 1 4098 ? 212.780 240.393 225.462 1.00 38.68  ? 4098 ASN A OD1   1 
ATOM   18759 N  ND2   . ASN A 1 4098 ? 210.819 239.568 226.171 1.00 35.74  ? 4098 ASN A ND2   1 
ATOM   18760 N  N     . VAL A 1 4099 ? 211.383 239.622 220.352 1.00 41.21  ? 4099 VAL A N     1 
ATOM   18761 C  CA    . VAL A 1 4099 ? 211.134 238.930 219.095 1.00 35.87  ? 4099 VAL A CA    1 
ATOM   18762 C  C     . VAL A 1 4099 ? 212.353 238.147 218.635 1.00 32.65  ? 4099 VAL A C     1 
ATOM   18763 O  O     . VAL A 1 4099 ? 212.236 237.293 217.750 1.00 43.99  ? 4099 VAL A O     1 
ATOM   18764 C  CB    . VAL A 1 4099 ? 210.684 239.921 218.006 1.00 33.17  ? 4099 VAL A CB    1 
ATOM   18765 C  CG1   . VAL A 1 4099 ? 209.494 240.725 218.486 1.00 32.22  ? 4099 VAL A CG1   1 
ATOM   18766 C  CG2   . VAL A 1 4099 ? 211.826 240.835 217.614 1.00 33.91  ? 4099 VAL A CG2   1 
ATOM   18767 N  N     . HIS A 1 4100 ? 213.525 238.410 219.214 1.00 32.54  ? 4100 HIS A N     1 
ATOM   18768 C  CA    . HIS A 1 4100 ? 214.716 237.646 218.868 1.00 36.24  ? 4100 HIS A CA    1 
ATOM   18769 C  C     . HIS A 1 4100 ? 214.619 236.195 219.314 1.00 40.68  ? 4100 HIS A C     1 
ATOM   18770 O  O     . HIS A 1 4100 ? 215.425 235.369 218.874 1.00 42.44  ? 4100 HIS A O     1 
ATOM   18771 C  CB    . HIS A 1 4100 ? 215.954 238.297 219.484 1.00 34.25  ? 4100 HIS A CB    1 
ATOM   18772 C  CG    . HIS A 1 4100 ? 215.932 238.341 220.979 1.00 37.74  ? 4100 HIS A CG    1 
ATOM   18773 N  ND1   . HIS A 1 4100 ? 215.242 239.302 221.685 1.00 45.10  ? 4100 HIS A ND1   1 
ATOM   18774 C  CD2   . HIS A 1 4100 ? 216.512 237.541 221.904 1.00 39.80  ? 4100 HIS A CD2   1 
ATOM   18775 C  CE1   . HIS A 1 4100 ? 215.398 239.093 222.979 1.00 40.93  ? 4100 HIS A CE1   1 
ATOM   18776 N  NE2   . HIS A 1 4100 ? 216.166 238.031 223.139 1.00 39.87  ? 4100 HIS A NE2   1 
ATOM   18777 N  N     . LEU A 1 4101 ? 213.657 235.869 220.177 1.00 38.75  ? 4101 LEU A N     1 
ATOM   18778 C  CA    . LEU A 1 4101 ? 213.465 234.502 220.639 1.00 35.69  ? 4101 LEU A CA    1 
ATOM   18779 C  C     . LEU A 1 4101 ? 212.693 233.644 219.649 1.00 43.12  ? 4101 LEU A C     1 
ATOM   18780 O  O     . LEU A 1 4101 ? 212.616 232.426 219.840 1.00 47.29  ? 4101 LEU A O     1 
ATOM   18781 C  CB    . LEU A 1 4101 ? 212.741 234.501 221.986 1.00 33.87  ? 4101 LEU A CB    1 
ATOM   18782 C  CG    . LEU A 1 4101 ? 213.459 235.207 223.136 1.00 37.15  ? 4101 LEU A CG    1 
ATOM   18783 C  CD1   . LEU A 1 4101 ? 212.626 235.147 224.398 1.00 37.90  ? 4101 LEU A CD1   1 
ATOM   18784 C  CD2   . LEU A 1 4101 ? 214.830 234.597 223.365 1.00 37.30  ? 4101 LEU A CD2   1 
ATOM   18785 N  N     . ALA A 1 4102 ? 212.125 234.241 218.604 1.00 46.52  ? 4102 ALA A N     1 
ATOM   18786 C  CA    . ALA A 1 4102 ? 211.381 233.516 217.576 1.00 44.40  ? 4102 ALA A CA    1 
ATOM   18787 C  C     . ALA A 1 4102 ? 211.880 233.946 216.203 1.00 42.43  ? 4102 ALA A C     1 
ATOM   18788 O  O     . ALA A 1 4102 ? 211.173 234.635 215.459 1.00 43.49  ? 4102 ALA A O     1 
ATOM   18789 C  CB    . ALA A 1 4102 ? 209.879 233.760 217.715 1.00 44.98  ? 4102 ALA A CB    1 
ATOM   18790 N  N     . PRO A 1 4103 ? 213.109 233.567 215.841 1.00 45.34  ? 4103 PRO A N     1 
ATOM   18791 C  CA    . PRO A 1 4103 ? 213.630 233.958 214.522 1.00 44.68  ? 4103 PRO A CA    1 
ATOM   18792 C  C     . PRO A 1 4103 ? 212.842 233.382 213.359 1.00 50.20  ? 4103 PRO A C     1 
ATOM   18793 O  O     . PRO A 1 4103 ? 212.762 234.020 212.302 1.00 56.43  ? 4103 PRO A O     1 
ATOM   18794 C  CB    . PRO A 1 4103 ? 215.070 233.432 214.548 1.00 45.94  ? 4103 PRO A CB    1 
ATOM   18795 C  CG    . PRO A 1 4103 ? 215.044 232.314 215.520 1.00 48.53  ? 4103 PRO A CG    1 
ATOM   18796 C  CD    . PRO A 1 4103 ? 214.044 232.693 216.568 1.00 49.23  ? 4103 PRO A CD    1 
ATOM   18797 N  N     . GLY A 1 4104 ? 212.268 232.187 213.513 1.00 48.57  ? 4104 GLY A N     1 
ATOM   18798 C  CA    . GLY A 1 4104 ? 211.476 231.615 212.437 1.00 49.36  ? 4104 GLY A CA    1 
ATOM   18799 C  C     . GLY A 1 4104 ? 210.197 232.387 212.177 1.00 50.40  ? 4104 GLY A C     1 
ATOM   18800 O  O     . GLY A 1 4104 ? 209.782 232.552 211.027 1.00 56.04  ? 4104 GLY A O     1 
ATOM   18801 N  N     . TRP A 1 4105 ? 209.553 232.865 213.240 1.00 44.17  ? 4105 TRP A N     1 
ATOM   18802 C  CA    . TRP A 1 4105 ? 208.328 233.638 213.092 1.00 44.29  ? 4105 TRP A CA    1 
ATOM   18803 C  C     . TRP A 1 4105 ? 208.593 235.032 212.538 1.00 51.11  ? 4105 TRP A C     1 
ATOM   18804 O  O     . TRP A 1 4105 ? 207.676 235.656 211.992 1.00 51.12  ? 4105 TRP A O     1 
ATOM   18805 C  CB    . TRP A 1 4105 ? 207.620 233.721 214.443 1.00 48.51  ? 4105 TRP A CB    1 
ATOM   18806 C  CG    . TRP A 1 4105 ? 206.348 234.493 214.437 1.00 49.30  ? 4105 TRP A CG    1 
ATOM   18807 C  CD1   . TRP A 1 4105 ? 205.131 234.056 214.013 1.00 50.51  ? 4105 TRP A CD1   1 
ATOM   18808 C  CD2   . TRP A 1 4105 ? 206.155 235.830 214.907 1.00 50.07  ? 4105 TRP A CD2   1 
ATOM   18809 N  NE1   . TRP A 1 4105 ? 204.191 235.043 214.175 1.00 54.12  ? 4105 TRP A NE1   1 
ATOM   18810 C  CE2   . TRP A 1 4105 ? 204.796 236.143 214.723 1.00 50.24  ? 4105 TRP A CE2   1 
ATOM   18811 C  CE3   . TRP A 1 4105 ? 207.000 236.797 215.457 1.00 48.22  ? 4105 TRP A CE3   1 
ATOM   18812 C  CZ2   . TRP A 1 4105 ? 204.263 237.377 215.070 1.00 50.77  ? 4105 TRP A CZ2   1 
ATOM   18813 C  CZ3   . TRP A 1 4105 ? 206.469 238.020 215.800 1.00 44.73  ? 4105 TRP A CZ3   1 
ATOM   18814 C  CH2   . TRP A 1 4105 ? 205.114 238.300 215.606 1.00 53.18  ? 4105 TRP A CH2   1 
ATOM   18815 N  N     . LEU A 1 4106 ? 209.824 235.530 212.659 1.00 50.47  ? 4106 LEU A N     1 
ATOM   18816 C  CA    . LEU A 1 4106 ? 210.138 236.854 212.138 1.00 44.54  ? 4106 LEU A CA    1 
ATOM   18817 C  C     . LEU A 1 4106 ? 210.125 236.872 210.614 1.00 53.28  ? 4106 LEU A C     1 
ATOM   18818 O  O     . LEU A 1 4106 ? 209.762 237.889 210.013 1.00 61.38  ? 4106 LEU A O     1 
ATOM   18819 C  CB    . LEU A 1 4106 ? 211.487 237.316 212.685 1.00 51.61  ? 4106 LEU A CB    1 
ATOM   18820 C  CG    . LEU A 1 4106 ? 211.380 237.935 214.080 1.00 49.35  ? 4106 LEU A CG    1 
ATOM   18821 C  CD1   . LEU A 1 4106 ? 212.728 238.377 214.605 1.00 46.84  ? 4106 LEU A CD1   1 
ATOM   18822 C  CD2   . LEU A 1 4106 ? 210.416 239.094 214.072 1.00 50.93  ? 4106 LEU A CD2   1 
ATOM   18823 N  N     . MET A 1 4107 ? 210.504 235.759 209.976 1.00 54.99  ? 4107 MET A N     1 
ATOM   18824 C  CA    . MET A 1 4107 ? 210.333 235.634 208.530 1.00 52.74  ? 4107 MET A CA    1 
ATOM   18825 C  C     . MET A 1 4107 ? 208.879 235.838 208.131 1.00 56.72  ? 4107 MET A C     1 
ATOM   18826 O  O     . MET A 1 4107 ? 208.574 236.647 207.245 1.00 63.09  ? 4107 MET A O     1 
ATOM   18827 C  CB    . MET A 1 4107 ? 210.801 234.255 208.061 1.00 55.65  ? 4107 MET A CB    1 
ATOM   18828 C  CG    . MET A 1 4107 ? 212.279 233.957 208.217 1.00 61.30  ? 4107 MET A CG    1 
ATOM   18829 S  SD    . MET A 1 4107 ? 213.317 235.028 207.213 1.00 75.93  ? 4107 MET A SD    1 
ATOM   18830 C  CE    . MET A 1 4107 ? 214.936 234.566 207.815 1.00 58.31  ? 4107 MET A CE    1 
ATOM   18831 N  N     . GLN A 1 4108 ? 207.967 235.118 208.785 1.00 53.43  ? 4108 GLN A N     1 
ATOM   18832 C  CA    . GLN A 1 4108 ? 206.551 235.234 208.462 1.00 53.25  ? 4108 GLN A CA    1 
ATOM   18833 C  C     . GLN A 1 4108 ? 206.030 236.632 208.758 1.00 52.84  ? 4108 GLN A C     1 
ATOM   18834 O  O     . GLN A 1 4108 ? 205.209 237.165 208.007 1.00 60.29  ? 4108 GLN A O     1 
ATOM   18835 C  CB    . GLN A 1 4108 ? 205.753 234.189 209.237 1.00 55.45  ? 4108 GLN A CB    1 
ATOM   18836 C  CG    . GLN A 1 4108 ? 206.499 232.888 209.464 1.00 61.46  ? 4108 GLN A CG    1 
ATOM   18837 C  CD    . GLN A 1 4108 ? 205.711 231.916 210.316 1.00 63.87  ? 4108 GLN A CD    1 
ATOM   18838 O  OE1   . GLN A 1 4108 ? 204.577 232.195 210.703 1.00 61.44  ? 4108 GLN A OE1   1 
ATOM   18839 N  NE2   . GLN A 1 4108 ? 206.308 230.768 210.613 1.00 61.14  ? 4108 GLN A NE2   1 
ATOM   18840 N  N     . LEU A 1 4109 ? 206.484 237.236 209.858 1.00 51.49  ? 4109 LEU A N     1 
ATOM   18841 C  CA    . LEU A 1 4109 ? 206.052 238.592 210.180 1.00 48.56  ? 4109 LEU A CA    1 
ATOM   18842 C  C     . LEU A 1 4109 ? 206.503 239.582 209.113 1.00 46.58  ? 4109 LEU A C     1 
ATOM   18843 O  O     . LEU A 1 4109 ? 205.737 240.465 208.712 1.00 53.86  ? 4109 LEU A O     1 
ATOM   18844 C  CB    . LEU A 1 4109 ? 206.580 239.003 211.552 1.00 55.79  ? 4109 LEU A CB    1 
ATOM   18845 C  CG    . LEU A 1 4109 ? 206.413 240.480 211.906 1.00 53.98  ? 4109 LEU A CG    1 
ATOM   18846 C  CD1   . LEU A 1 4109 ? 204.956 240.786 212.192 1.00 49.14  ? 4109 LEU A CD1   1 
ATOM   18847 C  CD2   . LEU A 1 4109 ? 207.286 240.845 213.090 1.00 55.36  ? 4109 LEU A CD2   1 
ATOM   18848 N  N     . GLU A 1 4110 ? 207.744 239.451 208.639 1.00 55.53  ? 4110 GLU A N     1 
ATOM   18849 C  CA    . GLU A 1 4110 ? 208.221 240.326 207.574 1.00 53.74  ? 4110 GLU A CA    1 
ATOM   18850 C  C     . GLU A 1 4110 ? 207.412 240.130 206.299 1.00 60.13  ? 4110 GLU A C     1 
ATOM   18851 O  O     . GLU A 1 4110 ? 207.052 241.105 205.626 1.00 62.51  ? 4110 GLU A O     1 
ATOM   18852 C  CB    . GLU A 1 4110 ? 209.706 240.075 207.315 1.00 50.06  ? 4110 GLU A CB    1 
ATOM   18853 C  CG    . GLU A 1 4110 ? 210.437 241.258 206.708 1.00 58.75  ? 4110 GLU A CG    1 
ATOM   18854 C  CD    . GLU A 1 4110 ? 210.433 241.236 205.195 1.00 66.45  ? 4110 GLU A CD    1 
ATOM   18855 O  OE1   . GLU A 1 4110 ? 210.677 240.158 204.615 1.00 66.18  ? 4110 GLU A OE1   1 
ATOM   18856 O  OE2   . GLU A 1 4110 ? 210.188 242.297 204.584 1.00 59.63  ? 4110 GLU A OE2   1 
ATOM   18857 N  N     . LYS A 1 4111 ? 207.109 238.875 205.953 1.00 60.77  ? 4111 LYS A N     1 
ATOM   18858 C  CA    . LYS A 1 4111 ? 206.309 238.616 204.758 1.00 51.79  ? 4111 LYS A CA    1 
ATOM   18859 C  C     . LYS A 1 4111 ? 204.916 239.215 204.891 1.00 58.24  ? 4111 LYS A C     1 
ATOM   18860 O  O     . LYS A 1 4111 ? 204.374 239.772 203.930 1.00 63.71  ? 4111 LYS A O     1 
ATOM   18861 C  CB    . LYS A 1 4111 ? 206.214 237.115 204.503 1.00 55.91  ? 4111 LYS A CB    1 
ATOM   18862 C  CG    . LYS A 1 4111 ? 207.556 236.449 204.393 1.00 60.91  ? 4111 LYS A CG    1 
ATOM   18863 C  CD    . LYS A 1 4111 ? 208.332 236.944 203.204 1.00 63.17  ? 4111 LYS A CD    1 
ATOM   18864 C  CE    . LYS A 1 4111 ? 209.682 236.278 203.175 1.00 63.90  ? 4111 LYS A CE    1 
ATOM   18865 N  NZ    . LYS A 1 4111 ? 209.530 234.828 202.905 1.00 61.72  ? 4111 LYS A NZ    1 
ATOM   18866 N  N     . LYS A 1 4112 ? 204.319 239.094 206.075 1.00 55.96  ? 4112 LYS A N     1 
ATOM   18867 C  CA    . LYS A 1 4112 ? 203.009 239.678 206.329 1.00 49.21  ? 4112 LYS A CA    1 
ATOM   18868 C  C     . LYS A 1 4112 ? 203.048 241.194 206.209 1.00 55.40  ? 4112 LYS A C     1 
ATOM   18869 O  O     . LYS A 1 4112 ? 202.124 241.807 205.664 1.00 58.49  ? 4112 LYS A O     1 
ATOM   18870 C  CB    . LYS A 1 4112 ? 202.533 239.262 207.718 1.00 52.45  ? 4112 LYS A CB    1 
ATOM   18871 C  CG    . LYS A 1 4112 ? 201.193 239.820 208.129 1.00 57.82  ? 4112 LYS A CG    1 
ATOM   18872 C  CD    . LYS A 1 4112 ? 200.815 239.302 209.501 1.00 55.49  ? 4112 LYS A CD    1 
ATOM   18873 C  CE    . LYS A 1 4112 ? 199.513 239.906 209.974 1.00 57.40  ? 4112 LYS A CE    1 
ATOM   18874 N  NZ    . LYS A 1 4112 ? 198.374 239.493 209.113 1.00 60.11  ? 4112 LYS A NZ    1 
ATOM   18875 N  N     . LEU A 1 4113 ? 204.110 241.816 206.722 1.00 61.12  ? 4113 LEU A N     1 
ATOM   18876 C  CA    . LEU A 1 4113 ? 204.206 243.271 206.689 1.00 61.07  ? 4113 LEU A CA    1 
ATOM   18877 C  C     . LEU A 1 4113 ? 204.416 243.786 205.272 1.00 62.18  ? 4113 LEU A C     1 
ATOM   18878 O  O     . LEU A 1 4113 ? 203.874 244.834 204.902 1.00 59.27  ? 4113 LEU A O     1 
ATOM   18879 C  CB    . LEU A 1 4113 ? 205.341 243.741 207.595 1.00 55.71  ? 4113 LEU A CB    1 
ATOM   18880 C  CG    . LEU A 1 4113 ? 205.088 243.711 209.099 1.00 54.19  ? 4113 LEU A CG    1 
ATOM   18881 C  CD1   . LEU A 1 4113 ? 206.376 244.018 209.839 1.00 61.57  ? 4113 LEU A CD1   1 
ATOM   18882 C  CD2   . LEU A 1 4113 ? 203.997 244.693 209.477 1.00 53.66  ? 4113 LEU A CD2   1 
ATOM   18883 N  N     . HIS A 1 4114 ? 205.206 243.069 204.466 1.00 62.36  ? 4114 HIS A N     1 
ATOM   18884 C  CA    . HIS A 1 4114 ? 205.520 243.553 203.125 1.00 59.04  ? 4114 HIS A CA    1 
ATOM   18885 C  C     . HIS A 1 4114 ? 204.268 243.675 202.266 1.00 63.97  ? 4114 HIS A C     1 
ATOM   18886 O  O     . HIS A 1 4114 ? 204.098 244.662 201.541 1.00 62.44  ? 4114 HIS A O     1 
ATOM   18887 C  CB    . HIS A 1 4114 ? 206.535 242.629 202.455 1.00 60.94  ? 4114 HIS A CB    1 
ATOM   18888 C  CG    . HIS A 1 4114 ? 206.860 243.015 201.046 1.00 66.86  ? 4114 HIS A CG    1 
ATOM   18889 N  ND1   . HIS A 1 4114 ? 207.626 244.117 200.734 1.00 66.36  ? 4114 HIS A ND1   1 
ATOM   18890 C  CD2   . HIS A 1 4114 ? 206.517 242.449 199.865 1.00 65.13  ? 4114 HIS A CD2   1 
ATOM   18891 C  CE1   . HIS A 1 4114 ? 207.744 244.211 199.422 1.00 60.97  ? 4114 HIS A CE1   1 
ATOM   18892 N  NE2   . HIS A 1 4114 ? 207.080 243.211 198.871 1.00 62.71  ? 4114 HIS A NE2   1 
ATOM   18893 N  N     . SER A 1 4115 ? 203.382 242.684 202.332 1.00 68.35  ? 4115 SER A N     1 
ATOM   18894 C  CA    . SER A 1 4115 ? 202.143 242.699 201.555 1.00 69.12  ? 4115 SER A CA    1 
ATOM   18895 C  C     . SER A 1 4115 ? 201.010 243.251 202.420 1.00 69.84  ? 4115 SER A C     1 
ATOM   18896 O  O     . SER A 1 4115 ? 200.091 242.545 202.837 1.00 74.29  ? 4115 SER A O     1 
ATOM   18897 C  CB    . SER A 1 4115 ? 201.825 241.304 201.037 1.00 67.11  ? 4115 SER A CB    1 
ATOM   18898 O  OG    . SER A 1 4115 ? 201.679 240.389 202.108 1.00 63.17  ? 4115 SER A OG    1 
ATOM   18899 N  N     . LEU A 1 4116 ? 201.093 244.552 202.684 1.00 67.41  ? 4116 LEU A N     1 
ATOM   18900 C  CA    . LEU A 1 4116 ? 200.140 245.191 203.577 1.00 68.14  ? 4116 LEU A CA    1 
ATOM   18901 C  C     . LEU A 1 4116 ? 200.083 246.680 203.275 1.00 71.99  ? 4116 LEU A C     1 
ATOM   18902 O  O     . LEU A 1 4116 ? 201.085 247.278 202.878 1.00 74.70  ? 4116 LEU A O     1 
ATOM   18903 C  CB    . LEU A 1 4116 ? 200.523 244.957 205.041 1.00 68.05  ? 4116 LEU A CB    1 
ATOM   18904 C  CG    . LEU A 1 4116 ? 199.392 244.890 206.064 1.00 68.62  ? 4116 LEU A CG    1 
ATOM   18905 C  CD1   . LEU A 1 4116 ? 198.339 243.894 205.622 1.00 69.69  ? 4116 LEU A CD1   1 
ATOM   18906 C  CD2   . LEU A 1 4116 ? 199.956 244.504 207.416 1.00 68.47  ? 4116 LEU A CD2   1 
ATOM   18907 N  N     . GLN A 1 4117 ? 198.903 247.266 203.467 1.00 72.37  ? 4117 GLN A N     1 
ATOM   18908 C  CA    . GLN A 1 4117 ? 198.682 248.704 203.313 1.00 69.12  ? 4117 GLN A CA    1 
ATOM   18909 C  C     . GLN A 1 4117 ? 197.978 249.206 204.572 1.00 69.13  ? 4117 GLN A C     1 
ATOM   18910 O  O     . GLN A 1 4117 ? 196.787 249.545 204.560 1.00 71.43  ? 4117 GLN A O     1 
ATOM   18911 C  CB    . GLN A 1 4117 ? 197.939 249.001 202.002 1.00 70.36  ? 4117 GLN A CB    1 
ATOM   18912 C  CG    . GLN A 1 4117 ? 196.478 248.558 201.899 1.00 72.93  ? 4117 GLN A CG    1 
ATOM   18913 C  CD    . GLN A 1 4117 ? 196.334 247.109 201.474 1.00 76.70  ? 4117 GLN A CD    1 
ATOM   18914 O  OE1   . GLN A 1 4117 ? 197.284 246.332 201.540 1.00 78.76  ? 4117 GLN A OE1   1 
ATOM   18915 N  NE2   . GLN A 1 4117 ? 195.138 246.740 201.030 1.00 73.90  ? 4117 GLN A NE2   1 
ATOM   18916 N  N     . PRO A 1 4118 ? 198.705 249.285 205.687 1.00 63.46  ? 4118 PRO A N     1 
ATOM   18917 C  CA    . PRO A 1 4118 ? 198.061 249.582 206.973 1.00 59.35  ? 4118 PRO A CA    1 
ATOM   18918 C  C     . PRO A 1 4118 ? 197.587 251.020 207.096 1.00 56.95  ? 4118 PRO A C     1 
ATOM   18919 O  O     . PRO A 1 4118 ? 197.822 251.843 206.207 1.00 63.50  ? 4118 PRO A O     1 
ATOM   18920 C  CB    . PRO A 1 4118 ? 199.163 249.272 207.990 1.00 56.01  ? 4118 PRO A CB    1 
ATOM   18921 C  CG    . PRO A 1 4118 ? 200.426 249.491 207.247 1.00 56.46  ? 4118 PRO A CG    1 
ATOM   18922 C  CD    . PRO A 1 4118 ? 200.163 249.123 205.818 1.00 60.50  ? 4118 PRO A CD    1 
ATOM   18923 N  N     . HIS A 1 4119 ? 196.910 251.320 208.202 1.00 48.52  ? 4119 HIS A N     1 
ATOM   18924 C  CA    . HIS A 1 4119 ? 196.451 252.671 208.480 1.00 50.02  ? 4119 HIS A CA    1 
ATOM   18925 C  C     . HIS A 1 4119 ? 197.630 253.640 208.510 1.00 54.85  ? 4119 HIS A C     1 
ATOM   18926 O  O     . HIS A 1 4119 ? 198.787 253.249 208.670 1.00 63.89  ? 4119 HIS A O     1 
ATOM   18927 C  CB    . HIS A 1 4119 ? 195.704 252.711 209.812 1.00 55.37  ? 4119 HIS A CB    1 
ATOM   18928 C  CG    . HIS A 1 4119 ? 194.890 253.949 210.015 1.00 59.63  ? 4119 HIS A CG    1 
ATOM   18929 N  ND1   . HIS A 1 4119 ? 195.278 254.962 210.864 1.00 60.47  ? 4119 HIS A ND1   1 
ATOM   18930 C  CD2   . HIS A 1 4119 ? 193.702 254.332 209.491 1.00 58.37  ? 4119 HIS A CD2   1 
ATOM   18931 C  CE1   . HIS A 1 4119 ? 194.369 255.920 210.849 1.00 57.48  ? 4119 HIS A CE1   1 
ATOM   18932 N  NE2   . HIS A 1 4119 ? 193.402 255.562 210.024 1.00 60.26  ? 4119 HIS A NE2   1 
ATOM   18933 N  N     . ALA A 1 4120 ? 197.319 254.927 208.351 1.00 52.56  ? 4120 ALA A N     1 
ATOM   18934 C  CA    . ALA A 1 4120 ? 198.371 255.938 208.317 1.00 51.26  ? 4120 ALA A CA    1 
ATOM   18935 C  C     . ALA A 1 4120 ? 199.092 256.039 209.655 1.00 57.10  ? 4120 ALA A C     1 
ATOM   18936 O  O     . ALA A 1 4120 ? 200.302 256.286 209.698 1.00 57.27  ? 4120 ALA A O     1 
ATOM   18937 C  CB    . ALA A 1 4120 ? 197.785 257.292 207.920 1.00 53.02  ? 4120 ALA A CB    1 
ATOM   18938 N  N     . CYS A 1 4121 ? 198.368 255.855 210.756 1.00 51.94  ? 4121 CYS A N     1 
ATOM   18939 C  CA    . CYS A 1 4121 ? 198.929 256.019 212.090 1.00 49.72  ? 4121 CYS A CA    1 
ATOM   18940 C  C     . CYS A 1 4121 ? 199.386 254.710 212.720 1.00 51.10  ? 4121 CYS A C     1 
ATOM   18941 O  O     . CYS A 1 4121 ? 199.827 254.719 213.874 1.00 51.61  ? 4121 CYS A O     1 
ATOM   18942 C  CB    . CYS A 1 4121 ? 197.908 256.699 213.006 1.00 49.70  ? 4121 CYS A CB    1 
ATOM   18943 S  SG    . CYS A 1 4121 ? 197.779 258.486 212.777 1.00 68.34  ? 4121 CYS A SG    1 
ATOM   18944 N  N     . PHE A 1 4122 ? 199.292 253.592 212.006 1.00 51.45  ? 4122 PHE A N     1 
ATOM   18945 C  CA    . PHE A 1 4122 ? 199.720 252.313 212.557 1.00 47.59  ? 4122 PHE A CA    1 
ATOM   18946 C  C     . PHE A 1 4122 ? 201.236 252.279 212.699 1.00 52.51  ? 4122 PHE A C     1 
ATOM   18947 O  O     . PHE A 1 4122 ? 201.965 252.686 211.790 1.00 58.04  ? 4122 PHE A O     1 
ATOM   18948 C  CB    . PHE A 1 4122 ? 199.245 251.166 211.667 1.00 46.48  ? 4122 PHE A CB    1 
ATOM   18949 C  CG    . PHE A 1 4122 ? 199.911 249.850 211.961 1.00 46.57  ? 4122 PHE A CG    1 
ATOM   18950 C  CD1   . PHE A 1 4122 ? 199.596 249.138 213.105 1.00 47.64  ? 4122 PHE A CD1   1 
ATOM   18951 C  CD2   . PHE A 1 4122 ? 200.846 249.321 211.090 1.00 50.70  ? 4122 PHE A CD2   1 
ATOM   18952 C  CE1   . PHE A 1 4122 ? 200.205 247.928 213.374 1.00 45.01  ? 4122 PHE A CE1   1 
ATOM   18953 C  CE2   . PHE A 1 4122 ? 201.455 248.112 211.355 1.00 44.47  ? 4122 PHE A CE2   1 
ATOM   18954 C  CZ    . PHE A 1 4122 ? 201.135 247.416 212.497 1.00 43.33  ? 4122 PHE A CZ    1 
ATOM   18955 N  N     . ARG A 1 4123 ? 201.709 251.795 213.844 1.00 45.96  ? 4123 ARG A N     1 
ATOM   18956 C  CA    . ARG A 1 4123 ? 203.132 251.620 214.090 1.00 41.69  ? 4123 ARG A CA    1 
ATOM   18957 C  C     . ARG A 1 4123 ? 203.358 250.258 214.722 1.00 40.73  ? 4123 ARG A C     1 
ATOM   18958 O  O     . ARG A 1 4123 ? 202.576 249.826 215.572 1.00 45.06  ? 4123 ARG A O     1 
ATOM   18959 C  CB    . ARG A 1 4123 ? 203.690 252.716 215.005 1.00 43.85  ? 4123 ARG A CB    1 
ATOM   18960 C  CG    . ARG A 1 4123 ? 203.691 254.103 214.395 1.00 40.66  ? 4123 ARG A CG    1 
ATOM   18961 C  CD    . ARG A 1 4123 ? 204.617 254.182 213.200 1.00 39.51  ? 4123 ARG A CD    1 
ATOM   18962 N  NE    . ARG A 1 4123 ? 204.604 255.507 212.594 1.00 47.01  ? 4123 ARG A NE    1 
ATOM   18963 C  CZ    . ARG A 1 4123 ? 203.649 255.953 211.791 1.00 46.16  ? 4123 ARG A CZ    1 
ATOM   18964 N  NH1   . ARG A 1 4123 ? 202.608 255.203 211.471 1.00 51.41  ? 4123 ARG A NH1   1 
ATOM   18965 N  NH2   . ARG A 1 4123 ? 203.739 257.184 211.296 1.00 47.70  ? 4123 ARG A NH2   1 
ATOM   18966 N  N     . LEU A 1 4124 ? 204.423 249.584 214.301 1.00 37.50  ? 4124 LEU A N     1 
ATOM   18967 C  CA    . LEU A 1 4124 ? 204.809 248.295 214.857 1.00 31.24  ? 4124 LEU A CA    1 
ATOM   18968 C  C     . LEU A 1 4124 ? 206.198 248.427 215.458 1.00 40.36  ? 4124 LEU A C     1 
ATOM   18969 O  O     . LEU A 1 4124 ? 207.149 248.786 214.756 1.00 46.07  ? 4124 LEU A O     1 
ATOM   18970 C  CB    . LEU A 1 4124 ? 204.779 247.199 213.791 1.00 37.64  ? 4124 LEU A CB    1 
ATOM   18971 C  CG    . LEU A 1 4124 ? 205.027 245.768 214.269 1.00 35.83  ? 4124 LEU A CG    1 
ATOM   18972 C  CD1   . LEU A 1 4124 ? 203.993 245.355 215.294 1.00 38.78  ? 4124 LEU A CD1   1 
ATOM   18973 C  CD2   . LEU A 1 4124 ? 205.015 244.812 213.099 1.00 37.42  ? 4124 LEU A CD2   1 
ATOM   18974 N  N     . PHE A 1 4125 ? 206.312 248.142 216.750 1.00 35.64  ? 4125 PHE A N     1 
ATOM   18975 C  CA    . PHE A 1 4125 ? 207.578 248.199 217.466 1.00 27.89  ? 4125 PHE A CA    1 
ATOM   18976 C  C     . PHE A 1 4125 ? 208.020 246.785 217.805 1.00 33.80  ? 4125 PHE A C     1 
ATOM   18977 O  O     . PHE A 1 4125 ? 207.227 245.988 218.313 1.00 43.37  ? 4125 PHE A O     1 
ATOM   18978 C  CB    . PHE A 1 4125 ? 207.453 249.040 218.737 1.00 32.92  ? 4125 PHE A CB    1 
ATOM   18979 C  CG    . PHE A 1 4125 ? 207.062 250.466 218.484 1.00 32.52  ? 4125 PHE A CG    1 
ATOM   18980 C  CD1   . PHE A 1 4125 ? 205.731 250.829 218.401 1.00 32.05  ? 4125 PHE A CD1   1 
ATOM   18981 C  CD2   . PHE A 1 4125 ? 208.027 251.443 218.329 1.00 33.26  ? 4125 PHE A CD2   1 
ATOM   18982 C  CE1   . PHE A 1 4125 ? 205.371 252.138 218.167 1.00 32.47  ? 4125 PHE A CE1   1 
ATOM   18983 C  CE2   . PHE A 1 4125 ? 207.671 252.754 218.094 1.00 34.60  ? 4125 PHE A CE2   1 
ATOM   18984 C  CZ    . PHE A 1 4125 ? 206.342 253.100 218.013 1.00 35.48  ? 4125 PHE A CZ    1 
ATOM   18985 N  N     . LEU A 1 4126 ? 209.279 246.472 217.514 1.00 31.81  ? 4126 LEU A N     1 
ATOM   18986 C  CA    . LEU A 1 4126 ? 209.845 245.155 217.790 1.00 29.67  ? 4126 LEU A CA    1 
ATOM   18987 C  C     . LEU A 1 4126 ? 211.097 245.354 218.635 1.00 36.47  ? 4126 LEU A C     1 
ATOM   18988 O  O     . LEU A 1 4126 ? 212.145 245.744 218.114 1.00 44.46  ? 4126 LEU A O     1 
ATOM   18989 C  CB    . LEU A 1 4126 ? 210.163 244.406 216.499 1.00 32.94  ? 4126 LEU A CB    1 
ATOM   18990 C  CG    . LEU A 1 4126 ? 209.029 244.237 215.488 1.00 31.12  ? 4126 LEU A CG    1 
ATOM   18991 C  CD1   . LEU A 1 4126 ? 209.537 243.546 214.242 1.00 37.24  ? 4126 LEU A CD1   1 
ATOM   18992 C  CD2   . LEU A 1 4126 ? 207.883 243.461 216.097 1.00 35.00  ? 4126 LEU A CD2   1 
ATOM   18993 N  N     . THR A 1 4127 ? 210.990 245.095 219.934 1.00 37.58  ? 4127 THR A N     1 
ATOM   18994 C  CA    . THR A 1 4127 ? 212.134 245.190 220.827 1.00 41.74  ? 4127 THR A CA    1 
ATOM   18995 C  C     . THR A 1 4127 ? 212.843 243.844 220.866 1.00 35.28  ? 4127 THR A C     1 
ATOM   18996 O  O     . THR A 1 4127 ? 212.209 242.810 221.094 1.00 40.66  ? 4127 THR A O     1 
ATOM   18997 C  CB    . THR A 1 4127 ? 211.707 245.601 222.236 1.00 39.14  ? 4127 THR A CB    1 
ATOM   18998 O  OG1   . THR A 1 4127 ? 211.047 244.505 222.874 1.00 35.45  ? 4127 THR A OG1   1 
ATOM   18999 C  CG2   . THR A 1 4127 ? 210.751 246.772 222.181 1.00 33.81  ? 4127 THR A CG2   1 
ATOM   19000 N  N     . MET A 1 4128 ? 214.152 243.858 220.638 1.00 35.16  ? 4128 MET A N     1 
ATOM   19001 C  CA    . MET A 1 4128 ? 214.922 242.627 220.651 1.00 41.59  ? 4128 MET A CA    1 
ATOM   19002 C  C     . MET A 1 4128 ? 216.337 242.919 221.118 1.00 43.01  ? 4128 MET A C     1 
ATOM   19003 O  O     . MET A 1 4128 ? 216.818 244.051 221.050 1.00 49.19  ? 4128 MET A O     1 
ATOM   19004 C  CB    . MET A 1 4128 ? 214.952 241.963 219.271 1.00 40.81  ? 4128 MET A CB    1 
ATOM   19005 C  CG    . MET A 1 4128 ? 215.741 242.732 218.227 1.00 42.33  ? 4128 MET A CG    1 
ATOM   19006 S  SD    . MET A 1 4128 ? 215.106 242.473 216.563 1.00 67.90  ? 4128 MET A SD    1 
ATOM   19007 C  CE    . MET A 1 4128 ? 214.107 243.937 216.355 1.00 45.39  ? 4128 MET A CE    1 
ATOM   19008 N  N     . GLU A 1 4129 ? 216.993 241.874 221.606 1.00 39.77  ? 4129 GLU A N     1 
ATOM   19009 C  CA    . GLU A 1 4129 ? 218.403 241.947 221.940 1.00 39.57  ? 4129 GLU A CA    1 
ATOM   19010 C  C     . GLU A 1 4129 ? 219.231 241.851 220.665 1.00 49.76  ? 4129 GLU A C     1 
ATOM   19011 O  O     . GLU A 1 4129 ? 218.807 241.259 219.670 1.00 60.42  ? 4129 GLU A O     1 
ATOM   19012 C  CB    . GLU A 1 4129 ? 218.770 240.824 222.912 1.00 42.44  ? 4129 GLU A CB    1 
ATOM   19013 C  CG    . GLU A 1 4129 ? 220.204 240.838 223.405 1.00 55.46  ? 4129 GLU A CG    1 
ATOM   19014 C  CD    . GLU A 1 4129 ? 220.483 239.731 224.400 1.00 59.93  ? 4129 GLU A CD    1 
ATOM   19015 O  OE1   . GLU A 1 4129 ? 219.559 238.942 224.687 1.00 56.72  ? 4129 GLU A OE1   1 
ATOM   19016 O  OE2   . GLU A 1 4129 ? 221.626 239.649 224.895 1.00 59.80  ? 4129 GLU A OE2   1 
ATOM   19017 N  N     . ILE A 1 4130 ? 220.420 242.447 220.694 1.00 41.68  ? 4130 ILE A N     1 
ATOM   19018 C  CA    . ILE A 1 4130 ? 221.288 242.438 219.523 1.00 40.88  ? 4130 ILE A CA    1 
ATOM   19019 C  C     . ILE A 1 4130 ? 221.994 241.092 219.444 1.00 49.57  ? 4130 ILE A C     1 
ATOM   19020 O  O     . ILE A 1 4130 ? 223.062 240.899 220.036 1.00 55.24  ? 4130 ILE A O     1 
ATOM   19021 C  CB    . ILE A 1 4130 ? 222.300 243.596 219.566 1.00 43.29  ? 4130 ILE A CB    1 
ATOM   19022 C  CG1   . ILE A 1 4130 ? 221.573 244.931 219.721 1.00 45.63  ? 4130 ILE A CG1   1 
ATOM   19023 C  CG2   . ILE A 1 4130 ? 223.153 243.605 218.311 1.00 41.63  ? 4130 ILE A CG2   1 
ATOM   19024 C  CD1   . ILE A 1 4130 ? 222.493 246.127 219.719 1.00 42.52  ? 4130 ILE A CD1   1 
ATOM   19025 N  N     . ASN A 1 4131 ? 221.397 240.152 218.719 1.00 46.34  ? 4131 ASN A N     1 
ATOM   19026 C  CA    . ASN A 1 4131 ? 221.947 238.819 218.536 1.00 48.80  ? 4131 ASN A CA    1 
ATOM   19027 C  C     . ASN A 1 4131 ? 221.812 238.424 217.074 1.00 49.57  ? 4131 ASN A C     1 
ATOM   19028 O  O     . ASN A 1 4131 ? 220.892 238.883 216.387 1.00 46.49  ? 4131 ASN A O     1 
ATOM   19029 C  CB    . ASN A 1 4131 ? 221.234 237.789 219.425 1.00 50.96  ? 4131 ASN A CB    1 
ATOM   19030 C  CG    . ASN A 1 4131 ? 219.781 237.616 219.058 1.00 55.59  ? 4131 ASN A CG    1 
ATOM   19031 O  OD1   . ASN A 1 4131 ? 219.104 238.575 218.694 1.00 55.94  ? 4131 ASN A OD1   1 
ATOM   19032 N  ND2   . ASN A 1 4131 ? 219.290 236.390 219.150 1.00 52.00  ? 4131 ASN A ND2   1 
ATOM   19033 N  N     . PRO A 1 4132 ? 222.715 237.576 216.570 1.00 47.41  ? 4132 PRO A N     1 
ATOM   19034 C  CA    . PRO A 1 4132 ? 222.707 237.250 215.134 1.00 46.99  ? 4132 PRO A CA    1 
ATOM   19035 C  C     . PRO A 1 4132 ? 221.495 236.459 214.671 1.00 51.23  ? 4132 PRO A C     1 
ATOM   19036 O  O     . PRO A 1 4132 ? 221.285 236.355 213.456 1.00 53.08  ? 4132 PRO A O     1 
ATOM   19037 C  CB    . PRO A 1 4132 ? 223.994 236.434 214.952 1.00 39.71  ? 4132 PRO A CB    1 
ATOM   19038 C  CG    . PRO A 1 4132 ? 224.349 235.960 216.316 1.00 45.93  ? 4132 PRO A CG    1 
ATOM   19039 C  CD    . PRO A 1 4132 ? 223.898 237.027 217.251 1.00 41.49  ? 4132 PRO A CD    1 
ATOM   19040 N  N     . LYS A 1 4133 ? 220.696 235.895 215.578 1.00 48.68  ? 4133 LYS A N     1 
ATOM   19041 C  CA    . LYS A 1 4133 ? 219.560 235.090 215.146 1.00 47.97  ? 4133 LYS A CA    1 
ATOM   19042 C  C     . LYS A 1 4133 ? 218.469 235.922 214.482 1.00 55.59  ? 4133 LYS A C     1 
ATOM   19043 O  O     . LYS A 1 4133 ? 217.571 235.348 213.857 1.00 57.12  ? 4133 LYS A O     1 
ATOM   19044 C  CB    . LYS A 1 4133 ? 218.975 234.315 216.327 1.00 52.40  ? 4133 LYS A CB    1 
ATOM   19045 C  CG    . LYS A 1 4133 ? 219.894 233.244 216.891 1.00 55.59  ? 4133 LYS A CG    1 
ATOM   19046 C  CD    . LYS A 1 4133 ? 219.185 232.410 217.944 1.00 54.42  ? 4133 LYS A CD    1 
ATOM   19047 C  CE    . LYS A 1 4133 ? 219.010 233.181 219.242 1.00 56.50  ? 4133 LYS A CE    1 
ATOM   19048 N  NZ    . LYS A 1 4133 ? 218.416 232.337 220.312 1.00 51.58  ? 4133 LYS A NZ    1 
ATOM   19049 N  N     . VAL A 1 4134 ? 218.521 237.243 214.599 1.00 55.77  ? 4134 VAL A N     1 
ATOM   19050 C  CA    . VAL A 1 4134 ? 217.507 238.096 213.965 1.00 49.96  ? 4134 VAL A CA    1 
ATOM   19051 C  C     . VAL A 1 4134 ? 217.659 238.018 212.450 1.00 51.91  ? 4134 VAL A C     1 
ATOM   19052 O  O     . VAL A 1 4134 ? 218.787 238.125 211.937 1.00 49.48  ? 4134 VAL A O     1 
ATOM   19053 C  CB    . VAL A 1 4134 ? 217.639 239.538 214.457 1.00 48.05  ? 4134 VAL A CB    1 
ATOM   19054 C  CG1   . VAL A 1 4134 ? 216.514 240.392 213.898 1.00 51.23  ? 4134 VAL A CG1   1 
ATOM   19055 C  CG2   . VAL A 1 4134 ? 217.624 239.576 215.974 1.00 48.92  ? 4134 VAL A CG2   1 
ATOM   19056 N  N     . PRO A 1 4135 ? 216.577 237.824 211.701 1.00 49.07  ? 4135 PRO A N     1 
ATOM   19057 C  CA    . PRO A 1 4135 ? 216.698 237.731 210.243 1.00 48.04  ? 4135 PRO A CA    1 
ATOM   19058 C  C     . PRO A 1 4135 ? 217.254 239.010 209.634 1.00 52.98  ? 4135 PRO A C     1 
ATOM   19059 O  O     . PRO A 1 4135 ? 217.002 240.115 210.118 1.00 61.82  ? 4135 PRO A O     1 
ATOM   19060 C  CB    . PRO A 1 4135 ? 215.260 237.468 209.784 1.00 44.69  ? 4135 PRO A CB    1 
ATOM   19061 C  CG    . PRO A 1 4135 ? 214.567 236.920 210.973 1.00 48.43  ? 4135 PRO A CG    1 
ATOM   19062 C  CD    . PRO A 1 4135 ? 215.208 237.553 212.166 1.00 49.92  ? 4135 PRO A CD    1 
ATOM   19063 N  N     . VAL A 1 4136 ? 218.034 238.843 208.564 1.00 44.69  ? 4136 VAL A N     1 
ATOM   19064 C  CA    . VAL A 1 4136 ? 218.588 239.988 207.848 1.00 38.00  ? 4136 VAL A CA    1 
ATOM   19065 C  C     . VAL A 1 4136 ? 217.491 240.748 207.115 1.00 40.23  ? 4136 VAL A C     1 
ATOM   19066 O  O     . VAL A 1 4136 ? 217.504 241.984 207.056 1.00 50.95  ? 4136 VAL A O     1 
ATOM   19067 C  CB    . VAL A 1 4136 ? 219.695 239.521 206.886 1.00 41.74  ? 4136 VAL A CB    1 
ATOM   19068 C  CG1   . VAL A 1 4136 ? 220.114 240.646 205.963 1.00 50.79  ? 4136 VAL A CG1   1 
ATOM   19069 C  CG2   . VAL A 1 4136 ? 220.887 239.004 207.666 1.00 47.50  ? 4136 VAL A CG2   1 
ATOM   19070 N  N     . ASN A 1 4137 ? 216.529 240.024 206.537 1.00 41.49  ? 4137 ASN A N     1 
ATOM   19071 C  CA    . ASN A 1 4137 ? 215.461 240.677 205.788 1.00 44.50  ? 4137 ASN A CA    1 
ATOM   19072 C  C     . ASN A 1 4137 ? 214.578 241.535 206.684 1.00 46.84  ? 4137 ASN A C     1 
ATOM   19073 O  O     . ASN A 1 4137 ? 214.116 242.601 206.261 1.00 49.36  ? 4137 ASN A O     1 
ATOM   19074 C  CB    . ASN A 1 4137 ? 214.636 239.630 205.033 1.00 48.39  ? 4137 ASN A CB    1 
ATOM   19075 C  CG    . ASN A 1 4137 ? 213.917 238.658 205.954 1.00 59.56  ? 4137 ASN A CG    1 
ATOM   19076 O  OD1   . ASN A 1 4137 ? 213.918 238.809 207.175 1.00 60.56  ? 4137 ASN A OD1   1 
ATOM   19077 N  ND2   . ASN A 1 4137 ? 213.288 237.651 205.362 1.00 59.31  ? 4137 ASN A ND2   1 
ATOM   19078 N  N     . LEU A 1 4138 ? 214.330 241.094 207.919 1.00 40.27  ? 4138 LEU A N     1 
ATOM   19079 C  CA    . LEU A 1 4138 ? 213.588 241.929 208.859 1.00 41.37  ? 4138 LEU A CA    1 
ATOM   19080 C  C     . LEU A 1 4138 ? 214.376 243.179 209.227 1.00 46.11  ? 4138 LEU A C     1 
ATOM   19081 O  O     . LEU A 1 4138 ? 213.797 244.262 209.373 1.00 54.93  ? 4138 LEU A O     1 
ATOM   19082 C  CB    . LEU A 1 4138 ? 213.233 241.132 210.113 1.00 46.93  ? 4138 LEU A CB    1 
ATOM   19083 C  CG    . LEU A 1 4138 ? 212.458 241.924 211.167 1.00 42.23  ? 4138 LEU A CG    1 
ATOM   19084 C  CD1   . LEU A 1 4138 ? 210.959 241.838 210.926 1.00 41.98  ? 4138 LEU A CD1   1 
ATOM   19085 C  CD2   . LEU A 1 4138 ? 212.813 241.454 212.565 1.00 44.85  ? 4138 LEU A CD2   1 
ATOM   19086 N  N     . LEU A 1 4139 ? 215.694 243.050 209.390 1.00 43.92  ? 4139 LEU A N     1 
ATOM   19087 C  CA    . LEU A 1 4139 ? 216.520 244.219 209.669 1.00 33.43  ? 4139 LEU A CA    1 
ATOM   19088 C  C     . LEU A 1 4139 ? 216.473 245.213 208.517 1.00 38.32  ? 4139 LEU A C     1 
ATOM   19089 O  O     . LEU A 1 4139 ? 216.422 246.428 208.735 1.00 46.56  ? 4139 LEU A O     1 
ATOM   19090 C  CB    . LEU A 1 4139 ? 217.961 243.794 209.945 1.00 34.08  ? 4139 LEU A CB    1 
ATOM   19091 C  CG    . LEU A 1 4139 ? 218.216 242.961 211.201 1.00 34.49  ? 4139 LEU A CG    1 
ATOM   19092 C  CD1   . LEU A 1 4139 ? 219.670 242.537 211.263 1.00 35.27  ? 4139 LEU A CD1   1 
ATOM   19093 C  CD2   . LEU A 1 4139 ? 217.830 243.731 212.447 1.00 41.75  ? 4139 LEU A CD2   1 
ATOM   19094 N  N     . ARG A 1 4140 ? 216.503 244.715 207.280 1.00 39.69  ? 4140 ARG A N     1 
ATOM   19095 C  CA    . ARG A 1 4140 ? 216.438 245.606 206.129 1.00 36.84  ? 4140 ARG A CA    1 
ATOM   19096 C  C     . ARG A 1 4140 ? 215.059 246.234 205.976 1.00 41.11  ? 4140 ARG A C     1 
ATOM   19097 O  O     . ARG A 1 4140 ? 214.951 247.383 205.535 1.00 48.14  ? 4140 ARG A O     1 
ATOM   19098 C  CB    . ARG A 1 4140 ? 216.817 244.853 204.856 1.00 35.49  ? 4140 ARG A CB    1 
ATOM   19099 C  CG    . ARG A 1 4140 ? 218.241 244.343 204.841 1.00 37.69  ? 4140 ARG A CG    1 
ATOM   19100 C  CD    . ARG A 1 4140 ? 218.536 243.597 203.558 1.00 43.94  ? 4140 ARG A CD    1 
ATOM   19101 N  NE    . ARG A 1 4140 ? 217.838 244.182 202.420 1.00 48.80  ? 4140 ARG A NE    1 
ATOM   19102 C  CZ    . ARG A 1 4140 ? 218.428 244.871 201.452 1.00 52.04  ? 4140 ARG A CZ    1 
ATOM   19103 N  NH1   . ARG A 1 4140 ? 219.733 245.086 201.453 1.00 50.71  ? 4140 ARG A NH1   1 
ATOM   19104 N  NH2   . ARG A 1 4140 ? 217.689 245.354 200.458 1.00 47.67  ? 4140 ARG A NH2   1 
ATOM   19105 N  N     . ALA A 1 4141 ? 214.000 245.504 206.327 1.00 37.61  ? 4141 ALA A N     1 
ATOM   19106 C  CA    . ALA A 1 4141 ? 212.645 246.006 206.143 1.00 38.65  ? 4141 ALA A CA    1 
ATOM   19107 C  C     . ALA A 1 4141 ? 212.259 247.078 207.153 1.00 34.98  ? 4141 ALA A C     1 
ATOM   19108 O  O     . ALA A 1 4141 ? 211.363 247.878 206.868 1.00 44.10  ? 4141 ALA A O     1 
ATOM   19109 C  CB    . ALA A 1 4141 ? 211.643 244.854 206.219 1.00 39.95  ? 4141 ALA A CB    1 
ATOM   19110 N  N     . GLY A 1 4142 ? 212.909 247.118 208.318 1.00 35.33  ? 4142 GLY A N     1 
ATOM   19111 C  CA    . GLY A 1 4142 ? 212.562 248.051 209.365 1.00 35.68  ? 4142 GLY A CA    1 
ATOM   19112 C  C     . GLY A 1 4142 ? 213.713 248.988 209.698 1.00 39.90  ? 4142 GLY A C     1 
ATOM   19113 O  O     . GLY A 1 4142 ? 214.841 248.827 209.222 1.00 46.94  ? 4142 GLY A O     1 
ATOM   19114 N  N     . ARG A 1 4143 ? 213.408 249.979 210.531 1.00 41.84  ? 4143 ARG A N     1 
ATOM   19115 C  CA    . ARG A 1 4143 ? 214.402 250.945 210.974 1.00 33.68  ? 4143 ARG A CA    1 
ATOM   19116 C  C     . ARG A 1 4143 ? 214.979 250.511 212.315 1.00 34.63  ? 4143 ARG A C     1 
ATOM   19117 O  O     . ARG A 1 4143 ? 214.234 250.212 213.252 1.00 46.53  ? 4143 ARG A O     1 
ATOM   19118 C  CB    . ARG A 1 4143 ? 213.798 252.344 211.083 1.00 36.30  ? 4143 ARG A CB    1 
ATOM   19119 C  CG    . ARG A 1 4143 ? 214.821 253.406 211.435 1.00 46.44  ? 4143 ARG A CG    1 
ATOM   19120 C  CD    . ARG A 1 4143 ? 214.535 254.725 210.746 1.00 44.81  ? 4143 ARG A CD    1 
ATOM   19121 N  NE    . ARG A 1 4143 ? 215.434 255.773 211.212 1.00 45.15  ? 4143 ARG A NE    1 
ATOM   19122 C  CZ    . ARG A 1 4143 ? 215.264 257.065 210.974 1.00 48.20  ? 4143 ARG A CZ    1 
ATOM   19123 N  NH1   . ARG A 1 4143 ? 214.239 257.508 210.265 1.00 48.46  ? 4143 ARG A NH1   1 
ATOM   19124 N  NH2   . ARG A 1 4143 ? 216.142 257.936 211.463 1.00 43.41  ? 4143 ARG A NH2   1 
ATOM   19125 N  N     . ILE A 1 4144 ? 216.303 250.484 212.401 1.00 32.97  ? 4144 ILE A N     1 
ATOM   19126 C  CA    . ILE A 1 4144 ? 217.003 249.969 213.571 1.00 38.23  ? 4144 ILE A CA    1 
ATOM   19127 C  C     . ILE A 1 4144 ? 217.342 251.124 214.502 1.00 37.44  ? 4144 ILE A C     1 
ATOM   19128 O  O     . ILE A 1 4144 ? 217.842 252.165 214.061 1.00 37.58  ? 4144 ILE A O     1 
ATOM   19129 C  CB    . ILE A 1 4144 ? 218.268 249.201 213.155 1.00 38.27  ? 4144 ILE A CB    1 
ATOM   19130 C  CG1   . ILE A 1 4144 ? 217.891 247.945 212.370 1.00 34.53  ? 4144 ILE A CG1   1 
ATOM   19131 C  CG2   . ILE A 1 4144 ? 219.099 248.832 214.368 1.00 39.17  ? 4144 ILE A CG2   1 
ATOM   19132 C  CD1   . ILE A 1 4144 ? 218.840 247.628 211.248 1.00 40.58  ? 4144 ILE A CD1   1 
ATOM   19133 N  N     . PHE A 1 4145 ? 217.054 250.947 215.790 1.00 40.93  ? 4145 PHE A N     1 
ATOM   19134 C  CA    . PHE A 1 4145 ? 217.392 251.917 216.829 1.00 33.61  ? 4145 PHE A CA    1 
ATOM   19135 C  C     . PHE A 1 4145 ? 218.169 251.172 217.909 1.00 38.09  ? 4145 PHE A C     1 
ATOM   19136 O  O     . PHE A 1 4145 ? 217.584 250.401 218.673 1.00 44.05  ? 4145 PHE A O     1 
ATOM   19137 C  CB    . PHE A 1 4145 ? 216.143 252.570 217.408 1.00 31.83  ? 4145 PHE A CB    1 
ATOM   19138 C  CG    . PHE A 1 4145 ? 215.478 253.538 216.478 1.00 40.86  ? 4145 PHE A CG    1 
ATOM   19139 C  CD1   . PHE A 1 4145 ? 215.996 254.805 216.285 1.00 44.04  ? 4145 PHE A CD1   1 
ATOM   19140 C  CD2   . PHE A 1 4145 ? 214.328 253.181 215.801 1.00 40.75  ? 4145 PHE A CD2   1 
ATOM   19141 C  CE1   . PHE A 1 4145 ? 215.381 255.692 215.429 1.00 40.65  ? 4145 PHE A CE1   1 
ATOM   19142 C  CE2   . PHE A 1 4145 ? 213.712 254.063 214.946 1.00 42.76  ? 4145 PHE A CE2   1 
ATOM   19143 C  CZ    . PHE A 1 4145 ? 214.237 255.319 214.760 1.00 39.82  ? 4145 PHE A CZ    1 
ATOM   19144 N  N     . VAL A 1 4146 ? 219.476 251.405 217.973 1.00 39.66  ? 4146 VAL A N     1 
ATOM   19145 C  CA    . VAL A 1 4146 ? 220.322 250.758 218.970 1.00 34.25  ? 4146 VAL A CA    1 
ATOM   19146 C  C     . VAL A 1 4146 ? 220.206 251.512 220.287 1.00 40.36  ? 4146 VAL A C     1 
ATOM   19147 O  O     . VAL A 1 4146 ? 220.344 252.740 220.327 1.00 46.14  ? 4146 VAL A O     1 
ATOM   19148 C  CB    . VAL A 1 4146 ? 221.780 250.703 218.493 1.00 35.93  ? 4146 VAL A CB    1 
ATOM   19149 C  CG1   . VAL A 1 4146 ? 222.689 250.315 219.640 1.00 36.96  ? 4146 VAL A CG1   1 
ATOM   19150 C  CG2   . VAL A 1 4146 ? 221.919 249.729 217.341 1.00 36.34  ? 4146 VAL A CG2   1 
ATOM   19151 N  N     . PHE A 1 4147 ? 219.937 250.783 221.367 1.00 44.40  ? 4147 PHE A N     1 
ATOM   19152 C  CA    . PHE A 1 4147 ? 219.868 251.360 222.702 1.00 39.69  ? 4147 PHE A CA    1 
ATOM   19153 C  C     . PHE A 1 4147 ? 220.976 250.771 223.563 1.00 40.02  ? 4147 PHE A C     1 
ATOM   19154 O  O     . PHE A 1 4147 ? 221.142 249.549 223.625 1.00 46.62  ? 4147 PHE A O     1 
ATOM   19155 C  CB    . PHE A 1 4147 ? 218.499 251.122 223.338 1.00 36.13  ? 4147 PHE A CB    1 
ATOM   19156 C  CG    . PHE A 1 4147 ? 217.412 251.946 222.726 1.00 40.27  ? 4147 PHE A CG    1 
ATOM   19157 C  CD1   . PHE A 1 4147 ? 217.159 253.231 223.174 1.00 48.21  ? 4147 PHE A CD1   1 
ATOM   19158 C  CD2   . PHE A 1 4147 ? 216.646 251.437 221.704 1.00 43.04  ? 4147 PHE A CD2   1 
ATOM   19159 C  CE1   . PHE A 1 4147 ? 216.164 253.985 222.607 1.00 46.88  ? 4147 PHE A CE1   1 
ATOM   19160 C  CE2   . PHE A 1 4147 ? 215.667 252.189 221.128 1.00 43.15  ? 4147 PHE A CE2   1 
ATOM   19161 C  CZ    . PHE A 1 4147 ? 215.417 253.464 221.582 1.00 40.77  ? 4147 PHE A CZ    1 
ATOM   19162 N  N     . GLU A 1 4148 ? 221.719 251.644 224.229 1.00 42.37  ? 4148 GLU A N     1 
ATOM   19163 C  CA    . GLU A 1 4148 ? 222.933 251.263 224.934 1.00 45.60  ? 4148 GLU A CA    1 
ATOM   19164 C  C     . GLU A 1 4148 ? 223.238 252.355 225.949 1.00 50.22  ? 4148 GLU A C     1 
ATOM   19165 O  O     . GLU A 1 4148 ? 222.566 253.395 225.965 1.00 52.44  ? 4148 GLU A O     1 
ATOM   19166 C  CB    . GLU A 1 4148 ? 224.096 251.065 223.948 1.00 46.22  ? 4148 GLU A CB    1 
ATOM   19167 C  CG    . GLU A 1 4148 ? 224.606 252.356 223.358 1.00 52.52  ? 4148 GLU A CG    1 
ATOM   19168 C  CD    . GLU A 1 4148 ? 225.613 252.132 222.259 1.00 58.11  ? 4148 GLU A CD    1 
ATOM   19169 O  OE1   . GLU A 1 4148 ? 226.322 251.108 222.304 1.00 51.67  ? 4148 GLU A OE1   1 
ATOM   19170 O  OE2   . GLU A 1 4148 ? 225.686 252.977 221.344 1.00 61.87  ? 4148 GLU A OE2   1 
ATOM   19171 N  N     . PRO A 1 4149 ? 224.207 252.139 226.837 1.00 45.62  ? 4149 PRO A N     1 
ATOM   19172 C  CA    . PRO A 1 4149 ? 224.561 253.182 227.809 1.00 45.18  ? 4149 PRO A CA    1 
ATOM   19173 C  C     . PRO A 1 4149 ? 224.973 254.466 227.114 1.00 52.38  ? 4149 PRO A C     1 
ATOM   19174 O  O     . PRO A 1 4149 ? 225.645 254.431 226.072 1.00 60.32  ? 4149 PRO A O     1 
ATOM   19175 C  CB    . PRO A 1 4149 ? 225.733 252.558 228.578 1.00 51.89  ? 4149 PRO A CB    1 
ATOM   19176 C  CG    . PRO A 1 4149 ? 225.452 251.105 228.525 1.00 55.13  ? 4149 PRO A CG    1 
ATOM   19177 C  CD    . PRO A 1 4149 ? 224.843 250.851 227.176 1.00 47.62  ? 4149 PRO A CD    1 
ATOM   19178 N  N     . PRO A 1 4150 ? 224.570 255.617 227.648 1.00 46.03  ? 4150 PRO A N     1 
ATOM   19179 C  CA    . PRO A 1 4150 ? 224.937 256.880 227.017 1.00 43.12  ? 4150 PRO A CA    1 
ATOM   19180 C  C     . PRO A 1 4150 ? 226.437 257.074 227.037 1.00 48.81  ? 4150 PRO A C     1 
ATOM   19181 O  O     . PRO A 1 4150 ? 227.130 256.620 227.968 1.00 51.24  ? 4150 PRO A O     1 
ATOM   19182 C  CB    . PRO A 1 4150 ? 224.220 257.927 227.881 1.00 47.21  ? 4150 PRO A CB    1 
ATOM   19183 C  CG    . PRO A 1 4150 ? 223.126 257.177 228.558 1.00 45.43  ? 4150 PRO A CG    1 
ATOM   19184 C  CD    . PRO A 1 4150 ? 223.673 255.812 228.797 1.00 49.99  ? 4150 PRO A CD    1 
ATOM   19185 N  N     . PRO A 1 4151 ? 226.989 257.751 226.031 1.00 49.33  ? 4151 PRO A N     1 
ATOM   19186 C  CA    . PRO A 1 4151 ? 228.455 257.880 225.892 1.00 47.24  ? 4151 PRO A CA    1 
ATOM   19187 C  C     . PRO A 1 4151 ? 229.046 259.048 226.676 1.00 46.19  ? 4151 PRO A C     1 
ATOM   19188 O  O     . PRO A 1 4151 ? 229.520 260.047 226.119 1.00 45.65  ? 4151 PRO A O     1 
ATOM   19189 C  CB    . PRO A 1 4151 ? 228.614 258.057 224.383 1.00 44.85  ? 4151 PRO A CB    1 
ATOM   19190 C  CG    . PRO A 1 4151 ? 227.392 258.829 223.993 1.00 42.03  ? 4151 PRO A CG    1 
ATOM   19191 C  CD    . PRO A 1 4151 ? 226.276 258.346 224.887 1.00 43.23  ? 4151 PRO A CD    1 
ATOM   19192 N  N     . GLY A 1 4152 ? 229.032 258.938 227.992 1.00 29.89  ? 4152 GLY A N     1 
ATOM   19193 C  CA    . GLY A 1 4152 ? 229.673 259.916 228.850 1.00 32.41  ? 4152 GLY A CA    1 
ATOM   19194 C  C     . GLY A 1 4152 ? 228.757 260.400 229.956 1.00 30.07  ? 4152 GLY A C     1 
ATOM   19195 O  O     . GLY A 1 4152 ? 227.559 260.121 229.982 1.00 37.60  ? 4152 GLY A O     1 
ATOM   19196 N  N     . VAL A 1 4153 ? 229.343 261.145 230.895 1.00 32.79  ? 4153 VAL A N     1 
ATOM   19197 C  CA    . VAL A 1 4153 ? 228.574 261.694 232.009 1.00 31.05  ? 4153 VAL A CA    1 
ATOM   19198 C  C     . VAL A 1 4153 ? 227.564 262.716 231.505 1.00 39.86  ? 4153 VAL A C     1 
ATOM   19199 O  O     . VAL A 1 4153 ? 226.402 262.726 231.925 1.00 48.07  ? 4153 VAL A O     1 
ATOM   19200 C  CB    . VAL A 1 4153 ? 229.516 262.305 233.061 1.00 29.78  ? 4153 VAL A CB    1 
ATOM   19201 C  CG1   . VAL A 1 4153 ? 228.722 263.020 234.133 1.00 32.67  ? 4153 VAL A CG1   1 
ATOM   19202 C  CG2   . VAL A 1 4153 ? 230.386 261.230 233.679 1.00 31.18  ? 4153 VAL A CG2   1 
ATOM   19203 N  N     . LYS A 1 4154 ? 227.995 263.595 230.598 1.00 38.70  ? 4154 LYS A N     1 
ATOM   19204 C  CA    . LYS A 1 4154 ? 227.114 264.641 230.089 1.00 30.97  ? 4154 LYS A CA    1 
ATOM   19205 C  C     . LYS A 1 4154 ? 225.917 264.051 229.355 1.00 33.89  ? 4154 LYS A C     1 
ATOM   19206 O  O     . LYS A 1 4154 ? 224.770 264.448 229.590 1.00 40.99  ? 4154 LYS A O     1 
ATOM   19207 C  CB    . LYS A 1 4154 ? 227.902 265.575 229.173 1.00 34.75  ? 4154 LYS A CB    1 
ATOM   19208 C  CG    . LYS A 1 4154 ? 227.069 266.637 228.487 1.00 37.01  ? 4154 LYS A CG    1 
ATOM   19209 C  CD    . LYS A 1 4154 ? 227.953 267.569 227.683 1.00 31.47  ? 4154 LYS A CD    1 
ATOM   19210 C  CE    . LYS A 1 4154 ? 227.130 268.581 226.913 1.00 35.40  ? 4154 LYS A CE    1 
ATOM   19211 N  NZ    . LYS A 1 4154 ? 227.995 269.559 226.198 1.00 49.28  ? 4154 LYS A NZ    1 
ATOM   19212 N  N     . ALA A 1 4155 ? 226.166 263.092 228.460 1.00 34.90  ? 4155 ALA A N     1 
ATOM   19213 C  CA    . ALA A 1 4155 ? 225.077 262.468 227.719 1.00 30.31  ? 4155 ALA A CA    1 
ATOM   19214 C  C     . ALA A 1 4155 ? 224.153 261.691 228.646 1.00 36.37  ? 4155 ALA A C     1 
ATOM   19215 O  O     . ALA A 1 4155 ? 222.929 261.704 228.471 1.00 48.09  ? 4155 ALA A O     1 
ATOM   19216 C  CB    . ALA A 1 4155 ? 225.640 261.556 226.632 1.00 31.57  ? 4155 ALA A CB    1 
ATOM   19217 N  N     . ASN A 1 4156 ? 224.723 261.007 229.639 1.00 29.36  ? 4156 ASN A N     1 
ATOM   19218 C  CA    . ASN A 1 4156 ? 223.912 260.249 230.585 1.00 28.37  ? 4156 ASN A CA    1 
ATOM   19219 C  C     . ASN A 1 4156 ? 223.004 261.170 231.391 1.00 33.62  ? 4156 ASN A C     1 
ATOM   19220 O  O     . ASN A 1 4156 ? 221.822 260.876 231.592 1.00 44.44  ? 4156 ASN A O     1 
ATOM   19221 C  CB    . ASN A 1 4156 ? 224.820 259.432 231.503 1.00 30.02  ? 4156 ASN A CB    1 
ATOM   19222 C  CG    . ASN A 1 4156 ? 224.094 258.292 232.179 1.00 38.20  ? 4156 ASN A CG    1 
ATOM   19223 O  OD1   . ASN A 1 4156 ? 222.869 258.206 232.137 1.00 46.51  ? 4156 ASN A OD1   1 
ATOM   19224 N  ND2   . ASN A 1 4156 ? 224.851 257.393 232.788 1.00 36.93  ? 4156 ASN A ND2   1 
ATOM   19225 N  N     . MET A 1 4157 ? 223.538 262.304 231.848 1.00 28.86  ? 4157 MET A N     1 
ATOM   19226 C  CA    . MET A 1 4157 ? 222.724 263.241 232.613 1.00 26.23  ? 4157 MET A CA    1 
ATOM   19227 C  C     . MET A 1 4157 ? 221.668 263.901 231.737 1.00 39.08  ? 4157 MET A C     1 
ATOM   19228 O  O     . MET A 1 4157 ? 220.554 264.172 232.198 1.00 44.95  ? 4157 MET A O     1 
ATOM   19229 C  CB    . MET A 1 4157 ? 223.610 264.295 233.270 1.00 26.67  ? 4157 MET A CB    1 
ATOM   19230 C  CG    . MET A 1 4157 ? 224.523 263.748 234.341 1.00 28.26  ? 4157 MET A CG    1 
ATOM   19231 S  SD    . MET A 1 4157 ? 225.650 264.999 234.960 1.00 55.45  ? 4157 MET A SD    1 
ATOM   19232 C  CE    . MET A 1 4157 ? 224.571 265.844 236.102 1.00 35.20  ? 4157 MET A CE    1 
ATOM   19233 N  N     . LEU A 1 4158 ? 222.000 264.178 230.473 1.00 46.68  ? 4158 LEU A N     1 
ATOM   19234 C  CA    . LEU A 1 4158 ? 221.003 264.719 229.556 1.00 37.56  ? 4158 LEU A CA    1 
ATOM   19235 C  C     . LEU A 1 4158 ? 219.864 263.733 229.344 1.00 41.13  ? 4158 LEU A C     1 
ATOM   19236 O  O     . LEU A 1 4158 ? 218.688 264.116 229.356 1.00 47.99  ? 4158 LEU A O     1 
ATOM   19237 C  CB    . LEU A 1 4158 ? 221.657 265.078 228.223 1.00 33.40  ? 4158 LEU A CB    1 
ATOM   19238 C  CG    . LEU A 1 4158 ? 222.445 266.385 228.191 1.00 36.70  ? 4158 LEU A CG    1 
ATOM   19239 C  CD1   . LEU A 1 4158 ? 223.007 266.630 226.805 1.00 38.75  ? 4158 LEU A CD1   1 
ATOM   19240 C  CD2   . LEU A 1 4158 ? 221.567 267.541 228.627 1.00 40.04  ? 4158 LEU A CD2   1 
ATOM   19241 N  N     . ARG A 1 4159 ? 220.195 262.452 229.165 1.00 29.14  ? 4159 ARG A N     1 
ATOM   19242 C  CA    . ARG A 1 4159 ? 219.161 261.431 229.037 1.00 33.19  ? 4159 ARG A CA    1 
ATOM   19243 C  C     . ARG A 1 4159 ? 218.324 261.334 230.304 1.00 44.80  ? 4159 ARG A C     1 
ATOM   19244 O  O     . ARG A 1 4159 ? 217.098 261.186 230.239 1.00 55.02  ? 4159 ARG A O     1 
ATOM   19245 C  CB    . ARG A 1 4159 ? 219.798 260.082 228.712 1.00 30.21  ? 4159 ARG A CB    1 
ATOM   19246 C  CG    . ARG A 1 4159 ? 218.866 259.109 228.018 1.00 37.34  ? 4159 ARG A CG    1 
ATOM   19247 C  CD    . ARG A 1 4159 ? 219.626 257.907 227.490 1.00 46.41  ? 4159 ARG A CD    1 
ATOM   19248 N  NE    . ARG A 1 4159 ? 220.534 258.273 226.410 1.00 57.32  ? 4159 ARG A NE    1 
ATOM   19249 C  CZ    . ARG A 1 4159 ? 221.181 257.404 225.646 1.00 56.96  ? 4159 ARG A CZ    1 
ATOM   19250 N  NH1   . ARG A 1 4159 ? 221.040 256.099 225.813 1.00 48.21  ? 4159 ARG A NH1   1 
ATOM   19251 N  NH2   . ARG A 1 4159 ? 221.989 257.855 224.691 1.00 48.76  ? 4159 ARG A NH2   1 
ATOM   19252 N  N     . THR A 1 4160 ? 218.971 261.412 231.468 1.00 48.44  ? 4160 THR A N     1 
ATOM   19253 C  CA    . THR A 1 4160 ? 218.245 261.332 232.731 1.00 35.85  ? 4160 THR A CA    1 
ATOM   19254 C  C     . THR A 1 4160 ? 217.264 262.488 232.876 1.00 34.01  ? 4160 THR A C     1 
ATOM   19255 O  O     . THR A 1 4160 ? 216.100 262.287 233.239 1.00 47.63  ? 4160 THR A O     1 
ATOM   19256 C  CB    . THR A 1 4160 ? 219.232 261.312 233.898 1.00 38.38  ? 4160 THR A CB    1 
ATOM   19257 O  OG1   . THR A 1 4160 ? 219.961 260.079 233.888 1.00 43.41  ? 4160 THR A OG1   1 
ATOM   19258 C  CG2   . THR A 1 4160 ? 218.501 261.448 235.216 1.00 39.48  ? 4160 THR A CG2   1 
ATOM   19259 N  N     . PHE A 1 4161 ? 217.714 263.709 232.584 1.00 36.26  ? 4161 PHE A N     1 
ATOM   19260 C  CA    . PHE A 1 4161 ? 216.833 264.865 232.708 1.00 41.03  ? 4161 PHE A CA    1 
ATOM   19261 C  C     . PHE A 1 4161 ? 215.728 264.853 231.663 1.00 47.57  ? 4161 PHE A C     1 
ATOM   19262 O  O     . PHE A 1 4161 ? 214.627 265.350 231.926 1.00 49.71  ? 4161 PHE A O     1 
ATOM   19263 C  CB    . PHE A 1 4161 ? 217.639 266.159 232.617 1.00 41.15  ? 4161 PHE A CB    1 
ATOM   19264 C  CG    . PHE A 1 4161 ? 218.307 266.544 233.902 1.00 46.10  ? 4161 PHE A CG    1 
ATOM   19265 C  CD1   . PHE A 1 4161 ? 217.555 266.807 235.033 1.00 39.53  ? 4161 PHE A CD1   1 
ATOM   19266 C  CD2   . PHE A 1 4161 ? 219.685 266.641 233.982 1.00 48.74  ? 4161 PHE A CD2   1 
ATOM   19267 C  CE1   . PHE A 1 4161 ? 218.162 267.161 236.216 1.00 38.08  ? 4161 PHE A CE1   1 
ATOM   19268 C  CE2   . PHE A 1 4161 ? 220.298 266.994 235.165 1.00 47.84  ? 4161 PHE A CE2   1 
ATOM   19269 C  CZ    . PHE A 1 4161 ? 219.535 267.255 236.283 1.00 46.79  ? 4161 PHE A CZ    1 
ATOM   19270 N  N     . SER A 1 4162 ? 215.991 264.302 230.477 1.00 44.40  ? 4162 SER A N     1 
ATOM   19271 C  CA    . SER A 1 4162 ? 214.929 264.177 229.487 1.00 45.07  ? 4162 SER A CA    1 
ATOM   19272 C  C     . SER A 1 4162 ? 213.901 263.127 229.887 1.00 47.37  ? 4162 SER A C     1 
ATOM   19273 O  O     . SER A 1 4162 ? 212.711 263.290 229.594 1.00 50.02  ? 4162 SER A O     1 
ATOM   19274 C  CB    . SER A 1 4162 ? 215.517 263.837 228.118 1.00 42.69  ? 4162 SER A CB    1 
ATOM   19275 O  OG    . SER A 1 4162 ? 216.107 262.551 228.122 1.00 46.24  ? 4162 SER A OG    1 
ATOM   19276 N  N     . SER A 1 4163 ? 214.334 262.053 230.549 1.00 41.98  ? 4163 SER A N     1 
ATOM   19277 C  CA    . SER A 1 4163 ? 213.410 260.986 230.923 1.00 40.85  ? 4163 SER A CA    1 
ATOM   19278 C  C     . SER A 1 4163 ? 212.435 261.443 232.002 1.00 47.47  ? 4163 SER A C     1 
ATOM   19279 O  O     . SER A 1 4163 ? 211.228 261.192 231.906 1.00 48.81  ? 4163 SER A O     1 
ATOM   19280 C  CB    . SER A 1 4163 ? 214.192 259.760 231.390 1.00 45.82  ? 4163 SER A CB    1 
ATOM   19281 O  OG    . SER A 1 4163 ? 214.729 259.963 232.684 1.00 53.86  ? 4163 SER A OG    1 
ATOM   19282 N  N     . ILE A 1 4164 ? 212.934 262.107 233.036 1.00 48.62  ? 4164 ILE A N     1 
ATOM   19283 C  CA    . ILE A 1 4164 ? 212.060 262.517 234.142 1.00 45.89  ? 4164 ILE A CA    1 
ATOM   19284 C  C     . ILE A 1 4164 ? 211.187 263.683 233.690 1.00 53.80  ? 4164 ILE A C     1 
ATOM   19285 O  O     . ILE A 1 4164 ? 211.709 264.658 233.120 1.00 56.06  ? 4164 ILE A O     1 
ATOM   19286 C  CB    . ILE A 1 4164 ? 212.888 262.894 235.370 1.00 44.01  ? 4164 ILE A CB    1 
ATOM   19287 C  CG1   . ILE A 1 4164 ? 213.779 261.730 235.797 1.00 50.05  ? 4164 ILE A CG1   1 
ATOM   19288 C  CG2   . ILE A 1 4164 ? 211.981 263.279 236.521 1.00 46.65  ? 4164 ILE A CG2   1 
ATOM   19289 C  CD1   . ILE A 1 4164 ? 215.125 262.164 236.321 1.00 49.36  ? 4164 ILE A CD1   1 
ATOM   19290 N  N     . PRO A 1 4165 ? 209.874 263.633 233.909 1.00 61.41  ? 4165 PRO A N     1 
ATOM   19291 C  CA    . PRO A 1 4165 ? 209.017 264.759 233.523 1.00 59.57  ? 4165 PRO A CA    1 
ATOM   19292 C  C     . PRO A 1 4165 ? 209.368 266.024 234.292 1.00 63.42  ? 4165 PRO A C     1 
ATOM   19293 O  O     . PRO A 1 4165 ? 209.864 265.978 235.420 1.00 64.76  ? 4165 PRO A O     1 
ATOM   19294 C  CB    . PRO A 1 4165 ? 207.607 264.268 233.871 1.00 53.65  ? 4165 PRO A CB    1 
ATOM   19295 C  CG    . PRO A 1 4165 ? 207.716 262.782 233.884 1.00 54.66  ? 4165 PRO A CG    1 
ATOM   19296 C  CD    . PRO A 1 4165 ? 209.091 262.485 234.392 1.00 58.48  ? 4165 PRO A CD    1 
ATOM   19297 N  N     . VAL A 1 4166 ? 209.110 267.167 233.654 1.00 64.94  ? 4166 VAL A N     1 
ATOM   19298 C  CA    . VAL A 1 4166 ? 209.442 268.457 234.253 1.00 64.50  ? 4166 VAL A CA    1 
ATOM   19299 C  C     . VAL A 1 4166 ? 208.617 268.696 235.511 1.00 64.94  ? 4166 VAL A C     1 
ATOM   19300 O  O     . VAL A 1 4166 ? 209.119 269.228 236.508 1.00 63.08  ? 4166 VAL A O     1 
ATOM   19301 C  CB    . VAL A 1 4166 ? 209.243 269.586 233.225 1.00 62.49  ? 4166 VAL A CB    1 
ATOM   19302 C  CG1   . VAL A 1 4166 ? 209.743 270.909 233.781 1.00 60.86  ? 4166 VAL A CG1   1 
ATOM   19303 C  CG2   . VAL A 1 4166 ? 209.948 269.245 231.923 1.00 62.97  ? 4166 VAL A CG2   1 
ATOM   19304 N  N     . SER A 1 4167 ? 207.338 268.314 235.483 1.00 64.89  ? 4167 SER A N     1 
ATOM   19305 C  CA    . SER A 1 4167 ? 206.459 268.577 236.619 1.00 64.28  ? 4167 SER A CA    1 
ATOM   19306 C  C     . SER A 1 4167 ? 206.875 267.793 237.856 1.00 63.36  ? 4167 SER A C     1 
ATOM   19307 O  O     . SER A 1 4167 ? 206.568 268.206 238.979 1.00 59.73  ? 4167 SER A O     1 
ATOM   19308 C  CB    . SER A 1 4167 ? 205.014 268.250 236.249 1.00 62.42  ? 4167 SER A CB    1 
ATOM   19309 O  OG    . SER A 1 4167 ? 204.852 266.863 236.013 1.00 66.81  ? 4167 SER A OG    1 
ATOM   19310 N  N     . ARG A 1 4168 ? 207.563 266.665 237.676 1.00 56.90  ? 4168 ARG A N     1 
ATOM   19311 C  CA    . ARG A 1 4168 ? 207.987 265.870 238.823 1.00 52.33  ? 4168 ARG A CA    1 
ATOM   19312 C  C     . ARG A 1 4168 ? 209.155 266.525 239.551 1.00 54.76  ? 4168 ARG A C     1 
ATOM   19313 O  O     . ARG A 1 4168 ? 209.186 266.553 240.786 1.00 57.54  ? 4168 ARG A O     1 
ATOM   19314 C  CB    . ARG A 1 4168 ? 208.355 264.459 238.371 1.00 47.53  ? 4168 ARG A CB    1 
ATOM   19315 C  CG    . ARG A 1 4168 ? 209.021 263.624 239.442 1.00 53.58  ? 4168 ARG A CG    1 
ATOM   19316 C  CD    . ARG A 1 4168 ? 209.242 262.200 238.975 1.00 55.98  ? 4168 ARG A CD    1 
ATOM   19317 N  NE    . ARG A 1 4168 ? 209.166 261.254 240.081 1.00 50.54  ? 4168 ARG A NE    1 
ATOM   19318 C  CZ    . ARG A 1 4168 ? 209.477 259.970 239.989 1.00 52.70  ? 4168 ARG A CZ    1 
ATOM   19319 N  NH1   . ARG A 1 4168 ? 209.902 259.441 238.854 1.00 56.25  ? 4168 ARG A NH1   1 
ATOM   19320 N  NH2   . ARG A 1 4168 ? 209.357 259.196 241.063 1.00 54.30  ? 4168 ARG A NH2   1 
ATOM   19321 N  N     . ILE A 1 4169 ? 210.127 267.052 238.804 1.00 56.82  ? 4169 ILE A N     1 
ATOM   19322 C  CA    . ILE A 1 4169 ? 211.275 267.703 239.429 1.00 57.03  ? 4169 ILE A CA    1 
ATOM   19323 C  C     . ILE A 1 4169 ? 210.861 269.020 240.070 1.00 59.67  ? 4169 ILE A C     1 
ATOM   19324 O  O     . ILE A 1 4169 ? 211.313 269.362 241.169 1.00 62.13  ? 4169 ILE A O     1 
ATOM   19325 C  CB    . ILE A 1 4169 ? 212.401 267.903 238.400 1.00 54.08  ? 4169 ILE A CB    1 
ATOM   19326 C  CG1   . ILE A 1 4169 ? 212.753 266.576 237.732 1.00 56.47  ? 4169 ILE A CG1   1 
ATOM   19327 C  CG2   . ILE A 1 4169 ? 213.626 268.501 239.059 1.00 52.11  ? 4169 ILE A CG2   1 
ATOM   19328 C  CD1   . ILE A 1 4169 ? 214.007 266.629 236.893 1.00 59.66  ? 4169 ILE A CD1   1 
ATOM   19329 N  N     . CYS A 1 4170 ? 210.003 269.782 239.397 1.00 71.38  ? 4170 CYS A N     1 
ATOM   19330 C  CA    . CYS A 1 4170 ? 209.534 271.069 239.906 1.00 71.95  ? 4170 CYS A CA    1 
ATOM   19331 C  C     . CYS A 1 4170 ? 208.278 270.824 240.732 1.00 71.53  ? 4170 CYS A C     1 
ATOM   19332 O  O     . CYS A 1 4170 ? 207.167 270.785 240.200 1.00 74.30  ? 4170 CYS A O     1 
ATOM   19333 C  CB    . CYS A 1 4170 ? 209.269 272.035 238.758 1.00 73.39  ? 4170 CYS A CB    1 
ATOM   19334 S  SG    . CYS A 1 4170 ? 210.548 272.043 237.484 1.00 88.37  ? 4170 CYS A SG    1 
ATOM   19335 N  N     . LYS A 1 4171 ? 208.452 270.664 242.041 1.00 70.21  ? 4171 LYS A N     1 
ATOM   19336 C  CA    . LYS A 1 4171 ? 207.340 270.389 242.938 1.00 71.70  ? 4171 LYS A CA    1 
ATOM   19337 C  C     . LYS A 1 4171 ? 207.515 271.270 244.173 1.00 75.21  ? 4171 LYS A C     1 
ATOM   19338 O  O     . LYS A 1 4171 ? 208.321 272.204 244.178 1.00 79.39  ? 4171 LYS A O     1 
ATOM   19339 C  CB    . LYS A 1 4171 ? 207.266 268.889 243.254 1.00 72.48  ? 4171 LYS A CB    1 
ATOM   19340 C  CG    . LYS A 1 4171 ? 205.886 268.405 243.674 1.00 69.79  ? 4171 LYS A CG    1 
ATOM   19341 C  CD    . LYS A 1 4171 ? 205.893 266.927 244.006 1.00 74.53  ? 4171 LYS A CD    1 
ATOM   19342 C  CE    . LYS A 1 4171 ? 204.542 266.476 244.535 1.00 73.33  ? 4171 LYS A CE    1 
ATOM   19343 N  NZ    . LYS A 1 4171 ? 204.556 265.048 244.955 1.00 73.86  ? 4171 LYS A NZ    1 
ATOM   19344 N  N     . SER A 1 4172 ? 206.747 270.976 245.224 1.00 79.29  ? 4172 SER A N     1 
ATOM   19345 C  CA    . SER A 1 4172 ? 206.620 271.885 246.363 1.00 78.54  ? 4172 SER A CA    1 
ATOM   19346 C  C     . SER A 1 4172 ? 207.949 272.284 246.997 1.00 77.95  ? 4172 SER A C     1 
ATOM   19347 O  O     . SER A 1 4172 ? 208.165 273.489 247.198 1.00 80.94  ? 4172 SER A O     1 
ATOM   19348 C  CB    . SER A 1 4172 ? 205.677 271.262 247.401 1.00 81.38  ? 4172 SER A CB    1 
ATOM   19349 O  OG    . SER A 1 4172 ? 204.413 270.972 246.832 1.00 83.88  ? 4172 SER A OG    1 
ATOM   19350 N  N     . PRO A 1 4173 ? 208.875 271.367 247.330 1.00 74.61  ? 4173 PRO A N     1 
ATOM   19351 C  CA    . PRO A 1 4173 ? 210.158 271.824 247.879 1.00 72.97  ? 4173 PRO A CA    1 
ATOM   19352 C  C     . PRO A 1 4173 ? 211.156 272.175 246.787 1.00 72.01  ? 4173 PRO A C     1 
ATOM   19353 O  O     . PRO A 1 4173 ? 211.363 271.398 245.851 1.00 73.13  ? 4173 PRO A O     1 
ATOM   19354 C  CB    . PRO A 1 4173 ? 210.626 270.633 248.722 1.00 66.06  ? 4173 PRO A CB    1 
ATOM   19355 C  CG    . PRO A 1 4173 ? 210.005 269.448 248.080 1.00 72.28  ? 4173 PRO A CG    1 
ATOM   19356 C  CD    . PRO A 1 4173 ? 208.788 269.894 247.310 1.00 71.29  ? 4173 PRO A CD    1 
ATOM   19357 N  N     . ASN A 1 4174 ? 211.779 273.350 246.897 1.00 69.29  ? 4174 ASN A N     1 
ATOM   19358 C  CA    . ASN A 1 4174 ? 212.734 273.788 245.886 1.00 73.43  ? 4174 ASN A CA    1 
ATOM   19359 C  C     . ASN A 1 4174 ? 214.024 272.980 245.918 1.00 76.21  ? 4174 ASN A C     1 
ATOM   19360 O  O     . ASN A 1 4174 ? 214.837 273.093 244.995 1.00 74.26  ? 4174 ASN A O     1 
ATOM   19361 C  CB    . ASN A 1 4174 ? 213.046 275.273 246.068 1.00 72.62  ? 4174 ASN A CB    1 
ATOM   19362 C  CG    . ASN A 1 4174 ? 211.897 276.163 245.649 1.00 73.47  ? 4174 ASN A CG    1 
ATOM   19363 O  OD1   . ASN A 1 4174 ? 210.916 275.697 245.071 1.00 71.58  ? 4174 ASN A OD1   1 
ATOM   19364 N  ND2   . ASN A 1 4174 ? 212.011 277.452 245.940 1.00 70.20  ? 4174 ASN A ND2   1 
ATOM   19365 N  N     . GLU A 1 4175 ? 214.229 272.178 246.960 1.00 67.13  ? 4175 GLU A N     1 
ATOM   19366 C  CA    . GLU A 1 4175 ? 215.393 271.313 247.074 1.00 56.85  ? 4175 GLU A CA    1 
ATOM   19367 C  C     . GLU A 1 4175 ? 215.222 269.999 246.325 1.00 58.26  ? 4175 GLU A C     1 
ATOM   19368 O  O     . GLU A 1 4175 ? 216.200 269.256 246.168 1.00 65.85  ? 4175 GLU A O     1 
ATOM   19369 C  CB    . GLU A 1 4175 ? 215.678 271.053 248.554 1.00 57.75  ? 4175 GLU A CB    1 
ATOM   19370 C  CG    . GLU A 1 4175 ? 216.126 272.300 249.301 1.00 62.57  ? 4175 GLU A CG    1 
ATOM   19371 C  CD    . GLU A 1 4175 ? 214.975 273.179 249.741 1.00 68.66  ? 4175 GLU A CD    1 
ATOM   19372 O  OE1   . GLU A 1 4175 ? 213.809 272.791 249.523 1.00 71.54  ? 4175 GLU A OE1   1 
ATOM   19373 O  OE2   . GLU A 1 4175 ? 215.238 274.271 250.286 1.00 67.43  ? 4175 GLU A OE2   1 
ATOM   19374 N  N     . ARG A 1 4176 ? 214.009 269.710 245.853 1.00 51.80  ? 4176 ARG A N     1 
ATOM   19375 C  CA    . ARG A 1 4176 ? 213.773 268.498 245.078 1.00 49.88  ? 4176 ARG A CA    1 
ATOM   19376 C  C     . ARG A 1 4176 ? 214.569 268.510 243.780 1.00 53.51  ? 4176 ARG A C     1 
ATOM   19377 O  O     . ARG A 1 4176 ? 215.091 267.473 243.358 1.00 59.08  ? 4176 ARG A O     1 
ATOM   19378 C  CB    . ARG A 1 4176 ? 212.279 268.348 244.797 1.00 49.50  ? 4176 ARG A CB    1 
ATOM   19379 C  CG    . ARG A 1 4176 ? 211.922 267.189 243.892 1.00 51.70  ? 4176 ARG A CG    1 
ATOM   19380 C  CD    . ARG A 1 4176 ? 210.420 267.058 243.756 1.00 54.03  ? 4176 ARG A CD    1 
ATOM   19381 N  NE    . ARG A 1 4176 ? 209.758 267.089 245.054 1.00 58.20  ? 4176 ARG A NE    1 
ATOM   19382 C  CZ    . ARG A 1 4176 ? 208.943 266.145 245.502 1.00 58.27  ? 4176 ARG A CZ    1 
ATOM   19383 N  NH1   . ARG A 1 4176 ? 208.651 265.081 244.774 1.00 52.65  ? 4176 ARG A NH1   1 
ATOM   19384 N  NH2   . ARG A 1 4176 ? 208.404 266.274 246.711 1.00 57.78  ? 4176 ARG A NH2   1 
ATOM   19385 N  N     . ALA A 1 4177 ? 214.670 269.671 243.132 1.00 54.96  ? 4177 ALA A N     1 
ATOM   19386 C  CA    . ALA A 1 4177 ? 215.457 269.768 241.908 1.00 46.31  ? 4177 ALA A CA    1 
ATOM   19387 C  C     . ALA A 1 4177 ? 216.927 269.475 242.173 1.00 44.39  ? 4177 ALA A C     1 
ATOM   19388 O  O     . ALA A 1 4177 ? 217.583 268.785 241.385 1.00 51.59  ? 4177 ALA A O     1 
ATOM   19389 C  CB    . ALA A 1 4177 ? 215.287 271.150 241.283 1.00 51.07  ? 4177 ALA A CB    1 
ATOM   19390 N  N     . ARG A 1 4178 ? 217.463 269.989 243.281 1.00 42.67  ? 4178 ARG A N     1 
ATOM   19391 C  CA    . ARG A 1 4178 ? 218.852 269.707 243.627 1.00 41.67  ? 4178 ARG A CA    1 
ATOM   19392 C  C     . ARG A 1 4178 ? 219.060 268.232 243.935 1.00 41.87  ? 4178 ARG A C     1 
ATOM   19393 O  O     . ARG A 1 4178 ? 220.081 267.652 243.549 1.00 51.22  ? 4178 ARG A O     1 
ATOM   19394 C  CB    . ARG A 1 4178 ? 219.286 270.566 244.810 1.00 45.42  ? 4178 ARG A CB    1 
ATOM   19395 C  CG    . ARG A 1 4178 ? 220.780 270.799 244.884 1.00 40.18  ? 4178 ARG A CG    1 
ATOM   19396 C  CD    . ARG A 1 4178 ? 221.076 272.135 245.526 1.00 46.82  ? 4178 ARG A CD    1 
ATOM   19397 N  NE    . ARG A 1 4178 ? 222.464 272.541 245.355 1.00 52.01  ? 4178 ARG A NE    1 
ATOM   19398 C  CZ    . ARG A 1 4178 ? 222.839 273.737 244.927 1.00 53.13  ? 4178 ARG A CZ    1 
ATOM   19399 N  NH1   . ARG A 1 4178 ? 221.952 274.665 244.610 1.00 51.27  ? 4178 ARG A NH1   1 
ATOM   19400 N  NH2   . ARG A 1 4178 ? 224.135 274.010 244.817 1.00 56.79  ? 4178 ARG A NH2   1 
ATOM   19401 N  N     . LEU A 1 4179 ? 218.114 267.608 244.641 1.00 45.15  ? 4179 LEU A N     1 
ATOM   19402 C  CA    . LEU A 1 4179 ? 218.236 266.178 244.909 1.00 39.41  ? 4179 LEU A CA    1 
ATOM   19403 C  C     . LEU A 1 4179 ? 218.183 265.365 243.623 1.00 37.65  ? 4179 LEU A C     1 
ATOM   19404 O  O     . LEU A 1 4179 ? 218.927 264.391 243.466 1.00 44.68  ? 4179 LEU A O     1 
ATOM   19405 C  CB    . LEU A 1 4179 ? 217.148 265.721 245.877 1.00 43.04  ? 4179 LEU A CB    1 
ATOM   19406 C  CG    . LEU A 1 4179 ? 217.281 266.285 247.286 1.00 40.81  ? 4179 LEU A CG    1 
ATOM   19407 C  CD1   . LEU A 1 4179 ? 216.098 265.883 248.133 1.00 45.73  ? 4179 LEU A CD1   1 
ATOM   19408 C  CD2   . LEU A 1 4179 ? 218.561 265.784 247.893 1.00 42.33  ? 4179 LEU A CD2   1 
ATOM   19409 N  N     . TYR A 1 4180 ? 217.306 265.744 242.693 1.00 38.71  ? 4180 TYR A N     1 
ATOM   19410 C  CA    . TYR A 1 4180 ? 217.246 265.051 241.411 1.00 32.42  ? 4180 TYR A CA    1 
ATOM   19411 C  C     . TYR A 1 4180 ? 218.535 265.233 240.623 1.00 39.56  ? 4180 TYR A C     1 
ATOM   19412 O  O     . TYR A 1 4180 ? 218.995 264.305 239.952 1.00 45.10  ? 4180 TYR A O     1 
ATOM   19413 C  CB    . TYR A 1 4180 ? 216.052 265.546 240.600 1.00 35.77  ? 4180 TYR A CB    1 
ATOM   19414 C  CG    . TYR A 1 4180 ? 214.782 264.771 240.846 1.00 39.02  ? 4180 TYR A CG    1 
ATOM   19415 C  CD1   . TYR A 1 4180 ? 214.123 264.849 242.061 1.00 40.43  ? 4180 TYR A CD1   1 
ATOM   19416 C  CD2   . TYR A 1 4180 ? 214.241 263.963 239.859 1.00 49.62  ? 4180 TYR A CD2   1 
ATOM   19417 C  CE1   . TYR A 1 4180 ? 212.963 264.144 242.286 1.00 39.45  ? 4180 TYR A CE1   1 
ATOM   19418 C  CE2   . TYR A 1 4180 ? 213.083 263.258 240.075 1.00 44.90  ? 4180 TYR A CE2   1 
ATOM   19419 C  CZ    . TYR A 1 4180 ? 212.449 263.352 241.290 1.00 46.98  ? 4180 TYR A CZ    1 
ATOM   19420 O  OH    . TYR A 1 4180 ? 211.293 262.647 241.506 1.00 54.03  ? 4180 TYR A OH    1 
ATOM   19421 N  N     . PHE A 1 4181 ? 219.129 266.427 240.680 1.00 41.66  ? 4181 PHE A N     1 
ATOM   19422 C  CA    . PHE A 1 4181 ? 220.407 266.636 240.007 1.00 27.37  ? 4181 PHE A CA    1 
ATOM   19423 C  C     . PHE A 1 4181 ? 221.504 265.782 240.625 1.00 36.17  ? 4181 PHE A C     1 
ATOM   19424 O  O     . PHE A 1 4181 ? 222.328 265.202 239.908 1.00 51.11  ? 4181 PHE A O     1 
ATOM   19425 C  CB    . PHE A 1 4181 ? 220.804 268.108 240.052 1.00 27.93  ? 4181 PHE A CB    1 
ATOM   19426 C  CG    . PHE A 1 4181 ? 222.167 268.374 239.485 1.00 39.03  ? 4181 PHE A CG    1 
ATOM   19427 C  CD1   . PHE A 1 4181 ? 222.339 268.563 238.129 1.00 41.28  ? 4181 PHE A CD1   1 
ATOM   19428 C  CD2   . PHE A 1 4181 ? 223.279 268.409 240.306 1.00 35.90  ? 4181 PHE A CD2   1 
ATOM   19429 C  CE1   . PHE A 1 4181 ? 223.587 268.798 237.608 1.00 45.00  ? 4181 PHE A CE1   1 
ATOM   19430 C  CE2   . PHE A 1 4181 ? 224.529 268.635 239.788 1.00 28.72  ? 4181 PHE A CE2   1 
ATOM   19431 C  CZ    . PHE A 1 4181 ? 224.683 268.831 238.440 1.00 41.01  ? 4181 PHE A CZ    1 
ATOM   19432 N  N     . LEU A 1 4182 ? 221.549 265.715 241.956 1.00 36.71  ? 4182 LEU A N     1 
ATOM   19433 C  CA    . LEU A 1 4182 ? 222.535 264.866 242.616 1.00 28.74  ? 4182 LEU A CA    1 
ATOM   19434 C  C     . LEU A 1 4182 ? 222.337 263.410 242.232 1.00 37.52  ? 4182 LEU A C     1 
ATOM   19435 O  O     . LEU A 1 4182 ? 223.306 262.680 242.002 1.00 44.30  ? 4182 LEU A O     1 
ATOM   19436 C  CB    . LEU A 1 4182 ? 222.445 265.030 244.130 1.00 25.14  ? 4182 LEU A CB    1 
ATOM   19437 C  CG    . LEU A 1 4182 ? 223.047 266.298 244.723 1.00 30.78  ? 4182 LEU A CG    1 
ATOM   19438 C  CD1   . LEU A 1 4182 ? 222.677 266.400 246.185 1.00 37.22  ? 4182 LEU A CD1   1 
ATOM   19439 C  CD2   . LEU A 1 4182 ? 224.551 266.293 244.545 1.00 41.45  ? 4182 LEU A CD2   1 
ATOM   19440 N  N     . LEU A 1 4183 ? 221.081 262.972 242.163 1.00 38.08  ? 4183 LEU A N     1 
ATOM   19441 C  CA    . LEU A 1 4183 ? 220.786 261.603 241.762 1.00 28.26  ? 4183 LEU A CA    1 
ATOM   19442 C  C     . LEU A 1 4183 ? 221.221 261.339 240.327 1.00 30.46  ? 4183 LEU A C     1 
ATOM   19443 O  O     . LEU A 1 4183 ? 221.769 260.274 240.025 1.00 45.02  ? 4183 LEU A O     1 
ATOM   19444 C  CB    . LEU A 1 4183 ? 219.295 261.337 241.942 1.00 30.95  ? 4183 LEU A CB    1 
ATOM   19445 C  CG    . LEU A 1 4183 ? 218.833 259.922 241.645 1.00 43.09  ? 4183 LEU A CG    1 
ATOM   19446 C  CD1   . LEU A 1 4183 ? 219.521 258.980 242.600 1.00 41.43  ? 4183 LEU A CD1   1 
ATOM   19447 C  CD2   . LEU A 1 4183 ? 217.333 259.853 241.809 1.00 38.11  ? 4183 LEU A CD2   1 
ATOM   19448 N  N     . ALA A 1 4184 ? 220.983 262.296 239.429 1.00 35.40  ? 4184 ALA A N     1 
ATOM   19449 C  CA    . ALA A 1 4184 ? 221.416 262.147 238.044 1.00 26.31  ? 4184 ALA A CA    1 
ATOM   19450 C  C     . ALA A 1 4184 ? 222.933 262.067 237.941 1.00 30.39  ? 4184 ALA A C     1 
ATOM   19451 O  O     . ALA A 1 4184 ? 223.466 261.240 237.192 1.00 37.35  ? 4184 ALA A O     1 
ATOM   19452 C  CB    . ALA A 1 4184 ? 220.885 263.305 237.203 1.00 31.44  ? 4184 ALA A CB    1 
ATOM   19453 N  N     . TRP A 1 4185 ? 223.644 262.921 238.679 1.00 29.49  ? 4185 TRP A N     1 
ATOM   19454 C  CA    . TRP A 1 4185 ? 225.103 262.871 238.669 1.00 31.92  ? 4185 TRP A CA    1 
ATOM   19455 C  C     . TRP A 1 4185 ? 225.617 261.551 239.225 1.00 33.39  ? 4185 TRP A C     1 
ATOM   19456 O  O     . TRP A 1 4185 ? 226.549 260.958 238.671 1.00 42.22  ? 4185 TRP A O     1 
ATOM   19457 C  CB    . TRP A 1 4185 ? 225.682 264.037 239.468 1.00 31.22  ? 4185 TRP A CB    1 
ATOM   19458 C  CG    . TRP A 1 4185 ? 227.166 263.945 239.637 1.00 31.93  ? 4185 TRP A CG    1 
ATOM   19459 C  CD1   . TRP A 1 4185 ? 227.838 263.408 240.694 1.00 33.73  ? 4185 TRP A CD1   1 
ATOM   19460 C  CD2   . TRP A 1 4185 ? 228.165 264.398 238.717 1.00 36.44  ? 4185 TRP A CD2   1 
ATOM   19461 N  NE1   . TRP A 1 4185 ? 229.191 263.499 240.491 1.00 39.75  ? 4185 TRP A NE1   1 
ATOM   19462 C  CE2   . TRP A 1 4185 ? 229.418 264.104 239.284 1.00 41.16  ? 4185 TRP A CE2   1 
ATOM   19463 C  CE3   . TRP A 1 4185 ? 228.120 265.027 237.470 1.00 31.27  ? 4185 TRP A CE3   1 
ATOM   19464 C  CZ2   . TRP A 1 4185 ? 230.616 264.416 238.647 1.00 36.24  ? 4185 TRP A CZ2   1 
ATOM   19465 C  CZ3   . TRP A 1 4185 ? 229.310 265.335 236.840 1.00 26.63  ? 4185 TRP A CZ3   1 
ATOM   19466 C  CH2   . TRP A 1 4185 ? 230.540 265.030 237.429 1.00 32.56  ? 4185 TRP A CH2   1 
ATOM   19467 N  N     . PHE A 1 4186 ? 225.027 261.082 240.325 1.00 29.72  ? 4186 PHE A N     1 
ATOM   19468 C  CA    . PHE A 1 4186 ? 225.428 259.807 240.906 1.00 19.66  ? 4186 PHE A CA    1 
ATOM   19469 C  C     . PHE A 1 4186 ? 225.195 258.667 239.926 1.00 21.95  ? 4186 PHE A C     1 
ATOM   19470 O  O     . PHE A 1 4186 ? 226.058 257.806 239.746 1.00 38.25  ? 4186 PHE A O     1 
ATOM   19471 C  CB    . PHE A 1 4186 ? 224.659 259.576 242.209 1.00 34.95  ? 4186 PHE A CB    1 
ATOM   19472 C  CG    . PHE A 1 4186 ? 224.867 258.218 242.813 1.00 36.94  ? 4186 PHE A CG    1 
ATOM   19473 C  CD1   . PHE A 1 4186 ? 225.988 257.948 243.574 1.00 37.44  ? 4186 PHE A CD1   1 
ATOM   19474 C  CD2   . PHE A 1 4186 ? 223.929 257.217 242.636 1.00 31.67  ? 4186 PHE A CD2   1 
ATOM   19475 C  CE1   . PHE A 1 4186 ? 226.175 256.704 244.133 1.00 33.36  ? 4186 PHE A CE1   1 
ATOM   19476 C  CE2   . PHE A 1 4186 ? 224.114 255.972 243.191 1.00 25.87  ? 4186 PHE A CE2   1 
ATOM   19477 C  CZ    . PHE A 1 4186 ? 225.236 255.716 243.942 1.00 26.10  ? 4186 PHE A CZ    1 
ATOM   19478 N  N     . HIS A 1 4187 ? 224.033 258.656 239.272 1.00 25.12  ? 4187 HIS A N     1 
ATOM   19479 C  CA    . HIS A 1 4187 ? 223.726 257.609 238.304 1.00 14.35  ? 4187 HIS A CA    1 
ATOM   19480 C  C     . HIS A 1 4187 ? 224.696 257.641 237.131 1.00 28.56  ? 4187 HIS A C     1 
ATOM   19481 O  O     . HIS A 1 4187 ? 225.165 256.592 236.674 1.00 38.92  ? 4187 HIS A O     1 
ATOM   19482 C  CB    . HIS A 1 4187 ? 222.285 257.767 237.823 1.00 23.13  ? 4187 HIS A CB    1 
ATOM   19483 C  CG    . HIS A 1 4187 ? 221.787 256.622 236.999 1.00 28.84  ? 4187 HIS A CG    1 
ATOM   19484 N  ND1   . HIS A 1 4187 ? 221.434 255.408 237.548 1.00 33.39  ? 4187 HIS A ND1   1 
ATOM   19485 C  CD2   . HIS A 1 4187 ? 221.568 256.510 235.668 1.00 32.90  ? 4187 HIS A CD2   1 
ATOM   19486 C  CE1   . HIS A 1 4187 ? 221.028 254.596 236.589 1.00 29.53  ? 4187 HIS A CE1   1 
ATOM   19487 N  NE2   . HIS A 1 4187 ? 221.098 255.241 235.439 1.00 34.17  ? 4187 HIS A NE2   1 
ATOM   19488 N  N     . ALA A 1 4188 ? 225.012 258.839 236.631 1.00 37.55  ? 4188 ALA A N     1 
ATOM   19489 C  CA    . ALA A 1 4188 ? 225.949 258.957 235.519 1.00 23.39  ? 4188 ALA A CA    1 
ATOM   19490 C  C     . ALA A 1 4188 ? 227.342 258.484 235.910 1.00 27.63  ? 4188 ALA A C     1 
ATOM   19491 O  O     . ALA A 1 4188 ? 228.000 257.779 235.138 1.00 39.37  ? 4188 ALA A O     1 
ATOM   19492 C  CB    . ALA A 1 4188 ? 225.992 260.400 235.022 1.00 25.76  ? 4188 ALA A CB    1 
ATOM   19493 N  N     . ILE A 1 4189 ? 227.812 258.862 237.100 1.00 30.50  ? 4189 ILE A N     1 
ATOM   19494 C  CA    . ILE A 1 4189 ? 229.129 258.423 237.554 1.00 29.63  ? 4189 ILE A CA    1 
ATOM   19495 C  C     . ILE A 1 4189 ? 229.152 256.913 237.741 1.00 33.99  ? 4189 ILE A C     1 
ATOM   19496 O  O     . ILE A 1 4189 ? 230.122 256.240 237.373 1.00 41.40  ? 4189 ILE A O     1 
ATOM   19497 C  CB    . ILE A 1 4189 ? 229.519 259.158 238.850 1.00 28.37  ? 4189 ILE A CB    1 
ATOM   19498 C  CG1   . ILE A 1 4189 ? 229.721 260.647 238.581 1.00 39.05  ? 4189 ILE A CG1   1 
ATOM   19499 C  CG2   . ILE A 1 4189 ? 230.768 258.551 239.457 1.00 24.20  ? 4189 ILE A CG2   1 
ATOM   19500 C  CD1   . ILE A 1 4189 ? 230.578 260.943 237.383 1.00 39.24  ? 4189 ILE A CD1   1 
ATOM   19501 N  N     . ILE A 1 4190 ? 228.084 256.357 238.315 1.00 36.47  ? 4190 ILE A N     1 
ATOM   19502 C  CA    . ILE A 1 4190 ? 228.027 254.924 238.579 1.00 32.25  ? 4190 ILE A CA    1 
ATOM   19503 C  C     . ILE A 1 4190 ? 228.036 254.136 237.276 1.00 37.32  ? 4190 ILE A C     1 
ATOM   19504 O  O     . ILE A 1 4190 ? 228.752 253.136 237.145 1.00 39.29  ? 4190 ILE A O     1 
ATOM   19505 C  CB    . ILE A 1 4190 ? 226.791 254.600 239.440 1.00 23.99  ? 4190 ILE A CB    1 
ATOM   19506 C  CG1   . ILE A 1 4190 ? 226.987 255.099 240.871 1.00 32.85  ? 4190 ILE A CG1   1 
ATOM   19507 C  CG2   . ILE A 1 4190 ? 226.515 253.124 239.451 1.00 35.04  ? 4190 ILE A CG2   1 
ATOM   19508 C  CD1   . ILE A 1 4190 ? 228.292 254.693 241.494 1.00 36.17  ? 4190 ILE A CD1   1 
ATOM   19509 N  N     . GLN A 1 4191 ? 227.250 254.573 236.288 1.00 31.35  ? 4191 GLN A N     1 
ATOM   19510 C  CA    . GLN A 1 4191 ? 227.178 253.832 235.033 1.00 18.66  ? 4191 GLN A CA    1 
ATOM   19511 C  C     . GLN A 1 4191 ? 228.445 253.998 234.203 1.00 33.30  ? 4191 GLN A C     1 
ATOM   19512 O  O     . GLN A 1 4191 ? 228.865 253.062 233.515 1.00 39.69  ? 4191 GLN A O     1 
ATOM   19513 C  CB    . GLN A 1 4191 ? 225.956 254.267 234.229 1.00 24.92  ? 4191 GLN A CB    1 
ATOM   19514 C  CG    . GLN A 1 4191 ? 224.682 253.550 234.618 1.00 28.72  ? 4191 GLN A CG    1 
ATOM   19515 C  CD    . GLN A 1 4191 ? 223.553 253.820 233.654 1.00 38.88  ? 4191 GLN A CD    1 
ATOM   19516 O  OE1   . GLN A 1 4191 ? 223.635 254.722 232.823 1.00 45.39  ? 4191 GLN A OE1   1 
ATOM   19517 N  NE2   . GLN A 1 4191 ? 222.491 253.033 233.750 1.00 44.48  ? 4191 GLN A NE2   1 
ATOM   19518 N  N     . GLU A 1 4192 ? 229.063 255.179 234.242 1.00 34.44  ? 4192 GLU A N     1 
ATOM   19519 C  CA    . GLU A 1 4192 ? 230.254 255.412 233.434 1.00 28.91  ? 4192 GLU A CA    1 
ATOM   19520 C  C     . GLU A 1 4192 ? 231.461 254.632 233.931 1.00 36.98  ? 4192 GLU A C     1 
ATOM   19521 O  O     . GLU A 1 4192 ? 232.380 254.378 233.147 1.00 43.26  ? 4192 GLU A O     1 
ATOM   19522 C  CB    . GLU A 1 4192 ? 230.585 256.902 233.391 1.00 25.35  ? 4192 GLU A CB    1 
ATOM   19523 C  CG    . GLU A 1 4192 ? 229.686 257.709 232.479 1.00 32.81  ? 4192 GLU A CG    1 
ATOM   19524 C  CD    . GLU A 1 4192 ? 229.582 257.111 231.094 1.00 56.74  ? 4192 GLU A CD    1 
ATOM   19525 O  OE1   . GLU A 1 4192 ? 230.630 256.963 230.430 1.00 53.83  ? 4192 GLU A OE1   1 
ATOM   19526 O  OE2   . GLU A 1 4192 ? 228.454 256.787 230.668 1.00 51.30  ? 4192 GLU A OE2   1 
ATOM   19527 N  N     . ARG A 1 4193 ? 231.489 254.254 235.210 1.00 33.07  ? 4193 ARG A N     1 
ATOM   19528 C  CA    . ARG A 1 4193 ? 232.584 253.437 235.716 1.00 25.80  ? 4193 ARG A CA    1 
ATOM   19529 C  C     . ARG A 1 4193 ? 232.528 252.010 235.191 1.00 31.97  ? 4193 ARG A C     1 
ATOM   19530 O  O     . ARG A 1 4193 ? 233.536 251.301 235.254 1.00 42.57  ? 4193 ARG A O     1 
ATOM   19531 C  CB    . ARG A 1 4193 ? 232.573 253.422 237.244 1.00 28.99  ? 4193 ARG A CB    1 
ATOM   19532 C  CG    . ARG A 1 4193 ? 232.987 254.728 237.886 1.00 28.65  ? 4193 ARG A CG    1 
ATOM   19533 C  CD    . ARG A 1 4193 ? 232.987 254.613 239.399 1.00 26.41  ? 4193 ARG A CD    1 
ATOM   19534 N  NE    . ARG A 1 4193 ? 234.018 253.696 239.871 1.00 27.70  ? 4193 ARG A NE    1 
ATOM   19535 C  CZ    . ARG A 1 4193 ? 235.132 254.071 240.483 1.00 21.27  ? 4193 ARG A CZ    1 
ATOM   19536 N  NH1   . ARG A 1 4193 ? 235.393 255.344 240.725 1.00 29.43  ? 4193 ARG A NH1   1 
ATOM   19537 N  NH2   . ARG A 1 4193 ? 236.009 253.146 240.856 1.00 23.87  ? 4193 ARG A NH2   1 
ATOM   19538 N  N     . LEU A 1 4194 ? 231.374 251.574 234.683 1.00 36.59  ? 4194 LEU A N     1 
ATOM   19539 C  CA    . LEU A 1 4194 ? 231.239 250.218 234.166 1.00 32.23  ? 4194 LEU A CA    1 
ATOM   19540 C  C     . LEU A 1 4194 ? 232.084 249.979 232.923 1.00 35.17  ? 4194 LEU A C     1 
ATOM   19541 O  O     . LEU A 1 4194 ? 232.401 248.825 232.620 1.00 30.23  ? 4194 LEU A O     1 
ATOM   19542 C  CB    . LEU A 1 4194 ? 229.771 249.921 233.862 1.00 31.31  ? 4194 LEU A CB    1 
ATOM   19543 C  CG    . LEU A 1 4194 ? 228.865 249.763 235.082 1.00 32.35  ? 4194 LEU A CG    1 
ATOM   19544 C  CD1   . LEU A 1 4194 ? 227.401 249.846 234.690 1.00 33.31  ? 4194 LEU A CD1   1 
ATOM   19545 C  CD2   . LEU A 1 4194 ? 229.156 248.456 235.791 1.00 29.60  ? 4194 LEU A CD2   1 
ATOM   19546 N  N     . ARG A 1 4195 ? 232.453 251.037 232.197 1.00 39.18  ? 4195 ARG A N     1 
ATOM   19547 C  CA    . ARG A 1 4195 ? 233.271 250.864 231.003 1.00 35.71  ? 4195 ARG A CA    1 
ATOM   19548 C  C     . ARG A 1 4195 ? 234.671 250.377 231.347 1.00 39.04  ? 4195 ARG A C     1 
ATOM   19549 O  O     . ARG A 1 4195 ? 235.400 249.908 230.467 1.00 41.66  ? 4195 ARG A O     1 
ATOM   19550 C  CB    . ARG A 1 4195 ? 233.342 252.176 230.224 1.00 34.16  ? 4195 ARG A CB    1 
ATOM   19551 C  CG    . ARG A 1 4195 ? 232.016 252.897 230.113 1.00 38.08  ? 4195 ARG A CG    1 
ATOM   19552 C  CD    . ARG A 1 4195 ? 232.096 254.043 229.119 1.00 44.01  ? 4195 ARG A CD    1 
ATOM   19553 N  NE    . ARG A 1 4195 ? 230.784 254.610 228.832 1.00 50.84  ? 4195 ARG A NE    1 
ATOM   19554 C  CZ    . ARG A 1 4195 ? 229.891 254.064 228.017 1.00 49.52  ? 4195 ARG A CZ    1 
ATOM   19555 N  NH1   . ARG A 1 4195 ? 230.139 252.935 227.376 1.00 40.12  ? 4195 ARG A NH1   1 
ATOM   19556 N  NH2   . ARG A 1 4195 ? 228.720 254.668 227.841 1.00 46.17  ? 4195 ARG A NH2   1 
ATOM   19557 N  N     . TYR A 1 4196 ? 235.065 250.486 232.615 1.00 34.31  ? 4196 TYR A N     1 
ATOM   19558 C  CA    . TYR A 1 4196 ? 236.379 250.053 233.080 1.00 35.15  ? 4196 TYR A CA    1 
ATOM   19559 C  C     . TYR A 1 4196 ? 236.146 248.886 234.034 1.00 39.86  ? 4196 TYR A C     1 
ATOM   19560 O  O     . TYR A 1 4196 ? 236.087 249.039 235.252 1.00 45.10  ? 4196 TYR A O     1 
ATOM   19561 C  CB    . TYR A 1 4196 ? 237.099 251.221 233.735 1.00 26.27  ? 4196 TYR A CB    1 
ATOM   19562 C  CG    . TYR A 1 4196 ? 236.938 252.493 232.933 1.00 36.65  ? 4196 TYR A CG    1 
ATOM   19563 C  CD1   . TYR A 1 4196 ? 236.142 253.528 233.394 1.00 42.23  ? 4196 TYR A CD1   1 
ATOM   19564 C  CD2   . TYR A 1 4196 ? 237.566 252.650 231.707 1.00 43.46  ? 4196 TYR A CD2   1 
ATOM   19565 C  CE1   . TYR A 1 4196 ? 235.980 254.684 232.663 1.00 42.40  ? 4196 TYR A CE1   1 
ATOM   19566 C  CE2   . TYR A 1 4196 ? 237.410 253.806 230.969 1.00 41.58  ? 4196 TYR A CE2   1 
ATOM   19567 C  CZ    . TYR A 1 4196 ? 236.616 254.819 231.453 1.00 40.30  ? 4196 TYR A CZ    1 
ATOM   19568 O  OH    . TYR A 1 4196 ? 236.457 255.973 230.723 1.00 41.54  ? 4196 TYR A OH    1 
ATOM   19569 N  N     . ALA A 1 4197 ? 236.017 247.694 233.448 1.00 39.83  ? 4197 ALA A N     1 
ATOM   19570 C  CA    . ALA A 1 4197 ? 235.385 246.579 234.152 1.00 34.31  ? 4197 ALA A CA    1 
ATOM   19571 C  C     . ALA A 1 4197 ? 236.139 246.128 235.396 1.00 48.95  ? 4197 ALA A C     1 
ATOM   19572 O  O     . ALA A 1 4197 ? 235.503 246.002 236.456 1.00 52.19  ? 4197 ALA A O     1 
ATOM   19573 C  CB    . ALA A 1 4197 ? 235.162 245.418 233.176 1.00 41.55  ? 4197 ALA A CB    1 
ATOM   19574 N  N     . PRO A 1 4198 ? 237.450 245.857 235.363 1.00 52.12  ? 4198 PRO A N     1 
ATOM   19575 C  CA    . PRO A 1 4198 ? 238.109 245.429 236.605 1.00 34.93  ? 4198 PRO A CA    1 
ATOM   19576 C  C     . PRO A 1 4198 ? 238.338 246.566 237.581 1.00 39.64  ? 4198 PRO A C     1 
ATOM   19577 O  O     . PRO A 1 4198 ? 238.412 246.323 238.791 1.00 47.86  ? 4198 PRO A O     1 
ATOM   19578 C  CB    . PRO A 1 4198 ? 239.440 244.837 236.117 1.00 36.67  ? 4198 PRO A CB    1 
ATOM   19579 C  CG    . PRO A 1 4198 ? 239.262 244.614 234.655 1.00 45.32  ? 4198 PRO A CG    1 
ATOM   19580 C  CD    . PRO A 1 4198 ? 238.355 245.711 234.211 1.00 41.37  ? 4198 PRO A CD    1 
ATOM   19581 N  N     . LEU A 1 4199 ? 238.435 247.802 237.099 1.00 34.12  ? 4199 LEU A N     1 
ATOM   19582 C  CA    . LEU A 1 4199 ? 238.877 248.923 237.917 1.00 26.09  ? 4199 LEU A CA    1 
ATOM   19583 C  C     . LEU A 1 4199 ? 237.719 249.787 238.406 1.00 34.37  ? 4199 LEU A C     1 
ATOM   19584 O  O     . LEU A 1 4199 ? 237.644 250.101 239.597 1.00 43.16  ? 4199 LEU A O     1 
ATOM   19585 C  CB    . LEU A 1 4199 ? 239.874 249.771 237.120 1.00 29.79  ? 4199 LEU A CB    1 
ATOM   19586 C  CG    . LEU A 1 4199 ? 240.539 250.937 237.840 1.00 29.77  ? 4199 LEU A CG    1 
ATOM   19587 C  CD1   . LEU A 1 4199 ? 241.376 250.406 238.982 1.00 37.49  ? 4199 LEU A CD1   1 
ATOM   19588 C  CD2   . LEU A 1 4199 ? 241.389 251.744 236.881 1.00 36.17  ? 4199 LEU A CD2   1 
ATOM   19589 N  N     . GLY A 1 4200 ? 236.816 250.185 237.506 1.00 37.19  ? 4200 GLY A N     1 
ATOM   19590 C  CA    . GLY A 1 4200 ? 235.670 250.978 237.924 1.00 27.58  ? 4200 GLY A CA    1 
ATOM   19591 C  C     . GLY A 1 4200 ? 234.766 250.234 238.887 1.00 36.24  ? 4200 GLY A C     1 
ATOM   19592 O  O     . GLY A 1 4200 ? 234.288 250.802 239.870 1.00 50.38  ? 4200 GLY A O     1 
ATOM   19593 N  N     . TRP A 1 4201 ? 234.518 248.958 238.613 1.00 34.55  ? 4201 TRP A N     1 
ATOM   19594 C  CA    . TRP A 1 4201 ? 233.815 248.065 239.524 1.00 28.09  ? 4201 TRP A CA    1 
ATOM   19595 C  C     . TRP A 1 4201 ? 234.588 246.754 239.550 1.00 40.84  ? 4201 TRP A C     1 
ATOM   19596 O  O     . TRP A 1 4201 ? 235.710 246.668 239.046 1.00 53.48  ? 4201 TRP A O     1 
ATOM   19597 C  CB    . TRP A 1 4201 ? 232.353 247.881 239.096 1.00 26.84  ? 4201 TRP A CB    1 
ATOM   19598 C  CG    . TRP A 1 4201 ? 231.518 249.107 239.279 1.00 37.33  ? 4201 TRP A CG    1 
ATOM   19599 C  CD1   . TRP A 1 4201 ? 231.076 249.950 238.306 1.00 38.20  ? 4201 TRP A CD1   1 
ATOM   19600 C  CD2   . TRP A 1 4201 ? 231.023 249.629 240.516 1.00 41.47  ? 4201 TRP A CD2   1 
ATOM   19601 N  NE1   . TRP A 1 4201 ? 230.336 250.966 238.858 1.00 33.60  ? 4201 TRP A NE1   1 
ATOM   19602 C  CE2   . TRP A 1 4201 ? 230.292 250.791 240.215 1.00 37.24  ? 4201 TRP A CE2   1 
ATOM   19603 C  CE3   . TRP A 1 4201 ? 231.129 249.227 241.849 1.00 37.87  ? 4201 TRP A CE3   1 
ATOM   19604 C  CZ2   . TRP A 1 4201 ? 229.670 251.552 241.196 1.00 39.17  ? 4201 TRP A CZ2   1 
ATOM   19605 C  CZ3   . TRP A 1 4201 ? 230.511 249.984 242.820 1.00 37.51  ? 4201 TRP A CZ3   1 
ATOM   19606 C  CH2   . TRP A 1 4201 ? 229.791 251.134 242.490 1.00 40.77  ? 4201 TRP A CH2   1 
ATOM   19607 N  N     . SER A 1 4202 ? 234.004 245.720 240.150 1.00 39.15  ? 4202 SER A N     1 
ATOM   19608 C  CA    . SER A 1 4202 ? 234.601 244.396 240.088 1.00 41.18  ? 4202 SER A CA    1 
ATOM   19609 C  C     . SER A 1 4202 ? 233.937 243.493 239.064 1.00 48.63  ? 4202 SER A C     1 
ATOM   19610 O  O     . SER A 1 4202 ? 234.568 242.536 238.606 1.00 55.92  ? 4202 SER A O     1 
ATOM   19611 C  CB    . SER A 1 4202 ? 234.555 243.717 241.463 1.00 46.02  ? 4202 SER A CB    1 
ATOM   19612 O  OG    . SER A 1 4202 ? 235.470 242.638 241.528 1.00 54.65  ? 4202 SER A OG    1 
ATOM   19613 N  N     . LYS A 1 4203 ? 232.693 243.779 238.691 1.00 41.73  ? 4203 LYS A N     1 
ATOM   19614 C  CA    . LYS A 1 4203 ? 231.996 243.034 237.657 1.00 42.94  ? 4203 LYS A CA    1 
ATOM   19615 C  C     . LYS A 1 4203 ? 230.988 243.958 236.994 1.00 45.48  ? 4203 LYS A C     1 
ATOM   19616 O  O     . LYS A 1 4203 ? 230.621 245.001 237.538 1.00 51.76  ? 4203 LYS A O     1 
ATOM   19617 C  CB    . LYS A 1 4203 ? 231.309 241.787 238.222 1.00 43.61  ? 4203 LYS A CB    1 
ATOM   19618 C  CG    . LYS A 1 4203 ? 230.612 242.009 239.544 1.00 44.25  ? 4203 LYS A CG    1 
ATOM   19619 C  CD    . LYS A 1 4203 ? 230.072 240.707 240.098 1.00 53.32  ? 4203 LYS A CD    1 
ATOM   19620 C  CE    . LYS A 1 4203 ? 231.201 239.736 240.397 1.00 49.87  ? 4203 LYS A CE    1 
ATOM   19621 N  NZ    . LYS A 1 4203 ? 232.159 240.288 241.392 1.00 45.19  ? 4203 LYS A NZ    1 
ATOM   19622 N  N     . LYS A 1 4204 ? 230.545 243.562 235.806 1.00 51.59  ? 4204 LYS A N     1 
ATOM   19623 C  CA    . LYS A 1 4204 ? 229.647 244.388 235.003 1.00 46.30  ? 4204 LYS A CA    1 
ATOM   19624 C  C     . LYS A 1 4204 ? 228.253 244.316 235.611 1.00 50.30  ? 4204 LYS A C     1 
ATOM   19625 O  O     . LYS A 1 4204 ? 227.421 243.495 235.226 1.00 48.16  ? 4204 LYS A O     1 
ATOM   19626 C  CB    . LYS A 1 4204 ? 229.654 243.929 233.551 1.00 47.40  ? 4204 LYS A CB    1 
ATOM   19627 C  CG    . LYS A 1 4204 ? 228.789 244.764 232.623 1.00 53.29  ? 4204 LYS A CG    1 
ATOM   19628 C  CD    . LYS A 1 4204 ? 229.346 246.167 232.468 1.00 52.21  ? 4204 LYS A CD    1 
ATOM   19629 C  CE    . LYS A 1 4204 ? 228.474 247.006 231.551 1.00 50.60  ? 4204 LYS A CE    1 
ATOM   19630 N  NZ    . LYS A 1 4204 ? 228.501 246.490 230.156 1.00 49.23  ? 4204 LYS A NZ    1 
ATOM   19631 N  N     . TYR A 1 4205 ? 227.999 245.187 236.583 1.00 39.10  ? 4205 TYR A N     1 
ATOM   19632 C  CA    . TYR A 1 4205 ? 226.676 245.274 237.181 1.00 34.77  ? 4205 TYR A CA    1 
ATOM   19633 C  C     . TYR A 1 4205 ? 225.694 245.910 236.208 1.00 41.23  ? 4205 TYR A C     1 
ATOM   19634 O  O     . TYR A 1 4205 ? 226.073 246.662 235.308 1.00 45.67  ? 4205 TYR A O     1 
ATOM   19635 C  CB    . TYR A 1 4205 ? 226.718 246.083 238.473 1.00 32.22  ? 4205 TYR A CB    1 
ATOM   19636 C  CG    . TYR A 1 4205 ? 227.533 245.453 239.571 1.00 33.70  ? 4205 TYR A CG    1 
ATOM   19637 C  CD1   . TYR A 1 4205 ? 227.172 244.231 240.114 1.00 37.23  ? 4205 TYR A CD1   1 
ATOM   19638 C  CD2   . TYR A 1 4205 ? 228.658 246.085 240.071 1.00 36.42  ? 4205 TYR A CD2   1 
ATOM   19639 C  CE1   . TYR A 1 4205 ? 227.913 243.655 241.120 1.00 36.12  ? 4205 TYR A CE1   1 
ATOM   19640 C  CE2   . TYR A 1 4205 ? 229.403 245.517 241.074 1.00 37.08  ? 4205 TYR A CE2   1 
ATOM   19641 C  CZ    . TYR A 1 4205 ? 229.027 244.303 241.597 1.00 42.28  ? 4205 TYR A CZ    1 
ATOM   19642 O  OH    . TYR A 1 4205 ? 229.772 243.734 242.600 1.00 50.12  ? 4205 TYR A OH    1 
ATOM   19643 N  N     . GLU A 1 4206 ? 224.418 245.595 236.392 1.00 42.08  ? 4206 GLU A N     1 
ATOM   19644 C  CA    . GLU A 1 4206 ? 223.376 246.088 235.495 1.00 38.12  ? 4206 GLU A CA    1 
ATOM   19645 C  C     . GLU A 1 4206 ? 222.679 247.307 236.096 1.00 45.78  ? 4206 GLU A C     1 
ATOM   19646 O  O     . GLU A 1 4206 ? 221.482 247.305 236.372 1.00 52.52  ? 4206 GLU A O     1 
ATOM   19647 C  CB    . GLU A 1 4206 ? 222.382 244.976 235.185 1.00 43.51  ? 4206 GLU A CB    1 
ATOM   19648 C  CG    . GLU A 1 4206 ? 222.987 243.832 234.393 1.00 46.88  ? 4206 GLU A CG    1 
ATOM   19649 C  CD    . GLU A 1 4206 ? 223.399 244.254 233.005 1.00 55.91  ? 4206 GLU A CD    1 
ATOM   19650 O  OE1   . GLU A 1 4206 ? 222.742 245.148 232.444 1.00 60.69  ? 4206 GLU A OE1   1 
ATOM   19651 O  OE2   . GLU A 1 4206 ? 224.379 243.691 232.474 1.00 53.96  ? 4206 GLU A OE2   1 
ATOM   19652 N  N     . PHE A 1 4207 ? 223.457 248.367 236.287 1.00 46.37  ? 4207 PHE A N     1 
ATOM   19653 C  CA    . PHE A 1 4207 ? 222.926 249.635 236.781 1.00 36.24  ? 4207 PHE A CA    1 
ATOM   19654 C  C     . PHE A 1 4207 ? 222.150 250.299 235.655 1.00 42.22  ? 4207 PHE A C     1 
ATOM   19655 O  O     . PHE A 1 4207 ? 222.732 250.915 234.761 1.00 46.51  ? 4207 PHE A O     1 
ATOM   19656 C  CB    . PHE A 1 4207 ? 224.058 250.527 237.275 1.00 38.42  ? 4207 PHE A CB    1 
ATOM   19657 C  CG    . PHE A 1 4207 ? 224.785 249.980 238.467 1.00 39.59  ? 4207 PHE A CG    1 
ATOM   19658 C  CD1   . PHE A 1 4207 ? 224.090 249.543 239.578 1.00 40.39  ? 4207 PHE A CD1   1 
ATOM   19659 C  CD2   . PHE A 1 4207 ? 226.165 249.894 238.473 1.00 39.08  ? 4207 PHE A CD2   1 
ATOM   19660 C  CE1   . PHE A 1 4207 ? 224.758 249.039 240.674 1.00 43.59  ? 4207 PHE A CE1   1 
ATOM   19661 C  CE2   . PHE A 1 4207 ? 226.836 249.394 239.568 1.00 34.40  ? 4207 PHE A CE2   1 
ATOM   19662 C  CZ    . PHE A 1 4207 ? 226.132 248.964 240.668 1.00 36.83  ? 4207 PHE A CZ    1 
ATOM   19663 N  N     . GLY A 1 4208 ? 220.827 250.180 235.690 1.00 43.81  ? 4208 GLY A N     1 
ATOM   19664 C  CA    . GLY A 1 4208 ? 220.016 250.654 234.588 1.00 44.36  ? 4208 GLY A CA    1 
ATOM   19665 C  C     . GLY A 1 4208 ? 218.941 251.645 234.973 1.00 40.82  ? 4208 GLY A C     1 
ATOM   19666 O  O     . GLY A 1 4208 ? 219.002 252.261 236.039 1.00 45.52  ? 4208 GLY A O     1 
ATOM   19667 N  N     . GLU A 1 4209 ? 217.945 251.805 234.099 1.00 48.66  ? 4209 GLU A N     1 
ATOM   19668 C  CA    . GLU A 1 4209 ? 216.894 252.783 234.345 1.00 47.25  ? 4209 GLU A CA    1 
ATOM   19669 C  C     . GLU A 1 4209 ? 216.003 252.383 235.512 1.00 47.04  ? 4209 GLU A C     1 
ATOM   19670 O  O     . GLU A 1 4209 ? 215.423 253.255 236.164 1.00 52.37  ? 4209 GLU A O     1 
ATOM   19671 C  CB    . GLU A 1 4209 ? 216.053 252.983 233.085 1.00 49.36  ? 4209 GLU A CB    1 
ATOM   19672 C  CG    . GLU A 1 4209 ? 216.579 254.064 232.157 1.00 55.48  ? 4209 GLU A CG    1 
ATOM   19673 C  CD    . GLU A 1 4209 ? 216.314 255.461 232.684 1.00 63.34  ? 4209 GLU A CD    1 
ATOM   19674 O  OE1   . GLU A 1 4209 ? 215.188 255.713 233.161 1.00 58.17  ? 4209 GLU A OE1   1 
ATOM   19675 O  OE2   . GLU A 1 4209 ? 217.232 256.307 232.622 1.00 61.38  ? 4209 GLU A OE2   1 
ATOM   19676 N  N     . SER A 1 4210 ? 215.875 251.084 235.789 1.00 41.60  ? 4210 SER A N     1 
ATOM   19677 C  CA    . SER A 1 4210 ? 215.051 250.652 236.914 1.00 40.31  ? 4210 SER A CA    1 
ATOM   19678 C  C     . SER A 1 4210 ? 215.603 251.180 238.231 1.00 45.68  ? 4210 SER A C     1 
ATOM   19679 O  O     . SER A 1 4210 ? 214.843 251.630 239.098 1.00 50.14  ? 4210 SER A O     1 
ATOM   19680 C  CB    . SER A 1 4210 ? 214.958 249.128 236.942 1.00 45.35  ? 4210 SER A CB    1 
ATOM   19681 O  OG    . SER A 1 4210 ? 216.237 248.538 236.803 1.00 54.02  ? 4210 SER A OG    1 
ATOM   19682 N  N     . ASP A 1 4211 ? 216.927 251.141 238.394 1.00 40.75  ? 4211 ASP A N     1 
ATOM   19683 C  CA    . ASP A 1 4211 ? 217.551 251.686 239.594 1.00 27.55  ? 4211 ASP A CA    1 
ATOM   19684 C  C     . ASP A 1 4211 ? 217.308 253.184 239.714 1.00 37.36  ? 4211 ASP A C     1 
ATOM   19685 O  O     . ASP A 1 4211 ? 217.015 253.685 240.805 1.00 54.78  ? 4211 ASP A O     1 
ATOM   19686 C  CB    . ASP A 1 4211 ? 219.048 251.390 239.578 1.00 38.97  ? 4211 ASP A CB    1 
ATOM   19687 C  CG    . ASP A 1 4211 ? 219.349 249.915 239.691 1.00 45.59  ? 4211 ASP A CG    1 
ATOM   19688 O  OD1   . ASP A 1 4211 ? 218.602 249.207 240.395 1.00 49.94  ? 4211 ASP A OD1   1 
ATOM   19689 O  OD2   . ASP A 1 4211 ? 220.331 249.460 239.073 1.00 48.09  ? 4211 ASP A OD2   1 
ATOM   19690 N  N     . LEU A 1 4212 ? 217.426 253.915 238.604 1.00 36.44  ? 4212 LEU A N     1 
ATOM   19691 C  CA    . LEU A 1 4212 ? 217.196 255.355 238.637 1.00 32.05  ? 4212 LEU A CA    1 
ATOM   19692 C  C     . LEU A 1 4212 ? 215.749 255.680 238.988 1.00 36.87  ? 4212 LEU A C     1 
ATOM   19693 O  O     . LEU A 1 4212 ? 215.489 256.604 239.765 1.00 49.17  ? 4212 LEU A O     1 
ATOM   19694 C  CB    . LEU A 1 4212 ? 217.578 255.976 237.296 1.00 38.99  ? 4212 LEU A CB    1 
ATOM   19695 C  CG    . LEU A 1 4212 ? 217.437 257.493 237.180 1.00 40.13  ? 4212 LEU A CG    1 
ATOM   19696 C  CD1   . LEU A 1 4212 ? 218.480 258.199 238.023 1.00 33.01  ? 4212 LEU A CD1   1 
ATOM   19697 C  CD2   . LEU A 1 4212 ? 217.545 257.912 235.729 1.00 44.76  ? 4212 LEU A CD2   1 
ATOM   19698 N  N     . ARG A 1 4213 ? 214.793 254.935 238.426 1.00 33.41  ? 4213 ARG A N     1 
ATOM   19699 C  CA    . ARG A 1 4213 ? 213.390 255.170 238.755 1.00 36.38  ? 4213 ARG A CA    1 
ATOM   19700 C  C     . ARG A 1 4213 ? 213.099 254.846 240.215 1.00 39.94  ? 4213 ARG A C     1 
ATOM   19701 O  O     . ARG A 1 4213 ? 212.357 255.577 240.880 1.00 49.91  ? 4213 ARG A O     1 
ATOM   19702 C  CB    . ARG A 1 4213 ? 212.484 254.357 237.832 1.00 45.73  ? 4213 ARG A CB    1 
ATOM   19703 C  CG    . ARG A 1 4213 ? 212.710 254.618 236.355 1.00 46.31  ? 4213 ARG A CG    1 
ATOM   19704 C  CD    . ARG A 1 4213 ? 211.410 254.617 235.573 1.00 44.28  ? 4213 ARG A CD    1 
ATOM   19705 N  NE    . ARG A 1 4213 ? 211.649 254.618 234.135 1.00 53.13  ? 4213 ARG A NE    1 
ATOM   19706 C  CZ    . ARG A 1 4213 ? 211.765 255.712 233.393 1.00 56.25  ? 4213 ARG A CZ    1 
ATOM   19707 N  NH1   . ARG A 1 4213 ? 211.672 256.920 233.924 1.00 46.96  ? 4213 ARG A NH1   1 
ATOM   19708 N  NH2   . ARG A 1 4213 ? 211.981 255.590 232.087 1.00 49.88  ? 4213 ARG A NH2   1 
ATOM   19709 N  N     . SER A 1 4214 ? 213.672 253.756 240.732 1.00 28.65  ? 4214 SER A N     1 
ATOM   19710 C  CA    . SER A 1 4214 ? 213.481 253.429 242.141 1.00 28.82  ? 4214 SER A CA    1 
ATOM   19711 C  C     . SER A 1 4214 ? 214.070 254.507 243.040 1.00 39.07  ? 4214 SER A C     1 
ATOM   19712 O  O     . SER A 1 4214 ? 213.475 254.871 244.061 1.00 46.82  ? 4214 SER A O     1 
ATOM   19713 C  CB    . SER A 1 4214 ? 214.104 252.071 242.453 1.00 34.72  ? 4214 SER A CB    1 
ATOM   19714 O  OG    . SER A 1 4214 ? 213.508 251.051 241.673 1.00 46.23  ? 4214 SER A OG    1 
ATOM   19715 N  N     . ALA A 1 4215 ? 215.242 255.030 242.678 1.00 38.24  ? 4215 ALA A N     1 
ATOM   19716 C  CA    . ALA A 1 4215 ? 215.859 256.086 243.470 1.00 22.17  ? 4215 ALA A CA    1 
ATOM   19717 C  C     . ALA A 1 4215 ? 215.042 257.371 243.418 1.00 32.56  ? 4215 ALA A C     1 
ATOM   19718 O  O     . ALA A 1 4215 ? 214.914 258.071 244.429 1.00 41.40  ? 4215 ALA A O     1 
ATOM   19719 C  CB    . ALA A 1 4215 ? 217.285 256.327 242.987 1.00 27.29  ? 4215 ALA A CB    1 
ATOM   19720 N  N     . CYS A 1 4216 ? 214.486 257.702 242.250 1.00 40.18  ? 4216 CYS A N     1 
ATOM   19721 C  CA    . CYS A 1 4216 ? 213.607 258.864 242.149 1.00 35.16  ? 4216 CYS A CA    1 
ATOM   19722 C  C     . CYS A 1 4216 ? 212.362 258.688 243.009 1.00 38.31  ? 4216 CYS A C     1 
ATOM   19723 O  O     . CYS A 1 4216 ? 211.920 259.633 243.672 1.00 42.83  ? 4216 CYS A O     1 
ATOM   19724 C  CB    . CYS A 1 4216 ? 213.214 259.106 240.692 1.00 40.57  ? 4216 CYS A CB    1 
ATOM   19725 S  SG    . CYS A 1 4216 ? 214.548 259.683 239.624 1.00 53.52  ? 4216 CYS A SG    1 
ATOM   19726 N  N     . ASP A 1 4217 ? 211.783 257.485 243.007 1.00 39.00  ? 4217 ASP A N     1 
ATOM   19727 C  CA    . ASP A 1 4217 ? 210.622 257.219 243.848 1.00 33.63  ? 4217 ASP A CA    1 
ATOM   19728 C  C     . ASP A 1 4217 ? 210.967 257.361 245.324 1.00 40.72  ? 4217 ASP A C     1 
ATOM   19729 O  O     . ASP A 1 4217 ? 210.186 257.921 246.101 1.00 48.86  ? 4217 ASP A O     1 
ATOM   19730 C  CB    . ASP A 1 4217 ? 210.074 255.823 243.560 1.00 42.95  ? 4217 ASP A CB    1 
ATOM   19731 C  CG    . ASP A 1 4217 ? 209.484 255.703 242.172 1.00 53.70  ? 4217 ASP A CG    1 
ATOM   19732 O  OD1   . ASP A 1 4217 ? 209.478 254.582 241.623 1.00 49.64  ? 4217 ASP A OD1   1 
ATOM   19733 O  OD2   . ASP A 1 4217 ? 209.023 256.727 241.628 1.00 55.75  ? 4217 ASP A OD2   1 
ATOM   19734 N  N     . THR A 1 4218 ? 212.131 256.850 245.730 1.00 39.36  ? 4218 THR A N     1 
ATOM   19735 C  CA    . THR A 1 4218 ? 212.563 256.989 247.118 1.00 32.38  ? 4218 THR A CA    1 
ATOM   19736 C  C     . THR A 1 4218 ? 212.751 258.452 247.499 1.00 42.19  ? 4218 THR A C     1 
ATOM   19737 O  O     . THR A 1 4218 ? 212.317 258.883 248.576 1.00 53.25  ? 4218 THR A O     1 
ATOM   19738 C  CB    . THR A 1 4218 ? 213.858 256.210 247.339 1.00 40.72  ? 4218 THR A CB    1 
ATOM   19739 O  OG1   . THR A 1 4218 ? 213.601 254.807 247.208 1.00 45.98  ? 4218 THR A OG1   1 
ATOM   19740 C  CG2   . THR A 1 4218 ? 214.437 256.502 248.710 1.00 45.38  ? 4218 THR A CG2   1 
ATOM   19741 N  N     . VAL A 1 4219 ? 213.400 259.230 246.628 1.00 45.01  ? 4219 VAL A N     1 
ATOM   19742 C  CA    . VAL A 1 4219 ? 213.601 260.648 246.909 1.00 39.75  ? 4219 VAL A CA    1 
ATOM   19743 C  C     . VAL A 1 4219 ? 212.262 261.354 247.050 1.00 37.24  ? 4219 VAL A C     1 
ATOM   19744 O  O     . VAL A 1 4219 ? 212.049 262.123 247.994 1.00 50.07  ? 4219 VAL A O     1 
ATOM   19745 C  CB    . VAL A 1 4219 ? 214.471 261.295 245.815 1.00 41.07  ? 4219 VAL A CB    1 
ATOM   19746 C  CG1   . VAL A 1 4219 ? 214.472 262.805 245.965 1.00 43.27  ? 4219 VAL A CG1   1 
ATOM   19747 C  CG2   . VAL A 1 4219 ? 215.892 260.762 245.886 1.00 37.66  ? 4219 VAL A CG2   1 
ATOM   19748 N  N     . ASP A 1 4220 ? 211.331 261.084 246.132 1.00 36.35  ? 4220 ASP A N     1 
ATOM   19749 C  CA    . ASP A 1 4220 ? 210.008 261.695 246.214 1.00 38.04  ? 4220 ASP A CA    1 
ATOM   19750 C  C     . ASP A 1 4220 ? 209.318 261.336 247.521 1.00 47.79  ? 4220 ASP A C     1 
ATOM   19751 O  O     . ASP A 1 4220 ? 208.807 262.212 248.226 1.00 58.27  ? 4220 ASP A O     1 
ATOM   19752 C  CB    . ASP A 1 4220 ? 209.150 261.255 245.029 1.00 44.64  ? 4220 ASP A CB    1 
ATOM   19753 C  CG    . ASP A 1 4220 ? 209.573 261.900 243.733 1.00 55.23  ? 4220 ASP A CG    1 
ATOM   19754 O  OD1   . ASP A 1 4220 ? 210.496 262.739 243.758 1.00 59.42  ? 4220 ASP A OD1   1 
ATOM   19755 O  OD2   . ASP A 1 4220 ? 208.985 261.567 242.684 1.00 52.70  ? 4220 ASP A OD2   1 
ATOM   19756 N  N     . THR A 1 4221 ? 209.303 260.046 247.863 1.00 46.14  ? 4221 THR A N     1 
ATOM   19757 C  CA    . THR A 1 4221 ? 208.573 259.595 249.042 1.00 46.93  ? 4221 THR A CA    1 
ATOM   19758 C  C     . THR A 1 4221 ? 209.137 260.216 250.312 1.00 47.85  ? 4221 THR A C     1 
ATOM   19759 O  O     . THR A 1 4221 ? 208.388 260.744 251.143 1.00 54.12  ? 4221 THR A O     1 
ATOM   19760 C  CB    . THR A 1 4221 ? 208.614 258.070 249.130 1.00 49.51  ? 4221 THR A CB    1 
ATOM   19761 O  OG1   . THR A 1 4221 ? 208.052 257.506 247.939 1.00 53.56  ? 4221 THR A OG1   1 
ATOM   19762 C  CG2   . THR A 1 4221 ? 207.826 257.586 250.333 1.00 49.09  ? 4221 THR A CG2   1 
ATOM   19763 N  N     . TRP A 1 4222 ? 210.460 260.187 250.471 1.00 41.28  ? 4222 TRP A N     1 
ATOM   19764 C  CA    . TRP A 1 4222 ? 211.034 260.682 251.715 1.00 43.37  ? 4222 TRP A CA    1 
ATOM   19765 C  C     . TRP A 1 4222 ? 211.025 262.203 251.791 1.00 48.53  ? 4222 TRP A C     1 
ATOM   19766 O  O     . TRP A 1 4222 ? 210.860 262.756 252.884 1.00 59.31  ? 4222 TRP A O     1 
ATOM   19767 C  CB    . TRP A 1 4222 ? 212.445 260.127 251.897 1.00 46.67  ? 4222 TRP A CB    1 
ATOM   19768 C  CG    . TRP A 1 4222 ? 212.421 258.687 252.303 1.00 50.38  ? 4222 TRP A CG    1 
ATOM   19769 C  CD1   . TRP A 1 4222 ? 212.509 257.604 251.482 1.00 45.75  ? 4222 TRP A CD1   1 
ATOM   19770 C  CD2   . TRP A 1 4222 ? 212.258 258.172 253.630 1.00 51.69  ? 4222 TRP A CD2   1 
ATOM   19771 N  NE1   . TRP A 1 4222 ? 212.428 256.447 252.214 1.00 42.35  ? 4222 TRP A NE1   1 
ATOM   19772 C  CE2   . TRP A 1 4222 ? 212.273 256.768 253.537 1.00 49.37  ? 4222 TRP A CE2   1 
ATOM   19773 C  CE3   . TRP A 1 4222 ? 212.108 258.761 254.888 1.00 52.42  ? 4222 TRP A CE3   1 
ATOM   19774 C  CZ2   . TRP A 1 4222 ? 212.146 255.945 254.652 1.00 47.75  ? 4222 TRP A CZ2   1 
ATOM   19775 C  CZ3   . TRP A 1 4222 ? 211.982 257.941 255.993 1.00 49.34  ? 4222 TRP A CZ3   1 
ATOM   19776 C  CH2   . TRP A 1 4222 ? 212.003 256.549 255.868 1.00 44.98  ? 4222 TRP A CH2   1 
ATOM   19777 N  N     . LEU A 1 4223 ? 211.178 262.900 250.660 1.00 55.37  ? 4223 LEU A N     1 
ATOM   19778 C  CA    . LEU A 1 4223 ? 211.034 264.350 250.677 1.00 53.57  ? 4223 LEU A CA    1 
ATOM   19779 C  C     . LEU A 1 4223 ? 209.608 264.757 251.021 1.00 52.83  ? 4223 LEU A C     1 
ATOM   19780 O  O     . LEU A 1 4223 ? 209.397 265.707 251.783 1.00 59.64  ? 4223 LEU A O     1 
ATOM   19781 C  CB    . LEU A 1 4223 ? 211.442 264.934 249.327 1.00 54.25  ? 4223 LEU A CB    1 
ATOM   19782 C  CG    . LEU A 1 4223 ? 212.105 266.308 249.390 1.00 56.93  ? 4223 LEU A CG    1 
ATOM   19783 C  CD1   . LEU A 1 4223 ? 213.199 266.325 250.443 1.00 54.62  ? 4223 LEU A CD1   1 
ATOM   19784 C  CD2   . LEU A 1 4223 ? 212.649 266.694 248.033 1.00 57.50  ? 4223 LEU A CD2   1 
ATOM   19785 N  N     . ASP A 1 4224 ? 208.617 264.057 250.466 1.00 50.09  ? 4224 ASP A N     1 
ATOM   19786 C  CA    . ASP A 1 4224 ? 207.229 264.352 250.799 1.00 53.96  ? 4224 ASP A CA    1 
ATOM   19787 C  C     . ASP A 1 4224 ? 206.950 264.080 252.270 1.00 63.34  ? 4224 ASP A C     1 
ATOM   19788 O  O     . ASP A 1 4224 ? 206.232 264.843 252.925 1.00 66.51  ? 4224 ASP A O     1 
ATOM   19789 C  CB    . ASP A 1 4224 ? 206.295 263.532 249.911 1.00 57.31  ? 4224 ASP A CB    1 
ATOM   19790 C  CG    . ASP A 1 4224 ? 206.334 263.974 248.464 1.00 63.93  ? 4224 ASP A CG    1 
ATOM   19791 O  OD1   . ASP A 1 4224 ? 206.825 265.090 248.197 1.00 65.05  ? 4224 ASP A OD1   1 
ATOM   19792 O  OD2   . ASP A 1 4224 ? 205.882 263.203 247.592 1.00 61.75  ? 4224 ASP A OD2   1 
ATOM   19793 N  N     . ASP A 1 4225 ? 207.504 262.990 252.804 1.00 62.93  ? 4225 ASP A N     1 
ATOM   19794 C  CA    . ASP A 1 4225 ? 207.312 262.684 254.217 1.00 60.94  ? 4225 ASP A CA    1 
ATOM   19795 C  C     . ASP A 1 4225 ? 207.952 263.743 255.109 1.00 60.09  ? 4225 ASP A C     1 
ATOM   19796 O  O     . ASP A 1 4225 ? 207.380 264.128 256.134 1.00 60.33  ? 4225 ASP A O     1 
ATOM   19797 C  CB    . ASP A 1 4225 ? 207.878 261.299 254.532 1.00 63.89  ? 4225 ASP A CB    1 
ATOM   19798 C  CG    . ASP A 1 4225 ? 207.587 260.859 255.952 1.00 72.99  ? 4225 ASP A CG    1 
ATOM   19799 O  OD1   . ASP A 1 4225 ? 206.425 260.501 256.240 1.00 72.25  ? 4225 ASP A OD1   1 
ATOM   19800 O  OD2   . ASP A 1 4225 ? 208.522 260.866 256.780 1.00 73.77  ? 4225 ASP A OD2   1 
ATOM   19801 N  N     . THR A 1 4226 ? 209.145 264.219 254.744 1.00 62.35  ? 4226 THR A N     1 
ATOM   19802 C  CA    . THR A 1 4226 ? 209.837 265.185 255.595 1.00 64.31  ? 4226 THR A CA    1 
ATOM   19803 C  C     . THR A 1 4226 ? 209.272 266.592 255.430 1.00 64.55  ? 4226 THR A C     1 
ATOM   19804 O  O     . THR A 1 4226 ? 209.176 267.344 256.406 1.00 63.90  ? 4226 THR A O     1 
ATOM   19805 C  CB    . THR A 1 4226 ? 211.334 265.171 255.298 1.00 61.76  ? 4226 THR A CB    1 
ATOM   19806 O  OG1   . THR A 1 4226 ? 211.792 263.816 255.238 1.00 71.37  ? 4226 THR A OG1   1 
ATOM   19807 C  CG2   . THR A 1 4226 ? 212.091 265.896 256.391 1.00 61.78  ? 4226 THR A CG2   1 
ATOM   19808 N  N     . ALA A 1 4227 ? 208.897 266.969 254.212 1.00 69.28  ? 4227 ALA A N     1 
ATOM   19809 C  CA    . ALA A 1 4227 ? 208.358 268.296 253.919 1.00 64.91  ? 4227 ALA A CA    1 
ATOM   19810 C  C     . ALA A 1 4227 ? 206.895 268.134 253.522 1.00 70.42  ? 4227 ALA A C     1 
ATOM   19811 O  O     . ALA A 1 4227 ? 206.589 267.737 252.394 1.00 67.48  ? 4227 ALA A O     1 
ATOM   19812 C  CB    . ALA A 1 4227 ? 209.162 268.982 252.820 1.00 60.85  ? 4227 ALA A CB    1 
ATOM   19813 N  N     . LYS A 1 4228 ? 205.991 268.450 254.451 1.00 75.66  ? 4228 LYS A N     1 
ATOM   19814 C  CA    . LYS A 1 4228 ? 204.555 268.267 254.235 1.00 75.73  ? 4228 LYS A CA    1 
ATOM   19815 C  C     . LYS A 1 4228 ? 204.008 269.431 253.406 1.00 77.14  ? 4228 LYS A C     1 
ATOM   19816 O  O     . LYS A 1 4228 ? 203.230 270.268 253.868 1.00 76.03  ? 4228 LYS A O     1 
ATOM   19817 C  CB    . LYS A 1 4228 ? 203.828 268.138 255.567 1.00 74.70  ? 4228 LYS A CB    1 
ATOM   19818 C  CG    . LYS A 1 4228 ? 204.399 267.089 256.525 1.00 74.18  ? 4228 LYS A CG    1 
ATOM   19819 C  CD    . LYS A 1 4228 ? 204.651 265.721 255.885 1.00 78.06  ? 4228 LYS A CD    1 
ATOM   19820 C  CE    . LYS A 1 4228 ? 203.451 265.193 255.101 1.00 77.12  ? 4228 LYS A CE    1 
ATOM   19821 N  NZ    . LYS A 1 4228 ? 203.483 263.709 254.978 1.00 74.48  ? 4228 LYS A NZ    1 
ATOM   19822 N  N     . GLY A 1 4229 ? 204.434 269.468 252.146 1.00 80.19  ? 4229 GLY A N     1 
ATOM   19823 C  CA    . GLY A 1 4229 ? 204.001 270.494 251.225 1.00 79.26  ? 4229 GLY A CA    1 
ATOM   19824 C  C     . GLY A 1 4229 ? 204.690 271.831 251.374 1.00 81.63  ? 4229 GLY A C     1 
ATOM   19825 O  O     . GLY A 1 4229 ? 204.326 272.776 250.663 1.00 84.87  ? 4229 GLY A O     1 
ATOM   19826 N  N     . ARG A 1 4230 ? 205.667 271.947 252.270 1.00 73.19  ? 4230 ARG A N     1 
ATOM   19827 C  CA    . ARG A 1 4230 ? 206.346 273.217 252.476 1.00 71.16  ? 4230 ARG A CA    1 
ATOM   19828 C  C     . ARG A 1 4230 ? 207.115 273.625 251.227 1.00 75.54  ? 4230 ARG A C     1 
ATOM   19829 O  O     . ARG A 1 4230 ? 207.677 272.785 250.520 1.00 78.24  ? 4230 ARG A O     1 
ATOM   19830 C  CB    . ARG A 1 4230 ? 207.295 273.126 253.669 1.00 73.13  ? 4230 ARG A CB    1 
ATOM   19831 C  CG    . ARG A 1 4230 ? 206.596 272.946 255.003 1.00 75.27  ? 4230 ARG A CG    1 
ATOM   19832 C  CD    . ARG A 1 4230 ? 207.425 272.093 255.948 1.00 77.07  ? 4230 ARG A CD    1 
ATOM   19833 N  NE    . ARG A 1 4230 ? 208.751 272.656 256.172 1.00 78.09  ? 4230 ARG A NE    1 
ATOM   19834 C  CZ    . ARG A 1 4230 ? 209.785 271.972 256.641 1.00 79.57  ? 4230 ARG A CZ    1 
ATOM   19835 N  NH1   . ARG A 1 4230 ? 209.685 270.688 256.941 1.00 75.48  ? 4230 ARG A NH1   1 
ATOM   19836 N  NH2   . ARG A 1 4230 ? 210.948 272.593 256.816 1.00 76.04  ? 4230 ARG A NH2   1 
ATOM   19837 N  N     . GLN A 1 4231 ? 207.128 274.931 250.953 1.00 81.15  ? 4231 GLN A N     1 
ATOM   19838 C  CA    . GLN A 1 4231 ? 207.833 275.430 249.778 1.00 78.49  ? 4231 GLN A CA    1 
ATOM   19839 C  C     . GLN A 1 4231 ? 209.339 275.251 249.917 1.00 75.31  ? 4231 GLN A C     1 
ATOM   19840 O  O     . GLN A 1 4231 ? 210.029 274.978 248.929 1.00 78.68  ? 4231 GLN A O     1 
ATOM   19841 C  CB    . GLN A 1 4231 ? 207.486 276.900 249.543 1.00 76.38  ? 4231 GLN A CB    1 
ATOM   19842 C  CG    . GLN A 1 4231 ? 206.030 277.140 249.191 1.00 78.67  ? 4231 GLN A CG    1 
ATOM   19843 C  CD    . GLN A 1 4231 ? 205.626 276.469 247.895 1.00 81.28  ? 4231 GLN A CD    1 
ATOM   19844 O  OE1   . GLN A 1 4231 ? 204.876 275.493 247.896 1.00 80.08  ? 4231 GLN A OE1   1 
ATOM   19845 N  NE2   . GLN A 1 4231 ? 206.125 276.988 246.779 1.00 78.56  ? 4231 GLN A NE2   1 
ATOM   19846 N  N     . ASN A 1 4232 ? 209.865 275.400 251.130 1.00 70.28  ? 4232 ASN A N     1 
ATOM   19847 C  CA    . ASN A 1 4232 ? 211.294 275.293 251.384 1.00 70.18  ? 4232 ASN A CA    1 
ATOM   19848 C  C     . ASN A 1 4232 ? 211.534 274.352 252.554 1.00 73.52  ? 4232 ASN A C     1 
ATOM   19849 O  O     . ASN A 1 4232 ? 210.791 274.380 253.540 1.00 74.19  ? 4232 ASN A O     1 
ATOM   19850 C  CB    . ASN A 1 4232 ? 211.906 276.664 251.684 1.00 68.70  ? 4232 ASN A CB    1 
ATOM   19851 C  CG    . ASN A 1 4232 ? 211.791 277.620 250.517 1.00 73.06  ? 4232 ASN A CG    1 
ATOM   19852 O  OD1   . ASN A 1 4232 ? 211.714 277.203 249.363 1.00 74.32  ? 4232 ASN A OD1   1 
ATOM   19853 N  ND2   . ASN A 1 4232 ? 211.778 278.914 250.813 1.00 73.20  ? 4232 ASN A ND2   1 
ATOM   19854 N  N     . ILE A 1 4233 ? 212.567 273.523 252.440 1.00 70.18  ? 4233 ILE A N     1 
ATOM   19855 C  CA    . ILE A 1 4233 ? 213.025 272.664 253.525 1.00 69.10  ? 4233 ILE A CA    1 
ATOM   19856 C  C     . ILE A 1 4233 ? 214.515 272.908 253.722 1.00 66.21  ? 4233 ILE A C     1 
ATOM   19857 O  O     . ILE A 1 4233 ? 215.256 273.081 252.749 1.00 68.46  ? 4233 ILE A O     1 
ATOM   19858 C  CB    . ILE A 1 4233 ? 212.731 271.177 253.248 1.00 66.75  ? 4233 ILE A CB    1 
ATOM   19859 C  CG1   . ILE A 1 4233 ? 212.991 270.340 254.502 1.00 66.39  ? 4233 ILE A CG1   1 
ATOM   19860 C  CG2   . ILE A 1 4233 ? 213.531 270.659 252.060 1.00 68.76  ? 4233 ILE A CG2   1 
ATOM   19861 C  CD1   . ILE A 1 4233 ? 212.438 268.946 254.426 1.00 70.54  ? 4233 ILE A CD1   1 
ATOM   19862 N  N     . SER A 1 4234 ? 214.943 272.958 254.975 1.00 56.76  ? 4234 SER A N     1 
ATOM   19863 C  CA    . SER A 1 4234 ? 216.351 273.177 255.258 1.00 62.85  ? 4234 SER A CA    1 
ATOM   19864 C  C     . SER A 1 4234 ? 217.172 272.002 254.732 1.00 70.99  ? 4234 SER A C     1 
ATOM   19865 O  O     . SER A 1 4234 ? 216.727 270.850 254.816 1.00 70.16  ? 4234 SER A O     1 
ATOM   19866 C  CB    . SER A 1 4234 ? 216.572 273.350 256.762 1.00 65.50  ? 4234 SER A CB    1 
ATOM   19867 O  OG    . SER A 1 4234 ? 217.953 273.431 257.066 1.00 64.32  ? 4234 SER A OG    1 
ATOM   19868 N  N     . PRO A 1 4235 ? 218.357 272.250 254.169 1.00 67.32  ? 4235 PRO A N     1 
ATOM   19869 C  CA    . PRO A 1 4235 ? 219.201 271.132 253.714 1.00 63.06  ? 4235 PRO A CA    1 
ATOM   19870 C  C     . PRO A 1 4235 ? 219.559 270.156 254.821 1.00 65.50  ? 4235 PRO A C     1 
ATOM   19871 O  O     . PRO A 1 4235 ? 219.774 268.969 254.550 1.00 70.67  ? 4235 PRO A O     1 
ATOM   19872 C  CB    . PRO A 1 4235 ? 220.440 271.844 253.159 1.00 62.78  ? 4235 PRO A CB    1 
ATOM   19873 C  CG    . PRO A 1 4235 ? 219.940 273.177 252.736 1.00 66.11  ? 4235 PRO A CG    1 
ATOM   19874 C  CD    . PRO A 1 4235 ? 218.885 273.554 253.736 1.00 63.39  ? 4235 PRO A CD    1 
ATOM   19875 N  N     . ASP A 1 4236 ? 219.642 270.628 256.065 1.00 62.47  ? 4236 ASP A N     1 
ATOM   19876 C  CA    . ASP A 1 4236 ? 219.893 269.724 257.182 1.00 61.79  ? 4236 ASP A CA    1 
ATOM   19877 C  C     . ASP A 1 4236 ? 218.688 268.830 257.454 1.00 66.12  ? 4236 ASP A C     1 
ATOM   19878 O  O     . ASP A 1 4236 ? 218.846 267.669 257.846 1.00 69.59  ? 4236 ASP A O     1 
ATOM   19879 C  CB    . ASP A 1 4236 ? 220.257 270.525 258.430 1.00 66.46  ? 4236 ASP A CB    1 
ATOM   19880 C  CG    . ASP A 1 4236 ? 221.498 271.368 258.237 1.00 72.02  ? 4236 ASP A CG    1 
ATOM   19881 O  OD1   . ASP A 1 4236 ? 222.610 270.800 258.241 1.00 72.87  ? 4236 ASP A OD1   1 
ATOM   19882 O  OD2   . ASP A 1 4236 ? 221.363 272.599 258.081 1.00 70.94  ? 4236 ASP A OD2   1 
ATOM   19883 N  N     . LYS A 1 4237 ? 217.477 269.355 257.258 1.00 59.57  ? 4237 LYS A N     1 
ATOM   19884 C  CA    . LYS A 1 4237 ? 216.277 268.583 257.559 1.00 58.05  ? 4237 LYS A CA    1 
ATOM   19885 C  C     . LYS A 1 4237 ? 216.000 267.503 256.522 1.00 64.32  ? 4237 LYS A C     1 
ATOM   19886 O  O     . LYS A 1 4237 ? 215.166 266.626 256.770 1.00 69.39  ? 4237 LYS A O     1 
ATOM   19887 C  CB    . LYS A 1 4237 ? 215.069 269.512 257.674 1.00 64.23  ? 4237 LYS A CB    1 
ATOM   19888 C  CG    . LYS A 1 4237 ? 215.208 270.575 258.747 1.00 65.89  ? 4237 LYS A CG    1 
ATOM   19889 C  CD    . LYS A 1 4237 ? 215.273 269.953 260.129 1.00 66.18  ? 4237 LYS A CD    1 
ATOM   19890 C  CE    . LYS A 1 4237 ? 215.265 271.018 261.210 1.00 65.26  ? 4237 LYS A CE    1 
ATOM   19891 N  NZ    . LYS A 1 4237 ? 216.528 271.808 261.216 1.00 65.44  ? 4237 LYS A NZ    1 
ATOM   19892 N  N     . ILE A 1 4238 ? 216.669 267.545 255.374 1.00 56.51  ? 4238 ILE A N     1 
ATOM   19893 C  CA    . ILE A 1 4238 ? 216.470 266.558 254.315 1.00 55.45  ? 4238 ILE A CA    1 
ATOM   19894 C  C     . ILE A 1 4238 ? 216.893 265.188 254.831 1.00 57.98  ? 4238 ILE A C     1 
ATOM   19895 O  O     . ILE A 1 4238 ? 217.969 265.061 255.433 1.00 53.60  ? 4238 ILE A O     1 
ATOM   19896 C  CB    . ILE A 1 4238 ? 217.245 266.946 253.045 1.00 54.87  ? 4238 ILE A CB    1 
ATOM   19897 C  CG1   . ILE A 1 4238 ? 216.713 268.263 252.481 1.00 55.59  ? 4238 ILE A CG1   1 
ATOM   19898 C  CG2   . ILE A 1 4238 ? 217.160 265.848 251.998 1.00 55.45  ? 4238 ILE A CG2   1 
ATOM   19899 C  CD1   . ILE A 1 4238 ? 217.410 268.707 251.220 1.00 57.87  ? 4238 ILE A CD1   1 
ATOM   19900 N  N     . PRO A 1 4239 ? 216.086 264.140 254.630 1.00 53.61  ? 4239 PRO A N     1 
ATOM   19901 C  CA    . PRO A 1 4239 ? 216.454 262.817 255.151 1.00 45.71  ? 4239 PRO A CA    1 
ATOM   19902 C  C     . PRO A 1 4239 ? 217.623 262.202 254.402 1.00 38.17  ? 4239 PRO A C     1 
ATOM   19903 O  O     . PRO A 1 4239 ? 217.437 261.306 253.576 1.00 53.35  ? 4239 PRO A O     1 
ATOM   19904 C  CB    . PRO A 1 4239 ? 215.172 261.998 254.958 1.00 46.48  ? 4239 PRO A CB    1 
ATOM   19905 C  CG    . PRO A 1 4239 ? 214.471 262.665 253.833 1.00 45.68  ? 4239 PRO A CG    1 
ATOM   19906 C  CD    . PRO A 1 4239 ? 214.771 264.128 253.967 1.00 49.67  ? 4239 PRO A CD    1 
ATOM   19907 N  N     . TRP A 1 4240 ? 218.833 262.686 254.682 1.00 40.66  ? 4240 TRP A N     1 
ATOM   19908 C  CA    . TRP A 1 4240 ? 220.016 262.180 253.995 1.00 45.61  ? 4240 TRP A CA    1 
ATOM   19909 C  C     . TRP A 1 4240 ? 220.273 260.718 254.333 1.00 38.29  ? 4240 TRP A C     1 
ATOM   19910 O  O     . TRP A 1 4240 ? 220.614 259.918 253.454 1.00 42.02  ? 4240 TRP A O     1 
ATOM   19911 C  CB    . TRP A 1 4240 ? 221.228 263.032 254.358 1.00 47.11  ? 4240 TRP A CB    1 
ATOM   19912 C  CG    . TRP A 1 4240 ? 221.142 264.428 253.853 1.00 48.34  ? 4240 TRP A CG    1 
ATOM   19913 C  CD1   . TRP A 1 4240 ? 221.052 265.562 254.600 1.00 43.34  ? 4240 TRP A CD1   1 
ATOM   19914 C  CD2   . TRP A 1 4240 ? 221.142 264.846 252.485 1.00 48.31  ? 4240 TRP A CD2   1 
ATOM   19915 N  NE1   . TRP A 1 4240 ? 220.995 266.662 253.783 1.00 51.12  ? 4240 TRP A NE1   1 
ATOM   19916 C  CE2   . TRP A 1 4240 ? 221.050 266.249 252.479 1.00 46.55  ? 4240 TRP A CE2   1 
ATOM   19917 C  CE3   . TRP A 1 4240 ? 221.213 264.170 251.264 1.00 44.53  ? 4240 TRP A CE3   1 
ATOM   19918 C  CZ2   . TRP A 1 4240 ? 221.025 266.988 251.303 1.00 44.94  ? 4240 TRP A CZ2   1 
ATOM   19919 C  CZ3   . TRP A 1 4240 ? 221.187 264.906 250.098 1.00 43.12  ? 4240 TRP A CZ3   1 
ATOM   19920 C  CH2   . TRP A 1 4240 ? 221.097 266.300 250.126 1.00 45.98  ? 4240 TRP A CH2   1 
ATOM   19921 N  N     . SER A 1 4241 ? 220.128 260.355 255.609 1.00 39.56  ? 4241 SER A N     1 
ATOM   19922 C  CA    . SER A 1 4241 ? 220.430 258.994 256.035 1.00 30.61  ? 4241 SER A CA    1 
ATOM   19923 C  C     . SER A 1 4241 ? 219.492 257.993 255.377 1.00 28.76  ? 4241 SER A C     1 
ATOM   19924 O  O     . SER A 1 4241 ? 219.919 256.916 254.948 1.00 39.77  ? 4241 SER A O     1 
ATOM   19925 C  CB    . SER A 1 4241 ? 220.348 258.892 257.557 1.00 41.29  ? 4241 SER A CB    1 
ATOM   19926 O  OG    . SER A 1 4241 ? 219.073 259.296 258.023 1.00 51.40  ? 4241 SER A OG    1 
ATOM   19927 N  N     . ALA A 1 4242 ? 218.206 258.335 255.285 1.00 34.54  ? 4242 ALA A N     1 
ATOM   19928 C  CA    . ALA A 1 4242 ? 217.245 257.444 254.644 1.00 28.40  ? 4242 ALA A CA    1 
ATOM   19929 C  C     . ALA A 1 4242 ? 217.612 257.189 253.191 1.00 29.64  ? 4242 ALA A C     1 
ATOM   19930 O  O     . ALA A 1 4242 ? 217.650 256.038 252.744 1.00 39.04  ? 4242 ALA A O     1 
ATOM   19931 C  CB    . ALA A 1 4242 ? 215.840 258.036 254.740 1.00 28.07  ? 4242 ALA A CB    1 
ATOM   19932 N  N     . LEU A 1 4243 ? 217.902 258.255 252.442 1.00 36.39  ? 4243 LEU A N     1 
ATOM   19933 C  CA    . LEU A 1 4243 ? 218.246 258.102 251.033 1.00 37.82  ? 4243 LEU A CA    1 
ATOM   19934 C  C     . LEU A 1 4243 ? 219.535 257.312 250.858 1.00 40.01  ? 4243 LEU A C     1 
ATOM   19935 O  O     . LEU A 1 4243 ? 219.602 256.407 250.020 1.00 45.15  ? 4243 LEU A O     1 
ATOM   19936 C  CB    . LEU A 1 4243 ? 218.367 259.473 250.371 1.00 39.63  ? 4243 LEU A CB    1 
ATOM   19937 C  CG    . LEU A 1 4243 ? 217.178 260.420 250.536 1.00 41.12  ? 4243 LEU A CG    1 
ATOM   19938 C  CD1   . LEU A 1 4243 ? 217.459 261.752 249.863 1.00 37.61  ? 4243 LEU A CD1   1 
ATOM   19939 C  CD2   . LEU A 1 4243 ? 215.910 259.793 249.984 1.00 40.01  ? 4243 LEU A CD2   1 
ATOM   19940 N  N     . LYS A 1 4244 ? 220.567 257.635 251.641 1.00 38.66  ? 4244 LYS A N     1 
ATOM   19941 C  CA    . LYS A 1 4244 ? 221.837 256.931 251.508 1.00 25.83  ? 4244 LYS A CA    1 
ATOM   19942 C  C     . LYS A 1 4244 ? 221.691 255.454 251.840 1.00 34.32  ? 4244 LYS A C     1 
ATOM   19943 O  O     . LYS A 1 4244 ? 222.177 254.596 251.094 1.00 47.99  ? 4244 LYS A O     1 
ATOM   19944 C  CB    . LYS A 1 4244 ? 222.891 257.574 252.406 1.00 23.96  ? 4244 LYS A CB    1 
ATOM   19945 C  CG    . LYS A 1 4244 ? 223.375 258.918 251.918 1.00 38.36  ? 4244 LYS A CG    1 
ATOM   19946 C  CD    . LYS A 1 4244 ? 224.560 259.397 252.730 1.00 36.83  ? 4244 LYS A CD    1 
ATOM   19947 C  CE    . LYS A 1 4244 ? 224.177 259.631 254.176 1.00 34.61  ? 4244 LYS A CE    1 
ATOM   19948 N  NZ    . LYS A 1 4244 ? 225.238 260.368 254.909 1.00 38.85  ? 4244 LYS A NZ    1 
ATOM   19949 N  N     . THR A 1 4245 ? 221.019 255.135 252.947 1.00 28.54  ? 4245 THR A N     1 
ATOM   19950 C  CA    . THR A 1 4245 ? 220.853 253.740 253.331 1.00 25.76  ? 4245 THR A CA    1 
ATOM   19951 C  C     . THR A 1 4245 ? 220.019 252.979 252.311 1.00 32.73  ? 4245 THR A C     1 
ATOM   19952 O  O     . THR A 1 4245 ? 220.357 251.848 251.951 1.00 45.45  ? 4245 THR A O     1 
ATOM   19953 C  CB    . THR A 1 4245 ? 220.219 253.647 254.716 1.00 33.00  ? 4245 THR A CB    1 
ATOM   19954 O  OG1   . THR A 1 4245 ? 221.015 254.380 255.654 1.00 40.84  ? 4245 THR A OG1   1 
ATOM   19955 C  CG2   . THR A 1 4245 ? 220.128 252.199 255.161 1.00 30.49  ? 4245 THR A CG2   1 
ATOM   19956 N  N     . LEU A 1 4246 ? 218.930 253.576 251.824 1.00 32.00  ? 4246 LEU A N     1 
ATOM   19957 C  CA    . LEU A 1 4246 ? 218.118 252.876 250.839 1.00 29.29  ? 4246 LEU A CA    1 
ATOM   19958 C  C     . LEU A 1 4246 ? 218.888 252.652 249.545 1.00 31.61  ? 4246 LEU A C     1 
ATOM   19959 O  O     . LEU A 1 4246 ? 218.850 251.555 248.984 1.00 45.30  ? 4246 LEU A O     1 
ATOM   19960 C  CB    . LEU A 1 4246 ? 216.820 253.637 250.587 1.00 31.57  ? 4246 LEU A CB    1 
ATOM   19961 C  CG    . LEU A 1 4246 ? 215.801 253.493 251.719 1.00 27.94  ? 4246 LEU A CG    1 
ATOM   19962 C  CD1   . LEU A 1 4246 ? 214.463 254.058 251.314 1.00 32.41  ? 4246 LEU A CD1   1 
ATOM   19963 C  CD2   . LEU A 1 4246 ? 215.660 252.041 252.131 1.00 37.55  ? 4246 LEU A CD2   1 
ATOM   19964 N  N     . MET A 1 4247 ? 219.632 253.655 249.076 1.00 33.14  ? 4247 MET A N     1 
ATOM   19965 C  CA    . MET A 1 4247 ? 220.371 253.485 247.829 1.00 28.69  ? 4247 MET A CA    1 
ATOM   19966 C  C     . MET A 1 4247 ? 221.530 252.511 247.984 1.00 36.41  ? 4247 MET A C     1 
ATOM   19967 O  O     . MET A 1 4247 ? 221.924 251.864 247.008 1.00 40.93  ? 4247 MET A O     1 
ATOM   19968 C  CB    . MET A 1 4247 ? 220.872 254.837 247.330 1.00 28.27  ? 4247 MET A CB    1 
ATOM   19969 C  CG    . MET A 1 4247 ? 219.752 255.762 246.900 1.00 36.20  ? 4247 MET A CG    1 
ATOM   19970 S  SD    . MET A 1 4247 ? 220.319 257.364 246.319 1.00 66.64  ? 4247 MET A SD    1 
ATOM   19971 C  CE    . MET A 1 4247 ? 218.746 258.164 246.018 1.00 47.99  ? 4247 MET A CE    1 
ATOM   19972 N  N     . ALA A 1 4248 ? 222.091 252.387 249.187 1.00 35.86  ? 4248 ALA A N     1 
ATOM   19973 C  CA    . ALA A 1 4248 ? 223.185 251.451 249.400 1.00 27.86  ? 4248 ALA A CA    1 
ATOM   19974 C  C     . ALA A 1 4248 ? 222.721 250.061 249.807 1.00 36.08  ? 4248 ALA A C     1 
ATOM   19975 O  O     . ALA A 1 4248 ? 223.544 249.140 249.833 1.00 42.54  ? 4248 ALA A O     1 
ATOM   19976 C  CB    . ALA A 1 4248 ? 224.139 251.994 250.465 1.00 28.24  ? 4248 ALA A CB    1 
ATOM   19977 N  N     . GLN A 1 4249 ? 221.440 249.878 250.124 1.00 41.85  ? 4249 GLN A N     1 
ATOM   19978 C  CA    . GLN A 1 4249 ? 220.989 248.579 250.605 1.00 27.71  ? 4249 GLN A CA    1 
ATOM   19979 C  C     . GLN A 1 4249 ? 219.970 247.923 249.679 1.00 34.17  ? 4249 GLN A C     1 
ATOM   19980 O  O     . GLN A 1 4249 ? 219.976 246.699 249.525 1.00 47.06  ? 4249 GLN A O     1 
ATOM   19981 C  CB    . GLN A 1 4249 ? 220.394 248.720 252.009 1.00 26.23  ? 4249 GLN A CB    1 
ATOM   19982 C  CG    . GLN A 1 4249 ? 221.382 249.178 253.072 1.00 32.09  ? 4249 GLN A CG    1 
ATOM   19983 C  CD    . GLN A 1 4249 ? 222.472 248.171 253.346 1.00 45.84  ? 4249 GLN A CD    1 
ATOM   19984 O  OE1   . GLN A 1 4249 ? 222.228 246.969 253.368 1.00 55.71  ? 4249 GLN A OE1   1 
ATOM   19985 N  NE2   . GLN A 1 4249 ? 223.691 248.657 253.546 1.00 47.11  ? 4249 GLN A NE2   1 
ATOM   19986 N  N     . SER A 1 4250 ? 219.092 248.710 249.057 1.00 26.30  ? 4250 SER A N     1 
ATOM   19987 C  CA    . SER A 1 4250 ? 217.953 248.178 248.321 1.00 28.35  ? 4250 SER A CA    1 
ATOM   19988 C  C     . SER A 1 4250 ? 217.985 248.522 246.842 1.00 36.47  ? 4250 SER A C     1 
ATOM   19989 O  O     . SER A 1 4250 ? 217.757 247.644 246.003 1.00 41.83  ? 4250 SER A O     1 
ATOM   19990 C  CB    . SER A 1 4250 ? 216.648 248.702 248.940 1.00 32.42  ? 4250 SER A CB    1 
ATOM   19991 O  OG    . SER A 1 4250 ? 216.523 248.301 250.290 1.00 46.41  ? 4250 SER A OG    1 
ATOM   19992 N  N     . ILE A 1 4251 ? 218.254 249.778 246.495 1.00 29.91  ? 4251 ILE A N     1 
ATOM   19993 C  CA    . ILE A 1 4251 ? 218.087 250.246 245.124 1.00 31.29  ? 4251 ILE A CA    1 
ATOM   19994 C  C     . ILE A 1 4251 ? 219.319 249.914 244.295 1.00 36.45  ? 4251 ILE A C     1 
ATOM   19995 O  O     . ILE A 1 4251 ? 219.235 249.167 243.313 1.00 43.44  ? 4251 ILE A O     1 
ATOM   19996 C  CB    . ILE A 1 4251 ? 217.791 251.755 245.093 1.00 28.42  ? 4251 ILE A CB    1 
ATOM   19997 C  CG1   . ILE A 1 4251 ? 216.520 252.060 245.887 1.00 26.45  ? 4251 ILE A CG1   1 
ATOM   19998 C  CG2   . ILE A 1 4251 ? 217.648 252.234 243.666 1.00 28.30  ? 4251 ILE A CG2   1 
ATOM   19999 C  CD1   . ILE A 1 4251 ? 216.483 253.447 246.474 1.00 38.70  ? 4251 ILE A CD1   1 
ATOM   20000 N  N     . TYR A 1 4252 ? 220.469 250.461 244.679 1.00 40.59  ? 4252 TYR A N     1 
ATOM   20001 C  CA    . TYR A 1 4252 ? 221.709 250.232 243.949 1.00 29.62  ? 4252 TYR A CA    1 
ATOM   20002 C  C     . TYR A 1 4252 ? 222.586 249.161 244.575 1.00 35.27  ? 4252 TYR A C     1 
ATOM   20003 O  O     . TYR A 1 4252 ? 223.342 248.500 243.858 1.00 41.44  ? 4252 TYR A O     1 
ATOM   20004 C  CB    . TYR A 1 4252 ? 222.513 251.531 243.843 1.00 24.06  ? 4252 TYR A CB    1 
ATOM   20005 C  CG    . TYR A 1 4252 ? 222.020 252.482 242.781 1.00 26.72  ? 4252 TYR A CG    1 
ATOM   20006 C  CD1   . TYR A 1 4252 ? 222.450 252.369 241.469 1.00 36.29  ? 4252 TYR A CD1   1 
ATOM   20007 C  CD2   . TYR A 1 4252 ? 221.130 253.498 243.091 1.00 30.32  ? 4252 TYR A CD2   1 
ATOM   20008 C  CE1   . TYR A 1 4252 ? 222.005 253.240 240.497 1.00 32.85  ? 4252 TYR A CE1   1 
ATOM   20009 C  CE2   . TYR A 1 4252 ? 220.682 254.372 242.126 1.00 26.07  ? 4252 TYR A CE2   1 
ATOM   20010 C  CZ    . TYR A 1 4252 ? 221.121 254.238 240.831 1.00 30.56  ? 4252 TYR A CZ    1 
ATOM   20011 O  OH    . TYR A 1 4252 ? 220.677 255.107 239.865 1.00 38.97  ? 4252 TYR A OH    1 
ATOM   20012 N  N     . GLY A 1 4253 ? 222.510 248.979 245.891 1.00 38.99  ? 4253 GLY A N     1 
ATOM   20013 C  CA    . GLY A 1 4253 ? 223.307 247.970 246.557 1.00 30.98  ? 4253 GLY A CA    1 
ATOM   20014 C  C     . GLY A 1 4253 ? 222.782 246.560 246.441 1.00 44.05  ? 4253 GLY A C     1 
ATOM   20015 O  O     . GLY A 1 4253 ? 223.481 245.622 246.834 1.00 57.06  ? 4253 GLY A O     1 
ATOM   20016 N  N     . GLY A 1 4254 ? 221.568 246.385 245.919 1.00 38.26  ? 4254 GLY A N     1 
ATOM   20017 C  CA    . GLY A 1 4254 ? 221.050 245.043 245.719 1.00 29.06  ? 4254 GLY A CA    1 
ATOM   20018 C  C     . GLY A 1 4254 ? 221.852 244.257 244.700 1.00 31.83  ? 4254 GLY A C     1 
ATOM   20019 O  O     . GLY A 1 4254 ? 222.142 243.076 244.900 1.00 46.54  ? 4254 GLY A O     1 
ATOM   20020 N  N     . ARG A 1 4255 ? 222.223 244.902 243.594 1.00 31.59  ? 4255 ARG A N     1 
ATOM   20021 C  CA    . ARG A 1 4255 ? 223.014 244.228 242.571 1.00 38.20  ? 4255 ARG A CA    1 
ATOM   20022 C  C     . ARG A 1 4255 ? 224.418 243.904 243.063 1.00 43.33  ? 4255 ARG A C     1 
ATOM   20023 O  O     . ARG A 1 4255 ? 225.022 242.928 242.606 1.00 46.59  ? 4255 ARG A O     1 
ATOM   20024 C  CB    . ARG A 1 4255 ? 223.089 245.092 241.315 1.00 38.52  ? 4255 ARG A CB    1 
ATOM   20025 C  CG    . ARG A 1 4255 ? 221.774 245.728 240.922 1.00 41.10  ? 4255 ARG A CG    1 
ATOM   20026 C  CD    . ARG A 1 4255 ? 221.880 246.397 239.568 1.00 39.19  ? 4255 ARG A CD    1 
ATOM   20027 N  NE    . ARG A 1 4255 ? 220.584 246.839 239.070 1.00 42.75  ? 4255 ARG A NE    1 
ATOM   20028 C  CZ    . ARG A 1 4255 ? 219.680 246.041 238.520 1.00 45.31  ? 4255 ARG A CZ    1 
ATOM   20029 N  NH1   . ARG A 1 4255 ? 219.894 244.743 238.387 1.00 39.31  ? 4255 ARG A NH1   1 
ATOM   20030 N  NH2   . ARG A 1 4255 ? 218.534 246.559 238.088 1.00 43.69  ? 4255 ARG A NH2   1 
ATOM   20031 N  N     . VAL A 1 4256 ? 224.948 244.702 243.986 1.00 36.74  ? 4256 VAL A N     1 
ATOM   20032 C  CA    . VAL A 1 4256 ? 226.329 244.545 244.426 1.00 37.63  ? 4256 VAL A CA    1 
ATOM   20033 C  C     . VAL A 1 4256 ? 226.440 243.300 245.296 1.00 46.79  ? 4256 VAL A C     1 
ATOM   20034 O  O     . VAL A 1 4256 ? 225.742 243.165 246.307 1.00 54.85  ? 4256 VAL A O     1 
ATOM   20035 C  CB    . VAL A 1 4256 ? 226.805 245.792 245.180 1.00 34.90  ? 4256 VAL A CB    1 
ATOM   20036 C  CG1   . VAL A 1 4256 ? 228.140 245.531 245.839 1.00 41.63  ? 4256 VAL A CG1   1 
ATOM   20037 C  CG2   . VAL A 1 4256 ? 226.892 246.975 244.234 1.00 34.26  ? 4256 VAL A CG2   1 
ATOM   20038 N  N     . ASP A 1 4257 ? 227.326 242.382 244.904 1.00 40.99  ? 4257 ASP A N     1 
ATOM   20039 C  CA    . ASP A 1 4257 ? 227.565 241.150 245.647 1.00 42.52  ? 4257 ASP A CA    1 
ATOM   20040 C  C     . ASP A 1 4257 ? 228.995 241.065 246.167 1.00 47.70  ? 4257 ASP A C     1 
ATOM   20041 O  O     . ASP A 1 4257 ? 229.474 239.971 246.479 1.00 52.88  ? 4257 ASP A O     1 
ATOM   20042 C  CB    . ASP A 1 4257 ? 227.244 239.929 244.782 1.00 46.53  ? 4257 ASP A CB    1 
ATOM   20043 C  CG    . ASP A 1 4257 ? 227.884 239.995 243.409 1.00 52.14  ? 4257 ASP A CG    1 
ATOM   20044 O  OD1   . ASP A 1 4257 ? 229.085 240.324 243.317 1.00 49.82  ? 4257 ASP A OD1   1 
ATOM   20045 O  OD2   . ASP A 1 4257 ? 227.183 239.708 242.416 1.00 61.77  ? 4257 ASP A OD2   1 
ATOM   20046 N  N     . ASN A 1 4258 ? 229.685 242.196 246.266 1.00 49.41  ? 4258 ASN A N     1 
ATOM   20047 C  CA    . ASN A 1 4258 ? 231.082 242.231 246.666 1.00 42.23  ? 4258 ASN A CA    1 
ATOM   20048 C  C     . ASN A 1 4258 ? 231.254 243.224 247.805 1.00 45.95  ? 4258 ASN A C     1 
ATOM   20049 O  O     . ASN A 1 4258 ? 230.606 244.273 247.826 1.00 53.50  ? 4258 ASN A O     1 
ATOM   20050 C  CB    . ASN A 1 4258 ? 231.979 242.614 245.483 1.00 39.47  ? 4258 ASN A CB    1 
ATOM   20051 C  CG    . ASN A 1 4258 ? 233.432 242.276 245.720 1.00 50.31  ? 4258 ASN A CG    1 
ATOM   20052 O  OD1   . ASN A 1 4258 ? 233.754 241.231 246.282 1.00 55.80  ? 4258 ASN A OD1   1 
ATOM   20053 N  ND2   . ASN A 1 4258 ? 234.321 243.163 245.294 1.00 54.13  ? 4258 ASN A ND2   1 
ATOM   20054 N  N     . GLU A 1 4259 ? 232.122 242.879 248.757 1.00 47.63  ? 4259 GLU A N     1 
ATOM   20055 C  CA    . GLU A 1 4259 ? 232.373 243.766 249.888 1.00 44.39  ? 4259 GLU A CA    1 
ATOM   20056 C  C     . GLU A 1 4259 ? 233.018 245.071 249.438 1.00 44.36  ? 4259 GLU A C     1 
ATOM   20057 O  O     . GLU A 1 4259 ? 232.661 246.149 249.925 1.00 48.73  ? 4259 GLU A O     1 
ATOM   20058 C  CB    . GLU A 1 4259 ? 233.253 243.057 250.916 1.00 46.09  ? 4259 GLU A CB    1 
ATOM   20059 C  CG    . GLU A 1 4259 ? 233.617 243.901 252.122 1.00 51.20  ? 4259 GLU A CG    1 
ATOM   20060 C  CD    . GLU A 1 4259 ? 233.786 243.071 253.379 1.00 64.15  ? 4259 GLU A CD    1 
ATOM   20061 O  OE1   . GLU A 1 4259 ? 233.877 241.831 253.264 1.00 59.62  ? 4259 GLU A OE1   1 
ATOM   20062 O  OE2   . GLU A 1 4259 ? 233.830 243.657 254.481 1.00 61.16  ? 4259 GLU A OE2   1 
ATOM   20063 N  N     . PHE A 1 4260 ? 233.963 244.995 248.503 1.00 37.35  ? 4260 PHE A N     1 
ATOM   20064 C  CA    . PHE A 1 4260 ? 234.678 246.177 248.041 1.00 35.83  ? 4260 PHE A CA    1 
ATOM   20065 C  C     . PHE A 1 4260 ? 233.850 247.035 247.094 1.00 45.27  ? 4260 PHE A C     1 
ATOM   20066 O  O     . PHE A 1 4260 ? 233.966 248.265 247.131 1.00 50.16  ? 4260 PHE A O     1 
ATOM   20067 C  CB    . PHE A 1 4260 ? 235.988 245.750 247.380 1.00 32.53  ? 4260 PHE A CB    1 
ATOM   20068 C  CG    . PHE A 1 4260 ? 236.797 244.806 248.220 1.00 39.45  ? 4260 PHE A CG    1 
ATOM   20069 C  CD1   . PHE A 1 4260 ? 237.673 245.286 249.176 1.00 41.05  ? 4260 PHE A CD1   1 
ATOM   20070 C  CD2   . PHE A 1 4260 ? 236.667 243.437 248.069 1.00 44.30  ? 4260 PHE A CD2   1 
ATOM   20071 C  CE1   . PHE A 1 4260 ? 238.410 244.422 249.957 1.00 36.52  ? 4260 PHE A CE1   1 
ATOM   20072 C  CE2   . PHE A 1 4260 ? 237.402 242.568 248.847 1.00 46.91  ? 4260 PHE A CE2   1 
ATOM   20073 C  CZ    . PHE A 1 4260 ? 238.275 243.062 249.792 1.00 43.91  ? 4260 PHE A CZ    1 
ATOM   20074 N  N     . ASP A 1 4261 ? 233.009 246.423 246.260 1.00 42.52  ? 4261 ASP A N     1 
ATOM   20075 C  CA    . ASP A 1 4261 ? 232.069 247.206 245.466 1.00 36.02  ? 4261 ASP A CA    1 
ATOM   20076 C  C     . ASP A 1 4261 ? 231.068 247.927 246.359 1.00 37.74  ? 4261 ASP A C     1 
ATOM   20077 O  O     . ASP A 1 4261 ? 230.714 249.082 246.099 1.00 43.07  ? 4261 ASP A O     1 
ATOM   20078 C  CB    . ASP A 1 4261 ? 231.348 246.307 244.468 1.00 38.11  ? 4261 ASP A CB    1 
ATOM   20079 C  CG    . ASP A 1 4261 ? 232.245 245.854 243.342 1.00 48.17  ? 4261 ASP A CG    1 
ATOM   20080 O  OD1   . ASP A 1 4261 ? 233.277 246.511 243.100 1.00 44.52  ? 4261 ASP A OD1   1 
ATOM   20081 O  OD2   . ASP A 1 4261 ? 231.915 244.837 242.701 1.00 52.88  ? 4261 ASP A OD2   1 
ATOM   20082 N  N     . GLN A 1 4262 ? 230.597 247.258 247.413 1.00 31.40  ? 4262 GLN A N     1 
ATOM   20083 C  CA    . GLN A 1 4262 ? 229.727 247.920 248.378 1.00 28.41  ? 4262 GLN A CA    1 
ATOM   20084 C  C     . GLN A 1 4262 ? 230.456 249.055 249.081 1.00 33.95  ? 4262 GLN A C     1 
ATOM   20085 O  O     . GLN A 1 4262 ? 229.869 250.108 249.349 1.00 47.60  ? 4262 GLN A O     1 
ATOM   20086 C  CB    . GLN A 1 4262 ? 229.200 246.910 249.394 1.00 26.43  ? 4262 GLN A CB    1 
ATOM   20087 C  CG    . GLN A 1 4262 ? 228.157 247.474 250.337 1.00 31.86  ? 4262 GLN A CG    1 
ATOM   20088 C  CD    . GLN A 1 4262 ? 226.845 247.763 249.643 1.00 36.09  ? 4262 GLN A CD    1 
ATOM   20089 O  OE1   . GLN A 1 4262 ? 226.261 246.889 249.005 1.00 42.44  ? 4262 GLN A OE1   1 
ATOM   20090 N  NE2   . GLN A 1 4262 ? 226.373 248.996 249.762 1.00 36.07  ? 4262 GLN A NE2   1 
ATOM   20091 N  N     . ARG A 1 4263 ? 231.737 248.855 249.390 1.00 35.67  ? 4263 ARG A N     1 
ATOM   20092 C  CA    . ARG A 1 4263 ? 232.541 249.918 249.985 1.00 33.37  ? 4263 ARG A CA    1 
ATOM   20093 C  C     . ARG A 1 4263 ? 232.624 251.129 249.063 1.00 37.06  ? 4263 ARG A C     1 
ATOM   20094 O  O     . ARG A 1 4263 ? 232.476 252.273 249.507 1.00 43.12  ? 4263 ARG A O     1 
ATOM   20095 C  CB    . ARG A 1 4263 ? 233.935 249.377 250.296 1.00 37.46  ? 4263 ARG A CB    1 
ATOM   20096 C  CG    . ARG A 1 4263 ? 234.843 250.317 251.045 1.00 41.08  ? 4263 ARG A CG    1 
ATOM   20097 C  CD    . ARG A 1 4263 ? 236.149 249.621 251.378 1.00 38.38  ? 4263 ARG A CD    1 
ATOM   20098 N  NE    . ARG A 1 4263 ? 236.886 249.240 250.178 1.00 42.95  ? 4263 ARG A NE    1 
ATOM   20099 C  CZ    . ARG A 1 4263 ? 238.071 248.645 250.183 1.00 44.97  ? 4263 ARG A CZ    1 
ATOM   20100 N  NH1   . ARG A 1 4263 ? 238.683 248.334 251.313 1.00 42.51  ? 4263 ARG A NH1   1 
ATOM   20101 N  NH2   . ARG A 1 4263 ? 238.658 248.358 249.026 1.00 41.42  ? 4263 ARG A NH2   1 
ATOM   20102 N  N     . LEU A 1 4264 ? 232.854 250.890 247.771 1.00 35.94  ? 4264 LEU A N     1 
ATOM   20103 C  CA    . LEU A 1 4264 ? 232.921 251.979 246.801 1.00 32.85  ? 4264 LEU A CA    1 
ATOM   20104 C  C     . LEU A 1 4264 ? 231.580 252.696 246.667 1.00 41.57  ? 4264 LEU A C     1 
ATOM   20105 O  O     . LEU A 1 4264 ? 231.529 253.933 246.604 1.00 50.67  ? 4264 LEU A O     1 
ATOM   20106 C  CB    . LEU A 1 4264 ? 233.375 251.426 245.452 1.00 28.21  ? 4264 LEU A CB    1 
ATOM   20107 C  CG    . LEU A 1 4264 ? 233.370 252.373 244.259 1.00 33.59  ? 4264 LEU A CG    1 
ATOM   20108 C  CD1   . LEU A 1 4264 ? 234.237 253.574 244.550 1.00 39.94  ? 4264 LEU A CD1   1 
ATOM   20109 C  CD2   . LEU A 1 4264 ? 233.851 251.642 243.023 1.00 33.47  ? 4264 LEU A CD2   1 
ATOM   20110 N  N     . LEU A 1 4265 ? 230.485 251.935 246.615 1.00 33.56  ? 4265 LEU A N     1 
ATOM   20111 C  CA    . LEU A 1 4265 ? 229.160 252.538 246.523 1.00 28.12  ? 4265 LEU A CA    1 
ATOM   20112 C  C     . LEU A 1 4265 ? 228.853 253.385 247.752 1.00 33.94  ? 4265 LEU A C     1 
ATOM   20113 O  O     . LEU A 1 4265 ? 228.305 254.489 247.636 1.00 39.41  ? 4265 LEU A O     1 
ATOM   20114 C  CB    . LEU A 1 4265 ? 228.106 251.447 246.344 1.00 25.78  ? 4265 LEU A CB    1 
ATOM   20115 C  CG    . LEU A 1 4265 ? 226.657 251.896 246.173 1.00 30.63  ? 4265 LEU A CG    1 
ATOM   20116 C  CD1   . LEU A 1 4265 ? 226.416 252.388 244.760 1.00 34.07  ? 4265 LEU A CD1   1 
ATOM   20117 C  CD2   . LEU A 1 4265 ? 225.712 250.762 246.512 1.00 34.64  ? 4265 LEU A CD2   1 
ATOM   20118 N  N     . ASN A 1 4266 ? 229.197 252.883 248.940 1.00 34.86  ? 4266 ASN A N     1 
ATOM   20119 C  CA    . ASN A 1 4266 ? 229.001 253.656 250.159 1.00 29.46  ? 4266 ASN A CA    1 
ATOM   20120 C  C     . ASN A 1 4266 ? 229.840 254.924 250.143 1.00 36.92  ? 4266 ASN A C     1 
ATOM   20121 O  O     . ASN A 1 4266 ? 229.375 255.986 250.568 1.00 41.63  ? 4266 ASN A O     1 
ATOM   20122 C  CB    . ASN A 1 4266 ? 229.343 252.809 251.383 1.00 31.28  ? 4266 ASN A CB    1 
ATOM   20123 C  CG    . ASN A 1 4266 ? 228.388 251.656 251.579 1.00 35.43  ? 4266 ASN A CG    1 
ATOM   20124 O  OD1   . ASN A 1 4266 ? 227.370 251.557 250.899 1.00 41.37  ? 4266 ASN A OD1   1 
ATOM   20125 N  ND2   . ASN A 1 4266 ? 228.714 250.774 252.513 1.00 35.69  ? 4266 ASN A ND2   1 
ATOM   20126 N  N     . THR A 1 4267 ? 231.087 254.830 249.675 1.00 33.99  ? 4267 THR A N     1 
ATOM   20127 C  CA    . THR A 1 4267 ? 231.925 256.020 249.569 1.00 31.97  ? 4267 THR A CA    1 
ATOM   20128 C  C     . THR A 1 4267 ? 231.267 257.074 248.691 1.00 36.51  ? 4267 THR A C     1 
ATOM   20129 O  O     . THR A 1 4267 ? 231.155 258.243 249.085 1.00 43.07  ? 4267 THR A O     1 
ATOM   20130 C  CB    . THR A 1 4267 ? 233.299 255.644 249.015 1.00 34.29  ? 4267 THR A CB    1 
ATOM   20131 O  OG1   . THR A 1 4267 ? 234.070 255.006 250.039 1.00 50.47  ? 4267 THR A OG1   1 
ATOM   20132 C  CG2   . THR A 1 4267 ? 234.038 256.878 248.527 1.00 34.99  ? 4267 THR A CG2   1 
ATOM   20133 N  N     . PHE A 1 4268 ? 230.794 256.669 247.511 1.00 35.70  ? 4268 PHE A N     1 
ATOM   20134 C  CA    . PHE A 1 4268 ? 230.143 257.618 246.611 1.00 30.88  ? 4268 PHE A CA    1 
ATOM   20135 C  C     . PHE A 1 4268 ? 228.894 258.223 247.242 1.00 32.45  ? 4268 PHE A C     1 
ATOM   20136 O  O     . PHE A 1 4268 ? 228.669 259.436 247.145 1.00 40.41  ? 4268 PHE A O     1 
ATOM   20137 C  CB    . PHE A 1 4268 ? 229.794 256.937 245.290 1.00 36.80  ? 4268 PHE A CB    1 
ATOM   20138 C  CG    . PHE A 1 4268 ? 230.915 256.936 244.296 1.00 42.44  ? 4268 PHE A CG    1 
ATOM   20139 C  CD1   . PHE A 1 4268 ? 231.624 258.093 244.037 1.00 41.83  ? 4268 PHE A CD1   1 
ATOM   20140 C  CD2   . PHE A 1 4268 ? 231.256 255.782 243.617 1.00 34.51  ? 4268 PHE A CD2   1 
ATOM   20141 C  CE1   . PHE A 1 4268 ? 232.654 258.098 243.122 1.00 37.48  ? 4268 PHE A CE1   1 
ATOM   20142 C  CE2   . PHE A 1 4268 ? 232.283 255.783 242.702 1.00 32.68  ? 4268 PHE A CE2   1 
ATOM   20143 C  CZ    . PHE A 1 4268 ? 232.983 256.941 242.455 1.00 34.63  ? 4268 PHE A CZ    1 
ATOM   20144 N  N     . LEU A 1 4269 ? 228.072 257.398 247.895 1.00 40.43  ? 4269 LEU A N     1 
ATOM   20145 C  CA    . LEU A 1 4269 ? 226.820 257.900 248.455 1.00 27.54  ? 4269 LEU A CA    1 
ATOM   20146 C  C     . LEU A 1 4269 ? 227.062 258.860 249.613 1.00 31.69  ? 4269 LEU A C     1 
ATOM   20147 O  O     . LEU A 1 4269 ? 226.404 259.901 249.705 1.00 38.29  ? 4269 LEU A O     1 
ATOM   20148 C  CB    . LEU A 1 4269 ? 225.937 256.736 248.899 1.00 29.73  ? 4269 LEU A CB    1 
ATOM   20149 C  CG    . LEU A 1 4269 ? 225.047 256.141 247.810 1.00 30.80  ? 4269 LEU A CG    1 
ATOM   20150 C  CD1   . LEU A 1 4269 ? 224.585 254.761 248.207 1.00 35.37  ? 4269 LEU A CD1   1 
ATOM   20151 C  CD2   . LEU A 1 4269 ? 223.863 257.044 247.546 1.00 37.76  ? 4269 LEU A CD2   1 
ATOM   20152 N  N     . GLU A 1 4270 ? 227.994 258.531 250.511 1.00 35.13  ? 4270 GLU A N     1 
ATOM   20153 C  CA    . GLU A 1 4270 ? 228.307 259.447 251.603 1.00 36.13  ? 4270 GLU A CA    1 
ATOM   20154 C  C     . GLU A 1 4270 ? 228.967 260.721 251.096 1.00 39.28  ? 4270 GLU A C     1 
ATOM   20155 O  O     . GLU A 1 4270 ? 228.823 261.777 251.720 1.00 39.65  ? 4270 GLU A O     1 
ATOM   20156 C  CB    . GLU A 1 4270 ? 229.204 258.773 252.641 1.00 34.09  ? 4270 GLU A CB    1 
ATOM   20157 C  CG    . GLU A 1 4270 ? 228.707 257.430 253.141 1.00 44.61  ? 4270 GLU A CG    1 
ATOM   20158 C  CD    . GLU A 1 4270 ? 229.811 256.603 253.772 1.00 54.43  ? 4270 GLU A CD    1 
ATOM   20159 O  OE1   . GLU A 1 4270 ? 230.994 256.853 253.460 1.00 52.12  ? 4270 GLU A OE1   1 
ATOM   20160 O  OE2   . GLU A 1 4270 ? 229.499 255.700 254.576 1.00 48.92  ? 4270 GLU A OE2   1 
ATOM   20161 N  N     . ARG A 1 4271 ? 229.696 260.648 249.980 1.00 42.68  ? 4271 ARG A N     1 
ATOM   20162 C  CA    . ARG A 1 4271 ? 230.313 261.854 249.443 1.00 34.61  ? 4271 ARG A CA    1 
ATOM   20163 C  C     . ARG A 1 4271 ? 229.283 262.770 248.794 1.00 36.30  ? 4271 ARG A C     1 
ATOM   20164 O  O     . ARG A 1 4271 ? 229.349 263.994 248.952 1.00 51.02  ? 4271 ARG A O     1 
ATOM   20165 C  CB    . ARG A 1 4271 ? 231.402 261.481 248.441 1.00 39.82  ? 4271 ARG A CB    1 
ATOM   20166 C  CG    . ARG A 1 4271 ? 232.586 262.426 248.434 1.00 45.06  ? 4271 ARG A CG    1 
ATOM   20167 C  CD    . ARG A 1 4271 ? 233.670 261.931 247.495 1.00 50.36  ? 4271 ARG A CD    1 
ATOM   20168 N  NE    . ARG A 1 4271 ? 233.110 261.327 246.293 1.00 51.76  ? 4271 ARG A NE    1 
ATOM   20169 C  CZ    . ARG A 1 4271 ? 232.626 262.012 245.267 1.00 52.53  ? 4271 ARG A CZ    1 
ATOM   20170 N  NH1   . ARG A 1 4271 ? 232.621 263.335 245.260 1.00 44.52  ? 4271 ARG A NH1   1 
ATOM   20171 N  NH2   . ARG A 1 4271 ? 232.133 261.354 244.222 1.00 47.04  ? 4271 ARG A NH2   1 
ATOM   20172 N  N     . LEU A 1 4272 ? 228.324 262.203 248.063 1.00 35.30  ? 4272 LEU A N     1 
ATOM   20173 C  CA    . LEU A 1 4272 ? 227.417 263.021 247.265 1.00 34.28  ? 4272 LEU A CA    1 
ATOM   20174 C  C     . LEU A 1 4272 ? 226.174 263.462 248.033 1.00 34.71  ? 4272 LEU A C     1 
ATOM   20175 O  O     . LEU A 1 4272 ? 225.767 264.624 247.939 1.00 36.78  ? 4272 LEU A O     1 
ATOM   20176 C  CB    . LEU A 1 4272 ? 227.009 262.261 246.001 1.00 40.10  ? 4272 LEU A CB    1 
ATOM   20177 C  CG    . LEU A 1 4272 ? 228.021 262.302 244.859 1.00 44.55  ? 4272 LEU A CG    1 
ATOM   20178 C  CD1   . LEU A 1 4272 ? 227.574 261.409 243.719 1.00 40.64  ? 4272 LEU A CD1   1 
ATOM   20179 C  CD2   . LEU A 1 4272 ? 228.220 263.728 244.378 1.00 40.64  ? 4272 LEU A CD2   1 
ATOM   20180 N  N     . PHE A 1 4273 ? 225.555 262.557 248.787 1.00 39.38  ? 4273 PHE A N     1 
ATOM   20181 C  CA    . PHE A 1 4273 ? 224.275 262.841 249.437 1.00 37.11  ? 4273 PHE A CA    1 
ATOM   20182 C  C     . PHE A 1 4273 ? 224.537 263.298 250.865 1.00 49.49  ? 4273 PHE A C     1 
ATOM   20183 O  O     . PHE A 1 4273 ? 224.586 262.500 251.801 1.00 52.36  ? 4273 PHE A O     1 
ATOM   20184 C  CB    . PHE A 1 4273 ? 223.368 261.618 249.387 1.00 29.07  ? 4273 PHE A CB    1 
ATOM   20185 C  CG    . PHE A 1 4273 ? 222.813 261.338 248.021 1.00 40.76  ? 4273 PHE A CG    1 
ATOM   20186 C  CD1   . PHE A 1 4273 ? 223.546 260.613 247.097 1.00 43.17  ? 4273 PHE A CD1   1 
ATOM   20187 C  CD2   . PHE A 1 4273 ? 221.564 261.808 247.657 1.00 43.72  ? 4273 PHE A CD2   1 
ATOM   20188 C  CE1   . PHE A 1 4273 ? 223.042 260.360 245.840 1.00 39.10  ? 4273 PHE A CE1   1 
ATOM   20189 C  CE2   . PHE A 1 4273 ? 221.055 261.557 246.401 1.00 40.32  ? 4273 PHE A CE2   1 
ATOM   20190 C  CZ    . PHE A 1 4273 ? 221.794 260.832 245.492 1.00 46.80  ? 4273 PHE A CZ    1 
ATOM   20191 N  N     . THR A 1 4274 ? 224.698 264.608 251.034 1.00 48.04  ? 4274 THR A N     1 
ATOM   20192 C  CA    . THR A 1 4274 ? 224.960 265.196 252.340 1.00 42.16  ? 4274 THR A CA    1 
ATOM   20193 C  C     . THR A 1 4274 ? 224.517 266.651 252.313 1.00 48.86  ? 4274 THR A C     1 
ATOM   20194 O  O     . THR A 1 4274 ? 224.243 267.217 251.254 1.00 52.08  ? 4274 THR A O     1 
ATOM   20195 C  CB    . THR A 1 4274 ? 226.437 265.082 252.722 1.00 51.44  ? 4274 THR A CB    1 
ATOM   20196 O  OG1   . THR A 1 4274 ? 226.627 265.582 254.051 1.00 55.39  ? 4274 THR A OG1   1 
ATOM   20197 C  CG2   . THR A 1 4274 ? 227.299 265.878 251.757 1.00 48.83  ? 4274 THR A CG2   1 
ATOM   20198 N  N     . THR A 1 4275 ? 224.443 267.250 253.506 1.00 60.61  ? 4275 THR A N     1 
ATOM   20199 C  CA    . THR A 1 4275 ? 224.022 268.644 253.610 1.00 54.74  ? 4275 THR A CA    1 
ATOM   20200 C  C     . THR A 1 4275 ? 224.991 269.576 252.898 1.00 58.20  ? 4275 THR A C     1 
ATOM   20201 O  O     . THR A 1 4275 ? 224.583 270.623 252.385 1.00 67.51  ? 4275 THR A O     1 
ATOM   20202 C  CB    . THR A 1 4275 ? 223.895 269.057 255.076 1.00 57.70  ? 4275 THR A CB    1 
ATOM   20203 O  OG1   . THR A 1 4275 ? 225.200 269.193 255.650 1.00 59.90  ? 4275 THR A OG1   1 
ATOM   20204 C  CG2   . THR A 1 4275 ? 223.126 268.013 255.859 1.00 60.35  ? 4275 THR A CG2   1 
ATOM   20205 N  N     . ARG A 1 4276 ? 226.275 269.214 252.856 1.00 52.52  ? 4276 ARG A N     1 
ATOM   20206 C  CA    . ARG A 1 4276 ? 227.274 270.056 252.213 1.00 53.75  ? 4276 ARG A CA    1 
ATOM   20207 C  C     . ARG A 1 4276 ? 227.073 270.154 250.709 1.00 54.77  ? 4276 ARG A C     1 
ATOM   20208 O  O     . ARG A 1 4276 ? 227.667 271.030 250.073 1.00 56.35  ? 4276 ARG A O     1 
ATOM   20209 C  CB    . ARG A 1 4276 ? 228.675 269.526 252.521 1.00 57.10  ? 4276 ARG A CB    1 
ATOM   20210 C  CG    . ARG A 1 4276 ? 229.055 269.539 254.000 1.00 58.74  ? 4276 ARG A CG    1 
ATOM   20211 C  CD    . ARG A 1 4276 ? 229.389 270.939 254.514 1.00 63.68  ? 4276 ARG A CD    1 
ATOM   20212 N  NE    . ARG A 1 4276 ? 228.217 271.787 254.701 1.00 65.62  ? 4276 ARG A NE    1 
ATOM   20213 C  CZ    . ARG A 1 4276 ? 227.387 271.705 255.731 1.00 65.46  ? 4276 ARG A CZ    1 
ATOM   20214 N  NH1   . ARG A 1 4276 ? 227.566 270.816 256.695 1.00 59.77  ? 4276 ARG A NH1   1 
ATOM   20215 N  NH2   . ARG A 1 4276 ? 226.350 272.536 255.796 1.00 61.77  ? 4276 ARG A NH2   1 
ATOM   20216 N  N     . SER A 1 4277 ? 226.253 269.279 250.125 1.00 54.54  ? 4277 SER A N     1 
ATOM   20217 C  CA    . SER A 1 4277 ? 225.981 269.350 248.696 1.00 51.32  ? 4277 SER A CA    1 
ATOM   20218 C  C     . SER A 1 4277 ? 225.169 270.581 248.323 1.00 54.45  ? 4277 SER A C     1 
ATOM   20219 O  O     . SER A 1 4277 ? 225.095 270.923 247.139 1.00 56.09  ? 4277 SER A O     1 
ATOM   20220 C  CB    . SER A 1 4277 ? 225.251 268.090 248.238 1.00 48.82  ? 4277 SER A CB    1 
ATOM   20221 O  OG    . SER A 1 4277 ? 223.877 268.161 248.569 1.00 57.25  ? 4277 SER A OG    1 
ATOM   20222 N  N     . PHE A 1 4278 ? 224.555 271.245 249.298 1.00 54.37  ? 4278 PHE A N     1 
ATOM   20223 C  CA    . PHE A 1 4278 ? 223.796 272.462 249.056 1.00 54.63  ? 4278 PHE A CA    1 
ATOM   20224 C  C     . PHE A 1 4278 ? 224.632 273.722 249.223 1.00 59.89  ? 4278 PHE A C     1 
ATOM   20225 O  O     . PHE A 1 4278 ? 224.130 274.820 248.966 1.00 61.51  ? 4278 PHE A O     1 
ATOM   20226 C  CB    . PHE A 1 4278 ? 222.583 272.516 249.985 1.00 51.99  ? 4278 PHE A CB    1 
ATOM   20227 C  CG    . PHE A 1 4278 ? 221.425 271.704 249.500 1.00 54.38  ? 4278 PHE A CG    1 
ATOM   20228 C  CD1   . PHE A 1 4278 ? 221.438 270.326 249.604 1.00 56.36  ? 4278 PHE A CD1   1 
ATOM   20229 C  CD2   . PHE A 1 4278 ? 220.330 272.315 248.923 1.00 52.63  ? 4278 PHE A CD2   1 
ATOM   20230 C  CE1   . PHE A 1 4278 ? 220.377 269.576 249.149 1.00 57.24  ? 4278 PHE A CE1   1 
ATOM   20231 C  CE2   . PHE A 1 4278 ? 219.271 271.570 248.466 1.00 52.32  ? 4278 PHE A CE2   1 
ATOM   20232 C  CZ    . PHE A 1 4278 ? 219.291 270.200 248.581 1.00 51.74  ? 4278 PHE A CZ    1 
ATOM   20233 N  N     . ASP A 1 4279 ? 225.886 273.590 249.643 1.00 65.47  ? 4279 ASP A N     1 
ATOM   20234 C  CA    . ASP A 1 4279 ? 226.781 274.731 249.707 1.00 62.19  ? 4279 ASP A CA    1 
ATOM   20235 C  C     . ASP A 1 4279 ? 227.164 275.180 248.300 1.00 66.88  ? 4279 ASP A C     1 
ATOM   20236 O  O     . ASP A 1 4279 ? 227.009 274.448 247.319 1.00 65.94  ? 4279 ASP A O     1 
ATOM   20237 C  CB    . ASP A 1 4279 ? 228.037 274.386 250.505 1.00 63.64  ? 4279 ASP A CB    1 
ATOM   20238 C  CG    . ASP A 1 4279 ? 227.730 274.004 251.936 1.00 71.60  ? 4279 ASP A CG    1 
ATOM   20239 O  OD1   . ASP A 1 4279 ? 226.552 274.104 252.341 1.00 70.20  ? 4279 ASP A OD1   1 
ATOM   20240 O  OD2   . ASP A 1 4279 ? 228.668 273.603 252.658 1.00 66.20  ? 4279 ASP A OD2   1 
ATOM   20241 N  N     . SER A 1 4280 ? 227.670 276.408 248.209 1.00 73.19  ? 4280 SER A N     1 
ATOM   20242 C  CA    . SER A 1 4280 ? 228.090 276.951 246.925 1.00 75.22  ? 4280 SER A CA    1 
ATOM   20243 C  C     . SER A 1 4280 ? 229.480 276.488 246.508 1.00 74.00  ? 4280 SER A C     1 
ATOM   20244 O  O     . SER A 1 4280 ? 229.836 276.635 245.335 1.00 69.93  ? 4280 SER A O     1 
ATOM   20245 C  CB    . SER A 1 4280 ? 228.050 278.480 246.966 1.00 74.70  ? 4280 SER A CB    1 
ATOM   20246 O  OG    . SER A 1 4280 ? 226.727 278.947 247.165 1.00 72.22  ? 4280 SER A OG    1 
ATOM   20247 N  N     . GLU A 1 4281 ? 230.265 275.931 247.428 1.00 72.33  ? 4281 GLU A N     1 
ATOM   20248 C  CA    . GLU A 1 4281 ? 231.626 275.498 247.144 1.00 72.66  ? 4281 GLU A CA    1 
ATOM   20249 C  C     . GLU A 1 4281 ? 231.743 273.990 246.961 1.00 73.48  ? 4281 GLU A C     1 
ATOM   20250 O  O     . GLU A 1 4281 ? 232.862 273.471 246.897 1.00 74.88  ? 4281 GLU A O     1 
ATOM   20251 C  CB    . GLU A 1 4281 ? 232.567 275.979 248.254 1.00 75.72  ? 4281 GLU A CB    1 
ATOM   20252 C  CG    . GLU A 1 4281 ? 232.217 275.483 249.656 1.00 77.62  ? 4281 GLU A CG    1 
ATOM   20253 C  CD    . GLU A 1 4281 ? 232.874 274.160 250.011 1.00 81.65  ? 4281 GLU A CD    1 
ATOM   20254 O  OE1   . GLU A 1 4281 ? 233.891 273.806 249.379 1.00 80.15  ? 4281 GLU A OE1   1 
ATOM   20255 O  OE2   . GLU A 1 4281 ? 232.373 273.474 250.927 1.00 79.10  ? 4281 GLU A OE2   1 
ATOM   20256 N  N     . PHE A 1 4282 ? 230.622 273.280 246.860 1.00 59.99  ? 4282 PHE A N     1 
ATOM   20257 C  CA    . PHE A 1 4282 ? 230.661 271.828 246.752 1.00 56.55  ? 4282 PHE A CA    1 
ATOM   20258 C  C     . PHE A 1 4282 ? 231.345 271.395 245.462 1.00 54.64  ? 4282 PHE A C     1 
ATOM   20259 O  O     . PHE A 1 4282 ? 231.121 271.972 244.395 1.00 56.83  ? 4282 PHE A O     1 
ATOM   20260 C  CB    . PHE A 1 4282 ? 229.249 271.250 246.814 1.00 56.60  ? 4282 PHE A CB    1 
ATOM   20261 C  CG    . PHE A 1 4282 ? 229.213 269.772 247.066 1.00 57.40  ? 4282 PHE A CG    1 
ATOM   20262 C  CD1   . PHE A 1 4282 ? 229.844 269.231 248.170 1.00 55.80  ? 4282 PHE A CD1   1 
ATOM   20263 C  CD2   . PHE A 1 4282 ? 228.548 268.924 246.198 1.00 57.90  ? 4282 PHE A CD2   1 
ATOM   20264 C  CE1   . PHE A 1 4282 ? 229.813 267.873 248.403 1.00 52.46  ? 4282 PHE A CE1   1 
ATOM   20265 C  CE2   . PHE A 1 4282 ? 228.512 267.566 246.427 1.00 53.21  ? 4282 PHE A CE2   1 
ATOM   20266 C  CZ    . PHE A 1 4282 ? 229.146 267.040 247.531 1.00 53.53  ? 4282 PHE A CZ    1 
ATOM   20267 N  N     . LYS A 1 4283 ? 232.185 270.370 245.569 1.00 54.77  ? 4283 LYS A N     1 
ATOM   20268 C  CA    . LYS A 1 4283 ? 232.960 269.847 244.451 1.00 51.60  ? 4283 LYS A CA    1 
ATOM   20269 C  C     . LYS A 1 4283 ? 232.389 268.488 244.070 1.00 56.02  ? 4283 LYS A C     1 
ATOM   20270 O  O     . LYS A 1 4283 ? 232.519 267.521 244.829 1.00 58.97  ? 4283 LYS A O     1 
ATOM   20271 C  CB    . LYS A 1 4283 ? 234.434 269.733 244.830 1.00 51.36  ? 4283 LYS A CB    1 
ATOM   20272 C  CG    . LYS A 1 4283 ? 235.113 271.065 245.066 1.00 56.15  ? 4283 LYS A CG    1 
ATOM   20273 C  CD    . LYS A 1 4283 ? 236.571 270.879 245.435 1.00 57.26  ? 4283 LYS A CD    1 
ATOM   20274 C  CE    . LYS A 1 4283 ? 237.242 272.212 245.712 1.00 59.96  ? 4283 LYS A CE    1 
ATOM   20275 N  NZ    . LYS A 1 4283 ? 238.671 272.042 246.088 1.00 59.02  ? 4283 LYS A NZ    1 
ATOM   20276 N  N     . LEU A 1 4284 ? 231.754 268.416 242.899 1.00 50.90  ? 4284 LEU A N     1 
ATOM   20277 C  CA    . LEU A 1 4284 ? 231.233 267.138 242.423 1.00 46.97  ? 4284 LEU A CA    1 
ATOM   20278 C  C     . LEU A 1 4284 ? 232.358 266.142 242.181 1.00 48.68  ? 4284 LEU A C     1 
ATOM   20279 O  O     . LEU A 1 4284 ? 232.231 264.959 242.516 1.00 54.63  ? 4284 LEU A O     1 
ATOM   20280 C  CB    . LEU A 1 4284 ? 230.417 267.345 241.150 1.00 39.57  ? 4284 LEU A CB    1 
ATOM   20281 C  CG    . LEU A 1 4284 ? 229.074 268.044 241.328 1.00 39.03  ? 4284 LEU A CG    1 
ATOM   20282 C  CD1   . LEU A 1 4284 ? 228.364 268.167 239.998 1.00 50.44  ? 4284 LEU A CD1   1 
ATOM   20283 C  CD2   . LEU A 1 4284 ? 228.219 267.286 242.319 1.00 47.52  ? 4284 LEU A CD2   1 
ATOM   20284 N  N     . ALA A 1 4285 ? 233.463 266.599 241.601 1.00 51.38  ? 4285 ALA A N     1 
ATOM   20285 C  CA    . ALA A 1 4285 ? 234.622 265.746 241.367 1.00 52.54  ? 4285 ALA A CA    1 
ATOM   20286 C  C     . ALA A 1 4285 ? 235.869 266.607 241.451 1.00 57.84  ? 4285 ALA A C     1 
ATOM   20287 O  O     . ALA A 1 4285 ? 236.032 267.539 240.660 1.00 63.97  ? 4285 ALA A O     1 
ATOM   20288 C  CB    . ALA A 1 4285 ? 234.535 265.051 240.008 1.00 53.43  ? 4285 ALA A CB    1 
ATOM   20289 N  N     . CYS A 1 4286 ? 236.738 266.302 242.408 1.00 76.56  ? 4286 CYS A N     1 
ATOM   20290 C  CA    . CYS A 1 4286 ? 237.959 267.067 242.589 1.00 75.45  ? 4286 CYS A CA    1 
ATOM   20291 C  C     . CYS A 1 4286 ? 239.046 266.576 241.642 1.00 77.86  ? 4286 CYS A C     1 
ATOM   20292 O  O     . CYS A 1 4286 ? 239.049 265.417 241.217 1.00 78.37  ? 4286 CYS A O     1 
ATOM   20293 C  CB    . CYS A 1 4286 ? 238.446 266.968 244.034 1.00 76.37  ? 4286 CYS A CB    1 
ATOM   20294 S  SG    . CYS A 1 4286 ? 237.181 267.312 245.276 1.00 87.93  ? 4286 CYS A SG    1 
ATOM   20295 N  N     . LYS A 1 4287 ? 239.972 267.481 241.320 1.00 83.19  ? 4287 LYS A N     1 
ATOM   20296 C  CA    . LYS A 1 4287 ? 241.163 267.208 240.505 1.00 84.63  ? 4287 LYS A CA    1 
ATOM   20297 C  C     . LYS A 1 4287 ? 240.843 266.333 239.291 1.00 82.60  ? 4287 LYS A C     1 
ATOM   20298 O  O     . LYS A 1 4287 ? 241.422 265.265 239.081 1.00 80.94  ? 4287 LYS A O     1 
ATOM   20299 C  CB    . LYS A 1 4287 ? 242.289 266.603 241.358 1.00 86.07  ? 4287 LYS A CB    1 
ATOM   20300 C  CG    . LYS A 1 4287 ? 241.987 265.278 242.059 1.00 83.40  ? 4287 LYS A CG    1 
ATOM   20301 C  CD    . LYS A 1 4287 ? 243.005 264.972 243.144 1.00 83.12  ? 4287 LYS A CD    1 
ATOM   20302 C  CE    . LYS A 1 4287 ? 242.980 266.026 244.238 1.00 82.67  ? 4287 LYS A CE    1 
ATOM   20303 N  NZ    . LYS A 1 4287 ? 243.947 265.714 245.327 1.00 81.37  ? 4287 LYS A NZ    1 
ATOM   20304 N  N     . VAL A 1 4288 ? 239.908 266.814 238.468 1.00 69.84  ? 4288 VAL A N     1 
ATOM   20305 C  CA    . VAL A 1 4288 ? 239.526 266.068 237.270 1.00 66.45  ? 4288 VAL A CA    1 
ATOM   20306 C  C     . VAL A 1 4288 ? 240.645 266.100 236.235 1.00 71.25  ? 4288 VAL A C     1 
ATOM   20307 O  O     . VAL A 1 4288 ? 240.806 265.162 235.445 1.00 74.48  ? 4288 VAL A O     1 
ATOM   20308 C  CB    . VAL A 1 4288 ? 238.200 266.601 236.699 1.00 60.81  ? 4288 VAL A CB    1 
ATOM   20309 C  CG1   . VAL A 1 4288 ? 237.063 266.290 237.651 1.00 66.72  ? 4288 VAL A CG1   1 
ATOM   20310 C  CG2   . VAL A 1 4288 ? 238.284 268.087 236.439 1.00 66.17  ? 4288 VAL A CG2   1 
ATOM   20311 N  N     . ASP A 1 4289 ? 241.425 267.177 236.208 1.00 83.84  ? 4289 ASP A N     1 
ATOM   20312 C  CA    . ASP A 1 4289 ? 242.599 267.244 235.343 1.00 82.41  ? 4289 ASP A CA    1 
ATOM   20313 C  C     . ASP A 1 4289 ? 243.585 268.224 235.958 1.00 88.62  ? 4289 ASP A C     1 
ATOM   20314 O  O     . ASP A 1 4289 ? 243.328 269.430 235.993 1.00 90.55  ? 4289 ASP A O     1 
ATOM   20315 C  CB    . ASP A 1 4289 ? 242.226 267.651 233.911 1.00 84.00  ? 4289 ASP A CB    1 
ATOM   20316 C  CG    . ASP A 1 4289 ? 241.550 269.008 233.837 1.00 88.24  ? 4289 ASP A CG    1 
ATOM   20317 O  OD1   . ASP A 1 4289 ? 240.460 269.166 234.422 1.00 88.18  ? 4289 ASP A OD1   1 
ATOM   20318 O  OD2   . ASP A 1 4289 ? 242.113 269.920 233.196 1.00 87.11  ? 4289 ASP A OD2   1 
ATOM   20319 N  N     . GLY A 1 4290 ? 244.707 267.705 236.448 1.00 95.60  ? 4290 GLY A N     1 
ATOM   20320 C  CA    . GLY A 1 4290 ? 245.644 268.537 237.174 1.00 93.65  ? 4290 GLY A CA    1 
ATOM   20321 C  C     . GLY A 1 4290 ? 245.015 269.118 238.423 1.00 94.80  ? 4290 GLY A C     1 
ATOM   20322 O  O     . GLY A 1 4290 ? 244.777 268.401 239.400 1.00 92.09  ? 4290 GLY A O     1 
ATOM   20323 N  N     . HIS A 1 4291 ? 244.737 270.423 238.401 1.00 98.60  ? 4291 HIS A N     1 
ATOM   20324 C  CA    . HIS A 1 4291 ? 244.098 271.099 239.519 1.00 100.42 ? 4291 HIS A CA    1 
ATOM   20325 C  C     . HIS A 1 4291 ? 242.616 271.369 239.306 1.00 101.05 ? 4291 HIS A C     1 
ATOM   20326 O  O     . HIS A 1 4291 ? 241.896 271.561 240.291 1.00 100.97 ? 4291 HIS A O     1 
ATOM   20327 C  CB    . HIS A 1 4291 ? 244.794 272.436 239.802 1.00 100.54 ? 4291 HIS A CB    1 
ATOM   20328 C  CG    . HIS A 1 4291 ? 244.370 273.538 238.882 1.00 103.97 ? 4291 HIS A CG    1 
ATOM   20329 N  ND1   . HIS A 1 4291 ? 244.443 273.431 237.510 1.00 101.85 ? 4291 HIS A ND1   1 
ATOM   20330 C  CD2   . HIS A 1 4291 ? 243.858 274.765 239.137 1.00 102.07 ? 4291 HIS A CD2   1 
ATOM   20331 C  CE1   . HIS A 1 4291 ? 243.999 274.547 236.959 1.00 101.61 ? 4291 HIS A CE1   1 
ATOM   20332 N  NE2   . HIS A 1 4291 ? 243.638 275.373 237.925 1.00 101.76 ? 4291 HIS A NE2   1 
ATOM   20333 N  N     . LYS A 1 4292 ? 242.150 271.389 238.059 1.00 89.70  ? 4292 LYS A N     1 
ATOM   20334 C  CA    . LYS A 1 4292 ? 240.764 271.735 237.771 1.00 88.04  ? 4292 LYS A CA    1 
ATOM   20335 C  C     . LYS A 1 4292 ? 239.824 270.695 238.368 1.00 89.71  ? 4292 LYS A C     1 
ATOM   20336 O  O     . LYS A 1 4292 ? 240.187 269.527 238.526 1.00 88.50  ? 4292 LYS A O     1 
ATOM   20337 C  CB    . LYS A 1 4292 ? 240.562 271.844 236.257 1.00 86.03  ? 4292 LYS A CB    1 
ATOM   20338 C  CG    . LYS A 1 4292 ? 239.157 272.231 235.821 1.00 90.65  ? 4292 LYS A CG    1 
ATOM   20339 C  CD    . LYS A 1 4292 ? 238.843 273.671 236.195 1.00 90.73  ? 4292 LYS A CD    1 
ATOM   20340 C  CE    . LYS A 1 4292 ? 237.483 274.094 235.667 1.00 89.85  ? 4292 LYS A CE    1 
ATOM   20341 N  NZ    . LYS A 1 4292 ? 237.136 275.480 236.083 1.00 89.30  ? 4292 LYS A NZ    1 
ATOM   20342 N  N     . ASP A 1 4293 ? 238.614 271.131 238.715 1.00 73.26  ? 4293 ASP A N     1 
ATOM   20343 C  CA    . ASP A 1 4293 ? 237.640 270.278 239.379 1.00 68.72  ? 4293 ASP A CA    1 
ATOM   20344 C  C     . ASP A 1 4293 ? 236.227 270.688 238.994 1.00 69.43  ? 4293 ASP A C     1 
ATOM   20345 O  O     . ASP A 1 4293 ? 235.991 271.829 238.587 1.00 72.83  ? 4293 ASP A O     1 
ATOM   20346 C  CB    . ASP A 1 4293 ? 237.814 270.333 240.900 1.00 67.79  ? 4293 ASP A CB    1 
ATOM   20347 C  CG    . ASP A 1 4293 ? 237.755 271.745 241.442 1.00 71.67  ? 4293 ASP A CG    1 
ATOM   20348 O  OD1   . ASP A 1 4293 ? 237.644 272.695 240.642 1.00 74.70  ? 4293 ASP A OD1   1 
ATOM   20349 O  OD2   . ASP A 1 4293 ? 237.830 271.907 242.674 1.00 72.82  ? 4293 ASP A OD2   1 
ATOM   20350 N  N     . ILE A 1 4294 ? 235.294 269.742 239.112 1.00 60.13  ? 4294 ILE A N     1 
ATOM   20351 C  CA    . ILE A 1 4294 ? 233.898 270.009 238.794 1.00 50.71  ? 4294 ILE A CA    1 
ATOM   20352 C  C     . ILE A 1 4294 ? 233.227 270.691 239.977 1.00 52.27  ? 4294 ILE A C     1 
ATOM   20353 O  O     . ILE A 1 4294 ? 233.371 270.261 241.129 1.00 57.58  ? 4294 ILE A O     1 
ATOM   20354 C  CB    . ILE A 1 4294 ? 233.172 268.705 238.424 1.00 50.44  ? 4294 ILE A CB    1 
ATOM   20355 C  CG1   . ILE A 1 4294 ? 233.865 268.011 237.251 1.00 43.94  ? 4294 ILE A CG1   1 
ATOM   20356 C  CG2   . ILE A 1 4294 ? 231.723 268.985 238.081 1.00 56.81  ? 4294 ILE A CG2   1 
ATOM   20357 C  CD1   . ILE A 1 4294 ? 233.890 268.826 235.987 1.00 54.01  ? 4294 ILE A CD1   1 
ATOM   20358 N  N     . GLN A 1 4295 ? 232.487 271.759 239.700 1.00 56.65  ? 4295 GLN A N     1 
ATOM   20359 C  CA    . GLN A 1 4295 ? 231.777 272.513 240.722 1.00 55.03  ? 4295 GLN A CA    1 
ATOM   20360 C  C     . GLN A 1 4295 ? 230.290 272.186 240.695 1.00 53.51  ? 4295 GLN A C     1 
ATOM   20361 O  O     . GLN A 1 4295 ? 229.693 272.010 239.630 1.00 56.24  ? 4295 GLN A O     1 
ATOM   20362 C  CB    . GLN A 1 4295 ? 231.971 274.020 240.535 1.00 59.68  ? 4295 GLN A CB    1 
ATOM   20363 C  CG    . GLN A 1 4295 ? 233.407 274.495 240.667 1.00 60.20  ? 4295 GLN A CG    1 
ATOM   20364 C  CD    . GLN A 1 4295 ? 233.995 274.191 242.030 1.00 62.90  ? 4295 GLN A CD    1 
ATOM   20365 O  OE1   . GLN A 1 4295 ? 234.955 273.432 242.150 1.00 66.38  ? 4295 GLN A OE1   1 
ATOM   20366 N  NE2   . GLN A 1 4295 ? 233.417 274.783 243.067 1.00 59.03  ? 4295 GLN A NE2   1 
ATOM   20367 N  N     . MET A 1 4296 ? 229.706 272.104 241.879 1.00 54.42  ? 4296 MET A N     1 
ATOM   20368 C  CA    . MET A 1 4296 ? 228.269 271.902 241.998 1.00 50.64  ? 4296 MET A CA    1 
ATOM   20369 C  C     . MET A 1 4296 ? 227.531 273.155 241.539 1.00 51.80  ? 4296 MET A C     1 
ATOM   20370 O  O     . MET A 1 4296 ? 227.916 274.267 241.919 1.00 57.98  ? 4296 MET A O     1 
ATOM   20371 C  CB    . MET A 1 4296 ? 227.909 271.571 243.444 1.00 52.54  ? 4296 MET A CB    1 
ATOM   20372 C  CG    . MET A 1 4296 ? 226.425 271.422 243.726 1.00 53.09  ? 4296 MET A CG    1 
ATOM   20373 S  SD    . MET A 1 4296 ? 225.711 269.914 243.053 1.00 64.42  ? 4296 MET A SD    1 
ATOM   20374 C  CE    . MET A 1 4296 ? 223.974 270.337 243.092 1.00 54.29  ? 4296 MET A CE    1 
ATOM   20375 N  N     . PRO A 1 4297 ? 226.491 273.025 240.720 1.00 52.72  ? 4297 PRO A N     1 
ATOM   20376 C  CA    . PRO A 1 4297 ? 225.709 274.202 240.321 1.00 51.39  ? 4297 PRO A CA    1 
ATOM   20377 C  C     . PRO A 1 4297 ? 225.095 274.895 241.527 1.00 55.56  ? 4297 PRO A C     1 
ATOM   20378 O  O     . PRO A 1 4297 ? 224.672 274.251 242.488 1.00 63.75  ? 4297 PRO A O     1 
ATOM   20379 C  CB    . PRO A 1 4297 ? 224.632 273.617 239.402 1.00 49.31  ? 4297 PRO A CB    1 
ATOM   20380 C  CG    . PRO A 1 4297 ? 225.167 272.314 238.954 1.00 53.81  ? 4297 PRO A CG    1 
ATOM   20381 C  CD    . PRO A 1 4297 ? 226.042 271.799 240.045 1.00 55.49  ? 4297 PRO A CD    1 
ATOM   20382 N  N     . ASP A 1 4298 ? 225.046 276.222 241.470 1.00 60.11  ? 4298 ASP A N     1 
ATOM   20383 C  CA    . ASP A 1 4298 ? 224.517 277.026 242.562 1.00 64.87  ? 4298 ASP A CA    1 
ATOM   20384 C  C     . ASP A 1 4298 ? 223.050 277.388 242.315 1.00 63.80  ? 4298 ASP A C     1 
ATOM   20385 O  O     . ASP A 1 4298 ? 222.456 278.141 243.090 1.00 58.74  ? 4298 ASP A O     1 
ATOM   20386 C  CB    . ASP A 1 4298 ? 225.388 278.282 242.732 1.00 65.44  ? 4298 ASP A CB    1 
ATOM   20387 C  CG    . ASP A 1 4298 ? 225.074 279.084 243.997 1.00 70.55  ? 4298 ASP A CG    1 
ATOM   20388 O  OD1   . ASP A 1 4298 ? 224.167 278.717 244.770 1.00 69.04  ? 4298 ASP A OD1   1 
ATOM   20389 O  OD2   . ASP A 1 4298 ? 225.759 280.106 244.220 1.00 65.82  ? 4298 ASP A OD2   1 
ATOM   20390 N  N     . GLY A 1 4299 ? 222.453 276.864 241.251 1.00 60.70  ? 4299 GLY A N     1 
ATOM   20391 C  CA    . GLY A 1 4299 ? 221.061 277.138 240.967 1.00 59.43  ? 4299 GLY A CA    1 
ATOM   20392 C  C     . GLY A 1 4299 ? 220.124 276.351 241.863 1.00 63.64  ? 4299 GLY A C     1 
ATOM   20393 O  O     . GLY A 1 4299 ? 220.524 275.478 242.634 1.00 66.39  ? 4299 GLY A O     1 
ATOM   20394 N  N     . ILE A 1 4300 ? 218.836 276.676 241.754 1.00 65.43  ? 4300 ILE A N     1 
ATOM   20395 C  CA    . ILE A 1 4300 ? 217.794 276.030 242.542 1.00 68.56  ? 4300 ILE A CA    1 
ATOM   20396 C  C     . ILE A 1 4300 ? 216.640 275.529 241.691 1.00 67.80  ? 4300 ILE A C     1 
ATOM   20397 O  O     . ILE A 1 4300 ? 215.666 275.006 242.240 1.00 72.55  ? 4300 ILE A O     1 
ATOM   20398 C  CB    . ILE A 1 4300 ? 217.263 276.963 243.649 1.00 67.50  ? 4300 ILE A CB    1 
ATOM   20399 C  CG1   . ILE A 1 4300 ? 216.627 278.209 243.032 1.00 68.44  ? 4300 ILE A CG1   1 
ATOM   20400 C  CG2   . ILE A 1 4300 ? 218.375 277.345 244.610 1.00 63.56  ? 4300 ILE A CG2   1 
ATOM   20401 C  CD1   . ILE A 1 4300 ? 215.878 279.065 244.024 1.00 69.44  ? 4300 ILE A CD1   1 
ATOM   20402 N  N     . ARG A 1 4301 ? 216.713 275.671 240.372 1.00 59.59  ? 4301 ARG A N     1 
ATOM   20403 C  CA    . ARG A 1 4301 ? 215.642 275.267 239.476 1.00 62.34  ? 4301 ARG A CA    1 
ATOM   20404 C  C     . ARG A 1 4301 ? 216.161 274.234 238.489 1.00 65.67  ? 4301 ARG A C     1 
ATOM   20405 O  O     . ARG A 1 4301 ? 217.358 274.179 238.200 1.00 67.60  ? 4301 ARG A O     1 
ATOM   20406 C  CB    . ARG A 1 4301 ? 215.070 276.466 238.713 1.00 63.28  ? 4301 ARG A CB    1 
ATOM   20407 C  CG    . ARG A 1 4301 ? 214.300 277.450 239.574 1.00 64.09  ? 4301 ARG A CG    1 
ATOM   20408 C  CD    . ARG A 1 4301 ? 214.020 278.739 238.819 1.00 65.17  ? 4301 ARG A CD    1 
ATOM   20409 N  NE    . ARG A 1 4301 ? 213.925 278.527 237.379 1.00 67.55  ? 4301 ARG A NE    1 
ATOM   20410 C  CZ    . ARG A 1 4301 ? 214.722 279.093 236.483 1.00 68.96  ? 4301 ARG A CZ    1 
ATOM   20411 N  NH1   . ARG A 1 4301 ? 215.700 279.908 236.844 1.00 66.14  ? 4301 ARG A NH1   1 
ATOM   20412 N  NH2   . ARG A 1 4301 ? 214.535 278.834 235.192 1.00 63.78  ? 4301 ARG A NH2   1 
ATOM   20413 N  N     . ARG A 1 4302 ? 215.242 273.415 237.972 1.00 59.20  ? 4302 ARG A N     1 
ATOM   20414 C  CA    . ARG A 1 4302 ? 215.624 272.376 237.020 1.00 54.55  ? 4302 ARG A CA    1 
ATOM   20415 C  C     . ARG A 1 4302 ? 216.315 272.968 235.799 1.00 63.87  ? 4302 ARG A C     1 
ATOM   20416 O  O     . ARG A 1 4302 ? 217.255 272.373 235.259 1.00 67.87  ? 4302 ARG A O     1 
ATOM   20417 C  CB    . ARG A 1 4302 ? 214.396 271.573 236.596 1.00 51.52  ? 4302 ARG A CB    1 
ATOM   20418 C  CG    . ARG A 1 4302 ? 214.683 270.579 235.486 1.00 57.72  ? 4302 ARG A CG    1 
ATOM   20419 C  CD    . ARG A 1 4302 ? 213.422 269.902 234.984 1.00 65.98  ? 4302 ARG A CD    1 
ATOM   20420 N  NE    . ARG A 1 4302 ? 213.700 268.996 233.876 1.00 65.57  ? 4302 ARG A NE    1 
ATOM   20421 C  CZ    . ARG A 1 4302 ? 214.074 269.381 232.663 1.00 61.72  ? 4302 ARG A CZ    1 
ATOM   20422 N  NH1   . ARG A 1 4302 ? 214.196 270.661 232.349 1.00 56.75  ? 4302 ARG A NH1   1 
ATOM   20423 N  NH2   . ARG A 1 4302 ? 214.321 268.460 231.737 1.00 60.43  ? 4302 ARG A NH2   1 
ATOM   20424 N  N     . GLU A 1 4303 ? 215.861 274.139 235.347 1.00 65.91  ? 4303 GLU A N     1 
ATOM   20425 C  CA    . GLU A 1 4303 ? 216.451 274.756 234.164 1.00 58.90  ? 4303 GLU A CA    1 
ATOM   20426 C  C     . GLU A 1 4303 ? 217.921 275.084 234.387 1.00 58.03  ? 4303 GLU A C     1 
ATOM   20427 O  O     . GLU A 1 4303 ? 218.750 274.880 233.495 1.00 62.64  ? 4303 GLU A O     1 
ATOM   20428 C  CB    . GLU A 1 4303 ? 215.672 276.014 233.780 1.00 60.40  ? 4303 GLU A CB    1 
ATOM   20429 C  CG    . GLU A 1 4303 ? 214.200 275.782 233.455 1.00 64.11  ? 4303 GLU A CG    1 
ATOM   20430 C  CD    . GLU A 1 4303 ? 213.334 275.609 234.689 1.00 70.68  ? 4303 GLU A CD    1 
ATOM   20431 O  OE1   . GLU A 1 4303 ? 213.271 276.546 235.511 1.00 70.12  ? 4303 GLU A OE1   1 
ATOM   20432 O  OE2   . GLU A 1 4303 ? 212.713 274.535 234.835 1.00 65.55  ? 4303 GLU A OE2   1 
ATOM   20433 N  N     . GLU A 1 4304 ? 218.263 275.588 235.575 1.00 54.84  ? 4304 GLU A N     1 
ATOM   20434 C  CA    . GLU A 1 4304 ? 219.655 275.911 235.870 1.00 56.06  ? 4304 GLU A CA    1 
ATOM   20435 C  C     . GLU A 1 4304 ? 220.532 274.665 235.831 1.00 63.82  ? 4304 GLU A C     1 
ATOM   20436 O  O     . GLU A 1 4304 ? 221.631 274.686 235.265 1.00 62.94  ? 4304 GLU A O     1 
ATOM   20437 C  CB    . GLU A 1 4304 ? 219.751 276.595 237.232 1.00 54.37  ? 4304 GLU A CB    1 
ATOM   20438 C  CG    . GLU A 1 4304 ? 218.749 277.720 237.425 1.00 63.49  ? 4304 GLU A CG    1 
ATOM   20439 C  CD    . GLU A 1 4304 ? 219.229 278.769 238.407 1.00 68.32  ? 4304 GLU A CD    1 
ATOM   20440 O  OE1   . GLU A 1 4304 ? 220.413 279.158 238.335 1.00 65.66  ? 4304 GLU A OE1   1 
ATOM   20441 O  OE2   . GLU A 1 4304 ? 218.419 279.207 239.251 1.00 68.92  ? 4304 GLU A OE2   1 
ATOM   20442 N  N     . PHE A 1 4305 ? 220.058 273.565 236.420 1.00 59.83  ? 4305 PHE A N     1 
ATOM   20443 C  CA    . PHE A 1 4305 ? 220.831 272.327 236.413 1.00 49.52  ? 4305 PHE A CA    1 
ATOM   20444 C  C     . PHE A 1 4305 ? 220.978 271.768 235.003 1.00 53.63  ? 4305 PHE A C     1 
ATOM   20445 O  O     . PHE A 1 4305 ? 222.056 271.290 234.628 1.00 61.80  ? 4305 PHE A O     1 
ATOM   20446 C  CB    . PHE A 1 4305 ? 220.177 271.302 237.335 1.00 48.94  ? 4305 PHE A CB    1 
ATOM   20447 C  CG    . PHE A 1 4305 ? 220.132 271.726 238.773 1.00 48.09  ? 4305 PHE A CG    1 
ATOM   20448 C  CD1   . PHE A 1 4305 ? 221.300 271.973 239.470 1.00 46.91  ? 4305 PHE A CD1   1 
ATOM   20449 C  CD2   . PHE A 1 4305 ? 218.925 271.875 239.428 1.00 48.92  ? 4305 PHE A CD2   1 
ATOM   20450 C  CE1   . PHE A 1 4305 ? 221.264 272.361 240.790 1.00 48.07  ? 4305 PHE A CE1   1 
ATOM   20451 C  CE2   . PHE A 1 4305 ? 218.884 272.265 240.747 1.00 48.86  ? 4305 PHE A CE2   1 
ATOM   20452 C  CZ    . PHE A 1 4305 ? 220.054 272.508 241.428 1.00 52.62  ? 4305 PHE A CZ    1 
ATOM   20453 N  N     . VAL A 1 4306 ? 219.909 271.816 234.208 1.00 44.60  ? 4306 VAL A N     1 
ATOM   20454 C  CA    . VAL A 1 4306 ? 219.976 271.304 232.842 1.00 47.04  ? 4306 VAL A CA    1 
ATOM   20455 C  C     . VAL A 1 4306 ? 220.942 272.139 232.009 1.00 50.59  ? 4306 VAL A C     1 
ATOM   20456 O  O     . VAL A 1 4306 ? 221.707 271.607 231.196 1.00 50.46  ? 4306 VAL A O     1 
ATOM   20457 C  CB    . VAL A 1 4306 ? 218.571 271.262 232.216 1.00 49.59  ? 4306 VAL A CB    1 
ATOM   20458 C  CG1   . VAL A 1 4306 ? 218.655 270.956 230.736 1.00 49.58  ? 4306 VAL A CG1   1 
ATOM   20459 C  CG2   . VAL A 1 4306 ? 217.717 270.225 232.916 1.00 54.69  ? 4306 VAL A CG2   1 
ATOM   20460 N  N     . GLN A 1 4307 ? 220.925 273.461 232.200 1.00 54.33  ? 4307 GLN A N     1 
ATOM   20461 C  CA    . GLN A 1 4307 ? 221.876 274.316 231.500 1.00 47.32  ? 4307 GLN A CA    1 
ATOM   20462 C  C     . GLN A 1 4307 ? 223.304 274.050 231.950 1.00 52.34  ? 4307 GLN A C     1 
ATOM   20463 O  O     . GLN A 1 4307 ? 224.229 274.102 231.134 1.00 61.52  ? 4307 GLN A O     1 
ATOM   20464 C  CB    . GLN A 1 4307 ? 221.521 275.787 231.707 1.00 49.35  ? 4307 GLN A CB    1 
ATOM   20465 C  CG    . GLN A 1 4307 ? 220.226 276.211 231.044 1.00 55.36  ? 4307 GLN A CG    1 
ATOM   20466 C  CD    . GLN A 1 4307 ? 219.855 277.645 231.359 1.00 61.28  ? 4307 GLN A CD    1 
ATOM   20467 O  OE1   . GLN A 1 4307 ? 220.273 278.198 232.377 1.00 65.23  ? 4307 GLN A OE1   1 
ATOM   20468 N  NE2   . GLN A 1 4307 ? 219.061 278.255 230.488 1.00 54.54  ? 4307 GLN A NE2   1 
ATOM   20469 N  N     . TRP A 1 4308 ? 223.508 273.769 233.238 1.00 46.97  ? 4308 TRP A N     1 
ATOM   20470 C  CA    . TRP A 1 4308 ? 224.838 273.385 233.698 1.00 48.19  ? 4308 TRP A CA    1 
ATOM   20471 C  C     . TRP A 1 4308 ? 225.297 272.103 233.018 1.00 46.53  ? 4308 TRP A C     1 
ATOM   20472 O  O     . TRP A 1 4308 ? 226.462 271.979 232.626 1.00 43.10  ? 4308 TRP A O     1 
ATOM   20473 C  CB    . TRP A 1 4308 ? 224.845 273.215 235.216 1.00 47.72  ? 4308 TRP A CB    1 
ATOM   20474 C  CG    . TRP A 1 4308 ? 226.190 272.871 235.780 1.00 49.73  ? 4308 TRP A CG    1 
ATOM   20475 C  CD1   . TRP A 1 4308 ? 227.147 273.742 236.204 1.00 51.08  ? 4308 TRP A CD1   1 
ATOM   20476 C  CD2   . TRP A 1 4308 ? 226.726 271.558 235.985 1.00 48.51  ? 4308 TRP A CD2   1 
ATOM   20477 N  NE1   . TRP A 1 4308 ? 228.245 273.057 236.659 1.00 52.30  ? 4308 TRP A NE1   1 
ATOM   20478 C  CE2   . TRP A 1 4308 ? 228.011 271.713 236.535 1.00 52.06  ? 4308 TRP A CE2   1 
ATOM   20479 C  CE3   . TRP A 1 4308 ? 226.244 270.267 235.755 1.00 44.30  ? 4308 TRP A CE3   1 
ATOM   20480 C  CZ2   . TRP A 1 4308 ? 228.819 270.628 236.858 1.00 46.14  ? 4308 TRP A CZ2   1 
ATOM   20481 C  CZ3   . TRP A 1 4308 ? 227.049 269.193 236.076 1.00 42.33  ? 4308 TRP A CZ3   1 
ATOM   20482 C  CH2   . TRP A 1 4308 ? 228.321 269.379 236.621 1.00 42.09  ? 4308 TRP A CH2   1 
ATOM   20483 N  N     . VAL A 1 4309 ? 224.389 271.136 232.871 1.00 50.50  ? 4309 VAL A N     1 
ATOM   20484 C  CA    . VAL A 1 4309 ? 224.730 269.889 232.194 1.00 44.14  ? 4309 VAL A CA    1 
ATOM   20485 C  C     . VAL A 1 4309 ? 225.090 270.146 230.735 1.00 47.05  ? 4309 VAL A C     1 
ATOM   20486 O  O     . VAL A 1 4309 ? 226.064 269.589 230.217 1.00 54.65  ? 4309 VAL A O     1 
ATOM   20487 C  CB    . VAL A 1 4309 ? 223.580 268.873 232.321 1.00 41.16  ? 4309 VAL A CB    1 
ATOM   20488 C  CG1   . VAL A 1 4309 ? 223.882 267.630 231.504 1.00 43.91  ? 4309 VAL A CG1   1 
ATOM   20489 C  CG2   . VAL A 1 4309 ? 223.365 268.502 233.772 1.00 39.23  ? 4309 VAL A CG2   1 
ATOM   20490 N  N     . GLU A 1 4310 ? 224.316 270.992 230.048 1.00 53.55  ? 4310 GLU A N     1 
ATOM   20491 C  CA    . GLU A 1 4310 ? 224.575 271.229 228.630 1.00 45.40  ? 4310 GLU A CA    1 
ATOM   20492 C  C     . GLU A 1 4310 ? 225.880 271.982 228.401 1.00 48.39  ? 4310 GLU A C     1 
ATOM   20493 O  O     . GLU A 1 4310 ? 226.551 271.755 227.389 1.00 56.76  ? 4310 GLU A O     1 
ATOM   20494 C  CB    . GLU A 1 4310 ? 223.412 271.986 227.991 1.00 44.80  ? 4310 GLU A CB    1 
ATOM   20495 C  CG    . GLU A 1 4310 ? 222.120 271.194 227.908 1.00 50.59  ? 4310 GLU A CG    1 
ATOM   20496 C  CD    . GLU A 1 4310 ? 220.893 272.081 227.846 1.00 59.21  ? 4310 GLU A CD    1 
ATOM   20497 O  OE1   . GLU A 1 4310 ? 219.768 271.542 227.806 1.00 60.71  ? 4310 GLU A OE1   1 
ATOM   20498 O  OE2   . GLU A 1 4310 ? 221.052 273.320 227.834 1.00 58.55  ? 4310 GLU A OE2   1 
ATOM   20499 N  N     . LEU A 1 4311 ? 226.261 272.876 229.313 1.00 46.07  ? 4311 LEU A N     1 
ATOM   20500 C  CA    . LEU A 1 4311 ? 227.536 273.575 229.224 1.00 44.50  ? 4311 LEU A CA    1 
ATOM   20501 C  C     . LEU A 1 4311 ? 228.671 272.819 229.904 1.00 48.64  ? 4311 LEU A C     1 
ATOM   20502 O  O     . LEU A 1 4311 ? 229.674 273.431 230.282 1.00 54.00  ? 4311 LEU A O     1 
ATOM   20503 C  CB    . LEU A 1 4311 ? 227.426 274.991 229.794 1.00 46.02  ? 4311 LEU A CB    1 
ATOM   20504 C  CG    . LEU A 1 4311 ? 226.737 276.083 228.962 1.00 49.50  ? 4311 LEU A CG    1 
ATOM   20505 C  CD1   . LEU A 1 4311 ? 225.229 275.922 228.841 1.00 46.88  ? 4311 LEU A CD1   1 
ATOM   20506 C  CD2   . LEU A 1 4311 ? 227.086 277.452 229.525 1.00 48.70  ? 4311 LEU A CD2   1 
ATOM   20507 N  N     . LEU A 1 4312 ? 228.531 271.508 230.076 1.00 51.41  ? 4312 LEU A N     1 
ATOM   20508 C  CA    . LEU A 1 4312 ? 229.662 270.715 230.535 1.00 48.10  ? 4312 LEU A CA    1 
ATOM   20509 C  C     . LEU A 1 4312 ? 230.724 270.638 229.441 1.00 45.80  ? 4312 LEU A C     1 
ATOM   20510 O  O     . LEU A 1 4312 ? 230.388 270.561 228.257 1.00 43.44  ? 4312 LEU A O     1 
ATOM   20511 C  CB    . LEU A 1 4312 ? 229.217 269.307 230.922 1.00 46.55  ? 4312 LEU A CB    1 
ATOM   20512 C  CG    . LEU A 1 4312 ? 228.731 269.100 232.355 1.00 40.26  ? 4312 LEU A CG    1 
ATOM   20513 C  CD1   . LEU A 1 4312 ? 228.480 267.629 232.624 1.00 37.00  ? 4312 LEU A CD1   1 
ATOM   20514 C  CD2   . LEU A 1 4312 ? 229.743 269.659 233.335 1.00 42.91  ? 4312 LEU A CD2   1 
ATOM   20515 N  N     . PRO A 1 4313 ? 232.004 270.666 229.805 1.00 52.92  ? 4313 PRO A N     1 
ATOM   20516 C  CA    . PRO A 1 4313 ? 233.059 270.564 228.790 1.00 48.55  ? 4313 PRO A CA    1 
ATOM   20517 C  C     . PRO A 1 4313 ? 233.041 269.207 228.104 1.00 48.57  ? 4313 PRO A C     1 
ATOM   20518 O  O     . PRO A 1 4313 ? 232.662 268.195 228.696 1.00 51.46  ? 4313 PRO A O     1 
ATOM   20519 C  CB    . PRO A 1 4313 ? 234.348 270.765 229.596 1.00 43.44  ? 4313 PRO A CB    1 
ATOM   20520 C  CG    . PRO A 1 4313 ? 233.918 271.424 230.861 1.00 50.84  ? 4313 PRO A CG    1 
ATOM   20521 C  CD    . PRO A 1 4313 ? 232.555 270.886 231.151 1.00 49.69  ? 4313 PRO A CD    1 
ATOM   20522 N  N     . ASP A 1 4314 ? 233.452 269.195 226.838 1.00 52.44  ? 4314 ASP A N     1 
ATOM   20523 C  CA    . ASP A 1 4314 ? 233.646 267.946 226.105 1.00 55.50  ? 4314 ASP A CA    1 
ATOM   20524 C  C     . ASP A 1 4314 ? 235.054 267.392 226.312 1.00 57.65  ? 4314 ASP A C     1 
ATOM   20525 O  O     . ASP A 1 4314 ? 235.782 267.102 225.361 1.00 58.48  ? 4314 ASP A O     1 
ATOM   20526 C  CB    . ASP A 1 4314 ? 233.342 268.180 224.625 1.00 54.88  ? 4314 ASP A CB    1 
ATOM   20527 C  CG    . ASP A 1 4314 ? 233.555 266.941 223.770 1.00 64.79  ? 4314 ASP A CG    1 
ATOM   20528 O  OD1   . ASP A 1 4314 ? 233.991 267.087 222.608 1.00 65.19  ? 4314 ASP A OD1   1 
ATOM   20529 O  OD2   . ASP A 1 4314 ? 233.292 265.824 224.261 1.00 59.61  ? 4314 ASP A OD2   1 
ATOM   20530 N  N     . THR A 1 4315 ? 235.470 267.268 227.572 1.00 52.04  ? 4315 THR A N     1 
ATOM   20531 C  CA    . THR A 1 4315 ? 236.813 266.827 227.933 1.00 48.85  ? 4315 THR A CA    1 
ATOM   20532 C  C     . THR A 1 4315 ? 236.722 265.821 229.080 1.00 52.36  ? 4315 THR A C     1 
ATOM   20533 O  O     . THR A 1 4315 ? 237.459 265.893 230.062 1.00 54.28  ? 4315 THR A O     1 
ATOM   20534 C  CB    . THR A 1 4315 ? 237.705 268.003 228.330 1.00 50.85  ? 4315 THR A CB    1 
ATOM   20535 O  OG1   . THR A 1 4315 ? 237.151 268.657 229.477 1.00 52.37  ? 4315 THR A OG1   1 
ATOM   20536 C  CG2   . THR A 1 4315 ? 237.826 269.005 227.193 1.00 53.14  ? 4315 THR A CG2   1 
ATOM   20537 N  N     . GLN A 1 4316 ? 235.793 264.878 228.958 1.00 39.57  ? 4316 GLN A N     1 
ATOM   20538 C  CA    . GLN A 1 4316 ? 235.588 263.903 230.020 1.00 35.47  ? 4316 GLN A CA    1 
ATOM   20539 C  C     . GLN A 1 4316 ? 236.773 262.953 230.108 1.00 40.65  ? 4316 GLN A C     1 
ATOM   20540 O  O     . GLN A 1 4316 ? 237.232 262.411 229.099 1.00 39.57  ? 4316 GLN A O     1 
ATOM   20541 C  CB    . GLN A 1 4316 ? 234.305 263.114 229.791 1.00 37.73  ? 4316 GLN A CB    1 
ATOM   20542 C  CG    . GLN A 1 4316 ? 233.966 262.187 230.944 1.00 32.19  ? 4316 GLN A CG    1 
ATOM   20543 C  CD    . GLN A 1 4316 ? 232.747 261.345 230.673 1.00 34.01  ? 4316 GLN A CD    1 
ATOM   20544 O  OE1   . GLN A 1 4316 ? 231.690 261.863 230.321 1.00 43.14  ? 4316 GLN A OE1   1 
ATOM   20545 N  NE2   . GLN A 1 4316 ? 232.882 260.037 230.842 1.00 28.90  ? 4316 GLN A NE2   1 
ATOM   20546 N  N     . THR A 1 4317 ? 237.260 262.755 231.322 1.00 41.84  ? 4317 THR A N     1 
ATOM   20547 C  CA    . THR A 1 4317 ? 238.348 261.855 231.651 1.00 39.03  ? 4317 THR A CA    1 
ATOM   20548 C  C     . THR A 1 4317 ? 237.906 260.956 232.796 1.00 41.60  ? 4317 THR A C     1 
ATOM   20549 O  O     . THR A 1 4317 ? 236.940 261.271 233.500 1.00 48.62  ? 4317 THR A O     1 
ATOM   20550 C  CB    . THR A 1 4317 ? 239.607 262.641 232.049 1.00 43.93  ? 4317 THR A CB    1 
ATOM   20551 O  OG1   . THR A 1 4317 ? 239.314 263.484 233.169 1.00 46.71  ? 4317 THR A OG1   1 
ATOM   20552 C  CG2   . THR A 1 4317 ? 240.095 263.494 230.893 1.00 42.84  ? 4317 THR A CG2   1 
ATOM   20553 N  N     . PRO A 1 4318 ? 238.574 259.817 233.003 1.00 37.40  ? 4318 PRO A N     1 
ATOM   20554 C  CA    . PRO A 1 4318 ? 238.184 258.942 234.120 1.00 31.89  ? 4318 PRO A CA    1 
ATOM   20555 C  C     . PRO A 1 4318 ? 238.260 259.612 235.480 1.00 33.73  ? 4318 PRO A C     1 
ATOM   20556 O  O     . PRO A 1 4318 ? 237.674 259.095 236.438 1.00 38.98  ? 4318 PRO A O     1 
ATOM   20557 C  CB    . PRO A 1 4318 ? 239.176 257.778 234.013 1.00 35.34  ? 4318 PRO A CB    1 
ATOM   20558 C  CG    . PRO A 1 4318 ? 239.560 257.752 232.589 1.00 33.29  ? 4318 PRO A CG    1 
ATOM   20559 C  CD    . PRO A 1 4318 ? 239.585 259.181 232.142 1.00 36.94  ? 4318 PRO A CD    1 
ATOM   20560 N  N     . SER A 1 4319 ? 238.956 260.744 235.601 1.00 37.36  ? 4319 SER A N     1 
ATOM   20561 C  CA    . SER A 1 4319 ? 239.031 261.432 236.884 1.00 33.60  ? 4319 SER A CA    1 
ATOM   20562 C  C     . SER A 1 4319 ? 237.691 262.034 237.287 1.00 36.95  ? 4319 SER A C     1 
ATOM   20563 O  O     . SER A 1 4319 ? 237.480 262.332 238.468 1.00 47.69  ? 4319 SER A O     1 
ATOM   20564 C  CB    . SER A 1 4319 ? 240.104 262.514 236.836 1.00 38.98  ? 4319 SER A CB    1 
ATOM   20565 O  OG    . SER A 1 4319 ? 241.389 261.945 236.677 1.00 50.79  ? 4319 SER A OG    1 
ATOM   20566 N  N     . TRP A 1 4320 ? 236.783 262.239 236.330 1.00 36.16  ? 4320 TRP A N     1 
ATOM   20567 C  CA    . TRP A 1 4320 ? 235.425 262.635 236.688 1.00 35.41  ? 4320 TRP A CA    1 
ATOM   20568 C  C     . TRP A 1 4320 ? 234.739 261.554 237.506 1.00 38.44  ? 4320 TRP A C     1 
ATOM   20569 O  O     . TRP A 1 4320 ? 233.885 261.854 238.347 1.00 41.63  ? 4320 TRP A O     1 
ATOM   20570 C  CB    . TRP A 1 4320 ? 234.597 262.937 235.438 1.00 34.77  ? 4320 TRP A CB    1 
ATOM   20571 C  CG    . TRP A 1 4320 ? 235.068 264.102 234.628 1.00 39.98  ? 4320 TRP A CG    1 
ATOM   20572 C  CD1   . TRP A 1 4320 ? 236.327 264.621 234.583 1.00 42.00  ? 4320 TRP A CD1   1 
ATOM   20573 C  CD2   . TRP A 1 4320 ? 234.274 264.903 233.747 1.00 42.60  ? 4320 TRP A CD2   1 
ATOM   20574 N  NE1   . TRP A 1 4320 ? 236.368 265.691 233.727 1.00 48.75  ? 4320 TRP A NE1   1 
ATOM   20575 C  CE2   . TRP A 1 4320 ? 235.119 265.885 233.200 1.00 46.26  ? 4320 TRP A CE2   1 
ATOM   20576 C  CE3   . TRP A 1 4320 ? 232.930 264.882 233.366 1.00 37.13  ? 4320 TRP A CE3   1 
ATOM   20577 C  CZ2   . TRP A 1 4320 ? 234.665 266.837 232.294 1.00 45.18  ? 4320 TRP A CZ2   1 
ATOM   20578 C  CZ3   . TRP A 1 4320 ? 232.482 265.827 232.467 1.00 30.09  ? 4320 TRP A CZ3   1 
ATOM   20579 C  CH2   . TRP A 1 4320 ? 233.346 266.790 231.940 1.00 40.98  ? 4320 TRP A CH2   1 
ATOM   20580 N  N     . LEU A 1 4321 ? 235.097 260.298 237.270 1.00 33.57  ? 4321 LEU A N     1 
ATOM   20581 C  CA    . LEU A 1 4321 ? 234.537 259.159 237.978 1.00 24.05  ? 4321 LEU A CA    1 
ATOM   20582 C  C     . LEU A 1 4321 ? 235.306 258.824 239.247 1.00 27.57  ? 4321 LEU A C     1 
ATOM   20583 O  O     . LEU A 1 4321 ? 234.939 257.874 239.944 1.00 35.43  ? 4321 LEU A O     1 
ATOM   20584 C  CB    . LEU A 1 4321 ? 234.518 257.938 237.056 1.00 32.74  ? 4321 LEU A CB    1 
ATOM   20585 C  CG    . LEU A 1 4321 ? 234.149 258.191 235.592 1.00 27.29  ? 4321 LEU A CG    1 
ATOM   20586 C  CD1   . LEU A 1 4321 ? 234.192 256.899 234.805 1.00 26.58  ? 4321 LEU A CD1   1 
ATOM   20587 C  CD2   . LEU A 1 4321 ? 232.785 258.837 235.475 1.00 31.91  ? 4321 LEU A CD2   1 
ATOM   20588 N  N     . GLY A 1 4322 ? 236.359 259.573 239.560 1.00 29.83  ? 4322 GLY A N     1 
ATOM   20589 C  CA    . GLY A 1 4322 ? 237.246 259.242 240.651 1.00 28.96  ? 4322 GLY A CA    1 
ATOM   20590 C  C     . GLY A 1 4322 ? 238.381 258.320 240.275 1.00 38.58  ? 4322 GLY A C     1 
ATOM   20591 O  O     . GLY A 1 4322 ? 239.250 258.060 241.114 1.00 47.81  ? 4322 GLY A O     1 
ATOM   20592 N  N     . LEU A 1 4323 ? 238.402 257.824 239.045 1.00 30.26  ? 4323 LEU A N     1 
ATOM   20593 C  CA    . LEU A 1 4323 ? 239.398 256.882 238.573 1.00 19.34  ? 4323 LEU A CA    1 
ATOM   20594 C  C     . LEU A 1 4323 ? 240.674 257.602 238.150 1.00 28.14  ? 4323 LEU A C     1 
ATOM   20595 O  O     . LEU A 1 4323 ? 240.668 258.811 237.913 1.00 36.83  ? 4323 LEU A O     1 
ATOM   20596 C  CB    . LEU A 1 4323 ? 238.830 256.089 237.402 1.00 24.99  ? 4323 LEU A CB    1 
ATOM   20597 C  CG    . LEU A 1 4323 ? 237.819 255.010 237.773 1.00 25.20  ? 4323 LEU A CG    1 
ATOM   20598 C  CD1   . LEU A 1 4323 ? 237.112 254.510 236.540 1.00 16.31  ? 4323 LEU A CD1   1 
ATOM   20599 C  CD2   . LEU A 1 4323 ? 238.513 253.873 238.485 1.00 34.55  ? 4323 LEU A CD2   1 
ATOM   20600 N  N     . PRO A 1 4324 ? 241.793 256.885 238.064 1.00 35.72  ? 4324 PRO A N     1 
ATOM   20601 C  CA    . PRO A 1 4324 ? 242.998 257.480 237.480 1.00 30.76  ? 4324 PRO A CA    1 
ATOM   20602 C  C     . PRO A 1 4324 ? 242.820 257.737 235.993 1.00 40.36  ? 4324 PRO A C     1 
ATOM   20603 O  O     . PRO A 1 4324 ? 242.060 257.051 235.306 1.00 50.76  ? 4324 PRO A O     1 
ATOM   20604 C  CB    . PRO A 1 4324 ? 244.077 256.423 237.740 1.00 32.93  ? 4324 PRO A CB    1 
ATOM   20605 C  CG    . PRO A 1 4324 ? 243.326 255.153 237.890 1.00 37.13  ? 4324 PRO A CG    1 
ATOM   20606 C  CD    . PRO A 1 4324 ? 242.045 255.523 238.563 1.00 46.56  ? 4324 PRO A CD    1 
ATOM   20607 N  N     . ASN A 1 4325 ? 243.541 258.743 235.496 1.00 40.27  ? 4325 ASN A N     1 
ATOM   20608 C  CA    . ASN A 1 4325 ? 243.403 259.138 234.099 1.00 37.31  ? 4325 ASN A CA    1 
ATOM   20609 C  C     . ASN A 1 4325 ? 243.979 258.110 233.136 1.00 43.04  ? 4325 ASN A C     1 
ATOM   20610 O  O     . ASN A 1 4325 ? 243.696 258.180 231.936 1.00 48.07  ? 4325 ASN A O     1 
ATOM   20611 C  CB    . ASN A 1 4325 ? 244.073 260.491 233.864 1.00 41.56  ? 4325 ASN A CB    1 
ATOM   20612 C  CG    . ASN A 1 4325 ? 243.172 261.652 234.213 1.00 45.66  ? 4325 ASN A CG    1 
ATOM   20613 O  OD1   . ASN A 1 4325 ? 241.972 261.619 233.951 1.00 40.52  ? 4325 ASN A OD1   1 
ATOM   20614 N  ND2   . ASN A 1 4325 ? 243.746 262.689 234.807 1.00 44.48  ? 4325 ASN A ND2   1 
ATOM   20615 N  N     . ASN A 1 4326 ? 244.778 257.167 233.622 1.00 42.63  ? 4326 ASN A N     1 
ATOM   20616 C  CA    . ASN A 1 4326 ? 245.367 256.144 232.770 1.00 40.61  ? 4326 ASN A CA    1 
ATOM   20617 C  C     . ASN A 1 4326 ? 244.452 254.944 232.568 1.00 39.05  ? 4326 ASN A C     1 
ATOM   20618 O  O     . ASN A 1 4326 ? 244.837 254.003 231.867 1.00 44.66  ? 4326 ASN A O     1 
ATOM   20619 C  CB    . ASN A 1 4326 ? 246.707 255.681 233.350 1.00 46.78  ? 4326 ASN A CB    1 
ATOM   20620 C  CG    . ASN A 1 4326 ? 246.614 255.320 234.819 1.00 50.22  ? 4326 ASN A CG    1 
ATOM   20621 O  OD1   . ASN A 1 4326 ? 245.859 254.430 235.206 1.00 51.77  ? 4326 ASN A OD1   1 
ATOM   20622 N  ND2   . ASN A 1 4326 ? 247.386 256.011 235.645 1.00 53.04  ? 4326 ASN A ND2   1 
ATOM   20623 N  N     . ALA A 1 4327 ? 243.258 254.954 233.161 1.00 40.30  ? 4327 ALA A N     1 
ATOM   20624 C  CA    . ALA A 1 4327 ? 242.348 253.824 233.019 1.00 48.76  ? 4327 ALA A CA    1 
ATOM   20625 C  C     . ALA A 1 4327 ? 241.871 253.654 231.583 1.00 56.79  ? 4327 ALA A C     1 
ATOM   20626 O  O     . ALA A 1 4327 ? 241.577 252.531 231.158 1.00 55.34  ? 4327 ALA A O     1 
ATOM   20627 C  CB    . ALA A 1 4327 ? 241.152 253.993 233.954 1.00 38.55  ? 4327 ALA A CB    1 
ATOM   20628 N  N     . GLU A 1 4328 ? 241.788 254.743 230.825 1.00 60.18  ? 4328 GLU A N     1 
ATOM   20629 C  CA    . GLU A 1 4328 ? 241.254 254.709 229.471 1.00 49.42  ? 4328 GLU A CA    1 
ATOM   20630 C  C     . GLU A 1 4328 ? 242.322 254.528 228.402 1.00 52.61  ? 4328 GLU A C     1 
ATOM   20631 O  O     . GLU A 1 4328 ? 241.973 254.350 227.233 1.00 61.18  ? 4328 GLU A O     1 
ATOM   20632 C  CB    . GLU A 1 4328 ? 240.469 255.993 229.188 1.00 42.63  ? 4328 GLU A CB    1 
ATOM   20633 C  CG    . GLU A 1 4328 ? 241.277 257.263 229.390 1.00 47.58  ? 4328 GLU A CG    1 
ATOM   20634 C  CD    . GLU A 1 4328 ? 240.598 258.486 228.812 1.00 59.08  ? 4328 GLU A CD    1 
ATOM   20635 O  OE1   . GLU A 1 4328 ? 239.520 258.335 228.200 1.00 57.16  ? 4328 GLU A OE1   1 
ATOM   20636 O  OE2   . GLU A 1 4328 ? 241.140 259.600 228.969 1.00 60.64  ? 4328 GLU A OE2   1 
ATOM   20637 N  N     . ARG A 1 4329 ? 243.606 254.556 228.765 1.00 51.65  ? 4329 ARG A N     1 
ATOM   20638 C  CA    . ARG A 1 4329 ? 244.660 254.522 227.755 1.00 51.41  ? 4329 ARG A CA    1 
ATOM   20639 C  C     . ARG A 1 4329 ? 244.617 253.236 226.938 1.00 55.67  ? 4329 ARG A C     1 
ATOM   20640 O  O     . ARG A 1 4329 ? 244.608 253.277 225.702 1.00 62.94  ? 4329 ARG A O     1 
ATOM   20641 C  CB    . ARG A 1 4329 ? 246.026 254.687 228.418 1.00 51.97  ? 4329 ARG A CB    1 
ATOM   20642 C  CG    . ARG A 1 4329 ? 247.191 254.473 227.474 1.00 57.29  ? 4329 ARG A CG    1 
ATOM   20643 C  CD    . ARG A 1 4329 ? 248.492 254.977 228.068 1.00 59.33  ? 4329 ARG A CD    1 
ATOM   20644 N  NE    . ARG A 1 4329 ? 248.477 256.417 228.286 1.00 60.77  ? 4329 ARG A NE    1 
ATOM   20645 C  CZ    . ARG A 1 4329 ? 249.427 257.244 227.872 1.00 62.85  ? 4329 ARG A CZ    1 
ATOM   20646 N  NH1   . ARG A 1 4329 ? 250.481 256.805 227.206 1.00 61.19  ? 4329 ARG A NH1   1 
ATOM   20647 N  NH2   . ARG A 1 4329 ? 249.316 258.543 228.133 1.00 59.21  ? 4329 ARG A NH2   1 
ATOM   20648 N  N     . VAL A 1 4330 ? 244.585 252.084 227.610 1.00 53.03  ? 4330 VAL A N     1 
ATOM   20649 C  CA    . VAL A 1 4330 ? 244.550 250.811 226.898 1.00 53.19  ? 4330 VAL A CA    1 
ATOM   20650 C  C     . VAL A 1 4330 ? 243.251 250.670 226.115 1.00 56.24  ? 4330 VAL A C     1 
ATOM   20651 O  O     . VAL A 1 4330 ? 243.251 250.230 224.957 1.00 60.41  ? 4330 VAL A O     1 
ATOM   20652 C  CB    . VAL A 1 4330 ? 244.752 249.647 227.885 1.00 52.75  ? 4330 VAL A CB    1 
ATOM   20653 C  CG1   . VAL A 1 4330 ? 244.215 248.350 227.306 1.00 51.21  ? 4330 VAL A CG1   1 
ATOM   20654 C  CG2   . VAL A 1 4330 ? 246.221 249.509 228.241 1.00 52.77  ? 4330 VAL A CG2   1 
ATOM   20655 N  N     . LEU A 1 4331 ? 242.126 251.040 226.730 1.00 54.05  ? 4331 LEU A N     1 
ATOM   20656 C  CA    . LEU A 1 4331 ? 240.842 250.942 226.046 1.00 51.49  ? 4331 LEU A CA    1 
ATOM   20657 C  C     . LEU A 1 4331 ? 240.794 251.852 224.825 1.00 53.51  ? 4331 LEU A C     1 
ATOM   20658 O  O     . LEU A 1 4331 ? 240.308 251.448 223.763 1.00 60.46  ? 4331 LEU A O     1 
ATOM   20659 C  CB    . LEU A 1 4331 ? 239.707 251.280 227.010 1.00 56.91  ? 4331 LEU A CB    1 
ATOM   20660 C  CG    . LEU A 1 4331 ? 238.296 251.153 226.436 1.00 60.34  ? 4331 LEU A CG    1 
ATOM   20661 C  CD1   . LEU A 1 4331 ? 238.009 249.717 226.032 1.00 57.51  ? 4331 LEU A CD1   1 
ATOM   20662 C  CD2   . LEU A 1 4331 ? 237.263 251.653 227.434 1.00 56.18  ? 4331 LEU A CD2   1 
ATOM   20663 N  N     . LEU A 1 4332 ? 241.293 253.082 224.955 1.00 47.42  ? 4332 LEU A N     1 
ATOM   20664 C  CA    . LEU A 1 4332 ? 241.298 253.998 223.819 1.00 47.00  ? 4332 LEU A CA    1 
ATOM   20665 C  C     . LEU A 1 4332 ? 242.213 253.502 222.706 1.00 52.48  ? 4332 LEU A C     1 
ATOM   20666 O  O     . LEU A 1 4332 ? 241.873 253.613 221.523 1.00 59.71  ? 4332 LEU A O     1 
ATOM   20667 C  CB    . LEU A 1 4332 ? 241.708 255.398 224.270 1.00 47.00  ? 4332 LEU A CB    1 
ATOM   20668 C  CG    . LEU A 1 4332 ? 240.652 256.186 225.045 1.00 45.24  ? 4332 LEU A CG    1 
ATOM   20669 C  CD1   . LEU A 1 4332 ? 241.092 257.624 225.234 1.00 48.55  ? 4332 LEU A CD1   1 
ATOM   20670 C  CD2   . LEU A 1 4332 ? 239.306 256.121 224.348 1.00 47.36  ? 4332 LEU A CD2   1 
ATOM   20671 N  N     . THR A 1 4333 ? 243.382 252.960 223.061 1.00 49.77  ? 4333 THR A N     1 
ATOM   20672 C  CA    . THR A 1 4333 ? 244.276 252.417 222.041 1.00 48.67  ? 4333 THR A CA    1 
ATOM   20673 C  C     . THR A 1 4333 ? 243.626 251.254 221.302 1.00 52.80  ? 4333 THR A C     1 
ATOM   20674 O  O     . THR A 1 4333 ? 243.680 251.183 220.065 1.00 56.29  ? 4333 THR A O     1 
ATOM   20675 C  CB    . THR A 1 4333 ? 245.590 251.974 222.680 1.00 47.97  ? 4333 THR A CB    1 
ATOM   20676 O  OG1   . THR A 1 4333 ? 246.199 253.085 223.347 1.00 54.42  ? 4333 THR A OG1   1 
ATOM   20677 C  CG2   . THR A 1 4333 ? 246.541 251.444 221.623 1.00 49.37  ? 4333 THR A CG2   1 
ATOM   20678 N  N     . THR A 1 4334 ? 242.995 250.342 222.044 1.00 50.59  ? 4334 THR A N     1 
ATOM   20679 C  CA    . THR A 1 4334 ? 242.319 249.213 221.417 1.00 49.48  ? 4334 THR A CA    1 
ATOM   20680 C  C     . THR A 1 4334 ? 241.169 249.680 220.534 1.00 50.69  ? 4334 THR A C     1 
ATOM   20681 O  O     . THR A 1 4334 ? 240.963 249.142 219.442 1.00 58.33  ? 4334 THR A O     1 
ATOM   20682 C  CB    . THR A 1 4334 ? 241.822 248.244 222.489 1.00 53.86  ? 4334 THR A CB    1 
ATOM   20683 O  OG1   . THR A 1 4334 ? 242.945 247.621 223.125 1.00 51.39  ? 4334 THR A OG1   1 
ATOM   20684 C  CG2   . THR A 1 4334 ? 240.940 247.168 221.877 1.00 52.64  ? 4334 THR A CG2   1 
ATOM   20685 N  N     . GLN A 1 4335 ? 240.418 250.689 220.980 1.00 40.59  ? 4335 GLN A N     1 
ATOM   20686 C  CA    . GLN A 1 4335 ? 239.310 251.196 220.178 1.00 43.28  ? 4335 GLN A CA    1 
ATOM   20687 C  C     . GLN A 1 4335 ? 239.802 251.866 218.901 1.00 49.03  ? 4335 GLN A C     1 
ATOM   20688 O  O     . GLN A 1 4335 ? 239.176 251.730 217.847 1.00 50.91  ? 4335 GLN A O     1 
ATOM   20689 C  CB    . GLN A 1 4335 ? 238.465 252.164 221.003 1.00 48.75  ? 4335 GLN A CB    1 
ATOM   20690 C  CG    . GLN A 1 4335 ? 237.487 251.475 221.935 1.00 53.38  ? 4335 GLN A CG    1 
ATOM   20691 C  CD    . GLN A 1 4335 ? 236.421 252.412 222.454 1.00 58.30  ? 4335 GLN A CD    1 
ATOM   20692 O  OE1   . GLN A 1 4335 ? 236.722 253.433 223.070 1.00 52.70  ? 4335 GLN A OE1   1 
ATOM   20693 N  NE2   . GLN A 1 4335 ? 235.163 252.069 222.208 1.00 57.68  ? 4335 GLN A NE2   1 
ATOM   20694 N  N     . GLY A 1 4336 ? 240.915 252.598 218.973 1.00 49.30  ? 4336 GLY A N     1 
ATOM   20695 C  CA    . GLY A 1 4336 ? 241.477 253.182 217.764 1.00 40.84  ? 4336 GLY A CA    1 
ATOM   20696 C  C     . GLY A 1 4336 ? 241.951 252.131 216.779 1.00 47.39  ? 4336 GLY A C     1 
ATOM   20697 O  O     . GLY A 1 4336 ? 241.721 252.244 215.569 1.00 47.59  ? 4336 GLY A O     1 
ATOM   20698 N  N     . VAL A 1 4337 ? 242.614 251.087 217.284 1.00 53.33  ? 4337 VAL A N     1 
ATOM   20699 C  CA    . VAL A 1 4337 ? 243.038 249.993 216.414 1.00 47.89  ? 4337 VAL A CA    1 
ATOM   20700 C  C     . VAL A 1 4337 ? 241.827 249.311 215.786 1.00 48.34  ? 4337 VAL A C     1 
ATOM   20701 O  O     . VAL A 1 4337 ? 241.836 248.965 214.598 1.00 54.53  ? 4337 VAL A O     1 
ATOM   20702 C  CB    . VAL A 1 4337 ? 243.911 249.000 217.201 1.00 51.38  ? 4337 VAL A CB    1 
ATOM   20703 C  CG1   . VAL A 1 4337 ? 244.148 247.738 216.390 1.00 55.33  ? 4337 VAL A CG1   1 
ATOM   20704 C  CG2   . VAL A 1 4337 ? 245.232 249.648 217.579 1.00 50.12  ? 4337 VAL A CG2   1 
ATOM   20705 N  N     . ASP A 1 4338 ? 240.764 249.115 216.568 1.00 51.85  ? 4338 ASP A N     1 
ATOM   20706 C  CA    . ASP A 1 4338 ? 239.553 248.496 216.042 1.00 50.65  ? 4338 ASP A CA    1 
ATOM   20707 C  C     . ASP A 1 4338 ? 238.889 249.375 214.991 1.00 48.55  ? 4338 ASP A C     1 
ATOM   20708 O  O     . ASP A 1 4338 ? 238.337 248.867 214.011 1.00 54.58  ? 4338 ASP A O     1 
ATOM   20709 C  CB    . ASP A 1 4338 ? 238.582 248.193 217.181 1.00 55.50  ? 4338 ASP A CB    1 
ATOM   20710 C  CG    . ASP A 1 4338 ? 238.939 246.925 217.926 1.00 65.27  ? 4338 ASP A CG    1 
ATOM   20711 O  OD1   . ASP A 1 4338 ? 238.197 246.550 218.858 1.00 65.02  ? 4338 ASP A OD1   1 
ATOM   20712 O  OD2   . ASP A 1 4338 ? 239.965 246.302 217.580 1.00 62.91  ? 4338 ASP A OD2   1 
ATOM   20713 N  N     . MET A 1 4339 ? 238.914 250.696 215.182 1.00 47.52  ? 4339 MET A N     1 
ATOM   20714 C  CA    . MET A 1 4339 ? 238.364 251.594 214.172 1.00 40.36  ? 4339 MET A CA    1 
ATOM   20715 C  C     . MET A 1 4339 ? 239.158 251.508 212.877 1.00 44.68  ? 4339 MET A C     1 
ATOM   20716 O  O     . MET A 1 4339 ? 238.579 251.502 211.783 1.00 52.24  ? 4339 MET A O     1 
ATOM   20717 C  CB    . MET A 1 4339 ? 238.344 253.032 214.687 1.00 49.00  ? 4339 MET A CB    1 
ATOM   20718 C  CG    . MET A 1 4339 ? 238.219 254.075 213.584 1.00 47.27  ? 4339 MET A CG    1 
ATOM   20719 S  SD    . MET A 1 4339 ? 238.543 255.762 214.124 1.00 61.94  ? 4339 MET A SD    1 
ATOM   20720 C  CE    . MET A 1 4339 ? 240.331 255.784 214.107 1.00 50.65  ? 4339 MET A CE    1 
ATOM   20721 N  N     . ILE A 1 4340 ? 240.486 251.444 212.980 1.00 57.49  ? 4340 ILE A N     1 
ATOM   20722 C  CA    . ILE A 1 4340 ? 241.310 251.270 211.785 1.00 50.48  ? 4340 ILE A CA    1 
ATOM   20723 C  C     . ILE A 1 4340 ? 240.960 249.964 211.086 1.00 46.30  ? 4340 ILE A C     1 
ATOM   20724 O  O     . ILE A 1 4340 ? 240.811 249.915 209.858 1.00 48.09  ? 4340 ILE A O     1 
ATOM   20725 C  CB    . ILE A 1 4340 ? 242.804 251.331 212.150 1.00 48.50  ? 4340 ILE A CB    1 
ATOM   20726 C  CG1   . ILE A 1 4340 ? 243.200 252.756 212.520 1.00 47.49  ? 4340 ILE A CG1   1 
ATOM   20727 C  CG2   . ILE A 1 4340 ? 243.654 250.839 210.995 1.00 52.62  ? 4340 ILE A CG2   1 
ATOM   20728 C  CD1   . ILE A 1 4340 ? 242.930 253.738 211.428 1.00 53.28  ? 4340 ILE A CD1   1 
ATOM   20729 N  N     . SER A 1 4341 ? 240.816 248.886 211.859 1.00 48.98  ? 4341 SER A N     1 
ATOM   20730 C  CA    . SER A 1 4341 ? 240.483 247.591 211.276 1.00 45.17  ? 4341 SER A CA    1 
ATOM   20731 C  C     . SER A 1 4341 ? 239.108 247.609 210.619 1.00 48.65  ? 4341 SER A C     1 
ATOM   20732 O  O     . SER A 1 4341 ? 238.901 246.965 209.588 1.00 52.72  ? 4341 SER A O     1 
ATOM   20733 C  CB    . SER A 1 4341 ? 240.555 246.503 212.345 1.00 49.27  ? 4341 SER A CB    1 
ATOM   20734 O  OG    . SER A 1 4341 ? 241.835 246.473 212.950 1.00 55.28  ? 4341 SER A OG    1 
ATOM   20735 N  N     . LYS A 1 4342 ? 238.151 248.324 211.212 1.00 52.92  ? 4342 LYS A N     1 
ATOM   20736 C  CA    . LYS A 1 4342 ? 236.818 248.410 210.622 1.00 45.15  ? 4342 LYS A CA    1 
ATOM   20737 C  C     . LYS A 1 4342 ? 236.834 249.218 209.332 1.00 47.91  ? 4342 LYS A C     1 
ATOM   20738 O  O     . LYS A 1 4342 ? 236.155 248.864 208.362 1.00 58.83  ? 4342 LYS A O     1 
ATOM   20739 C  CB    . LYS A 1 4342 ? 235.835 249.018 211.621 1.00 45.94  ? 4342 LYS A CB    1 
ATOM   20740 C  CG    . LYS A 1 4342 ? 235.425 248.081 212.739 1.00 46.30  ? 4342 LYS A CG    1 
ATOM   20741 C  CD    . LYS A 1 4342 ? 234.683 248.827 213.830 1.00 45.01  ? 4342 LYS A CD    1 
ATOM   20742 C  CE    . LYS A 1 4342 ? 234.417 247.928 215.023 1.00 45.21  ? 4342 LYS A CE    1 
ATOM   20743 N  NZ    . LYS A 1 4342 ? 233.781 246.650 214.610 1.00 55.25  ? 4342 LYS A NZ    1 
ATOM   20744 N  N     . MET A 1 4343 ? 237.591 250.318 209.304 1.00 48.35  ? 4343 MET A N     1 
ATOM   20745 C  CA    . MET A 1 4343 ? 237.722 251.087 208.071 1.00 46.41  ? 4343 MET A CA    1 
ATOM   20746 C  C     . MET A 1 4343 ? 238.385 250.259 206.979 1.00 55.68  ? 4343 MET A C     1 
ATOM   20747 O  O     . MET A 1 4343 ? 238.022 250.363 205.802 1.00 61.01  ? 4343 MET A O     1 
ATOM   20748 C  CB    . MET A 1 4343 ? 238.519 252.366 208.319 1.00 47.11  ? 4343 MET A CB    1 
ATOM   20749 C  CG    . MET A 1 4343 ? 237.838 253.376 209.214 1.00 51.64  ? 4343 MET A CG    1 
ATOM   20750 S  SD    . MET A 1 4343 ? 238.882 254.810 209.516 1.00 68.89  ? 4343 MET A SD    1 
ATOM   20751 C  CE    . MET A 1 4343 ? 238.856 255.589 207.906 1.00 56.71  ? 4343 MET A CE    1 
ATOM   20752 N  N     . LEU A 1 4344 ? 239.369 249.440 207.351 1.00 62.10  ? 4344 LEU A N     1 
ATOM   20753 C  CA    . LEU A 1 4344 ? 240.064 248.620 206.365 1.00 55.53  ? 4344 LEU A CA    1 
ATOM   20754 C  C     . LEU A 1 4344 ? 239.209 247.447 205.898 1.00 52.14  ? 4344 LEU A C     1 
ATOM   20755 O  O     . LEU A 1 4344 ? 239.306 247.037 204.736 1.00 59.07  ? 4344 LEU A O     1 
ATOM   20756 C  CB    . LEU A 1 4344 ? 241.380 248.118 206.953 1.00 55.93  ? 4344 LEU A CB    1 
ATOM   20757 C  CG    . LEU A 1 4344 ? 242.339 247.407 206.005 1.00 56.81  ? 4344 LEU A CG    1 
ATOM   20758 C  CD1   . LEU A 1 4344 ? 242.803 248.376 204.939 1.00 56.45  ? 4344 LEU A CD1   1 
ATOM   20759 C  CD2   . LEU A 1 4344 ? 243.519 246.845 206.772 1.00 57.23  ? 4344 LEU A CD2   1 
ATOM   20760 N  N     . LYS A 1 4345 ? 238.371 246.899 206.781 1.00 52.13  ? 4345 LYS A N     1 
ATOM   20761 C  CA    . LYS A 1 4345 ? 237.559 245.732 206.457 1.00 57.94  ? 4345 LYS A CA    1 
ATOM   20762 C  C     . LYS A 1 4345 ? 236.581 246.000 205.326 1.00 58.34  ? 4345 LYS A C     1 
ATOM   20763 O  O     . LYS A 1 4345 ? 236.211 245.069 204.604 1.00 62.09  ? 4345 LYS A O     1 
ATOM   20764 C  CB    . LYS A 1 4345 ? 236.787 245.274 207.695 1.00 53.22  ? 4345 LYS A CB    1 
ATOM   20765 C  CG    . LYS A 1 4345 ? 236.268 243.850 207.625 1.00 52.60  ? 4345 LYS A CG    1 
ATOM   20766 C  CD    . LYS A 1 4345 ? 236.167 243.226 209.009 1.00 55.25  ? 4345 LYS A CD    1 
ATOM   20767 C  CE    . LYS A 1 4345 ? 235.665 244.226 210.039 1.00 59.71  ? 4345 LYS A CE    1 
ATOM   20768 N  NZ    . LYS A 1 4345 ? 235.816 243.722 211.431 1.00 53.96  ? 4345 LYS A NZ    1 
ATOM   20769 N  N     . MET A 1 4346 ? 236.152 247.244 205.165 1.00 54.69  ? 4346 MET A N     1 
ATOM   20770 C  CA    . MET A 1 4346 ? 235.198 247.645 204.141 1.00 57.96  ? 4346 MET A CA    1 
ATOM   20771 C  C     . MET A 1 4346 ? 235.787 248.716 203.226 1.00 59.74  ? 4346 MET A C     1 
ATOM   20772 O  O     . MET A 1 4346 ? 235.149 249.719 202.902 1.00 57.58  ? 4346 MET A O     1 
ATOM   20773 C  CB    . MET A 1 4346 ? 233.885 248.065 204.798 1.00 53.44  ? 4346 MET A CB    1 
ATOM   20774 C  CG    . MET A 1 4346 ? 233.942 249.291 205.686 1.00 50.75  ? 4346 MET A CG    1 
ATOM   20775 S  SD    . MET A 1 4346 ? 232.315 249.574 206.404 1.00 65.66  ? 4346 MET A SD    1 
ATOM   20776 C  CE    . MET A 1 4346 ? 232.615 251.014 207.413 1.00 55.85  ? 4346 MET A CE    1 
ATOM   20777 N  N     . GLN A 1 4347 ? 237.024 248.485 202.795 1.00 68.69  ? 4347 GLN A N     1 
ATOM   20778 C  CA    . GLN A 1 4347 ? 237.702 249.307 201.801 1.00 67.32  ? 4347 GLN A CA    1 
ATOM   20779 C  C     . GLN A 1 4347 ? 237.108 249.123 200.409 1.00 67.93  ? 4347 GLN A C     1 
ATOM   20780 O  O     . GLN A 1 4347 ? 235.920 248.845 200.257 1.00 65.91  ? 4347 GLN A O     1 
ATOM   20781 C  CB    . GLN A 1 4347 ? 239.194 248.970 201.776 1.00 62.02  ? 4347 GLN A CB    1 
ATOM   20782 C  CG    . GLN A 1 4347 ? 240.030 249.859 200.874 1.00 67.99  ? 4347 GLN A CG    1 
ATOM   20783 C  CD    . GLN A 1 4347 ? 240.284 251.225 201.466 1.00 66.23  ? 4347 GLN A CD    1 
ATOM   20784 O  OE1   . GLN A 1 4347 ? 240.476 251.362 202.671 1.00 66.96  ? 4347 GLN A OE1   1 
ATOM   20785 N  NE2   . GLN A 1 4347 ? 240.298 252.245 200.617 1.00 63.82  ? 4347 GLN A NE2   1 
ATOM   20786 N  N     . PRO A 1 4374 ? 251.038 218.852 205.204 1.00 76.81  ? 4374 PRO A N     1 
ATOM   20787 C  CA    . PRO A 1 4374 ? 250.503 220.211 205.096 1.00 79.62  ? 4374 PRO A CA    1 
ATOM   20788 C  C     . PRO A 1 4374 ? 251.344 221.228 205.860 1.00 79.15  ? 4374 PRO A C     1 
ATOM   20789 O  O     . PRO A 1 4374 ? 252.257 220.845 206.590 1.00 78.09  ? 4374 PRO A O     1 
ATOM   20790 C  CB    . PRO A 1 4374 ? 249.099 220.092 205.709 1.00 77.78  ? 4374 PRO A CB    1 
ATOM   20791 C  CG    . PRO A 1 4374 ? 248.868 218.610 205.964 1.00 76.12  ? 4374 PRO A CG    1 
ATOM   20792 C  CD    . PRO A 1 4374 ? 249.964 217.853 205.289 1.00 76.57  ? 4374 PRO A CD    1 
ATOM   20793 N  N     . ALA A 1 4375 ? 251.038 222.514 205.683 1.00 79.56  ? 4375 ALA A N     1 
ATOM   20794 C  CA    . ALA A 1 4375 ? 251.792 223.553 206.376 1.00 81.57  ? 4375 ALA A CA    1 
ATOM   20795 C  C     . ALA A 1 4375 ? 251.439 223.599 207.856 1.00 83.80  ? 4375 ALA A C     1 
ATOM   20796 O  O     . ALA A 1 4375 ? 252.312 223.842 208.703 1.00 81.41  ? 4375 ALA A O     1 
ATOM   20797 C  CB    . ALA A 1 4375 ? 251.540 224.911 205.721 1.00 78.90  ? 4375 ALA A CB    1 
ATOM   20798 N  N     . TRP A 1 4376 ? 250.163 223.377 208.188 1.00 80.22  ? 4376 TRP A N     1 
ATOM   20799 C  CA    . TRP A 1 4376 ? 249.760 223.394 209.589 1.00 78.73  ? 4376 TRP A CA    1 
ATOM   20800 C  C     . TRP A 1 4376 ? 250.476 222.302 210.366 1.00 77.05  ? 4376 TRP A C     1 
ATOM   20801 O  O     . TRP A 1 4376 ? 250.869 222.516 211.516 1.00 77.74  ? 4376 TRP A O     1 
ATOM   20802 C  CB    . TRP A 1 4376 ? 248.234 223.268 209.702 1.00 73.99  ? 4376 TRP A CB    1 
ATOM   20803 C  CG    . TRP A 1 4376 ? 247.658 221.880 209.534 1.00 79.54  ? 4376 TRP A CG    1 
ATOM   20804 C  CD1   . TRP A 1 4376 ? 246.936 221.421 208.471 1.00 80.46  ? 4376 TRP A CD1   1 
ATOM   20805 C  CD2   . TRP A 1 4376 ? 247.654 220.819 210.503 1.00 80.88  ? 4376 TRP A CD2   1 
ATOM   20806 N  NE1   . TRP A 1 4376 ? 246.543 220.123 208.688 1.00 81.46  ? 4376 TRP A NE1   1 
ATOM   20807 C  CE2   . TRP A 1 4376 ? 246.966 219.733 209.930 1.00 81.68  ? 4376 TRP A CE2   1 
ATOM   20808 C  CE3   . TRP A 1 4376 ? 248.187 220.674 211.787 1.00 78.79  ? 4376 TRP A CE3   1 
ATOM   20809 C  CZ2   . TRP A 1 4376 ? 246.799 218.521 210.595 1.00 77.35  ? 4376 TRP A CZ2   1 
ATOM   20810 C  CZ3   . TRP A 1 4376 ? 248.027 219.468 212.441 1.00 78.03  ? 4376 TRP A CZ3   1 
ATOM   20811 C  CH2   . TRP A 1 4376 ? 247.337 218.410 211.847 1.00 77.28  ? 4376 TRP A CH2   1 
ATOM   20812 N  N     . MET A 1 4377 ? 250.682 221.143 209.739 1.00 71.12  ? 4377 MET A N     1 
ATOM   20813 C  CA    . MET A 1 4377 ? 251.417 220.064 210.385 1.00 71.77  ? 4377 MET A CA    1 
ATOM   20814 C  C     . MET A 1 4377 ? 252.843 220.486 210.718 1.00 74.03  ? 4377 MET A C     1 
ATOM   20815 O  O     . MET A 1 4377 ? 253.324 220.242 211.829 1.00 79.47  ? 4377 MET A O     1 
ATOM   20816 C  CB    . MET A 1 4377 ? 251.408 218.832 209.482 1.00 73.84  ? 4377 MET A CB    1 
ATOM   20817 C  CG    . MET A 1 4377 ? 252.036 217.604 210.089 1.00 75.79  ? 4377 MET A CG    1 
ATOM   20818 S  SD    . MET A 1 4377 ? 251.970 216.199 208.966 1.00 90.34  ? 4377 MET A SD    1 
ATOM   20819 C  CE    . MET A 1 4377 ? 250.223 215.814 209.030 1.00 77.29  ? 4377 MET A CE    1 
ATOM   20820 N  N     . ARG A 1 4378 ? 253.527 221.143 209.779 1.00 75.62  ? 4378 ARG A N     1 
ATOM   20821 C  CA    . ARG A 1 4378 ? 254.907 221.550 210.024 1.00 75.89  ? 4378 ARG A CA    1 
ATOM   20822 C  C     . ARG A 1 4378 ? 255.000 222.632 211.094 1.00 74.29  ? 4378 ARG A C     1 
ATOM   20823 O  O     . ARG A 1 4378 ? 255.857 222.554 211.987 1.00 74.80  ? 4378 ARG A O     1 
ATOM   20824 C  CB    . ARG A 1 4378 ? 255.556 222.032 208.726 1.00 77.71  ? 4378 ARG A CB    1 
ATOM   20825 C  CG    . ARG A 1 4378 ? 255.649 220.975 207.630 1.00 76.45  ? 4378 ARG A CG    1 
ATOM   20826 C  CD    . ARG A 1 4378 ? 256.915 220.121 207.727 1.00 75.90  ? 4378 ARG A CD    1 
ATOM   20827 N  NE    . ARG A 1 4378 ? 257.073 219.468 209.022 1.00 79.07  ? 4378 ARG A NE    1 
ATOM   20828 C  CZ    . ARG A 1 4378 ? 256.605 218.262 209.315 1.00 77.23  ? 4378 ARG A CZ    1 
ATOM   20829 N  NH1   . ARG A 1 4378 ? 255.922 217.552 208.432 1.00 73.03  ? 4378 ARG A NH1   1 
ATOM   20830 N  NH2   . ARG A 1 4378 ? 256.824 217.758 210.526 1.00 73.82  ? 4378 ARG A NH2   1 
ATOM   20831 N  N     . THR A 1 4379 ? 254.137 223.650 211.027 1.00 71.05  ? 4379 THR A N     1 
ATOM   20832 C  CA    . THR A 1 4379 ? 254.215 224.707 212.031 1.00 72.42  ? 4379 THR A CA    1 
ATOM   20833 C  C     . THR A 1 4379 ? 253.833 224.184 213.412 1.00 71.83  ? 4379 THR A C     1 
ATOM   20834 O  O     . THR A 1 4379 ? 254.444 224.573 214.414 1.00 68.89  ? 4379 THR A O     1 
ATOM   20835 C  CB    . THR A 1 4379 ? 253.351 225.908 211.636 1.00 70.73  ? 4379 THR A CB    1 
ATOM   20836 O  OG1   . THR A 1 4379 ? 253.420 226.902 212.666 1.00 73.47  ? 4379 THR A OG1   1 
ATOM   20837 C  CG2   . THR A 1 4379 ? 251.908 225.513 211.436 1.00 69.71  ? 4379 THR A CG2   1 
ATOM   20838 N  N     . LEU A 1 4380 ? 252.849 223.281 213.489 1.00 66.43  ? 4380 LEU A N     1 
ATOM   20839 C  CA    . LEU A 1 4380 ? 252.495 222.691 214.775 1.00 64.20  ? 4380 LEU A CA    1 
ATOM   20840 C  C     . LEU A 1 4380 ? 253.612 221.803 215.303 1.00 61.90  ? 4380 LEU A C     1 
ATOM   20841 O  O     . LEU A 1 4380 ? 253.858 221.766 216.511 1.00 69.97  ? 4380 LEU A O     1 
ATOM   20842 C  CB    . LEU A 1 4380 ? 251.196 221.901 214.654 1.00 62.28  ? 4380 LEU A CB    1 
ATOM   20843 C  CG    . LEU A 1 4380 ? 250.674 221.323 215.970 1.00 65.01  ? 4380 LEU A CG    1 
ATOM   20844 C  CD1   . LEU A 1 4380 ? 250.363 222.431 216.961 1.00 66.89  ? 4380 LEU A CD1   1 
ATOM   20845 C  CD2   . LEU A 1 4380 ? 249.458 220.457 215.729 1.00 65.90  ? 4380 LEU A CD2   1 
ATOM   20846 N  N     . HIS A 1 4381 ? 254.294 221.072 214.418 1.00 58.22  ? 4381 HIS A N     1 
ATOM   20847 C  CA    . HIS A 1 4381 ? 255.434 220.273 214.850 1.00 60.88  ? 4381 HIS A CA    1 
ATOM   20848 C  C     . HIS A 1 4381 ? 256.522 221.154 215.445 1.00 63.95  ? 4381 HIS A C     1 
ATOM   20849 O  O     . HIS A 1 4381 ? 257.057 220.854 216.521 1.00 63.24  ? 4381 HIS A O     1 
ATOM   20850 C  CB    . HIS A 1 4381 ? 255.978 219.468 213.671 1.00 62.89  ? 4381 HIS A CB    1 
ATOM   20851 C  CG    . HIS A 1 4381 ? 257.156 218.612 214.013 1.00 64.84  ? 4381 HIS A CG    1 
ATOM   20852 N  ND1   . HIS A 1 4381 ? 258.434 219.115 214.125 1.00 64.26  ? 4381 HIS A ND1   1 
ATOM   20853 C  CD2   . HIS A 1 4381 ? 257.252 217.285 214.260 1.00 67.21  ? 4381 HIS A CD2   1 
ATOM   20854 C  CE1   . HIS A 1 4381 ? 259.265 218.135 214.432 1.00 65.01  ? 4381 HIS A CE1   1 
ATOM   20855 N  NE2   . HIS A 1 4381 ? 258.573 217.014 214.519 1.00 66.05  ? 4381 HIS A NE2   1 
ATOM   20856 N  N     . THR A 1 4382 ? 256.852 222.254 214.765 1.00 68.20  ? 4382 THR A N     1 
ATOM   20857 C  CA    . THR A 1 4382 ? 257.864 223.165 215.292 1.00 65.59  ? 4382 THR A CA    1 
ATOM   20858 C  C     . THR A 1 4382 ? 257.428 223.762 216.625 1.00 65.72  ? 4382 THR A C     1 
ATOM   20859 O  O     . THR A 1 4382 ? 258.221 223.829 217.573 1.00 67.55  ? 4382 THR A O     1 
ATOM   20860 C  CB    . THR A 1 4382 ? 258.151 224.274 214.281 1.00 66.92  ? 4382 THR A CB    1 
ATOM   20861 O  OG1   . THR A 1 4382 ? 258.428 223.695 213.000 1.00 67.49  ? 4382 THR A OG1   1 
ATOM   20862 C  CG2   . THR A 1 4382 ? 259.347 225.098 214.725 1.00 67.38  ? 4382 THR A CG2   1 
ATOM   20863 N  N     . THR A 1 4383 ? 256.164 224.183 216.718 1.00 61.97  ? 4383 THR A N     1 
ATOM   20864 C  CA    . THR A 1 4383 ? 255.660 224.785 217.947 1.00 59.54  ? 4383 THR A CA    1 
ATOM   20865 C  C     . THR A 1 4383 ? 255.711 223.799 219.107 1.00 61.01  ? 4383 THR A C     1 
ATOM   20866 O  O     . THR A 1 4383 ? 256.131 224.147 220.216 1.00 58.92  ? 4383 THR A O     1 
ATOM   20867 C  CB    . THR A 1 4383 ? 254.230 225.281 217.728 1.00 54.96  ? 4383 THR A CB    1 
ATOM   20868 O  OG1   . THR A 1 4383 ? 254.188 226.119 216.567 1.00 61.00  ? 4383 THR A OG1   1 
ATOM   20869 C  CG2   . THR A 1 4383 ? 253.756 226.071 218.924 1.00 57.88  ? 4383 THR A CG2   1 
ATOM   20870 N  N     . ALA A 1 4384 ? 255.289 222.556 218.867 1.00 63.71  ? 4384 ALA A N     1 
ATOM   20871 C  CA    . ALA A 1 4384 ? 255.267 221.562 219.932 1.00 58.57  ? 4384 ALA A CA    1 
ATOM   20872 C  C     . ALA A 1 4384 ? 256.676 221.166 220.351 1.00 61.32  ? 4384 ALA A C     1 
ATOM   20873 O  O     . ALA A 1 4384 ? 256.931 220.945 221.539 1.00 67.79  ? 4384 ALA A O     1 
ATOM   20874 C  CB    . ALA A 1 4384 ? 254.468 220.338 219.491 1.00 58.13  ? 4384 ALA A CB    1 
ATOM   20875 N  N     . SER A 1 4385 ? 257.606 221.068 219.397 1.00 60.73  ? 4385 SER A N     1 
ATOM   20876 C  CA    . SER A 1 4385 ? 258.991 220.785 219.763 1.00 59.80  ? 4385 SER A CA    1 
ATOM   20877 C  C     . SER A 1 4385 ? 259.575 221.909 220.610 1.00 63.23  ? 4385 SER A C     1 
ATOM   20878 O  O     . SER A 1 4385 ? 260.256 221.656 221.614 1.00 65.62  ? 4385 SER A O     1 
ATOM   20879 C  CB    . SER A 1 4385 ? 259.831 220.566 218.505 1.00 60.33  ? 4385 SER A CB    1 
ATOM   20880 O  OG    . SER A 1 4385 ? 259.263 219.563 217.683 1.00 61.78  ? 4385 SER A OG    1 
ATOM   20881 N  N     . ASN A 1 4386 ? 259.307 223.161 220.226 1.00 62.66  ? 4386 ASN A N     1 
ATOM   20882 C  CA    . ASN A 1 4386 ? 259.793 224.292 221.009 1.00 59.90  ? 4386 ASN A CA    1 
ATOM   20883 C  C     . ASN A 1 4386 ? 259.184 224.298 222.405 1.00 63.08  ? 4386 ASN A C     1 
ATOM   20884 O  O     . ASN A 1 4386 ? 259.875 224.589 223.386 1.00 65.79  ? 4386 ASN A O     1 
ATOM   20885 C  CB    . ASN A 1 4386 ? 259.493 225.602 220.283 1.00 61.98  ? 4386 ASN A CB    1 
ATOM   20886 C  CG    . ASN A 1 4386 ? 260.374 225.810 219.065 1.00 70.85  ? 4386 ASN A CG    1 
ATOM   20887 O  OD1   . ASN A 1 4386 ? 261.161 224.938 218.700 1.00 66.97  ? 4386 ASN A OD1   1 
ATOM   20888 N  ND2   . ASN A 1 4386 ? 260.240 226.966 218.425 1.00 68.29  ? 4386 ASN A ND2   1 
ATOM   20889 N  N     . TRP A 1 4387 ? 257.891 223.987 222.513 1.00 64.57  ? 4387 TRP A N     1 
ATOM   20890 C  CA    . TRP A 1 4387 ? 257.254 223.916 223.824 1.00 55.95  ? 4387 TRP A CA    1 
ATOM   20891 C  C     . TRP A 1 4387 ? 257.859 222.811 224.677 1.00 55.70  ? 4387 TRP A C     1 
ATOM   20892 O  O     . TRP A 1 4387 ? 258.131 223.015 225.865 1.00 61.12  ? 4387 TRP A O     1 
ATOM   20893 C  CB    . TRP A 1 4387 ? 255.751 223.705 223.666 1.00 54.84  ? 4387 TRP A CB    1 
ATOM   20894 C  CG    . TRP A 1 4387 ? 255.025 224.940 223.270 1.00 54.40  ? 4387 TRP A CG    1 
ATOM   20895 C  CD1   . TRP A 1 4387 ? 255.480 226.219 223.365 1.00 57.00  ? 4387 TRP A CD1   1 
ATOM   20896 C  CD2   . TRP A 1 4387 ? 253.713 225.020 222.708 1.00 56.59  ? 4387 TRP A CD2   1 
ATOM   20897 N  NE1   . TRP A 1 4387 ? 254.531 227.094 222.899 1.00 59.98  ? 4387 TRP A NE1   1 
ATOM   20898 C  CE2   . TRP A 1 4387 ? 253.436 226.381 222.490 1.00 58.67  ? 4387 TRP A CE2   1 
ATOM   20899 C  CE3   . TRP A 1 4387 ? 252.744 224.072 222.370 1.00 58.52  ? 4387 TRP A CE3   1 
ATOM   20900 C  CZ2   . TRP A 1 4387 ? 252.232 226.819 221.952 1.00 61.92  ? 4387 TRP A CZ2   1 
ATOM   20901 C  CZ3   . TRP A 1 4387 ? 251.552 224.508 221.834 1.00 57.66  ? 4387 TRP A CZ3   1 
ATOM   20902 C  CH2   . TRP A 1 4387 ? 251.307 225.868 221.626 1.00 58.66  ? 4387 TRP A CH2   1 
ATOM   20903 N  N     . LEU A 1 4388 ? 258.083 221.634 224.089 1.00 56.64  ? 4388 LEU A N     1 
ATOM   20904 C  CA    . LEU A 1 4388 ? 258.690 220.539 224.837 1.00 56.54  ? 4388 LEU A CA    1 
ATOM   20905 C  C     . LEU A 1 4388 ? 260.077 220.909 225.331 1.00 59.60  ? 4388 LEU A C     1 
ATOM   20906 O  O     . LEU A 1 4388 ? 260.461 220.531 226.444 1.00 63.42  ? 4388 LEU A O     1 
ATOM   20907 C  CB    . LEU A 1 4388 ? 258.755 219.281 223.973 1.00 57.33  ? 4388 LEU A CB    1 
ATOM   20908 C  CG    . LEU A 1 4388 ? 257.500 218.413 223.930 1.00 55.29  ? 4388 LEU A CG    1 
ATOM   20909 C  CD1   . LEU A 1 4388 ? 257.650 217.321 222.888 1.00 61.38  ? 4388 LEU A CD1   1 
ATOM   20910 C  CD2   . LEU A 1 4388 ? 257.218 217.815 225.295 1.00 57.20  ? 4388 LEU A CD2   1 
ATOM   20911 N  N     . HIS A 1 4389 ? 260.847 221.636 224.520 1.00 69.38  ? 4389 HIS A N     1 
ATOM   20912 C  CA    . HIS A 1 4389 ? 262.136 222.129 224.995 1.00 69.64  ? 4389 HIS A CA    1 
ATOM   20913 C  C     . HIS A 1 4389 ? 261.961 223.151 226.114 1.00 68.81  ? 4389 HIS A C     1 
ATOM   20914 O  O     . HIS A 1 4389 ? 262.734 223.164 227.078 1.00 70.42  ? 4389 HIS A O     1 
ATOM   20915 C  CB    . HIS A 1 4389 ? 262.931 222.731 223.839 1.00 66.31  ? 4389 HIS A CB    1 
ATOM   20916 C  CG    . HIS A 1 4389 ? 264.255 223.293 224.249 1.00 73.95  ? 4389 HIS A CG    1 
ATOM   20917 N  ND1   . HIS A 1 4389 ? 265.349 222.500 224.520 1.00 74.38  ? 4389 HIS A ND1   1 
ATOM   20918 C  CD2   . HIS A 1 4389 ? 264.660 224.571 224.440 1.00 72.57  ? 4389 HIS A CD2   1 
ATOM   20919 C  CE1   . HIS A 1 4389 ? 266.372 223.265 224.858 1.00 74.80  ? 4389 HIS A CE1   1 
ATOM   20920 N  NE2   . HIS A 1 4389 ? 265.980 224.526 224.817 1.00 73.54  ? 4389 HIS A NE2   1 
ATOM   20921 N  N     . LEU A 1 4390 ? 260.951 224.017 226.000 1.00 60.62  ? 4390 LEU A N     1 
ATOM   20922 C  CA    . LEU A 1 4390 ? 260.759 225.085 226.977 1.00 61.68  ? 4390 LEU A CA    1 
ATOM   20923 C  C     . LEU A 1 4390 ? 260.329 224.537 228.333 1.00 63.84  ? 4390 LEU A C     1 
ATOM   20924 O  O     . LEU A 1 4390 ? 260.907 224.890 229.368 1.00 65.91  ? 4390 LEU A O     1 
ATOM   20925 C  CB    . LEU A 1 4390 ? 259.728 226.083 226.451 1.00 62.99  ? 4390 LEU A CB    1 
ATOM   20926 C  CG    . LEU A 1 4390 ? 259.428 227.316 227.303 1.00 63.66  ? 4390 LEU A CG    1 
ATOM   20927 C  CD1   . LEU A 1 4390 ? 260.667 228.180 227.457 1.00 66.03  ? 4390 LEU A CD1   1 
ATOM   20928 C  CD2   . LEU A 1 4390 ? 258.288 228.114 226.695 1.00 63.62  ? 4390 LEU A CD2   1 
ATOM   20929 N  N     . ILE A 1 4391 ? 259.317 223.678 228.348 1.00 58.79  ? 4391 ILE A N     1 
ATOM   20930 C  CA    . ILE A 1 4391 ? 258.754 223.182 229.611 1.00 53.37  ? 4391 ILE A CA    1 
ATOM   20931 C  C     . ILE A 1 4391 ? 259.772 222.278 230.296 1.00 53.81  ? 4391 ILE A C     1 
ATOM   20932 O  O     . ILE A 1 4391 ? 260.444 221.485 229.613 1.00 59.31  ? 4391 ILE A O     1 
ATOM   20933 C  CB    . ILE A 1 4391 ? 257.440 222.443 229.346 1.00 52.09  ? 4391 ILE A CB    1 
ATOM   20934 C  CG1   . ILE A 1 4391 ? 256.507 223.308 228.501 1.00 54.78  ? 4391 ILE A CG1   1 
ATOM   20935 C  CG2   . ILE A 1 4391 ? 256.740 222.106 230.638 1.00 55.89  ? 4391 ILE A CG2   1 
ATOM   20936 C  CD1   . ILE A 1 4391 ? 255.215 222.624 228.132 1.00 53.91  ? 4391 ILE A CD1   1 
ATOM   20937 N  N     . PRO A 1 4392 ? 259.937 222.365 231.618 1.00 55.40  ? 4392 PRO A N     1 
ATOM   20938 C  CA    . PRO A 1 4392 ? 260.931 221.523 232.296 1.00 57.03  ? 4392 PRO A CA    1 
ATOM   20939 C  C     . PRO A 1 4392 ? 260.650 220.041 232.107 1.00 53.29  ? 4392 PRO A C     1 
ATOM   20940 O  O     . PRO A 1 4392 ? 259.503 219.610 231.979 1.00 57.32  ? 4392 PRO A O     1 
ATOM   20941 C  CB    . PRO A 1 4392 ? 260.798 221.936 233.765 1.00 53.56  ? 4392 PRO A CB    1 
ATOM   20942 C  CG    . PRO A 1 4392 ? 260.300 223.333 233.706 1.00 56.33  ? 4392 PRO A CG    1 
ATOM   20943 C  CD    . PRO A 1 4392 ? 259.382 223.389 232.520 1.00 52.34  ? 4392 PRO A CD    1 
ATOM   20944 N  N     . GLN A 1 4393 ? 261.729 219.258 232.080 1.00 56.93  ? 4393 GLN A N     1 
ATOM   20945 C  CA    . GLN A 1 4393 ? 261.618 217.842 231.745 1.00 61.32  ? 4393 GLN A CA    1 
ATOM   20946 C  C     . GLN A 1 4393 ? 260.905 217.057 232.839 1.00 59.98  ? 4393 GLN A C     1 
ATOM   20947 O  O     . GLN A 1 4393 ? 259.987 216.278 232.558 1.00 61.52  ? 4393 GLN A O     1 
ATOM   20948 C  CB    . GLN A 1 4393 ? 263.006 217.258 231.483 1.00 62.24  ? 4393 GLN A CB    1 
ATOM   20949 C  CG    . GLN A 1 4393 ? 263.861 218.095 230.550 1.00 62.11  ? 4393 GLN A CG    1 
ATOM   20950 C  CD    . GLN A 1 4393 ? 263.800 217.610 229.119 1.00 64.41  ? 4393 GLN A CD    1 
ATOM   20951 O  OE1   . GLN A 1 4393 ? 263.786 216.408 228.859 1.00 60.79  ? 4393 GLN A OE1   1 
ATOM   20952 N  NE2   . GLN A 1 4393 ? 263.760 218.546 228.178 1.00 62.82  ? 4393 GLN A NE2   1 
ATOM   20953 N  N     . THR A 1 4394 ? 261.310 217.244 234.094 1.00 57.89  ? 4394 THR A N     1 
ATOM   20954 C  CA    . THR A 1 4394 ? 260.813 216.410 235.178 1.00 64.07  ? 4394 THR A CA    1 
ATOM   20955 C  C     . THR A 1 4394 ? 260.625 217.240 236.439 1.00 63.74  ? 4394 THR A C     1 
ATOM   20956 O  O     . THR A 1 4394 ? 261.172 218.336 236.579 1.00 67.79  ? 4394 THR A O     1 
ATOM   20957 C  CB    . THR A 1 4394 ? 261.756 215.233 235.464 1.00 65.94  ? 4394 THR A CB    1 
ATOM   20958 O  OG1   . THR A 1 4394 ? 261.075 214.258 236.263 1.00 66.17  ? 4394 THR A OG1   1 
ATOM   20959 C  CG2   . THR A 1 4394 ? 263.000 215.708 236.197 1.00 62.16  ? 4394 THR A CG2   1 
ATOM   20960 N  N     . LEU A 1 4395 ? 259.831 216.693 237.359 1.00 52.77  ? 4395 LEU A N     1 
ATOM   20961 C  CA    . LEU A 1 4395 ? 259.549 217.322 238.644 1.00 50.99  ? 4395 LEU A CA    1 
ATOM   20962 C  C     . LEU A 1 4395 ? 259.513 216.234 239.705 1.00 51.53  ? 4395 LEU A C     1 
ATOM   20963 O  O     . LEU A 1 4395 ? 258.689 215.318 239.626 1.00 56.11  ? 4395 LEU A O     1 
ATOM   20964 C  CB    . LEU A 1 4395 ? 258.225 218.090 238.602 1.00 50.43  ? 4395 LEU A CB    1 
ATOM   20965 C  CG    . LEU A 1 4395 ? 257.801 218.838 239.864 1.00 42.47  ? 4395 LEU A CG    1 
ATOM   20966 C  CD1   . LEU A 1 4395 ? 258.931 219.706 240.376 1.00 49.30  ? 4395 LEU A CD1   1 
ATOM   20967 C  CD2   . LEU A 1 4395 ? 256.572 219.678 239.580 1.00 46.37  ? 4395 LEU A CD2   1 
ATOM   20968 N  N     . SER A 1 4396 ? 260.400 216.332 240.691 1.00 51.36  ? 4396 SER A N     1 
ATOM   20969 C  CA    . SER A 1 4396 ? 260.589 215.273 241.674 1.00 54.65  ? 4396 SER A CA    1 
ATOM   20970 C  C     . SER A 1 4396 ? 259.643 215.458 242.853 1.00 53.16  ? 4396 SER A C     1 
ATOM   20971 O  O     . SER A 1 4396 ? 259.515 216.563 243.386 1.00 59.01  ? 4396 SER A O     1 
ATOM   20972 C  CB    . SER A 1 4396 ? 262.038 215.252 242.163 1.00 53.33  ? 4396 SER A CB    1 
ATOM   20973 O  OG    . SER A 1 4396 ? 262.934 215.005 241.094 1.00 57.47  ? 4396 SER A OG    1 
ATOM   20974 N  N     . HIS A 1 4397 ? 258.995 214.370 243.261 1.00 49.09  ? 4397 HIS A N     1 
ATOM   20975 C  CA    . HIS A 1 4397 ? 258.087 214.409 244.398 1.00 53.31  ? 4397 HIS A CA    1 
ATOM   20976 C  C     . HIS A 1 4397 ? 258.849 214.679 245.691 1.00 54.43  ? 4397 HIS A C     1 
ATOM   20977 O  O     . HIS A 1 4397 ? 260.037 214.373 245.815 1.00 52.92  ? 4397 HIS A O     1 
ATOM   20978 C  CB    . HIS A 1 4397 ? 257.322 213.092 244.521 1.00 49.28  ? 4397 HIS A CB    1 
ATOM   20979 C  CG    . HIS A 1 4397 ? 256.194 212.951 243.549 1.00 52.32  ? 4397 HIS A CG    1 
ATOM   20980 N  ND1   . HIS A 1 4397 ? 255.292 211.911 243.604 1.00 51.49  ? 4397 HIS A ND1   1 
ATOM   20981 C  CD2   . HIS A 1 4397 ? 255.821 213.715 242.496 1.00 54.11  ? 4397 HIS A CD2   1 
ATOM   20982 C  CE1   . HIS A 1 4397 ? 254.412 212.041 242.628 1.00 53.23  ? 4397 HIS A CE1   1 
ATOM   20983 N  NE2   . HIS A 1 4397 ? 254.711 213.128 241.940 1.00 53.60  ? 4397 HIS A NE2   1 
ATOM   20984 N  N     . LEU A 1 4398 ? 258.149 215.262 246.661 1.00 54.97  ? 4398 LEU A N     1 
ATOM   20985 C  CA    . LEU A 1 4398 ? 258.743 215.507 247.968 1.00 56.24  ? 4398 LEU A CA    1 
ATOM   20986 C  C     . LEU A 1 4398 ? 258.799 214.213 248.770 1.00 60.91  ? 4398 LEU A C     1 
ATOM   20987 O  O     . LEU A 1 4398 ? 257.804 213.490 248.872 1.00 60.58  ? 4398 LEU A O     1 
ATOM   20988 C  CB    . LEU A 1 4398 ? 257.946 216.567 248.727 1.00 57.05  ? 4398 LEU A CB    1 
ATOM   20989 C  CG    . LEU A 1 4398 ? 258.016 217.991 248.179 1.00 54.65  ? 4398 LEU A CG    1 
ATOM   20990 C  CD1   . LEU A 1 4398 ? 257.600 218.992 249.238 1.00 50.86  ? 4398 LEU A CD1   1 
ATOM   20991 C  CD2   . LEU A 1 4398 ? 259.411 218.293 247.679 1.00 58.24  ? 4398 LEU A CD2   1 
ATOM   20992 N  N     . LYS A 1 4399 ? 259.964 213.926 249.343 1.00 65.40  ? 4399 LYS A N     1 
ATOM   20993 C  CA    . LYS A 1 4399 ? 260.153 212.679 250.072 1.00 63.31  ? 4399 LYS A CA    1 
ATOM   20994 C  C     . LYS A 1 4399 ? 259.401 212.725 251.397 1.00 64.86  ? 4399 LYS A C     1 
ATOM   20995 O  O     . LYS A 1 4399 ? 259.587 213.645 252.199 1.00 64.71  ? 4399 LYS A O     1 
ATOM   20996 C  CB    . LYS A 1 4399 ? 261.646 212.425 250.293 1.00 66.20  ? 4399 LYS A CB    1 
ATOM   20997 C  CG    . LYS A 1 4399 ? 261.994 211.134 251.032 1.00 67.08  ? 4399 LYS A CG    1 
ATOM   20998 C  CD    . LYS A 1 4399 ? 262.153 211.340 252.533 1.00 68.86  ? 4399 LYS A CD    1 
ATOM   20999 C  CE    . LYS A 1 4399 ? 263.416 212.129 252.846 1.00 69.14  ? 4399 LYS A CE    1 
ATOM   21000 N  NZ    . LYS A 1 4399 ? 263.605 212.335 254.308 1.00 66.86  ? 4399 LYS A NZ    1 
ATOM   21001 N  N     . ARG A 1 4400 ? 258.557 211.723 251.626 1.00 66.76  ? 4400 ARG A N     1 
ATOM   21002 C  CA    . ARG A 1 4400 ? 257.735 211.654 252.825 1.00 64.99  ? 4400 ARG A CA    1 
ATOM   21003 C  C     . ARG A 1 4400 ? 258.530 211.070 253.985 1.00 70.59  ? 4400 ARG A C     1 
ATOM   21004 O  O     . ARG A 1 4400 ? 259.246 210.078 253.829 1.00 72.62  ? 4400 ARG A O     1 
ATOM   21005 C  CB    . ARG A 1 4400 ? 256.489 210.805 252.572 1.00 67.77  ? 4400 ARG A CB    1 
ATOM   21006 C  CG    . ARG A 1 4400 ? 255.300 211.583 252.046 1.00 67.34  ? 4400 ARG A CG    1 
ATOM   21007 C  CD    . ARG A 1 4400 ? 254.013 210.800 252.221 1.00 66.34  ? 4400 ARG A CD    1 
ATOM   21008 N  NE    . ARG A 1 4400 ? 252.836 211.653 252.106 1.00 70.86  ? 4400 ARG A NE    1 
ATOM   21009 C  CZ    . ARG A 1 4400 ? 251.655 211.376 252.641 1.00 72.48  ? 4400 ARG A CZ    1 
ATOM   21010 N  NH1   . ARG A 1 4400 ? 251.456 210.272 253.343 1.00 69.63  ? 4400 ARG A NH1   1 
ATOM   21011 N  NH2   . ARG A 1 4400 ? 250.649 212.228 252.470 1.00 68.54  ? 4400 ARG A NH2   1 
ATOM   21012 N  N     . THR A 1 4401 ? 258.392 211.693 255.151 1.00 78.02  ? 4401 THR A N     1 
ATOM   21013 C  CA    . THR A 1 4401 ? 259.068 211.262 256.364 1.00 78.46  ? 4401 THR A CA    1 
ATOM   21014 C  C     . THR A 1 4401 ? 258.056 211.257 257.502 1.00 76.21  ? 4401 THR A C     1 
ATOM   21015 O  O     . THR A 1 4401 ? 257.005 211.897 257.422 1.00 79.69  ? 4401 THR A O     1 
ATOM   21016 C  CB    . THR A 1 4401 ? 260.263 212.177 256.693 1.00 76.35  ? 4401 THR A CB    1 
ATOM   21017 O  OG1   . THR A 1 4401 ? 261.016 212.422 255.500 1.00 75.21  ? 4401 THR A OG1   1 
ATOM   21018 C  CG2   . THR A 1 4401 ? 261.185 211.530 257.715 1.00 73.38  ? 4401 THR A CG2   1 
ATOM   21019 N  N     . VAL A 1 4402 ? 258.377 210.514 258.564 1.00 81.03  ? 4402 VAL A N     1 
ATOM   21020 C  CA    . VAL A 1 4402 ? 257.469 210.408 259.703 1.00 82.88  ? 4402 VAL A CA    1 
ATOM   21021 C  C     . VAL A 1 4402 ? 257.211 211.780 260.311 1.00 85.10  ? 4402 VAL A C     1 
ATOM   21022 O  O     . VAL A 1 4402 ? 256.069 212.128 260.635 1.00 85.87  ? 4402 VAL A O     1 
ATOM   21023 C  CB    . VAL A 1 4402 ? 258.034 209.423 260.742 1.00 83.10  ? 4402 VAL A CB    1 
ATOM   21024 C  CG1   . VAL A 1 4402 ? 257.188 209.435 262.005 1.00 82.10  ? 4402 VAL A CG1   1 
ATOM   21025 C  CG2   . VAL A 1 4402 ? 258.112 208.023 260.156 1.00 80.81  ? 4402 VAL A CG2   1 
ATOM   21026 N  N     . GLU A 1 4403 ? 258.263 212.584 260.469 1.00 81.36  ? 4403 GLU A N     1 
ATOM   21027 C  CA    . GLU A 1 4403 ? 258.104 213.931 260.998 1.00 81.07  ? 4403 GLU A CA    1 
ATOM   21028 C  C     . GLU A 1 4403 ? 257.623 214.924 259.948 1.00 82.34  ? 4403 GLU A C     1 
ATOM   21029 O  O     . GLU A 1 4403 ? 257.201 216.028 260.308 1.00 85.99  ? 4403 GLU A O     1 
ATOM   21030 C  CB    . GLU A 1 4403 ? 259.424 214.415 261.604 1.00 79.33  ? 4403 GLU A CB    1 
ATOM   21031 C  CG    . GLU A 1 4403 ? 260.488 214.771 260.581 1.00 81.97  ? 4403 GLU A CG    1 
ATOM   21032 C  CD    . GLU A 1 4403 ? 261.601 213.742 260.516 1.00 87.18  ? 4403 GLU A CD    1 
ATOM   21033 O  OE1   . GLU A 1 4403 ? 261.443 212.654 261.108 1.00 85.29  ? 4403 GLU A OE1   1 
ATOM   21034 O  OE2   . GLU A 1 4403 ? 262.636 214.023 259.876 1.00 87.17  ? 4403 GLU A OE2   1 
ATOM   21035 N  N     . ASN A 1 4404 ? 257.679 214.563 258.666 1.00 71.97  ? 4404 ASN A N     1 
ATOM   21036 C  CA    . ASN A 1 4404 ? 257.206 215.455 257.614 1.00 67.59  ? 4404 ASN A CA    1 
ATOM   21037 C  C     . ASN A 1 4404 ? 255.687 215.471 257.501 1.00 66.66  ? 4404 ASN A C     1 
ATOM   21038 O  O     . ASN A 1 4404 ? 255.114 216.496 257.117 1.00 73.50  ? 4404 ASN A O     1 
ATOM   21039 C  CB    . ASN A 1 4404 ? 257.818 215.057 256.270 1.00 67.93  ? 4404 ASN A CB    1 
ATOM   21040 C  CG    . ASN A 1 4404 ? 259.209 215.613 256.078 1.00 70.16  ? 4404 ASN A CG    1 
ATOM   21041 O  OD1   . ASN A 1 4404 ? 259.652 216.481 256.829 1.00 72.96  ? 4404 ASN A OD1   1 
ATOM   21042 N  ND2   . ASN A 1 4404 ? 259.908 215.120 255.064 1.00 68.76  ? 4404 ASN A ND2   1 
ATOM   21043 N  N     . ILE A 1 4405 ? 255.024 214.359 257.825 1.00 66.68  ? 4405 ILE A N     1 
ATOM   21044 C  CA    . ILE A 1 4405 ? 253.587 214.244 257.585 1.00 71.35  ? 4405 ILE A CA    1 
ATOM   21045 C  C     . ILE A 1 4405 ? 252.814 215.281 258.390 1.00 73.08  ? 4405 ILE A C     1 
ATOM   21046 O  O     . ILE A 1 4405 ? 251.889 215.921 257.878 1.00 70.80  ? 4405 ILE A O     1 
ATOM   21047 C  CB    . ILE A 1 4405 ? 253.107 212.815 257.899 1.00 75.63  ? 4405 ILE A CB    1 
ATOM   21048 C  CG1   . ILE A 1 4405 ? 253.848 211.804 257.029 1.00 70.76  ? 4405 ILE A CG1   1 
ATOM   21049 C  CG2   . ILE A 1 4405 ? 251.605 212.697 257.692 1.00 74.58  ? 4405 ILE A CG2   1 
ATOM   21050 C  CD1   . ILE A 1 4405 ? 253.622 212.009 255.557 1.00 67.83  ? 4405 ILE A CD1   1 
ATOM   21051 N  N     . LYS A 1 4406 ? 253.177 215.465 259.660 1.00 69.74  ? 4406 LYS A N     1 
ATOM   21052 C  CA    . LYS A 1 4406 ? 252.425 216.371 260.520 1.00 67.89  ? 4406 LYS A CA    1 
ATOM   21053 C  C     . LYS A 1 4406 ? 252.626 217.837 260.156 1.00 67.69  ? 4406 LYS A C     1 
ATOM   21054 O  O     . LYS A 1 4406 ? 251.803 218.673 260.543 1.00 67.51  ? 4406 LYS A O     1 
ATOM   21055 C  CB    . LYS A 1 4406 ? 252.807 216.142 261.982 1.00 72.27  ? 4406 LYS A CB    1 
ATOM   21056 C  CG    . LYS A 1 4406 ? 252.618 214.709 262.455 1.00 71.89  ? 4406 LYS A CG    1 
ATOM   21057 C  CD    . LYS A 1 4406 ? 253.149 214.516 263.866 1.00 69.84  ? 4406 LYS A CD    1 
ATOM   21058 C  CE    . LYS A 1 4406 ? 253.711 213.119 264.062 1.00 71.02  ? 4406 LYS A CE    1 
ATOM   21059 N  NZ    . LYS A 1 4406 ? 254.514 212.672 262.890 1.00 72.98  ? 4406 LYS A NZ    1 
ATOM   21060 N  N     . ASP A 1 4407 ? 253.684 218.167 259.428 1.00 60.56  ? 4407 ASP A N     1 
ATOM   21061 C  CA    . ASP A 1 4407 ? 253.959 219.557 259.071 1.00 57.46  ? 4407 ASP A CA    1 
ATOM   21062 C  C     . ASP A 1 4407 ? 252.926 220.063 258.072 1.00 59.78  ? 4407 ASP A C     1 
ATOM   21063 O  O     . ASP A 1 4407 ? 252.704 219.412 257.043 1.00 61.70  ? 4407 ASP A O     1 
ATOM   21064 C  CB    . ASP A 1 4407 ? 255.367 219.679 258.494 1.00 57.06  ? 4407 ASP A CB    1 
ATOM   21065 C  CG    . ASP A 1 4407 ? 255.902 221.100 258.544 1.00 65.39  ? 4407 ASP A CG    1 
ATOM   21066 O  OD1   . ASP A 1 4407 ? 255.148 222.041 258.227 1.00 65.60  ? 4407 ASP A OD1   1 
ATOM   21067 O  OD2   . ASP A 1 4407 ? 257.083 221.277 258.906 1.00 64.71  ? 4407 ASP A OD2   1 
ATOM   21068 N  N     . PRO A 1 4408 ? 252.272 221.201 258.326 1.00 55.52  ? 4408 PRO A N     1 
ATOM   21069 C  CA    . PRO A 1 4408 ? 251.314 221.719 257.337 1.00 53.71  ? 4408 PRO A CA    1 
ATOM   21070 C  C     . PRO A 1 4408 ? 251.978 222.307 256.106 1.00 52.25  ? 4408 PRO A C     1 
ATOM   21071 O  O     . PRO A 1 4408 ? 251.462 222.134 254.994 1.00 56.28  ? 4408 PRO A O     1 
ATOM   21072 C  CB    . PRO A 1 4408 ? 250.541 222.784 258.126 1.00 47.15  ? 4408 PRO A CB    1 
ATOM   21073 C  CG    . PRO A 1 4408 ? 251.482 223.212 259.194 1.00 44.69  ? 4408 PRO A CG    1 
ATOM   21074 C  CD    . PRO A 1 4408 ? 252.279 221.998 259.564 1.00 50.72  ? 4408 PRO A CD    1 
ATOM   21075 N  N     . LEU A 1 4409 ? 253.106 223.004 256.268 1.00 46.45  ? 4409 LEU A N     1 
ATOM   21076 C  CA    . LEU A 1 4409 ? 253.809 223.545 255.111 1.00 43.60  ? 4409 LEU A CA    1 
ATOM   21077 C  C     . LEU A 1 4409 ? 254.317 222.431 254.207 1.00 52.26  ? 4409 LEU A C     1 
ATOM   21078 O  O     . LEU A 1 4409 ? 254.217 222.526 252.976 1.00 60.53  ? 4409 LEU A O     1 
ATOM   21079 C  CB    . LEU A 1 4409 ? 254.964 224.434 255.567 1.00 43.16  ? 4409 LEU A CB    1 
ATOM   21080 C  CG    . LEU A 1 4409 ? 254.611 225.892 255.864 1.00 51.72  ? 4409 LEU A CG    1 
ATOM   21081 C  CD1   . LEU A 1 4409 ? 255.852 226.673 256.251 1.00 50.59  ? 4409 LEU A CD1   1 
ATOM   21082 C  CD2   . LEU A 1 4409 ? 253.923 226.531 254.672 1.00 53.27  ? 4409 LEU A CD2   1 
ATOM   21083 N  N     . PHE A 1 4410 ? 254.860 221.363 254.796 1.00 54.33  ? 4410 PHE A N     1 
ATOM   21084 C  CA    . PHE A 1 4410 ? 255.304 220.239 253.983 1.00 48.65  ? 4410 PHE A CA    1 
ATOM   21085 C  C     . PHE A 1 4410 ? 254.137 219.590 253.259 1.00 53.31  ? 4410 PHE A C     1 
ATOM   21086 O  O     . PHE A 1 4410 ? 254.270 219.196 252.100 1.00 63.51  ? 4410 PHE A O     1 
ATOM   21087 C  CB    . PHE A 1 4410 ? 256.030 219.195 254.827 1.00 51.66  ? 4410 PHE A CB    1 
ATOM   21088 C  CG    . PHE A 1 4410 ? 256.371 217.947 254.060 1.00 54.90  ? 4410 PHE A CG    1 
ATOM   21089 C  CD1   . PHE A 1 4410 ? 257.503 217.897 253.266 1.00 56.41  ? 4410 PHE A CD1   1 
ATOM   21090 C  CD2   . PHE A 1 4410 ? 255.544 216.837 254.107 1.00 53.51  ? 4410 PHE A CD2   1 
ATOM   21091 C  CE1   . PHE A 1 4410 ? 257.812 216.760 252.550 1.00 55.48  ? 4410 PHE A CE1   1 
ATOM   21092 C  CE2   . PHE A 1 4410 ? 255.849 215.699 253.391 1.00 53.50  ? 4410 PHE A CE2   1 
ATOM   21093 C  CZ    . PHE A 1 4410 ? 256.983 215.661 252.613 1.00 58.13  ? 4410 PHE A CZ    1 
ATOM   21094 N  N     . ARG A 1 4411 ? 252.996 219.442 253.931 1.00 43.55  ? 4411 ARG A N     1 
ATOM   21095 C  CA    . ARG A 1 4411 ? 251.840 218.833 253.283 1.00 43.31  ? 4411 ARG A CA    1 
ATOM   21096 C  C     . ARG A 1 4411 ? 251.359 219.678 252.111 1.00 52.77  ? 4411 ARG A C     1 
ATOM   21097 O  O     . ARG A 1 4411 ? 251.063 219.147 251.030 1.00 60.54  ? 4411 ARG A O     1 
ATOM   21098 C  CB    . ARG A 1 4411 ? 250.723 218.628 254.302 1.00 47.65  ? 4411 ARG A CB    1 
ATOM   21099 C  CG    . ARG A 1 4411 ? 250.880 217.368 255.126 1.00 51.57  ? 4411 ARG A CG    1 
ATOM   21100 C  CD    . ARG A 1 4411 ? 249.572 216.969 255.776 1.00 52.24  ? 4411 ARG A CD    1 
ATOM   21101 N  NE    . ARG A 1 4411 ? 249.042 218.039 256.610 1.00 57.82  ? 4411 ARG A NE    1 
ATOM   21102 C  CZ    . ARG A 1 4411 ? 248.713 217.898 257.886 1.00 61.34  ? 4411 ARG A CZ    1 
ATOM   21103 N  NH1   . ARG A 1 4411 ? 248.826 216.734 258.505 1.00 56.43  ? 4411 ARG A NH1   1 
ATOM   21104 N  NH2   . ARG A 1 4411 ? 248.260 218.952 258.559 1.00 56.58  ? 4411 ARG A NH2   1 
ATOM   21105 N  N     . PHE A 1 4412 ? 251.296 220.999 252.298 1.00 47.80  ? 4412 PHE A N     1 
ATOM   21106 C  CA    . PHE A 1 4412 ? 250.904 221.881 251.204 1.00 44.07  ? 4412 PHE A CA    1 
ATOM   21107 C  C     . PHE A 1 4412 ? 251.868 221.767 250.032 1.00 43.76  ? 4412 PHE A C     1 
ATOM   21108 O  O     . PHE A 1 4412 ? 251.448 221.615 248.878 1.00 48.17  ? 4412 PHE A O     1 
ATOM   21109 C  CB    . PHE A 1 4412 ? 250.835 223.328 251.684 1.00 36.00  ? 4412 PHE A CB    1 
ATOM   21110 C  CG    . PHE A 1 4412 ? 250.894 224.326 250.567 1.00 40.77  ? 4412 PHE A CG    1 
ATOM   21111 C  CD1   . PHE A 1 4412 ? 249.787 224.556 249.771 1.00 42.66  ? 4412 PHE A CD1   1 
ATOM   21112 C  CD2   . PHE A 1 4412 ? 252.061 225.015 250.294 1.00 46.16  ? 4412 PHE A CD2   1 
ATOM   21113 C  CE1   . PHE A 1 4412 ? 249.840 225.463 248.737 1.00 41.31  ? 4412 PHE A CE1   1 
ATOM   21114 C  CE2   . PHE A 1 4412 ? 252.119 225.917 249.258 1.00 45.01  ? 4412 PHE A CE2   1 
ATOM   21115 C  CZ    . PHE A 1 4412 ? 251.007 226.141 248.479 1.00 46.12  ? 4412 PHE A CZ    1 
ATOM   21116 N  N     . PHE A 1 4413 ? 253.172 221.845 250.308 1.00 39.95  ? 4413 PHE A N     1 
ATOM   21117 C  CA    . PHE A 1 4413 ? 254.150 221.797 249.228 1.00 40.15  ? 4413 PHE A CA    1 
ATOM   21118 C  C     . PHE A 1 4413 ? 254.170 220.434 248.549 1.00 48.48  ? 4413 PHE A C     1 
ATOM   21119 O  O     . PHE A 1 4413 ? 254.379 220.354 247.336 1.00 56.68  ? 4413 PHE A O     1 
ATOM   21120 C  CB    . PHE A 1 4413 ? 255.533 222.160 249.760 1.00 45.12  ? 4413 PHE A CB    1 
ATOM   21121 C  CG    . PHE A 1 4413 ? 255.751 223.636 249.906 1.00 45.52  ? 4413 PHE A CG    1 
ATOM   21122 C  CD1   . PHE A 1 4413 ? 255.570 224.482 248.828 1.00 47.72  ? 4413 PHE A CD1   1 
ATOM   21123 C  CD2   . PHE A 1 4413 ? 256.125 224.179 251.120 1.00 46.17  ? 4413 PHE A CD2   1 
ATOM   21124 C  CE1   . PHE A 1 4413 ? 255.766 225.840 248.958 1.00 51.02  ? 4413 PHE A CE1   1 
ATOM   21125 C  CE2   . PHE A 1 4413 ? 256.322 225.536 251.254 1.00 45.63  ? 4413 PHE A CE2   1 
ATOM   21126 C  CZ    . PHE A 1 4413 ? 256.142 226.366 250.172 1.00 49.12  ? 4413 PHE A CZ    1 
ATOM   21127 N  N     . GLU A 1 4414 ? 253.950 219.359 249.307 1.00 43.83  ? 4414 GLU A N     1 
ATOM   21128 C  CA    . GLU A 1 4414 ? 253.883 218.028 248.721 1.00 37.44  ? 4414 GLU A CA    1 
ATOM   21129 C  C     . GLU A 1 4414 ? 252.695 217.900 247.779 1.00 48.74  ? 4414 GLU A C     1 
ATOM   21130 O  O     . GLU A 1 4414 ? 252.825 217.353 246.678 1.00 53.12  ? 4414 GLU A O     1 
ATOM   21131 C  CB    . GLU A 1 4414 ? 253.806 216.981 249.830 1.00 40.81  ? 4414 GLU A CB    1 
ATOM   21132 C  CG    . GLU A 1 4414 ? 253.471 215.588 249.348 1.00 55.05  ? 4414 GLU A CG    1 
ATOM   21133 C  CD    . GLU A 1 4414 ? 252.807 214.750 250.419 1.00 61.72  ? 4414 GLU A CD    1 
ATOM   21134 O  OE1   . GLU A 1 4414 ? 251.874 215.255 251.079 1.00 57.10  ? 4414 GLU A OE1   1 
ATOM   21135 O  OE2   . GLU A 1 4414 ? 253.216 213.585 250.600 1.00 64.96  ? 4414 GLU A OE2   1 
ATOM   21136 N  N     . ARG A 1 4415 ? 251.527 218.400 248.192 1.00 48.68  ? 4415 ARG A N     1 
ATOM   21137 C  CA    . ARG A 1 4415 ? 250.378 218.385 247.292 1.00 41.14  ? 4415 ARG A CA    1 
ATOM   21138 C  C     . ARG A 1 4415 ? 250.632 219.232 246.053 1.00 44.77  ? 4415 ARG A C     1 
ATOM   21139 O  O     . ARG A 1 4415 ? 250.261 218.832 244.941 1.00 51.97  ? 4415 ARG A O     1 
ATOM   21140 C  CB    . ARG A 1 4415 ? 249.128 218.873 248.019 1.00 45.11  ? 4415 ARG A CB    1 
ATOM   21141 C  CG    . ARG A 1 4415 ? 247.850 218.695 247.222 1.00 50.43  ? 4415 ARG A CG    1 
ATOM   21142 C  CD    . ARG A 1 4415 ? 246.625 219.026 248.054 1.00 45.84  ? 4415 ARG A CD    1 
ATOM   21143 N  NE    . ARG A 1 4415 ? 246.404 220.463 248.144 1.00 50.99  ? 4415 ARG A NE    1 
ATOM   21144 C  CZ    . ARG A 1 4415 ? 245.472 221.031 248.895 1.00 51.26  ? 4415 ARG A CZ    1 
ATOM   21145 N  NH1   . ARG A 1 4415 ? 244.659 220.312 249.650 1.00 50.62  ? 4415 ARG A NH1   1 
ATOM   21146 N  NH2   . ARG A 1 4415 ? 245.355 222.355 248.891 1.00 51.06  ? 4415 ARG A NH2   1 
ATOM   21147 N  N     . GLU A 1 4416 ? 251.263 220.397 246.226 1.00 45.09  ? 4416 GLU A N     1 
ATOM   21148 C  CA    . GLU A 1 4416 ? 251.600 221.242 245.085 1.00 40.97  ? 4416 GLU A CA    1 
ATOM   21149 C  C     . GLU A 1 4416 ? 252.506 220.511 244.106 1.00 43.37  ? 4416 GLU A C     1 
ATOM   21150 O  O     . GLU A 1 4416 ? 252.269 220.534 242.893 1.00 49.64  ? 4416 GLU A O     1 
ATOM   21151 C  CB    . GLU A 1 4416 ? 252.279 222.522 245.565 1.00 40.72  ? 4416 GLU A CB    1 
ATOM   21152 C  CG    . GLU A 1 4416 ? 251.343 223.526 246.185 1.00 50.95  ? 4416 GLU A CG    1 
ATOM   21153 C  CD    . GLU A 1 4416 ? 250.291 224.005 245.218 1.00 53.43  ? 4416 GLU A CD    1 
ATOM   21154 O  OE1   . GLU A 1 4416 ? 250.634 224.785 244.308 1.00 53.67  ? 4416 GLU A OE1   1 
ATOM   21155 O  OE2   . GLU A 1 4416 ? 249.122 223.597 245.361 1.00 58.44  ? 4416 GLU A OE2   1 
ATOM   21156 N  N     . VAL A 1 4417 ? 253.550 219.858 244.616 1.00 43.90  ? 4417 VAL A N     1 
ATOM   21157 C  CA    . VAL A 1 4417 ? 254.494 219.168 243.746 1.00 43.39  ? 4417 VAL A CA    1 
ATOM   21158 C  C     . VAL A 1 4417 ? 253.826 217.988 243.056 1.00 47.32  ? 4417 VAL A C     1 
ATOM   21159 O  O     . VAL A 1 4417 ? 254.080 217.725 241.878 1.00 57.00  ? 4417 VAL A O     1 
ATOM   21160 C  CB    . VAL A 1 4417 ? 255.739 218.736 244.540 1.00 38.79  ? 4417 VAL A CB    1 
ATOM   21161 C  CG1   . VAL A 1 4417 ? 256.636 217.873 243.681 1.00 40.70  ? 4417 VAL A CG1   1 
ATOM   21162 C  CG2   . VAL A 1 4417 ? 256.499 219.954 245.024 1.00 33.60  ? 4417 VAL A CG2   1 
ATOM   21163 N  N     . LYS A 1 4418 ? 252.963 217.259 243.767 1.00 45.89  ? 4418 LYS A N     1 
ATOM   21164 C  CA    . LYS A 1 4418 ? 252.266 216.141 243.137 1.00 42.23  ? 4418 LYS A CA    1 
ATOM   21165 C  C     . LYS A 1 4418 ? 251.366 216.616 242.002 1.00 46.11  ? 4418 LYS A C     1 
ATOM   21166 O  O     . LYS A 1 4418 ? 251.383 216.043 240.904 1.00 53.54  ? 4418 LYS A O     1 
ATOM   21167 C  CB    . LYS A 1 4418 ? 251.452 215.371 244.175 1.00 45.22  ? 4418 LYS A CB    1 
ATOM   21168 C  CG    . LYS A 1 4418 ? 252.284 214.531 245.123 1.00 46.27  ? 4418 LYS A CG    1 
ATOM   21169 C  CD    . LYS A 1 4418 ? 251.397 213.763 246.083 1.00 49.82  ? 4418 LYS A CD    1 
ATOM   21170 C  CE    . LYS A 1 4418 ? 252.216 212.915 247.039 1.00 52.99  ? 4418 LYS A CE    1 
ATOM   21171 N  NZ    . LYS A 1 4418 ? 251.348 212.196 248.012 1.00 55.28  ? 4418 LYS A NZ    1 
ATOM   21172 N  N     . MET A 1 4419 ? 250.576 217.667 242.244 1.00 41.66  ? 4419 MET A N     1 
ATOM   21173 C  CA    . MET A 1 4419 ? 249.707 218.186 241.192 1.00 40.28  ? 4419 MET A CA    1 
ATOM   21174 C  C     . MET A 1 4419 ? 250.517 218.711 240.015 1.00 44.57  ? 4419 MET A C     1 
ATOM   21175 O  O     . MET A 1 4419 ? 250.172 218.457 238.852 1.00 49.35  ? 4419 MET A O     1 
ATOM   21176 C  CB    . MET A 1 4419 ? 248.801 219.283 241.749 1.00 48.70  ? 4419 MET A CB    1 
ATOM   21177 C  CG    . MET A 1 4419 ? 247.609 218.765 242.529 1.00 52.76  ? 4419 MET A CG    1 
ATOM   21178 S  SD    . MET A 1 4419 ? 246.512 220.085 243.076 1.00 62.85  ? 4419 MET A SD    1 
ATOM   21179 C  CE    . MET A 1 4419 ? 247.620 221.044 244.100 1.00 46.16  ? 4419 MET A CE    1 
ATOM   21180 N  N     . GLY A 1 4420 ? 251.598 219.440 240.295 1.00 44.21  ? 4420 GLY A N     1 
ATOM   21181 C  CA    . GLY A 1 4420 ? 252.424 219.960 239.222 1.00 37.10  ? 4420 GLY A CA    1 
ATOM   21182 C  C     . GLY A 1 4420 ? 253.085 218.865 238.412 1.00 41.87  ? 4420 GLY A C     1 
ATOM   21183 O  O     . GLY A 1 4420 ? 253.156 218.952 237.187 1.00 54.85  ? 4420 GLY A O     1 
ATOM   21184 N  N     . ALA A 1 4421 ? 253.575 217.820 239.081 1.00 45.38  ? 4421 ALA A N     1 
ATOM   21185 C  CA    . ALA A 1 4421 ? 254.195 216.706 238.375 1.00 37.23  ? 4421 ALA A CA    1 
ATOM   21186 C  C     . ALA A 1 4421 ? 253.183 215.968 237.511 1.00 39.61  ? 4421 ALA A C     1 
ATOM   21187 O  O     . ALA A 1 4421 ? 253.491 215.594 236.374 1.00 52.28  ? 4421 ALA A O     1 
ATOM   21188 C  CB    . ALA A 1 4421 ? 254.849 215.754 239.373 1.00 38.43  ? 4421 ALA A CB    1 
ATOM   21189 N  N     . LYS A 1 4422 ? 251.971 215.751 238.026 1.00 43.70  ? 4422 LYS A N     1 
ATOM   21190 C  CA    . LYS A 1 4422 ? 250.949 215.085 237.223 1.00 46.09  ? 4422 LYS A CA    1 
ATOM   21191 C  C     . LYS A 1 4422 ? 250.584 215.910 235.994 1.00 51.08  ? 4422 LYS A C     1 
ATOM   21192 O  O     . LYS A 1 4422 ? 250.526 215.379 234.875 1.00 53.11  ? 4422 LYS A O     1 
ATOM   21193 C  CB    . LYS A 1 4422 ? 249.709 214.814 238.073 1.00 43.79  ? 4422 LYS A CB    1 
ATOM   21194 C  CG    . LYS A 1 4422 ? 248.644 214.008 237.359 1.00 52.92  ? 4422 LYS A CG    1 
ATOM   21195 C  CD    . LYS A 1 4422 ? 247.462 213.726 238.266 1.00 52.77  ? 4422 LYS A CD    1 
ATOM   21196 C  CE    . LYS A 1 4422 ? 246.467 212.799 237.590 1.00 55.35  ? 4422 LYS A CE    1 
ATOM   21197 N  NZ    . LYS A 1 4422 ? 245.809 213.449 236.424 1.00 50.88  ? 4422 LYS A NZ    1 
ATOM   21198 N  N     . LEU A 1 4423 ? 250.342 217.210 236.180 1.00 50.03  ? 4423 LEU A N     1 
ATOM   21199 C  CA    . LEU A 1 4423 ? 250.002 218.065 235.048 1.00 40.52  ? 4423 LEU A CA    1 
ATOM   21200 C  C     . LEU A 1 4423 ? 251.153 218.147 234.054 1.00 43.91  ? 4423 LEU A C     1 
ATOM   21201 O  O     . LEU A 1 4423 ? 250.931 218.133 232.839 1.00 53.76  ? 4423 LEU A O     1 
ATOM   21202 C  CB    . LEU A 1 4423 ? 249.612 219.458 235.541 1.00 47.37  ? 4423 LEU A CB    1 
ATOM   21203 C  CG    . LEU A 1 4423 ? 249.190 220.492 234.496 1.00 50.69  ? 4423 LEU A CG    1 
ATOM   21204 C  CD1   . LEU A 1 4423 ? 248.282 219.879 233.444 1.00 47.64  ? 4423 LEU A CD1   1 
ATOM   21205 C  CD2   . LEU A 1 4423 ? 248.513 221.674 235.163 1.00 52.44  ? 4423 LEU A CD2   1 
ATOM   21206 N  N     . LEU A 1 4424 ? 252.388 218.238 234.551 1.00 41.97  ? 4424 LEU A N     1 
ATOM   21207 C  CA    . LEU A 1 4424 ? 253.552 218.302 233.678 1.00 41.03  ? 4424 LEU A CA    1 
ATOM   21208 C  C     . LEU A 1 4424 ? 253.699 217.029 232.860 1.00 47.06  ? 4424 LEU A C     1 
ATOM   21209 O  O     . LEU A 1 4424 ? 253.979 217.086 231.658 1.00 55.66  ? 4424 LEU A O     1 
ATOM   21210 C  CB    . LEU A 1 4424 ? 254.803 218.557 234.518 1.00 40.89  ? 4424 LEU A CB    1 
ATOM   21211 C  CG    . LEU A 1 4424 ? 256.175 218.351 233.881 1.00 47.22  ? 4424 LEU A CG    1 
ATOM   21212 C  CD1   . LEU A 1 4424 ? 256.368 219.309 232.734 1.00 48.70  ? 4424 LEU A CD1   1 
ATOM   21213 C  CD2   . LEU A 1 4424 ? 257.265 218.537 234.918 1.00 41.16  ? 4424 LEU A CD2   1 
ATOM   21214 N  N     . GLN A 1 4425 ? 253.512 215.870 233.493 1.00 45.56  ? 4425 GLN A N     1 
ATOM   21215 C  CA    . GLN A 1 4425 ? 253.590 214.609 232.766 1.00 43.26  ? 4425 GLN A CA    1 
ATOM   21216 C  C     . GLN A 1 4425 ? 252.516 214.530 231.691 1.00 44.00  ? 4425 GLN A C     1 
ATOM   21217 O  O     . GLN A 1 4425 ? 252.796 214.139 230.550 1.00 51.60  ? 4425 GLN A O     1 
ATOM   21218 C  CB    . GLN A 1 4425 ? 253.465 213.440 233.741 1.00 44.71  ? 4425 GLN A CB    1 
ATOM   21219 C  CG    . GLN A 1 4425 ? 253.456 212.076 233.083 1.00 53.82  ? 4425 GLN A CG    1 
ATOM   21220 C  CD    . GLN A 1 4425 ? 252.715 211.042 233.905 1.00 59.20  ? 4425 GLN A CD    1 
ATOM   21221 O  OE1   . GLN A 1 4425 ? 251.497 210.898 233.792 1.00 58.32  ? 4425 GLN A OE1   1 
ATOM   21222 N  NE2   . GLN A 1 4425 ? 253.447 210.314 234.740 1.00 57.02  ? 4425 GLN A NE2   1 
ATOM   21223 N  N     . ASP A 1 4426 ? 251.283 214.918 232.030 1.00 46.75  ? 4426 ASP A N     1 
ATOM   21224 C  CA    . ASP A 1 4426 ? 250.211 214.892 231.039 1.00 44.13  ? 4426 ASP A CA    1 
ATOM   21225 C  C     . ASP A 1 4426 ? 250.510 215.824 229.871 1.00 47.99  ? 4426 ASP A C     1 
ATOM   21226 O  O     . ASP A 1 4426 ? 250.340 215.443 228.706 1.00 52.44  ? 4426 ASP A O     1 
ATOM   21227 C  CB    . ASP A 1 4426 ? 248.884 215.266 231.695 1.00 51.29  ? 4426 ASP A CB    1 
ATOM   21228 C  CG    . ASP A 1 4426 ? 248.365 214.183 232.618 1.00 63.31  ? 4426 ASP A CG    1 
ATOM   21229 O  OD1   . ASP A 1 4426 ? 248.952 213.082 232.633 1.00 57.03  ? 4426 ASP A OD1   1 
ATOM   21230 O  OD2   . ASP A 1 4426 ? 247.368 214.433 233.329 1.00 61.97  ? 4426 ASP A OD2   1 
ATOM   21231 N  N     . VAL A 1 4427 ? 250.969 217.043 230.161 1.00 54.11  ? 4427 VAL A N     1 
ATOM   21232 C  CA    . VAL A 1 4427 ? 251.227 218.023 229.111 1.00 47.35  ? 4427 VAL A CA    1 
ATOM   21233 C  C     . VAL A 1 4427 ? 252.368 217.559 228.212 1.00 47.84  ? 4427 VAL A C     1 
ATOM   21234 O  O     . VAL A 1 4427 ? 252.292 217.664 226.982 1.00 55.30  ? 4427 VAL A O     1 
ATOM   21235 C  CB    . VAL A 1 4427 ? 251.517 219.402 229.731 1.00 45.45  ? 4427 VAL A CB    1 
ATOM   21236 C  CG1   . VAL A 1 4427 ? 252.161 220.326 228.715 1.00 47.16  ? 4427 VAL A CG1   1 
ATOM   21237 C  CG2   . VAL A 1 4427 ? 250.238 220.013 230.270 1.00 51.57  ? 4427 VAL A CG2   1 
ATOM   21238 N  N     . ARG A 1 4428 ? 253.443 217.042 228.810 1.00 46.55  ? 4428 ARG A N     1 
ATOM   21239 C  CA    . ARG A 1 4428 ? 254.577 216.585 228.016 1.00 47.74  ? 4428 ARG A CA    1 
ATOM   21240 C  C     . ARG A 1 4428 ? 254.203 215.388 227.152 1.00 52.23  ? 4428 ARG A C     1 
ATOM   21241 O  O     . ARG A 1 4428 ? 254.616 215.306 225.989 1.00 52.62  ? 4428 ARG A O     1 
ATOM   21242 C  CB    . ARG A 1 4428 ? 255.755 216.254 228.928 1.00 49.09  ? 4428 ARG A CB    1 
ATOM   21243 C  CG    . ARG A 1 4428 ? 256.443 217.483 229.492 1.00 47.84  ? 4428 ARG A CG    1 
ATOM   21244 C  CD    . ARG A 1 4428 ? 257.788 217.144 230.101 1.00 52.50  ? 4428 ARG A CD    1 
ATOM   21245 N  NE    . ARG A 1 4428 ? 258.774 216.785 229.091 1.00 56.51  ? 4428 ARG A NE    1 
ATOM   21246 C  CZ    . ARG A 1 4428 ? 259.440 217.660 228.351 1.00 53.59  ? 4428 ARG A CZ    1 
ATOM   21247 N  NH1   . ARG A 1 4428 ? 259.243 218.962 228.475 1.00 53.97  ? 4428 ARG A NH1   1 
ATOM   21248 N  NH2   . ARG A 1 4428 ? 260.328 217.219 227.466 1.00 54.91  ? 4428 ARG A NH2   1 
ATOM   21249 N  N     . GLN A 1 4429 ? 253.417 214.451 227.692 1.00 56.85  ? 4429 GLN A N     1 
ATOM   21250 C  CA    . GLN A 1 4429 ? 252.974 213.321 226.882 1.00 53.25  ? 4429 GLN A CA    1 
ATOM   21251 C  C     . GLN A 1 4429 ? 252.077 213.778 225.738 1.00 51.86  ? 4429 GLN A C     1 
ATOM   21252 O  O     . GLN A 1 4429 ? 252.188 213.271 224.615 1.00 59.17  ? 4429 GLN A O     1 
ATOM   21253 C  CB    . GLN A 1 4429 ? 252.254 212.296 227.756 1.00 50.95  ? 4429 GLN A CB    1 
ATOM   21254 C  CG    . GLN A 1 4429 ? 251.957 210.980 227.054 1.00 53.06  ? 4429 GLN A CG    1 
ATOM   21255 C  CD    . GLN A 1 4429 ? 253.194 210.348 226.445 1.00 60.22  ? 4429 GLN A CD    1 
ATOM   21256 O  OE1   . GLN A 1 4429 ? 253.496 210.552 225.269 1.00 56.65  ? 4429 GLN A OE1   1 
ATOM   21257 N  NE2   . GLN A 1 4429 ? 253.916 209.573 227.244 1.00 58.12  ? 4429 GLN A NE2   1 
ATOM   21258 N  N     . ASP A 1 4430 ? 251.183 214.736 225.999 1.00 43.70  ? 4430 ASP A N     1 
ATOM   21259 C  CA    . ASP A 1 4430 ? 250.322 215.252 224.940 1.00 46.76  ? 4430 ASP A CA    1 
ATOM   21260 C  C     . ASP A 1 4430 ? 251.135 215.930 223.846 1.00 53.06  ? 4430 ASP A C     1 
ATOM   21261 O  O     . ASP A 1 4430 ? 250.860 215.752 222.654 1.00 56.57  ? 4430 ASP A O     1 
ATOM   21262 C  CB    . ASP A 1 4430 ? 249.303 216.225 225.525 1.00 52.73  ? 4430 ASP A CB    1 
ATOM   21263 C  CG    . ASP A 1 4430 ? 248.258 215.533 226.369 1.00 61.91  ? 4430 ASP A CG    1 
ATOM   21264 O  OD1   . ASP A 1 4430 ? 248.313 214.291 226.484 1.00 59.26  ? 4430 ASP A OD1   1 
ATOM   21265 O  OD2   . ASP A 1 4430 ? 247.381 216.230 226.919 1.00 63.22  ? 4430 ASP A OD2   1 
ATOM   21266 N  N     . LEU A 1 4431 ? 252.139 216.718 224.233 1.00 55.65  ? 4431 LEU A N     1 
ATOM   21267 C  CA    . LEU A 1 4431 ? 252.976 217.384 223.241 1.00 47.90  ? 4431 LEU A CA    1 
ATOM   21268 C  C     . LEU A 1 4431 ? 253.794 216.377 222.443 1.00 52.37  ? 4431 LEU A C     1 
ATOM   21269 O  O     . LEU A 1 4431 ? 253.982 216.544 221.233 1.00 57.31  ? 4431 LEU A O     1 
ATOM   21270 C  CB    . LEU A 1 4431 ? 253.886 218.403 223.922 1.00 51.63  ? 4431 LEU A CB    1 
ATOM   21271 C  CG    . LEU A 1 4431 ? 253.207 219.680 224.414 1.00 52.06  ? 4431 LEU A CG    1 
ATOM   21272 C  CD1   . LEU A 1 4431 ? 254.223 220.613 225.046 1.00 56.20  ? 4431 LEU A CD1   1 
ATOM   21273 C  CD2   . LEU A 1 4431 ? 252.477 220.367 223.276 1.00 51.07  ? 4431 LEU A CD2   1 
ATOM   21274 N  N     . ALA A 1 4432 ? 254.291 215.326 223.100 1.00 53.22  ? 4432 ALA A N     1 
ATOM   21275 C  CA    . ALA A 1 4432 ? 255.007 214.279 222.379 1.00 49.08  ? 4432 ALA A CA    1 
ATOM   21276 C  C     . ALA A 1 4432 ? 254.095 213.576 221.382 1.00 57.69  ? 4432 ALA A C     1 
ATOM   21277 O  O     . ALA A 1 4432 ? 254.510 213.269 220.259 1.00 63.44  ? 4432 ALA A O     1 
ATOM   21278 C  CB    . ALA A 1 4432 ? 255.602 213.275 223.365 1.00 50.88  ? 4432 ALA A CB    1 
ATOM   21279 N  N     . ASP A 1 4433 ? 252.847 213.311 221.776 1.00 58.82  ? 4433 ASP A N     1 
ATOM   21280 C  CA    . ASP A 1 4433 ? 251.894 212.698 220.856 1.00 50.92  ? 4433 ASP A CA    1 
ATOM   21281 C  C     . ASP A 1 4433 ? 251.594 213.614 219.676 1.00 56.88  ? 4433 ASP A C     1 
ATOM   21282 O  O     . ASP A 1 4433 ? 251.472 213.149 218.537 1.00 64.19  ? 4433 ASP A O     1 
ATOM   21283 C  CB    . ASP A 1 4433 ? 250.608 212.337 221.596 1.00 54.76  ? 4433 ASP A CB    1 
ATOM   21284 C  CG    . ASP A 1 4433 ? 250.816 211.242 222.619 1.00 64.68  ? 4433 ASP A CG    1 
ATOM   21285 O  OD1   . ASP A 1 4433 ? 251.976 210.828 222.818 1.00 64.70  ? 4433 ASP A OD1   1 
ATOM   21286 O  OD2   . ASP A 1 4433 ? 249.821 210.794 223.227 1.00 62.72  ? 4433 ASP A OD2   1 
ATOM   21287 N  N     . VAL A 1 4434 ? 251.469 214.918 219.930 1.00 56.34  ? 4434 VAL A N     1 
ATOM   21288 C  CA    . VAL A 1 4434 ? 251.252 215.872 218.844 1.00 53.36  ? 4434 VAL A CA    1 
ATOM   21289 C  C     . VAL A 1 4434 ? 252.441 215.874 217.892 1.00 53.81  ? 4434 VAL A C     1 
ATOM   21290 O  O     . VAL A 1 4434 ? 252.275 215.907 216.667 1.00 59.93  ? 4434 VAL A O     1 
ATOM   21291 C  CB    . VAL A 1 4434 ? 250.975 217.276 219.412 1.00 53.74  ? 4434 VAL A CB    1 
ATOM   21292 C  CG1   . VAL A 1 4434 ? 251.215 218.339 218.357 1.00 57.98  ? 4434 VAL A CG1   1 
ATOM   21293 C  CG2   . VAL A 1 4434 ? 249.555 217.361 219.924 1.00 56.28  ? 4434 VAL A CG2   1 
ATOM   21294 N  N     . VAL A 1 4435 ? 253.658 215.840 218.439 1.00 57.34  ? 4435 VAL A N     1 
ATOM   21295 C  CA    . VAL A 1 4435 ? 254.854 215.797 217.601 1.00 59.11  ? 4435 VAL A CA    1 
ATOM   21296 C  C     . VAL A 1 4435 ? 254.863 214.536 216.746 1.00 63.79  ? 4435 VAL A C     1 
ATOM   21297 O  O     . VAL A 1 4435 ? 255.151 214.585 215.544 1.00 66.31  ? 4435 VAL A O     1 
ATOM   21298 C  CB    . VAL A 1 4435 ? 256.119 215.897 218.473 1.00 58.32  ? 4435 VAL A CB    1 
ATOM   21299 C  CG1   . VAL A 1 4435 ? 257.324 215.346 217.732 1.00 61.06  ? 4435 VAL A CG1   1 
ATOM   21300 C  CG2   . VAL A 1 4435 ? 256.365 217.333 218.884 1.00 60.14  ? 4435 VAL A CG2   1 
ATOM   21301 N  N     . GLN A 1 4436 ? 254.543 213.388 217.349 1.00 63.26  ? 4436 GLN A N     1 
ATOM   21302 C  CA    . GLN A 1 4436 ? 254.541 212.135 216.598 1.00 57.73  ? 4436 GLN A CA    1 
ATOM   21303 C  C     . GLN A 1 4436 ? 253.484 212.147 215.502 1.00 60.62  ? 4436 GLN A C     1 
ATOM   21304 O  O     . GLN A 1 4436 ? 253.718 211.636 214.401 1.00 66.87  ? 4436 GLN A O     1 
ATOM   21305 C  CB    . GLN A 1 4436 ? 254.323 210.953 217.541 1.00 62.30  ? 4436 GLN A CB    1 
ATOM   21306 C  CG    . GLN A 1 4436 ? 255.418 210.768 218.576 1.00 64.31  ? 4436 GLN A CG    1 
ATOM   21307 C  CD    . GLN A 1 4436 ? 256.755 210.409 217.961 1.00 72.39  ? 4436 GLN A CD    1 
ATOM   21308 O  OE1   . GLN A 1 4436 ? 256.826 209.951 216.823 1.00 72.96  ? 4436 GLN A OE1   1 
ATOM   21309 N  NE2   . GLN A 1 4436 ? 257.827 210.620 218.716 1.00 69.33  ? 4436 GLN A NE2   1 
ATOM   21310 N  N     . VAL A 1 4437 ? 252.310 212.716 215.784 1.00 56.67  ? 4437 VAL A N     1 
ATOM   21311 C  CA    . VAL A 1 4437 ? 251.282 212.838 214.754 1.00 59.29  ? 4437 VAL A CA    1 
ATOM   21312 C  C     . VAL A 1 4437 ? 251.777 213.729 213.623 1.00 64.76  ? 4437 VAL A C     1 
ATOM   21313 O  O     . VAL A 1 4437 ? 251.602 213.420 212.438 1.00 68.07  ? 4437 VAL A O     1 
ATOM   21314 C  CB    . VAL A 1 4437 ? 249.973 213.375 215.357 1.00 57.84  ? 4437 VAL A CB    1 
ATOM   21315 C  CG1   . VAL A 1 4437 ? 249.079 213.929 214.262 1.00 60.34  ? 4437 VAL A CG1   1 
ATOM   21316 C  CG2   . VAL A 1 4437 ? 249.256 212.288 216.124 1.00 62.25  ? 4437 VAL A CG2   1 
ATOM   21317 N  N     . CYS A 1 4438 ? 252.414 214.847 213.975 1.00 69.30  ? 4438 CYS A N     1 
ATOM   21318 C  CA    . CYS A 1 4438 ? 252.906 215.778 212.969 1.00 66.00  ? 4438 CYS A CA    1 
ATOM   21319 C  C     . CYS A 1 4438 ? 254.088 215.221 212.187 1.00 65.65  ? 4438 CYS A C     1 
ATOM   21320 O  O     . CYS A 1 4438 ? 254.383 215.721 211.098 1.00 71.09  ? 4438 CYS A O     1 
ATOM   21321 C  CB    . CYS A 1 4438 ? 253.283 217.103 213.628 1.00 66.32  ? 4438 CYS A CB    1 
ATOM   21322 S  SG    . CYS A 1 4438 ? 251.865 218.072 214.185 1.00 63.53  ? 4438 CYS A SG    1 
ATOM   21323 N  N     . GLU A 1 4439 ? 254.770 214.208 212.711 1.00 66.22  ? 4439 GLU A N     1 
ATOM   21324 C  CA    . GLU A 1 4439 ? 255.800 213.509 211.958 1.00 68.73  ? 4439 GLU A CA    1 
ATOM   21325 C  C     . GLU A 1 4439 ? 255.230 212.413 211.070 1.00 72.10  ? 4439 GLU A C     1 
ATOM   21326 O  O     . GLU A 1 4439 ? 255.990 211.767 210.342 1.00 73.86  ? 4439 GLU A O     1 
ATOM   21327 C  CB    . GLU A 1 4439 ? 256.841 212.906 212.905 1.00 69.71  ? 4439 GLU A CB    1 
ATOM   21328 C  CG    . GLU A 1 4439 ? 257.741 213.922 213.578 1.00 69.90  ? 4439 GLU A CG    1 
ATOM   21329 C  CD    . GLU A 1 4439 ? 258.772 213.274 214.480 1.00 76.02  ? 4439 GLU A CD    1 
ATOM   21330 O  OE1   . GLU A 1 4439 ? 258.709 212.041 214.666 1.00 73.54  ? 4439 GLU A OE1   1 
ATOM   21331 O  OE2   . GLU A 1 4439 ? 259.646 213.996 215.003 1.00 76.75  ? 4439 GLU A OE2   1 
ATOM   21332 N  N     . GLY A 1 4440 ? 253.919 212.188 211.115 1.00 68.16  ? 4440 GLY A N     1 
ATOM   21333 C  CA    . GLY A 1 4440 ? 253.319 211.128 210.334 1.00 65.14  ? 4440 GLY A CA    1 
ATOM   21334 C  C     . GLY A 1 4440 ? 253.595 209.736 210.847 1.00 68.48  ? 4440 GLY A C     1 
ATOM   21335 O  O     . GLY A 1 4440 ? 253.490 208.774 210.084 1.00 71.99  ? 4440 GLY A O     1 
ATOM   21336 N  N     . LYS A 1 4441 ? 253.947 209.598 212.125 1.00 69.53  ? 4441 LYS A N     1 
ATOM   21337 C  CA    . LYS A 1 4441 ? 254.294 208.296 212.685 1.00 70.96  ? 4441 LYS A CA    1 
ATOM   21338 C  C     . LYS A 1 4441 ? 253.088 207.606 213.318 1.00 75.25  ? 4441 LYS A C     1 
ATOM   21339 O  O     . LYS A 1 4441 ? 252.723 206.496 212.919 1.00 80.53  ? 4441 LYS A O     1 
ATOM   21340 C  CB    . LYS A 1 4441 ? 255.422 208.450 213.710 1.00 67.58  ? 4441 LYS A CB    1 
ATOM   21341 C  CG    . LYS A 1 4441 ? 256.796 208.632 213.095 1.00 71.87  ? 4441 LYS A CG    1 
ATOM   21342 C  CD    . LYS A 1 4441 ? 257.881 208.541 214.152 1.00 74.88  ? 4441 LYS A CD    1 
ATOM   21343 C  CE    . LYS A 1 4441 ? 259.262 208.745 213.554 1.00 72.15  ? 4441 LYS A CE    1 
ATOM   21344 N  NZ    . LYS A 1 4441 ? 260.303 208.853 214.613 1.00 73.04  ? 4441 LYS A NZ    1 
ATOM   21345 N  N     . LYS A 1 4442 ? 252.463 208.247 214.299 1.00 61.42  ? 4442 LYS A N     1 
ATOM   21346 C  CA    . LYS A 1 4442 ? 251.361 207.644 215.032 1.00 57.14  ? 4442 LYS A CA    1 
ATOM   21347 C  C     . LYS A 1 4442 ? 250.020 208.136 214.499 1.00 59.63  ? 4442 LYS A C     1 
ATOM   21348 O  O     . LYS A 1 4442 ? 249.914 209.207 213.898 1.00 57.10  ? 4442 LYS A O     1 
ATOM   21349 C  CB    . LYS A 1 4442 ? 251.484 207.935 216.531 1.00 62.65  ? 4442 LYS A CB    1 
ATOM   21350 C  CG    . LYS A 1 4442 ? 250.817 209.215 216.987 1.00 64.25  ? 4442 LYS A CG    1 
ATOM   21351 C  CD    . LYS A 1 4442 ? 251.117 209.498 218.448 1.00 64.40  ? 4442 LYS A CD    1 
ATOM   21352 C  CE    . LYS A 1 4442 ? 250.746 208.320 219.326 1.00 62.64  ? 4442 LYS A CE    1 
ATOM   21353 N  NZ    . LYS A 1 4442 ? 249.276 208.241 219.540 1.00 64.66  ? 4442 LYS A NZ    1 
ATOM   21354 N  N     . LYS A 1 4443 ? 248.990 207.323 214.726 1.00 63.82  ? 4443 LYS A N     1 
ATOM   21355 C  CA    . LYS A 1 4443 ? 247.667 207.560 214.167 1.00 64.24  ? 4443 LYS A CA    1 
ATOM   21356 C  C     . LYS A 1 4443 ? 246.880 208.518 215.053 1.00 62.79  ? 4443 LYS A C     1 
ATOM   21357 O  O     . LYS A 1 4443 ? 246.902 208.410 216.281 1.00 66.47  ? 4443 LYS A O     1 
ATOM   21358 C  CB    . LYS A 1 4443 ? 246.918 206.233 214.002 1.00 63.99  ? 4443 LYS A CB    1 
ATOM   21359 C  CG    . LYS A 1 4443 ? 245.517 206.332 213.400 1.00 67.73  ? 4443 LYS A CG    1 
ATOM   21360 C  CD    . LYS A 1 4443 ? 244.426 206.430 214.460 1.00 67.36  ? 4443 LYS A CD    1 
ATOM   21361 C  CE    . LYS A 1 4443 ? 244.251 205.120 215.208 1.00 68.38  ? 4443 LYS A CE    1 
ATOM   21362 N  NZ    . LYS A 1 4443 ? 243.176 205.214 216.235 1.00 65.06  ? 4443 LYS A NZ    1 
ATOM   21363 N  N     . GLN A 1 4444 ? 246.182 209.452 214.416 1.00 55.08  ? 4444 GLN A N     1 
ATOM   21364 C  CA    . GLN A 1 4444 ? 245.450 210.479 215.144 1.00 52.34  ? 4444 GLN A CA    1 
ATOM   21365 C  C     . GLN A 1 4444 ? 244.137 209.927 215.686 1.00 55.02  ? 4444 GLN A C     1 
ATOM   21366 O  O     . GLN A 1 4444 ? 243.319 209.381 214.942 1.00 62.82  ? 4444 GLN A O     1 
ATOM   21367 C  CB    . GLN A 1 4444 ? 245.187 211.671 214.226 1.00 56.58  ? 4444 GLN A CB    1 
ATOM   21368 C  CG    . GLN A 1 4444 ? 244.625 212.897 214.911 1.00 62.08  ? 4444 GLN A CG    1 
ATOM   21369 C  CD    . GLN A 1 4444 ? 244.484 214.067 213.957 1.00 67.61  ? 4444 GLN A CD    1 
ATOM   21370 O  OE1   . GLN A 1 4444 ? 244.112 215.170 214.355 1.00 66.82  ? 4444 GLN A OE1   1 
ATOM   21371 N  NE2   . GLN A 1 4444 ? 244.784 213.830 212.686 1.00 59.58  ? 4444 GLN A NE2   1 
ATOM   21372 N  N     . THR A 1 4445 ? 243.934 210.082 216.991 1.00 52.50  ? 4445 THR A N     1 
ATOM   21373 C  CA    . THR A 1 4445 ? 242.747 209.597 217.680 1.00 49.78  ? 4445 THR A CA    1 
ATOM   21374 C  C     . THR A 1 4445 ? 241.789 210.755 217.942 1.00 52.29  ? 4445 THR A C     1 
ATOM   21375 O  O     . THR A 1 4445 ? 242.043 211.901 217.563 1.00 61.10  ? 4445 THR A O     1 
ATOM   21376 C  CB    . THR A 1 4445 ? 243.127 208.897 218.985 1.00 48.59  ? 4445 THR A CB    1 
ATOM   21377 O  OG1   . THR A 1 4445 ? 243.698 209.848 219.891 1.00 47.20  ? 4445 THR A OG1   1 
ATOM   21378 C  CG2   . THR A 1 4445 ? 244.138 207.795 218.722 1.00 50.86  ? 4445 THR A CG2   1 
ATOM   21379 N  N     . ASN A 1 4446 ? 240.669 210.441 218.599 1.00 47.97  ? 4446 ASN A N     1 
ATOM   21380 C  CA    . ASN A 1 4446 ? 239.673 211.466 218.899 1.00 47.45  ? 4446 ASN A CA    1 
ATOM   21381 C  C     . ASN A 1 4446 ? 240.243 212.538 219.817 1.00 49.20  ? 4446 ASN A C     1 
ATOM   21382 O  O     . ASN A 1 4446 ? 240.134 213.739 219.531 1.00 58.08  ? 4446 ASN A O     1 
ATOM   21383 C  CB    . ASN A 1 4446 ? 238.441 210.827 219.539 1.00 49.37  ? 4446 ASN A CB    1 
ATOM   21384 C  CG    . ASN A 1 4446 ? 237.371 210.484 218.530 1.00 47.98  ? 4446 ASN A CG    1 
ATOM   21385 O  OD1   . ASN A 1 4446 ? 237.149 211.218 217.570 1.00 54.72  ? 4446 ASN A OD1   1 
ATOM   21386 N  ND2   . ASN A 1 4446 ? 236.694 209.365 218.747 1.00 42.77  ? 4446 ASN A ND2   1 
ATOM   21387 N  N     . TYR A 1 4447 ? 240.853 212.123 220.929 1.00 48.30  ? 4447 TYR A N     1 
ATOM   21388 C  CA    . TYR A 1 4447 ? 241.434 213.088 221.852 1.00 49.69  ? 4447 TYR A CA    1 
ATOM   21389 C  C     . TYR A 1 4447 ? 242.564 213.859 221.190 1.00 47.89  ? 4447 TYR A C     1 
ATOM   21390 O  O     . TYR A 1 4447 ? 242.688 215.074 221.378 1.00 52.16  ? 4447 TYR A O     1 
ATOM   21391 C  CB    . TYR A 1 4447 ? 241.933 212.384 223.111 1.00 48.81  ? 4447 TYR A CB    1 
ATOM   21392 C  CG    . TYR A 1 4447 ? 242.855 213.241 223.942 1.00 50.04  ? 4447 TYR A CG    1 
ATOM   21393 C  CD1   . TYR A 1 4447 ? 242.348 214.274 224.716 1.00 48.04  ? 4447 TYR A CD1   1 
ATOM   21394 C  CD2   . TYR A 1 4447 ? 244.225 213.028 223.950 1.00 55.06  ? 4447 TYR A CD2   1 
ATOM   21395 C  CE1   . TYR A 1 4447 ? 243.174 215.066 225.477 1.00 55.15  ? 4447 TYR A CE1   1 
ATOM   21396 C  CE2   . TYR A 1 4447 ? 245.063 213.819 224.709 1.00 54.52  ? 4447 TYR A CE2   1 
ATOM   21397 C  CZ    . TYR A 1 4447 ? 244.529 214.836 225.471 1.00 59.33  ? 4447 TYR A CZ    1 
ATOM   21398 O  OH    . TYR A 1 4447 ? 245.345 215.633 226.233 1.00 58.42  ? 4447 TYR A OH    1 
ATOM   21399 N  N     . LEU A 1 4448 ? 243.402 213.168 220.415 1.00 51.55  ? 4448 LEU A N     1 
ATOM   21400 C  CA    . LEU A 1 4448 ? 244.451 213.853 219.673 1.00 47.31  ? 4448 LEU A CA    1 
ATOM   21401 C  C     . LEU A 1 4448 ? 243.871 214.797 218.631 1.00 47.01  ? 4448 LEU A C     1 
ATOM   21402 O  O     . LEU A 1 4448 ? 244.418 215.881 218.417 1.00 58.94  ? 4448 LEU A O     1 
ATOM   21403 C  CB    . LEU A 1 4448 ? 245.384 212.841 219.014 1.00 49.26  ? 4448 LEU A CB    1 
ATOM   21404 C  CG    . LEU A 1 4448 ? 246.499 212.315 219.918 1.00 51.47  ? 4448 LEU A CG    1 
ATOM   21405 C  CD1   . LEU A 1 4448 ? 247.414 211.373 219.158 1.00 50.37  ? 4448 LEU A CD1   1 
ATOM   21406 C  CD2   . LEU A 1 4448 ? 247.285 213.471 220.509 1.00 51.15  ? 4448 LEU A CD2   1 
ATOM   21407 N  N     . ARG A 1 4449 ? 242.771 214.412 217.980 1.00 48.76  ? 4449 ARG A N     1 
ATOM   21408 C  CA    . ARG A 1 4449 ? 242.115 215.324 217.048 1.00 48.83  ? 4449 ARG A CA    1 
ATOM   21409 C  C     . ARG A 1 4449 ? 241.697 216.610 217.745 1.00 51.10  ? 4449 ARG A C     1 
ATOM   21410 O  O     . ARG A 1 4449 ? 241.990 217.711 217.263 1.00 60.62  ? 4449 ARG A O     1 
ATOM   21411 C  CB    . ARG A 1 4449 ? 240.898 214.652 216.413 1.00 52.65  ? 4449 ARG A CB    1 
ATOM   21412 C  CG    . ARG A 1 4449 ? 241.166 213.996 215.074 1.00 53.17  ? 4449 ARG A CG    1 
ATOM   21413 C  CD    . ARG A 1 4449 ? 239.894 213.403 214.494 1.00 53.57  ? 4449 ARG A CD    1 
ATOM   21414 N  NE    . ARG A 1 4449 ? 239.601 212.092 215.059 1.00 56.74  ? 4449 ARG A NE    1 
ATOM   21415 C  CZ    . ARG A 1 4449 ? 240.179 210.965 214.669 1.00 58.82  ? 4449 ARG A CZ    1 
ATOM   21416 N  NH1   . ARG A 1 4449 ? 241.079 210.949 213.701 1.00 57.26  ? 4449 ARG A NH1   1 
ATOM   21417 N  NH2   . ARG A 1 4449 ? 239.843 209.824 215.265 1.00 52.22  ? 4449 ARG A NH2   1 
ATOM   21418 N  N     . THR A 1 4450 ? 241.023 216.490 218.891 1.00 53.70  ? 4450 THR A N     1 
ATOM   21419 C  CA    . THR A 1 4450 ? 240.579 217.679 219.613 1.00 54.15  ? 4450 THR A CA    1 
ATOM   21420 C  C     . THR A 1 4450 ? 241.763 218.520 220.075 1.00 46.80  ? 4450 THR A C     1 
ATOM   21421 O  O     . THR A 1 4450 ? 241.764 219.749 219.924 1.00 50.71  ? 4450 THR A O     1 
ATOM   21422 C  CB    . THR A 1 4450 ? 239.711 217.276 220.804 1.00 51.19  ? 4450 THR A CB    1 
ATOM   21423 O  OG1   . THR A 1 4450 ? 238.661 216.410 220.359 1.00 53.84  ? 4450 THR A OG1   1 
ATOM   21424 C  CG2   . THR A 1 4450 ? 239.101 218.503 221.455 1.00 51.90  ? 4450 THR A CG2   1 
ATOM   21425 N  N     . LEU A 1 4451 ? 242.786 217.871 220.636 1.00 49.79  ? 4451 LEU A N     1 
ATOM   21426 C  CA    . LEU A 1 4451 ? 243.939 218.599 221.153 1.00 52.20  ? 4451 LEU A CA    1 
ATOM   21427 C  C     . LEU A 1 4451 ? 244.674 219.334 220.041 1.00 54.02  ? 4451 LEU A C     1 
ATOM   21428 O  O     . LEU A 1 4451 ? 245.069 220.492 220.210 1.00 59.69  ? 4451 LEU A O     1 
ATOM   21429 C  CB    . LEU A 1 4451 ? 244.873 217.633 221.882 1.00 50.47  ? 4451 LEU A CB    1 
ATOM   21430 C  CG    . LEU A 1 4451 ? 246.291 218.097 222.206 1.00 48.86  ? 4451 LEU A CG    1 
ATOM   21431 C  CD1   . LEU A 1 4451 ? 246.277 219.076 223.356 1.00 55.85  ? 4451 LEU A CD1   1 
ATOM   21432 C  CD2   . LEU A 1 4451 ? 247.155 216.904 222.546 1.00 54.42  ? 4451 LEU A CD2   1 
ATOM   21433 N  N     . ILE A 1 4452 ? 244.857 218.683 218.891 1.00 54.56  ? 4452 ILE A N     1 
ATOM   21434 C  CA    . ILE A 1 4452 ? 245.519 219.325 217.762 1.00 53.92  ? 4452 ILE A CA    1 
ATOM   21435 C  C     . ILE A 1 4452 ? 244.680 220.474 217.226 1.00 54.66  ? 4452 ILE A C     1 
ATOM   21436 O  O     . ILE A 1 4452 ? 245.214 221.528 216.861 1.00 62.20  ? 4452 ILE A O     1 
ATOM   21437 C  CB    . ILE A 1 4452 ? 245.830 218.284 216.672 1.00 53.42  ? 4452 ILE A CB    1 
ATOM   21438 C  CG1   . ILE A 1 4452 ? 246.924 217.331 217.153 1.00 53.88  ? 4452 ILE A CG1   1 
ATOM   21439 C  CG2   . ILE A 1 4452 ? 246.212 218.959 215.372 1.00 55.76  ? 4452 ILE A CG2   1 
ATOM   21440 C  CD1   . ILE A 1 4452 ? 247.129 216.149 216.256 1.00 54.12  ? 4452 ILE A CD1   1 
ATOM   21441 N  N     . ASN A 1 4453 ? 243.357 220.299 217.168 1.00 55.38  ? 4453 ASN A N     1 
ATOM   21442 C  CA    . ASN A 1 4453 ? 242.504 221.388 216.707 1.00 55.01  ? 4453 ASN A CA    1 
ATOM   21443 C  C     . ASN A 1 4453 ? 242.645 222.611 217.605 1.00 56.99  ? 4453 ASN A C     1 
ATOM   21444 O  O     . ASN A 1 4453 ? 242.823 223.732 217.114 1.00 60.21  ? 4453 ASN A O     1 
ATOM   21445 C  CB    . ASN A 1 4453 ? 241.050 220.919 216.643 1.00 58.38  ? 4453 ASN A CB    1 
ATOM   21446 C  CG    . ASN A 1 4453 ? 240.062 222.069 216.614 1.00 63.77  ? 4453 ASN A CG    1 
ATOM   21447 O  OD1   . ASN A 1 4453 ? 239.667 222.592 217.656 1.00 67.43  ? 4453 ASN A OD1   1 
ATOM   21448 N  ND2   . ASN A 1 4453 ? 239.654 222.466 215.416 1.00 62.52  ? 4453 ASN A ND2   1 
ATOM   21449 N  N     . GLU A 1 4454 ? 242.594 222.413 218.926 1.00 59.43  ? 4454 GLU A N     1 
ATOM   21450 C  CA    . GLU A 1 4454 ? 242.750 223.546 219.837 1.00 55.53  ? 4454 GLU A CA    1 
ATOM   21451 C  C     . GLU A 1 4454 ? 244.143 224.157 219.743 1.00 59.04  ? 4454 GLU A C     1 
ATOM   21452 O  O     . GLU A 1 4454 ? 244.288 225.384 219.776 1.00 62.88  ? 4454 GLU A O     1 
ATOM   21453 C  CB    . GLU A 1 4454 ? 242.448 223.132 221.278 1.00 51.77  ? 4454 GLU A CB    1 
ATOM   21454 C  CG    . GLU A 1 4454 ? 241.205 222.288 221.446 1.00 58.72  ? 4454 GLU A CG    1 
ATOM   21455 C  CD    . GLU A 1 4454 ? 240.724 222.236 222.880 1.00 64.98  ? 4454 GLU A CD    1 
ATOM   21456 O  OE1   . GLU A 1 4454 ? 240.745 221.140 223.476 1.00 65.38  ? 4454 GLU A OE1   1 
ATOM   21457 O  OE2   . GLU A 1 4454 ? 240.321 223.292 223.410 1.00 68.33  ? 4454 GLU A OE2   1 
ATOM   21458 N  N     . LEU A 1 4455 ? 245.181 223.324 219.636 1.00 56.98  ? 4455 LEU A N     1 
ATOM   21459 C  CA    . LEU A 1 4455 ? 246.543 223.847 219.587 1.00 54.05  ? 4455 LEU A CA    1 
ATOM   21460 C  C     . LEU A 1 4455 ? 246.776 224.679 218.332 1.00 57.08  ? 4455 LEU A C     1 
ATOM   21461 O  O     . LEU A 1 4455 ? 247.393 225.748 218.396 1.00 61.33  ? 4455 LEU A O     1 
ATOM   21462 C  CB    . LEU A 1 4455 ? 247.549 222.700 219.665 1.00 57.44  ? 4455 LEU A CB    1 
ATOM   21463 C  CG    . LEU A 1 4455 ? 247.808 222.129 221.059 1.00 59.96  ? 4455 LEU A CG    1 
ATOM   21464 C  CD1   . LEU A 1 4455 ? 249.033 221.233 221.050 1.00 57.93  ? 4455 LEU A CD1   1 
ATOM   21465 C  CD2   . LEU A 1 4455 ? 247.964 223.244 222.076 1.00 55.69  ? 4455 LEU A CD2   1 
ATOM   21466 N  N     . VAL A 1 4456 ? 246.300 224.203 217.180 1.00 62.69  ? 4456 VAL A N     1 
ATOM   21467 C  CA    . VAL A 1 4456 ? 246.446 224.971 215.948 1.00 63.73  ? 4456 VAL A CA    1 
ATOM   21468 C  C     . VAL A 1 4456 ? 245.606 226.241 216.005 1.00 65.76  ? 4456 VAL A C     1 
ATOM   21469 O  O     . VAL A 1 4456 ? 246.061 227.320 215.608 1.00 67.33  ? 4456 VAL A O     1 
ATOM   21470 C  CB    . VAL A 1 4456 ? 246.085 224.105 214.729 1.00 60.14  ? 4456 VAL A CB    1 
ATOM   21471 C  CG1   . VAL A 1 4456 ? 246.134 224.933 213.460 1.00 59.27  ? 4456 VAL A CG1   1 
ATOM   21472 C  CG2   . VAL A 1 4456 ? 247.034 222.931 214.620 1.00 62.07  ? 4456 VAL A CG2   1 
ATOM   21473 N  N     . LYS A 1 4457 ? 244.373 226.139 216.503 1.00 62.60  ? 4457 LYS A N     1 
ATOM   21474 C  CA    . LYS A 1 4457 ? 243.502 227.304 216.573 1.00 63.21  ? 4457 LYS A CA    1 
ATOM   21475 C  C     . LYS A 1 4457 ? 243.904 228.284 217.668 1.00 63.27  ? 4457 LYS A C     1 
ATOM   21476 O  O     . LYS A 1 4457 ? 243.350 229.387 217.719 1.00 59.18  ? 4457 LYS A O     1 
ATOM   21477 C  CB    . LYS A 1 4457 ? 242.055 226.855 216.775 1.00 64.45  ? 4457 LYS A CB    1 
ATOM   21478 C  CG    . LYS A 1 4457 ? 241.029 227.763 216.120 1.00 64.45  ? 4457 LYS A CG    1 
ATOM   21479 C  CD    . LYS A 1 4457 ? 239.616 227.254 216.343 1.00 63.73  ? 4457 LYS A CD    1 
ATOM   21480 C  CE    . LYS A 1 4457 ? 239.509 225.769 216.042 1.00 64.77  ? 4457 LYS A CE    1 
ATOM   21481 N  NZ    . LYS A 1 4457 ? 239.952 225.452 214.656 1.00 64.75  ? 4457 LYS A NZ    1 
ATOM   21482 N  N     . GLY A 1 4458 ? 244.842 227.916 218.539 1.00 64.38  ? 4458 GLY A N     1 
ATOM   21483 C  CA    . GLY A 1 4458 ? 245.345 228.824 219.549 1.00 57.61  ? 4458 GLY A CA    1 
ATOM   21484 C  C     . GLY A 1 4458 ? 244.589 228.841 220.857 1.00 61.79  ? 4458 GLY A C     1 
ATOM   21485 O  O     . GLY A 1 4458 ? 244.928 229.642 221.735 1.00 62.07  ? 4458 GLY A O     1 
ATOM   21486 N  N     . ILE A 1 4459 ? 243.579 227.994 221.020 1.00 66.20  ? 4459 ILE A N     1 
ATOM   21487 C  CA    . ILE A 1 4459 ? 242.817 227.910 222.261 1.00 64.35  ? 4459 ILE A CA    1 
ATOM   21488 C  C     . ILE A 1 4459 ? 243.499 226.930 223.202 1.00 63.30  ? 4459 ILE A C     1 
ATOM   21489 O  O     . ILE A 1 4459 ? 243.948 225.856 222.786 1.00 70.96  ? 4459 ILE A O     1 
ATOM   21490 C  CB    . ILE A 1 4459 ? 241.355 227.499 221.992 1.00 61.08  ? 4459 ILE A CB    1 
ATOM   21491 C  CG1   . ILE A 1 4459 ? 240.628 228.568 221.174 1.00 66.43  ? 4459 ILE A CG1   1 
ATOM   21492 C  CG2   . ILE A 1 4459 ? 240.617 227.234 223.293 1.00 59.72  ? 4459 ILE A CG2   1 
ATOM   21493 C  CD1   . ILE A 1 4459 ? 240.729 228.394 219.685 1.00 65.04  ? 4459 ILE A CD1   1 
ATOM   21494 N  N     . LEU A 1 4460 ? 243.597 227.309 224.471 1.00 61.50  ? 4460 LEU A N     1 
ATOM   21495 C  CA    . LEU A 1 4460 ? 244.181 226.429 225.471 1.00 61.45  ? 4460 LEU A CA    1 
ATOM   21496 C  C     . LEU A 1 4460 ? 243.338 225.165 225.604 1.00 65.84  ? 4460 LEU A C     1 
ATOM   21497 O  O     . LEU A 1 4460 ? 242.116 225.258 225.783 1.00 61.05  ? 4460 LEU A O     1 
ATOM   21498 C  CB    . LEU A 1 4460 ? 244.273 227.141 226.818 1.00 58.29  ? 4460 LEU A CB    1 
ATOM   21499 C  CG    . LEU A 1 4460 ? 244.557 226.254 228.030 1.00 58.47  ? 4460 LEU A CG    1 
ATOM   21500 C  CD1   . LEU A 1 4460 ? 245.991 225.763 228.010 1.00 61.43  ? 4460 LEU A CD1   1 
ATOM   21501 C  CD2   . LEU A 1 4460 ? 244.256 226.997 229.318 1.00 58.96  ? 4460 LEU A CD2   1 
ATOM   21502 N  N     . PRO A 1 4461 ? 243.936 223.979 225.502 1.00 65.31  ? 4461 PRO A N     1 
ATOM   21503 C  CA    . PRO A 1 4461 ? 243.159 222.746 225.672 1.00 56.95  ? 4461 PRO A CA    1 
ATOM   21504 C  C     . PRO A 1 4461 ? 242.527 222.683 227.053 1.00 57.78  ? 4461 PRO A C     1 
ATOM   21505 O  O     . PRO A 1 4461 ? 243.144 223.045 228.056 1.00 61.04  ? 4461 PRO A O     1 
ATOM   21506 C  CB    . PRO A 1 4461 ? 244.204 221.643 225.476 1.00 56.48  ? 4461 PRO A CB    1 
ATOM   21507 C  CG    . PRO A 1 4461 ? 245.271 222.280 224.655 1.00 57.83  ? 4461 PRO A CG    1 
ATOM   21508 C  CD    . PRO A 1 4461 ? 245.327 223.706 225.103 1.00 61.48  ? 4461 PRO A CD    1 
ATOM   21509 N  N     . ARG A 1 4462 ? 241.279 222.214 227.098 1.00 58.50  ? 4462 ARG A N     1 
ATOM   21510 C  CA    . ARG A 1 4462 ? 240.580 222.115 228.374 1.00 65.44  ? 4462 ARG A CA    1 
ATOM   21511 C  C     . ARG A 1 4462 ? 241.171 221.019 229.247 1.00 64.76  ? 4462 ARG A C     1 
ATOM   21512 O  O     . ARG A 1 4462 ? 241.035 221.060 230.475 1.00 67.05  ? 4462 ARG A O     1 
ATOM   21513 C  CB    . ARG A 1 4462 ? 239.090 221.868 228.141 1.00 61.53  ? 4462 ARG A CB    1 
ATOM   21514 C  CG    . ARG A 1 4462 ? 238.359 223.001 227.427 1.00 63.87  ? 4462 ARG A CG    1 
ATOM   21515 C  CD    . ARG A 1 4462 ? 238.312 224.280 228.258 1.00 69.05  ? 4462 ARG A CD    1 
ATOM   21516 N  NE    . ARG A 1 4462 ? 239.500 225.107 228.078 1.00 73.19  ? 4462 ARG A NE    1 
ATOM   21517 C  CZ    . ARG A 1 4462 ? 239.826 226.132 228.854 1.00 69.58  ? 4462 ARG A CZ    1 
ATOM   21518 N  NH1   . ARG A 1 4462 ? 239.078 226.483 229.887 1.00 66.66  ? 4462 ARG A NH1   1 
ATOM   21519 N  NH2   . ARG A 1 4462 ? 240.931 226.821 228.587 1.00 66.72  ? 4462 ARG A NH2   1 
ATOM   21520 N  N     . SER A 1 4463 ? 241.824 220.032 228.635 1.00 56.13  ? 4463 SER A N     1 
ATOM   21521 C  CA    . SER A 1 4463 ? 242.474 218.969 229.388 1.00 55.59  ? 4463 SER A CA    1 
ATOM   21522 C  C     . SER A 1 4463 ? 243.747 219.434 230.081 1.00 61.24  ? 4463 SER A C     1 
ATOM   21523 O  O     . SER A 1 4463 ? 244.321 218.666 230.861 1.00 62.20  ? 4463 SER A O     1 
ATOM   21524 C  CB    . SER A 1 4463 ? 242.777 217.789 228.463 1.00 59.64  ? 4463 SER A CB    1 
ATOM   21525 O  OG    . SER A 1 4463 ? 243.737 218.141 227.483 1.00 64.62  ? 4463 SER A OG    1 
ATOM   21526 N  N     . TRP A 1 4464 ? 244.213 220.653 229.806 1.00 62.95  ? 4464 TRP A N     1 
ATOM   21527 C  CA    . TRP A 1 4464 ? 245.404 221.188 230.453 1.00 57.95  ? 4464 TRP A CA    1 
ATOM   21528 C  C     . TRP A 1 4464 ? 245.102 222.209 231.541 1.00 58.25  ? 4464 TRP A C     1 
ATOM   21529 O  O     . TRP A 1 4464 ? 245.971 222.464 232.381 1.00 64.49  ? 4464 TRP A O     1 
ATOM   21530 C  CB    . TRP A 1 4464 ? 246.333 221.833 229.419 1.00 55.47  ? 4464 TRP A CB    1 
ATOM   21531 C  CG    . TRP A 1 4464 ? 246.909 220.867 228.437 1.00 55.61  ? 4464 TRP A CG    1 
ATOM   21532 C  CD1   . TRP A 1 4464 ? 246.641 219.534 228.345 1.00 56.82  ? 4464 TRP A CD1   1 
ATOM   21533 C  CD2   . TRP A 1 4464 ? 247.864 221.156 227.412 1.00 57.65  ? 4464 TRP A CD2   1 
ATOM   21534 N  NE1   . TRP A 1 4464 ? 247.365 218.975 227.323 1.00 58.52  ? 4464 TRP A NE1   1 
ATOM   21535 C  CE2   . TRP A 1 4464 ? 248.125 219.951 226.734 1.00 59.60  ? 4464 TRP A CE2   1 
ATOM   21536 C  CE3   . TRP A 1 4464 ? 248.523 222.317 226.998 1.00 55.01  ? 4464 TRP A CE3   1 
ATOM   21537 C  CZ2   . TRP A 1 4464 ? 249.014 219.873 225.668 1.00 55.09  ? 4464 TRP A CZ2   1 
ATOM   21538 C  CZ3   . TRP A 1 4464 ? 249.404 222.237 225.940 1.00 57.63  ? 4464 TRP A CZ3   1 
ATOM   21539 C  CH2   . TRP A 1 4464 ? 249.642 221.025 225.288 1.00 57.47  ? 4464 TRP A CH2   1 
ATOM   21540 N  N     . SER A 1 4465 ? 243.908 222.794 231.552 1.00 58.08  ? 4465 SER A N     1 
ATOM   21541 C  CA    . SER A 1 4465 ? 243.575 223.856 232.500 1.00 63.94  ? 4465 SER A CA    1 
ATOM   21542 C  C     . SER A 1 4465 ? 243.133 223.231 233.817 1.00 64.03  ? 4465 SER A C     1 
ATOM   21543 O  O     . SER A 1 4465 ? 241.955 222.941 234.032 1.00 65.13  ? 4465 SER A O     1 
ATOM   21544 C  CB    . SER A 1 4465 ? 242.497 224.766 231.928 1.00 62.70  ? 4465 SER A CB    1 
ATOM   21545 O  OG    . SER A 1 4465 ? 241.325 224.033 231.623 1.00 65.25  ? 4465 SER A OG    1 
ATOM   21546 N  N     . HIS A 1 4466 ? 244.094 223.027 234.718 1.00 60.34  ? 4466 HIS A N     1 
ATOM   21547 C  CA    . HIS A 1 4466 ? 243.817 222.493 236.043 1.00 53.95  ? 4466 HIS A CA    1 
ATOM   21548 C  C     . HIS A 1 4466 ? 244.004 223.511 237.158 1.00 60.57  ? 4466 HIS A C     1 
ATOM   21549 O  O     . HIS A 1 4466 ? 243.927 223.137 238.333 1.00 65.43  ? 4466 HIS A O     1 
ATOM   21550 C  CB    . HIS A 1 4466 ? 244.695 221.267 236.325 1.00 56.37  ? 4466 HIS A CB    1 
ATOM   21551 C  CG    . HIS A 1 4466 ? 244.360 220.079 235.480 1.00 61.61  ? 4466 HIS A CG    1 
ATOM   21552 N  ND1   . HIS A 1 4466 ? 245.142 219.672 234.421 1.00 65.88  ? 4466 HIS A ND1   1 
ATOM   21553 C  CD2   . HIS A 1 4466 ? 243.325 219.207 235.540 1.00 58.95  ? 4466 HIS A CD2   1 
ATOM   21554 C  CE1   . HIS A 1 4466 ? 244.604 218.602 233.865 1.00 62.52  ? 4466 HIS A CE1   1 
ATOM   21555 N  NE2   . HIS A 1 4466 ? 243.500 218.301 234.523 1.00 62.82  ? 4466 HIS A NE2   1 
ATOM   21556 N  N     . TYR A 1 4467 ? 244.246 224.777 236.832 1.00 60.36  ? 4467 TYR A N     1 
ATOM   21557 C  CA    . TYR A 1 4467 ? 244.322 225.825 237.836 1.00 51.31  ? 4467 TYR A CA    1 
ATOM   21558 C  C     . TYR A 1 4467 ? 243.640 227.071 237.296 1.00 53.89  ? 4467 TYR A C     1 
ATOM   21559 O  O     . TYR A 1 4467 ? 243.312 227.150 236.110 1.00 61.63  ? 4467 TYR A O     1 
ATOM   21560 C  CB    . TYR A 1 4467 ? 245.774 226.126 238.247 1.00 55.01  ? 4467 TYR A CB    1 
ATOM   21561 C  CG    . TYR A 1 4467 ? 246.747 226.360 237.110 1.00 52.66  ? 4467 TYR A CG    1 
ATOM   21562 C  CD1   . TYR A 1 4467 ? 246.766 227.561 236.419 1.00 58.04  ? 4467 TYR A CD1   1 
ATOM   21563 C  CD2   . TYR A 1 4467 ? 247.657 225.382 236.739 1.00 51.10  ? 4467 TYR A CD2   1 
ATOM   21564 C  CE1   . TYR A 1 4467 ? 247.663 227.779 235.391 1.00 60.93  ? 4467 TYR A CE1   1 
ATOM   21565 C  CE2   . TYR A 1 4467 ? 248.553 225.590 235.711 1.00 52.34  ? 4467 TYR A CE2   1 
ATOM   21566 C  CZ    . TYR A 1 4467 ? 248.551 226.790 235.040 1.00 55.47  ? 4467 TYR A CZ    1 
ATOM   21567 O  OH    . TYR A 1 4467 ? 249.441 227.005 234.015 1.00 56.93  ? 4467 TYR A OH    1 
ATOM   21568 N  N     . THR A 1 4468 ? 243.413 228.038 238.183 1.00 55.78  ? 4468 THR A N     1 
ATOM   21569 C  CA    . THR A 1 4468 ? 242.709 229.252 237.797 1.00 55.34  ? 4468 THR A CA    1 
ATOM   21570 C  C     . THR A 1 4468 ? 243.520 230.043 236.780 1.00 59.67  ? 4468 THR A C     1 
ATOM   21571 O  O     . THR A 1 4468 ? 244.704 230.319 236.986 1.00 61.56  ? 4468 THR A O     1 
ATOM   21572 C  CB    . THR A 1 4468 ? 242.423 230.111 239.027 1.00 58.40  ? 4468 THR A CB    1 
ATOM   21573 O  OG1   . THR A 1 4468 ? 241.459 229.452 239.856 1.00 61.96  ? 4468 THR A OG1   1 
ATOM   21574 C  CG2   . THR A 1 4468 ? 241.876 231.456 238.605 1.00 60.39  ? 4468 THR A CG2   1 
ATOM   21575 N  N     . VAL A 1 4469 ? 242.867 230.407 235.682 1.00 58.63  ? 4469 VAL A N     1 
ATOM   21576 C  CA    . VAL A 1 4469 ? 243.514 231.082 234.562 1.00 56.24  ? 4469 VAL A CA    1 
ATOM   21577 C  C     . VAL A 1 4469 ? 242.591 232.202 234.095 1.00 58.57  ? 4469 VAL A C     1 
ATOM   21578 O  O     . VAL A 1 4469 ? 241.363 232.044 234.142 1.00 62.61  ? 4469 VAL A O     1 
ATOM   21579 C  CB    . VAL A 1 4469 ? 243.827 230.082 233.433 1.00 58.33  ? 4469 VAL A CB    1 
ATOM   21580 C  CG1   . VAL A 1 4469 ? 244.064 230.781 232.108 1.00 58.85  ? 4469 VAL A CG1   1 
ATOM   21581 C  CG2   . VAL A 1 4469 ? 245.026 229.237 233.794 1.00 54.30  ? 4469 VAL A CG2   1 
ATOM   21582 N  N     . PRO A 1 4470 ? 243.123 233.345 233.663 1.00 53.05  ? 4470 PRO A N     1 
ATOM   21583 C  CA    . PRO A 1 4470 ? 242.268 234.372 233.057 1.00 54.56  ? 4470 PRO A CA    1 
ATOM   21584 C  C     . PRO A 1 4470 ? 241.517 233.823 231.851 1.00 65.17  ? 4470 PRO A C     1 
ATOM   21585 O  O     . PRO A 1 4470 ? 242.021 232.976 231.112 1.00 71.66  ? 4470 PRO A O     1 
ATOM   21586 C  CB    . PRO A 1 4470 ? 243.260 235.468 232.657 1.00 54.59  ? 4470 PRO A CB    1 
ATOM   21587 C  CG    . PRO A 1 4470 ? 244.410 235.284 233.580 1.00 55.07  ? 4470 PRO A CG    1 
ATOM   21588 C  CD    . PRO A 1 4470 ? 244.503 233.817 233.859 1.00 56.01  ? 4470 PRO A CD    1 
ATOM   21589 N  N     . ALA A 1 4471 ? 240.291 234.319 231.665 1.00 55.28  ? 4471 ALA A N     1 
ATOM   21590 C  CA    . ALA A 1 4471 ? 239.370 233.716 230.706 1.00 52.37  ? 4471 ALA A CA    1 
ATOM   21591 C  C     . ALA A 1 4471 ? 239.881 233.794 229.272 1.00 56.35  ? 4471 ALA A C     1 
ATOM   21592 O  O     . ALA A 1 4471 ? 239.494 232.970 228.435 1.00 52.43  ? 4471 ALA A O     1 
ATOM   21593 C  CB    . ALA A 1 4471 ? 238.000 234.384 230.813 1.00 54.43  ? 4471 ALA A CB    1 
ATOM   21594 N  N     . GLY A 1 4472 ? 240.732 234.766 228.962 1.00 59.99  ? 4472 GLY A N     1 
ATOM   21595 C  CA    . GLY A 1 4472 ? 241.195 234.978 227.607 1.00 62.30  ? 4472 GLY A CA    1 
ATOM   21596 C  C     . GLY A 1 4472 ? 242.619 234.564 227.306 1.00 67.22  ? 4472 GLY A C     1 
ATOM   21597 O  O     . GLY A 1 4472 ? 243.132 234.917 226.238 1.00 65.27  ? 4472 GLY A O     1 
ATOM   21598 N  N     . MET A 1 4473 ? 243.278 233.833 228.201 1.00 66.36  ? 4473 MET A N     1 
ATOM   21599 C  CA    . MET A 1 4473 ? 244.678 233.482 227.995 1.00 64.75  ? 4473 MET A CA    1 
ATOM   21600 C  C     . MET A 1 4473 ? 244.825 232.420 226.910 1.00 62.05  ? 4473 MET A C     1 
ATOM   21601 O  O     . MET A 1 4473 ? 244.060 231.454 226.854 1.00 59.88  ? 4473 MET A O     1 
ATOM   21602 C  CB    . MET A 1 4473 ? 245.296 233.000 229.308 1.00 59.71  ? 4473 MET A CB    1 
ATOM   21603 C  CG    . MET A 1 4473 ? 246.732 232.522 229.182 1.00 61.52  ? 4473 MET A CG    1 
ATOM   21604 S  SD    . MET A 1 4473 ? 247.301 231.572 230.603 1.00 62.65  ? 4473 MET A SD    1 
ATOM   21605 C  CE    . MET A 1 4473 ? 247.210 232.803 231.894 1.00 56.67  ? 4473 MET A CE    1 
ATOM   21606 N  N     . THR A 1 4474 ? 245.823 232.605 226.046 1.00 60.80  ? 4474 THR A N     1 
ATOM   21607 C  CA    . THR A 1 4474 ? 246.068 231.707 224.929 1.00 62.81  ? 4474 THR A CA    1 
ATOM   21608 C  C     . THR A 1 4474 ? 247.023 230.588 225.341 1.00 60.69  ? 4474 THR A C     1 
ATOM   21609 O  O     . THR A 1 4474 ? 247.296 230.371 226.523 1.00 66.11  ? 4474 THR A O     1 
ATOM   21610 C  CB    . THR A 1 4474 ? 246.617 232.478 223.729 1.00 64.39  ? 4474 THR A CB    1 
ATOM   21611 O  OG1   . THR A 1 4474 ? 247.969 232.873 223.988 1.00 62.45  ? 4474 THR A OG1   1 
ATOM   21612 C  CG2   . THR A 1 4474 ? 245.774 233.714 223.457 1.00 59.81  ? 4474 THR A CG2   1 
ATOM   21613 N  N     . VAL A 1 4475 ? 247.541 229.861 224.348 1.00 57.52  ? 4475 VAL A N     1 
ATOM   21614 C  CA    . VAL A 1 4475 ? 248.347 228.682 224.647 1.00 56.92  ? 4475 VAL A CA    1 
ATOM   21615 C  C     . VAL A 1 4475 ? 249.801 229.063 224.888 1.00 60.36  ? 4475 VAL A C     1 
ATOM   21616 O  O     . VAL A 1 4475 ? 250.485 228.441 225.705 1.00 64.77  ? 4475 VAL A O     1 
ATOM   21617 C  CB    . VAL A 1 4475 ? 248.224 227.639 223.523 1.00 61.83  ? 4475 VAL A CB    1 
ATOM   21618 C  CG1   . VAL A 1 4475 ? 248.872 226.336 223.950 1.00 59.07  ? 4475 VAL A CG1   1 
ATOM   21619 C  CG2   . VAL A 1 4475 ? 246.783 227.419 223.158 1.00 60.58  ? 4475 VAL A CG2   1 
ATOM   21620 N  N     . ILE A 1 4476 ? 250.310 230.065 224.167 1.00 55.56  ? 4476 ILE A N     1 
ATOM   21621 C  CA    . ILE A 1 4476 ? 251.697 230.481 224.366 1.00 56.89  ? 4476 ILE A CA    1 
ATOM   21622 C  C     . ILE A 1 4476 ? 251.883 231.067 225.760 1.00 60.58  ? 4476 ILE A C     1 
ATOM   21623 O  O     . ILE A 1 4476 ? 252.835 230.726 226.479 1.00 63.69  ? 4476 ILE A O     1 
ATOM   21624 C  CB    . ILE A 1 4476 ? 252.120 231.480 223.273 1.00 58.93  ? 4476 ILE A CB    1 
ATOM   21625 C  CG1   . ILE A 1 4476 ? 251.924 230.872 221.883 1.00 60.23  ? 4476 ILE A CG1   1 
ATOM   21626 C  CG2   . ILE A 1 4476 ? 253.566 231.902 223.469 1.00 58.23  ? 4476 ILE A CG2   1 
ATOM   21627 C  CD1   . ILE A 1 4476 ? 250.708 231.394 221.153 1.00 56.53  ? 4476 ILE A CD1   1 
ATOM   21628 N  N     . GLN A 1 4477 ? 250.971 231.954 226.165 1.00 58.74  ? 4477 GLN A N     1 
ATOM   21629 C  CA    . GLN A 1 4477 ? 251.024 232.514 227.510 1.00 55.86  ? 4477 GLN A CA    1 
ATOM   21630 C  C     . GLN A 1 4477 ? 250.875 231.424 228.559 1.00 58.49  ? 4477 GLN A C     1 
ATOM   21631 O  O     . GLN A 1 4477 ? 251.570 231.442 229.582 1.00 60.17  ? 4477 GLN A O     1 
ATOM   21632 C  CB    . GLN A 1 4477 ? 249.932 233.566 227.687 1.00 51.30  ? 4477 GLN A CB    1 
ATOM   21633 C  CG    . GLN A 1 4477 ? 249.767 234.510 226.516 1.00 54.33  ? 4477 GLN A CG    1 
ATOM   21634 C  CD    . GLN A 1 4477 ? 248.622 235.480 226.719 1.00 59.02  ? 4477 GLN A CD    1 
ATOM   21635 O  OE1   . GLN A 1 4477 ? 247.470 235.075 226.860 1.00 60.44  ? 4477 GLN A OE1   1 
ATOM   21636 N  NE2   . GLN A 1 4477 ? 248.936 236.768 226.740 1.00 59.70  ? 4477 GLN A NE2   1 
ATOM   21637 N  N     . TRP A 1 4478 ? 249.969 230.473 228.327 1.00 51.63  ? 4478 TRP A N     1 
ATOM   21638 C  CA    . TRP A 1 4478 ? 249.773 229.399 229.292 1.00 47.91  ? 4478 TRP A CA    1 
ATOM   21639 C  C     . TRP A 1 4478 ? 251.015 228.531 229.405 1.00 50.60  ? 4478 TRP A C     1 
ATOM   21640 O  O     . TRP A 1 4478 ? 251.372 228.096 230.501 1.00 60.60  ? 4478 TRP A O     1 
ATOM   21641 C  CB    . TRP A 1 4478 ? 248.564 228.548 228.912 1.00 51.39  ? 4478 TRP A CB    1 
ATOM   21642 C  CG    . TRP A 1 4478 ? 248.171 227.587 229.994 1.00 49.16  ? 4478 TRP A CG    1 
ATOM   21643 C  CD1   . TRP A 1 4478 ? 247.231 227.787 230.958 1.00 48.93  ? 4478 TRP A CD1   1 
ATOM   21644 C  CD2   . TRP A 1 4478 ? 248.719 226.284 230.231 1.00 52.33  ? 4478 TRP A CD2   1 
ATOM   21645 N  NE1   . TRP A 1 4478 ? 247.152 226.688 231.777 1.00 55.83  ? 4478 TRP A NE1   1 
ATOM   21646 C  CE2   . TRP A 1 4478 ? 248.056 225.752 231.352 1.00 56.12  ? 4478 TRP A CE2   1 
ATOM   21647 C  CE3   . TRP A 1 4478 ? 249.701 225.514 229.602 1.00 47.94  ? 4478 TRP A CE3   1 
ATOM   21648 C  CZ2   . TRP A 1 4478 ? 248.345 224.488 231.857 1.00 53.30  ? 4478 TRP A CZ2   1 
ATOM   21649 C  CZ3   . TRP A 1 4478 ? 249.985 224.262 230.105 1.00 44.27  ? 4478 TRP A CZ3   1 
ATOM   21650 C  CH2   . TRP A 1 4478 ? 249.310 223.761 231.221 1.00 49.38  ? 4478 TRP A CH2   1 
ATOM   21651 N  N     . VAL A 1 4479 ? 251.682 228.259 228.284 1.00 43.60  ? 4479 VAL A N     1 
ATOM   21652 C  CA    . VAL A 1 4479 ? 252.891 227.444 228.321 1.00 49.50  ? 4479 VAL A CA    1 
ATOM   21653 C  C     . VAL A 1 4479 ? 253.993 228.165 229.083 1.00 52.92  ? 4479 VAL A C     1 
ATOM   21654 O  O     . VAL A 1 4479 ? 254.695 227.561 229.901 1.00 56.63  ? 4479 VAL A O     1 
ATOM   21655 C  CB    . VAL A 1 4479 ? 253.330 227.070 226.894 1.00 49.96  ? 4479 VAL A CB    1 
ATOM   21656 C  CG1   . VAL A 1 4479 ? 254.797 226.681 226.872 1.00 55.76  ? 4479 VAL A CG1   1 
ATOM   21657 C  CG2   . VAL A 1 4479 ? 252.476 225.934 226.368 1.00 48.97  ? 4479 VAL A CG2   1 
ATOM   21658 N  N     . SER A 1 4480 ? 254.160 229.468 228.838 1.00 52.69  ? 4480 SER A N     1 
ATOM   21659 C  CA    . SER A 1 4480 ? 255.172 230.222 229.575 1.00 50.35  ? 4480 SER A CA    1 
ATOM   21660 C  C     . SER A 1 4480 ? 254.864 230.253 231.071 1.00 57.53  ? 4480 SER A C     1 
ATOM   21661 O  O     . SER A 1 4480 ? 255.755 230.039 231.907 1.00 58.65  ? 4480 SER A O     1 
ATOM   21662 C  CB    . SER A 1 4480 ? 255.277 231.639 229.017 1.00 52.68  ? 4480 SER A CB    1 
ATOM   21663 O  OG    . SER A 1 4480 ? 255.761 231.624 227.686 1.00 58.73  ? 4480 SER A OG    1 
ATOM   21664 N  N     . ASP A 1 4481 ? 253.602 230.505 231.426 1.00 56.80  ? 4481 ASP A N     1 
ATOM   21665 C  CA    . ASP A 1 4481 ? 253.211 230.539 232.831 1.00 50.89  ? 4481 ASP A CA    1 
ATOM   21666 C  C     . ASP A 1 4481 ? 253.398 229.180 233.492 1.00 56.32  ? 4481 ASP A C     1 
ATOM   21667 O  O     . ASP A 1 4481 ? 253.876 229.096 234.628 1.00 61.71  ? 4481 ASP A O     1 
ATOM   21668 C  CB    . ASP A 1 4481 ? 251.761 230.998 232.955 1.00 49.38  ? 4481 ASP A CB    1 
ATOM   21669 C  CG    . ASP A 1 4481 ? 251.417 231.467 234.350 1.00 61.45  ? 4481 ASP A CG    1 
ATOM   21670 O  OD1   . ASP A 1 4481 ? 252.351 231.733 235.134 1.00 63.80  ? 4481 ASP A OD1   1 
ATOM   21671 O  OD2   . ASP A 1 4481 ? 250.213 231.566 234.664 1.00 60.07  ? 4481 ASP A OD2   1 
ATOM   21672 N  N     . PHE A 1 4482 ? 253.020 228.107 232.797 1.00 47.34  ? 4482 PHE A N     1 
ATOM   21673 C  CA    . PHE A 1 4482 ? 253.181 226.764 233.334 1.00 43.14  ? 4482 PHE A CA    1 
ATOM   21674 C  C     . PHE A 1 4482 ? 254.650 226.417 233.511 1.00 46.51  ? 4482 PHE A C     1 
ATOM   21675 O  O     . PHE A 1 4482 ? 255.026 225.760 234.486 1.00 58.66  ? 4482 PHE A O     1 
ATOM   21676 C  CB    . PHE A 1 4482 ? 252.491 225.758 232.416 1.00 44.11  ? 4482 PHE A CB    1 
ATOM   21677 C  CG    . PHE A 1 4482 ? 252.570 224.344 232.898 1.00 50.14  ? 4482 PHE A CG    1 
ATOM   21678 C  CD1   . PHE A 1 4482 ? 251.932 223.959 234.061 1.00 51.46  ? 4482 PHE A CD1   1 
ATOM   21679 C  CD2   . PHE A 1 4482 ? 253.280 223.396 232.183 1.00 50.26  ? 4482 PHE A CD2   1 
ATOM   21680 C  CE1   . PHE A 1 4482 ? 252.003 222.660 234.505 1.00 48.95  ? 4482 PHE A CE1   1 
ATOM   21681 C  CE2   . PHE A 1 4482 ? 253.353 222.095 232.623 1.00 51.06  ? 4482 PHE A CE2   1 
ATOM   21682 C  CZ    . PHE A 1 4482 ? 252.713 221.727 233.785 1.00 52.49  ? 4482 PHE A CZ    1 
ATOM   21683 N  N     . SER A 1 4483 ? 255.497 226.841 232.572 1.00 41.89  ? 4483 SER A N     1 
ATOM   21684 C  CA    . SER A 1 4483 ? 256.930 226.627 232.725 1.00 46.64  ? 4483 SER A CA    1 
ATOM   21685 C  C     . SER A 1 4483 ? 257.455 227.337 233.963 1.00 51.21  ? 4483 SER A C     1 
ATOM   21686 O  O     . SER A 1 4483 ? 258.245 226.769 234.723 1.00 56.01  ? 4483 SER A O     1 
ATOM   21687 C  CB    . SER A 1 4483 ? 257.669 227.106 231.477 1.00 51.28  ? 4483 SER A CB    1 
ATOM   21688 O  OG    . SER A 1 4483 ? 257.238 226.400 230.329 1.00 57.29  ? 4483 SER A OG    1 
ATOM   21689 N  N     . GLU A 1 4484 ? 257.018 228.578 234.189 1.00 54.41  ? 4484 GLU A N     1 
ATOM   21690 C  CA    . GLU A 1 4484 ? 257.456 229.295 235.385 1.00 53.28  ? 4484 GLU A CA    1 
ATOM   21691 C  C     . GLU A 1 4484 ? 256.969 228.607 236.658 1.00 54.50  ? 4484 GLU A C     1 
ATOM   21692 O  O     . GLU A 1 4484 ? 257.714 228.497 237.642 1.00 54.90  ? 4484 GLU A O     1 
ATOM   21693 C  CB    . GLU A 1 4484 ? 256.978 230.744 235.333 1.00 51.92  ? 4484 GLU A CB    1 
ATOM   21694 C  CG    . GLU A 1 4484 ? 257.617 231.547 234.217 1.00 56.15  ? 4484 GLU A CG    1 
ATOM   21695 C  CD    . GLU A 1 4484 ? 259.106 231.746 234.424 1.00 61.57  ? 4484 GLU A CD    1 
ATOM   21696 O  OE1   . GLU A 1 4484 ? 259.543 231.828 235.591 1.00 60.88  ? 4484 GLU A OE1   1 
ATOM   21697 O  OE2   . GLU A 1 4484 ? 259.844 231.815 233.418 1.00 61.72  ? 4484 GLU A OE2   1 
ATOM   21698 N  N     . ARG A 1 4485 ? 255.721 228.135 236.655 1.00 46.83  ? 4485 ARG A N     1 
ATOM   21699 C  CA    . ARG A 1 4485 ? 255.185 227.434 237.819 1.00 46.85  ? 4485 ARG A CA    1 
ATOM   21700 C  C     . ARG A 1 4485 ? 255.960 226.154 238.102 1.00 51.13  ? 4485 ARG A C     1 
ATOM   21701 O  O     . ARG A 1 4485 ? 256.272 225.848 239.259 1.00 58.01  ? 4485 ARG A O     1 
ATOM   21702 C  CB    . ARG A 1 4485 ? 253.705 227.124 237.602 1.00 44.14  ? 4485 ARG A CB    1 
ATOM   21703 C  CG    . ARG A 1 4485 ? 252.830 228.351 237.480 1.00 44.05  ? 4485 ARG A CG    1 
ATOM   21704 C  CD    . ARG A 1 4485 ? 251.378 227.976 237.281 1.00 45.79  ? 4485 ARG A CD    1 
ATOM   21705 N  NE    . ARG A 1 4485 ? 250.521 229.152 237.209 1.00 48.55  ? 4485 ARG A NE    1 
ATOM   21706 C  CZ    . ARG A 1 4485 ? 249.493 229.378 238.014 1.00 47.70  ? 4485 ARG A CZ    1 
ATOM   21707 N  NH1   . ARG A 1 4485 ? 249.163 228.525 238.968 1.00 51.51  ? 4485 ARG A NH1   1 
ATOM   21708 N  NH2   . ARG A 1 4485 ? 248.778 230.487 237.856 1.00 47.20  ? 4485 ARG A NH2   1 
ATOM   21709 N  N     . ILE A 1 4486 ? 256.278 225.391 237.056 1.00 46.41  ? 4486 ILE A N     1 
ATOM   21710 C  CA    . ILE A 1 4486 ? 257.026 224.153 237.239 1.00 41.23  ? 4486 ILE A CA    1 
ATOM   21711 C  C     . ILE A 1 4486 ? 258.445 224.447 237.706 1.00 47.09  ? 4486 ILE A C     1 
ATOM   21712 O  O     . ILE A 1 4486 ? 259.019 223.688 238.489 1.00 55.42  ? 4486 ILE A O     1 
ATOM   21713 C  CB    . ILE A 1 4486 ? 257.007 223.318 235.946 1.00 42.98  ? 4486 ILE A CB    1 
ATOM   21714 C  CG1   . ILE A 1 4486 ? 255.577 222.903 235.605 1.00 43.67  ? 4486 ILE A CG1   1 
ATOM   21715 C  CG2   . ILE A 1 4486 ? 257.873 222.082 236.093 1.00 45.16  ? 4486 ILE A CG2   1 
ATOM   21716 C  CD1   . ILE A 1 4486 ? 254.870 222.174 236.716 1.00 44.35  ? 4486 ILE A CD1   1 
ATOM   21717 N  N     . LYS A 1 4487 ? 259.039 225.546 237.235 1.00 44.40  ? 4487 LYS A N     1 
ATOM   21718 C  CA    . LYS A 1 4487 ? 260.361 225.925 237.726 1.00 41.70  ? 4487 LYS A CA    1 
ATOM   21719 C  C     . LYS A 1 4487 ? 260.321 226.272 239.209 1.00 50.04  ? 4487 LYS A C     1 
ATOM   21720 O  O     . LYS A 1 4487 ? 261.223 225.897 239.969 1.00 57.37  ? 4487 LYS A O     1 
ATOM   21721 C  CB    . LYS A 1 4487 ? 260.910 227.096 236.913 1.00 47.03  ? 4487 LYS A CB    1 
ATOM   21722 C  CG    . LYS A 1 4487 ? 261.255 226.743 235.480 1.00 52.90  ? 4487 LYS A CG    1 
ATOM   21723 C  CD    . LYS A 1 4487 ? 261.809 227.939 234.731 1.00 54.76  ? 4487 LYS A CD    1 
ATOM   21724 C  CE    . LYS A 1 4487 ? 262.034 227.607 233.268 1.00 54.97  ? 4487 LYS A CE    1 
ATOM   21725 N  NZ    . LYS A 1 4487 ? 263.100 226.584 233.095 1.00 55.18  ? 4487 LYS A NZ    1 
ATOM   21726 N  N     . GLN A 1 4488 ? 259.281 226.988 239.643 1.00 46.01  ? 4488 GLN A N     1 
ATOM   21727 C  CA    . GLN A 1 4488 ? 259.141 227.273 241.069 1.00 41.95  ? 4488 GLN A CA    1 
ATOM   21728 C  C     . GLN A 1 4488 ? 258.959 225.990 241.870 1.00 47.32  ? 4488 GLN A C     1 
ATOM   21729 O  O     . GLN A 1 4488 ? 259.520 225.843 242.962 1.00 49.59  ? 4488 GLN A O     1 
ATOM   21730 C  CB    . GLN A 1 4488 ? 257.971 228.223 241.317 1.00 43.72  ? 4488 GLN A CB    1 
ATOM   21731 C  CG    . GLN A 1 4488 ? 257.603 228.342 242.787 1.00 46.20  ? 4488 GLN A CG    1 
ATOM   21732 C  CD    . GLN A 1 4488 ? 256.400 229.221 243.027 1.00 47.47  ? 4488 GLN A CD    1 
ATOM   21733 O  OE1   . GLN A 1 4488 ? 256.418 230.089 243.897 1.00 47.37  ? 4488 GLN A OE1   1 
ATOM   21734 N  NE2   . GLN A 1 4488 ? 255.345 229.002 242.257 1.00 53.39  ? 4488 GLN A NE2   1 
ATOM   21735 N  N     . LEU A 1 4489 ? 258.167 225.053 241.346 1.00 52.22  ? 4489 LEU A N     1 
ATOM   21736 C  CA    . LEU A 1 4489 ? 257.999 223.769 242.021 1.00 42.16  ? 4489 LEU A CA    1 
ATOM   21737 C  C     . LEU A 1 4489 ? 259.308 222.993 242.086 1.00 40.96  ? 4489 LEU A C     1 
ATOM   21738 O  O     . LEU A 1 4489 ? 259.578 222.316 243.083 1.00 49.28  ? 4489 LEU A O     1 
ATOM   21739 C  CB    . LEU A 1 4489 ? 256.922 222.945 241.319 1.00 41.89  ? 4489 LEU A CB    1 
ATOM   21740 C  CG    . LEU A 1 4489 ? 255.484 223.374 241.599 1.00 39.58  ? 4489 LEU A CG    1 
ATOM   21741 C  CD1   . LEU A 1 4489 ? 254.510 222.444 240.909 1.00 39.48  ? 4489 LEU A CD1   1 
ATOM   21742 C  CD2   . LEU A 1 4489 ? 255.224 223.411 243.091 1.00 46.81  ? 4489 LEU A CD2   1 
ATOM   21743 N  N     . GLN A 1 4490 ? 260.126 223.070 241.034 1.00 46.43  ? 4490 GLN A N     1 
ATOM   21744 C  CA    . GLN A 1 4490 ? 261.441 222.438 241.061 1.00 44.43  ? 4490 GLN A CA    1 
ATOM   21745 C  C     . GLN A 1 4490 ? 262.324 223.062 242.131 1.00 48.84  ? 4490 GLN A C     1 
ATOM   21746 O  O     . GLN A 1 4490 ? 263.053 222.355 242.835 1.00 53.84  ? 4490 GLN A O     1 
ATOM   21747 C  CB    . GLN A 1 4490 ? 262.111 222.553 239.693 1.00 44.92  ? 4490 GLN A CB    1 
ATOM   21748 C  CG    . GLN A 1 4490 ? 261.518 221.664 238.621 1.00 50.21  ? 4490 GLN A CG    1 
ATOM   21749 C  CD    . GLN A 1 4490 ? 262.364 221.637 237.366 1.00 55.30  ? 4490 GLN A CD    1 
ATOM   21750 O  OE1   . GLN A 1 4490 ? 262.791 222.678 236.869 1.00 55.77  ? 4490 GLN A OE1   1 
ATOM   21751 N  NE2   . GLN A 1 4490 ? 262.612 220.443 236.845 1.00 55.77  ? 4490 GLN A NE2   1 
ATOM   21752 N  N     . ASN A 1 4491 ? 262.279 224.389 242.259 1.00 49.78  ? 4491 ASN A N     1 
ATOM   21753 C  CA    . ASN A 1 4491 ? 263.041 225.056 243.311 1.00 50.73  ? 4491 ASN A CA    1 
ATOM   21754 C  C     . ASN A 1 4491 ? 262.568 224.624 244.693 1.00 47.55  ? 4491 ASN A C     1 
ATOM   21755 O  O     . ASN A 1 4491 ? 263.385 224.401 245.594 1.00 51.50  ? 4491 ASN A O     1 
ATOM   21756 C  CB    . ASN A 1 4491 ? 262.936 226.571 243.157 1.00 52.58  ? 4491 ASN A CB    1 
ATOM   21757 C  CG    . ASN A 1 4491 ? 263.537 227.067 241.861 1.00 54.08  ? 4491 ASN A CG    1 
ATOM   21758 O  OD1   . ASN A 1 4491 ? 264.149 226.303 241.117 1.00 53.66  ? 4491 ASN A OD1   1 
ATOM   21759 N  ND2   . ASN A 1 4491 ? 263.365 228.352 241.583 1.00 50.99  ? 4491 ASN A ND2   1 
ATOM   21760 N  N     . ILE A 1 4492 ? 261.253 224.504 244.877 1.00 46.54  ? 4492 ILE A N     1 
ATOM   21761 C  CA    . ILE A 1 4492 ? 260.710 224.050 246.156 1.00 51.16  ? 4492 ILE A CA    1 
ATOM   21762 C  C     . ILE A 1 4492 ? 261.169 222.629 246.460 1.00 53.22  ? 4492 ILE A C     1 
ATOM   21763 O  O     . ILE A 1 4492 ? 261.560 222.315 247.591 1.00 55.20  ? 4492 ILE A O     1 
ATOM   21764 C  CB    . ILE A 1 4492 ? 259.174 224.158 246.150 1.00 47.53  ? 4492 ILE A CB    1 
ATOM   21765 C  CG1   . ILE A 1 4492 ? 258.739 225.623 246.169 1.00 48.73  ? 4492 ILE A CG1   1 
ATOM   21766 C  CG2   . ILE A 1 4492 ? 258.579 223.402 247.324 1.00 44.87  ? 4492 ILE A CG2   1 
ATOM   21767 C  CD1   . ILE A 1 4492 ? 257.323 225.839 245.693 1.00 50.92  ? 4492 ILE A CD1   1 
ATOM   21768 N  N     . SER A 1 4493 ? 261.119 221.747 245.459 1.00 54.81  ? 4493 SER A N     1 
ATOM   21769 C  CA    . SER A 1 4493 ? 261.557 220.369 245.658 1.00 48.24  ? 4493 SER A CA    1 
ATOM   21770 C  C     . SER A 1 4493 ? 263.038 220.304 245.999 1.00 52.64  ? 4493 SER A C     1 
ATOM   21771 O  O     . SER A 1 4493 ? 263.448 219.535 246.875 1.00 56.14  ? 4493 SER A O     1 
ATOM   21772 C  CB    . SER A 1 4493 ? 261.260 219.538 244.411 1.00 49.72  ? 4493 SER A CB    1 
ATOM   21773 O  OG    . SER A 1 4493 ? 259.893 219.176 244.353 1.00 55.30  ? 4493 SER A OG    1 
ATOM   21774 N  N     . LEU A 1 4494 ? 263.857 221.104 245.314 1.00 54.71  ? 4494 LEU A N     1 
ATOM   21775 C  CA    . LEU A 1 4494 ? 265.287 221.119 245.598 1.00 55.10  ? 4494 LEU A CA    1 
ATOM   21776 C  C     . LEU A 1 4494 ? 265.564 221.634 247.004 1.00 55.84  ? 4494 LEU A C     1 
ATOM   21777 O  O     . LEU A 1 4494 ? 266.423 221.097 247.712 1.00 56.01  ? 4494 LEU A O     1 
ATOM   21778 C  CB    . LEU A 1 4494 ? 266.015 221.967 244.557 1.00 56.30  ? 4494 LEU A CB    1 
ATOM   21779 C  CG    . LEU A 1 4494 ? 267.537 222.034 244.673 1.00 60.59  ? 4494 LEU A CG    1 
ATOM   21780 C  CD1   . LEU A 1 4494 ? 268.139 220.652 244.484 1.00 59.29  ? 4494 LEU A CD1   1 
ATOM   21781 C  CD2   . LEU A 1 4494 ? 268.107 223.012 243.661 1.00 58.74  ? 4494 LEU A CD2   1 
ATOM   21782 N  N     . ALA A 1 4495 ? 264.847 222.679 247.425 1.00 64.34  ? 4495 ALA A N     1 
ATOM   21783 C  CA    . ALA A 1 4495 ? 265.023 223.202 248.777 1.00 63.77  ? 4495 ALA A CA    1 
ATOM   21784 C  C     . ALA A 1 4495 ? 264.602 222.182 249.827 1.00 61.43  ? 4495 ALA A C     1 
ATOM   21785 O  O     . ALA A 1 4495 ? 265.267 222.037 250.859 1.00 64.53  ? 4495 ALA A O     1 
ATOM   21786 C  CB    . ALA A 1 4495 ? 264.234 224.500 248.943 1.00 59.27  ? 4495 ALA A CB    1 
ATOM   21787 N  N     . ALA A 1 4496 ? 263.496 221.473 249.589 1.00 59.47  ? 4496 ALA A N     1 
ATOM   21788 C  CA    . ALA A 1 4496 ? 263.059 220.446 250.529 1.00 59.79  ? 4496 ALA A CA    1 
ATOM   21789 C  C     . ALA A 1 4496 ? 264.060 219.300 250.603 1.00 65.73  ? 4496 ALA A C     1 
ATOM   21790 O  O     . ALA A 1 4496 ? 264.340 218.779 251.689 1.00 66.03  ? 4496 ALA A O     1 
ATOM   21791 C  CB    . ALA A 1 4496 ? 261.677 219.928 250.138 1.00 58.51  ? 4496 ALA A CB    1 
ATOM   21792 N  N     . ALA A 1 4497 ? 264.604 218.886 249.456 1.00 68.83  ? 4497 ALA A N     1 
ATOM   21793 C  CA    . ALA A 1 4497 ? 265.564 217.787 249.446 1.00 65.22  ? 4497 ALA A CA    1 
ATOM   21794 C  C     . ALA A 1 4497 ? 266.872 218.181 250.121 1.00 66.94  ? 4497 ALA A C     1 
ATOM   21795 O  O     . ALA A 1 4497 ? 267.457 217.384 250.862 1.00 66.39  ? 4497 ALA A O     1 
ATOM   21796 C  CB    . ALA A 1 4497 ? 265.818 217.326 248.012 1.00 62.67  ? 4497 ALA A CB    1 
ATOM   21797 N  N     . SER A 1 4498 ? 267.349 219.402 249.870 1.00 69.99  ? 4498 SER A N     1 
ATOM   21798 C  CA    . SER A 1 4498 ? 268.613 219.842 250.455 1.00 71.02  ? 4498 SER A CA    1 
ATOM   21799 C  C     . SER A 1 4498 ? 268.519 219.920 251.973 1.00 68.63  ? 4498 SER A C     1 
ATOM   21800 O  O     . SER A 1 4498 ? 269.435 219.498 252.687 1.00 69.06  ? 4498 SER A O     1 
ATOM   21801 C  CB    . SER A 1 4498 ? 269.017 221.195 249.869 1.00 70.37  ? 4498 SER A CB    1 
ATOM   21802 O  OG    . SER A 1 4498 ? 269.214 221.106 248.469 1.00 75.08  ? 4498 SER A OG    1 
ATOM   21803 N  N     . GLY A 1 4499 ? 267.416 220.458 252.483 1.00 72.24  ? 4499 GLY A N     1 
ATOM   21804 C  CA    . GLY A 1 4499 ? 267.210 220.535 253.914 1.00 73.44  ? 4499 GLY A CA    1 
ATOM   21805 C  C     . GLY A 1 4499 ? 266.094 219.627 254.384 1.00 74.77  ? 4499 GLY A C     1 
ATOM   21806 O  O     . GLY A 1 4499 ? 266.282 218.416 254.525 1.00 73.26  ? 4499 GLY A O     1 
ATOM   21807 N  N     . GLY A 1 4500 ? 264.923 220.205 254.626 1.00 78.85  ? 4500 GLY A N     1 
ATOM   21808 C  CA    . GLY A 1 4500 ? 263.784 219.420 255.057 1.00 80.74  ? 4500 GLY A CA    1 
ATOM   21809 C  C     . GLY A 1 4500 ? 262.552 220.294 255.163 1.00 81.33  ? 4500 GLY A C     1 
ATOM   21810 O  O     . GLY A 1 4500 ? 262.404 221.272 254.430 1.00 80.69  ? 4500 GLY A O     1 
ATOM   21811 N  N     . ALA A 1 4501 ? 261.668 219.918 256.088 1.00 79.41  ? 4501 ALA A N     1 
ATOM   21812 C  CA    . ALA A 1 4501 ? 260.490 220.736 256.351 1.00 82.09  ? 4501 ALA A CA    1 
ATOM   21813 C  C     . ALA A 1 4501 ? 260.866 222.067 256.987 1.00 82.78  ? 4501 ALA A C     1 
ATOM   21814 O  O     . ALA A 1 4501 ? 260.083 223.023 256.935 1.00 80.95  ? 4501 ALA A O     1 
ATOM   21815 C  CB    . ALA A 1 4501 ? 259.510 219.973 257.241 1.00 81.38  ? 4501 ALA A CB    1 
ATOM   21816 N  N     . LYS A 1 4502 ? 262.053 222.148 257.594 1.00 80.00  ? 4502 LYS A N     1 
ATOM   21817 C  CA    . LYS A 1 4502 ? 262.505 223.406 258.181 1.00 80.52  ? 4502 LYS A CA    1 
ATOM   21818 C  C     . LYS A 1 4502 ? 262.814 224.437 257.103 1.00 79.22  ? 4502 LYS A C     1 
ATOM   21819 O  O     . LYS A 1 4502 ? 262.571 225.635 257.290 1.00 80.77  ? 4502 LYS A O     1 
ATOM   21820 C  CB    . LYS A 1 4502 ? 263.737 223.167 259.055 1.00 79.70  ? 4502 LYS A CB    1 
ATOM   21821 C  CG    . LYS A 1 4502 ? 263.442 222.680 260.467 1.00 81.78  ? 4502 LYS A CG    1 
ATOM   21822 C  CD    . LYS A 1 4502 ? 262.998 221.225 260.479 1.00 83.93  ? 4502 LYS A CD    1 
ATOM   21823 C  CE    . LYS A 1 4502 ? 264.145 220.297 260.113 1.00 83.32  ? 4502 LYS A CE    1 
ATOM   21824 N  NZ    . LYS A 1 4502 ? 263.747 218.864 260.178 1.00 81.51  ? 4502 LYS A NZ    1 
ATOM   21825 N  N     . GLU A 1 4503 ? 263.360 223.991 255.971 1.00 69.28  ? 4503 GLU A N     1 
ATOM   21826 C  CA    . GLU A 1 4503 ? 263.707 224.918 254.901 1.00 67.92  ? 4503 GLU A CA    1 
ATOM   21827 C  C     . GLU A 1 4503 ? 262.468 225.435 254.181 1.00 70.30  ? 4503 GLU A C     1 
ATOM   21828 O  O     . GLU A 1 4503 ? 262.488 226.545 253.637 1.00 74.12  ? 4503 GLU A O     1 
ATOM   21829 C  CB    . GLU A 1 4503 ? 264.660 224.239 253.915 1.00 70.98  ? 4503 GLU A CB    1 
ATOM   21830 C  CG    . GLU A 1 4503 ? 265.095 225.110 252.747 1.00 73.91  ? 4503 GLU A CG    1 
ATOM   21831 C  CD    . GLU A 1 4503 ? 265.581 226.476 253.188 1.00 77.31  ? 4503 GLU A CD    1 
ATOM   21832 O  OE1   . GLU A 1 4503 ? 266.531 226.539 253.996 1.00 77.21  ? 4503 GLU A OE1   1 
ATOM   21833 O  OE2   . GLU A 1 4503 ? 265.015 227.488 252.723 1.00 71.64  ? 4503 GLU A OE2   1 
ATOM   21834 N  N     . LEU A 1 4504 ? 261.381 224.660 254.179 1.00 60.40  ? 4504 LEU A N     1 
ATOM   21835 C  CA    . LEU A 1 4504 ? 260.164 225.083 253.496 1.00 61.22  ? 4504 LEU A CA    1 
ATOM   21836 C  C     . LEU A 1 4504 ? 259.575 226.352 254.096 1.00 64.27  ? 4504 LEU A C     1 
ATOM   21837 O  O     . LEU A 1 4504 ? 258.781 227.027 253.434 1.00 67.44  ? 4504 LEU A O     1 
ATOM   21838 C  CB    . LEU A 1 4504 ? 259.130 223.959 253.529 1.00 60.37  ? 4504 LEU A CB    1 
ATOM   21839 C  CG    . LEU A 1 4504 ? 259.474 222.716 252.711 1.00 58.93  ? 4504 LEU A CG    1 
ATOM   21840 C  CD1   . LEU A 1 4504 ? 258.466 221.619 252.966 1.00 61.02  ? 4504 LEU A CD1   1 
ATOM   21841 C  CD2   . LEU A 1 4504 ? 259.528 223.054 251.234 1.00 61.79  ? 4504 LEU A CD2   1 
ATOM   21842 N  N     . LYS A 1 4505 ? 259.938 226.687 255.333 1.00 60.83  ? 4505 LYS A N     1 
ATOM   21843 C  CA    . LYS A 1 4505 ? 259.509 227.939 255.939 1.00 54.05  ? 4505 LYS A CA    1 
ATOM   21844 C  C     . LYS A 1 4505 ? 260.264 229.144 255.395 1.00 59.54  ? 4505 LYS A C     1 
ATOM   21845 O  O     . LYS A 1 4505 ? 259.699 230.241 255.343 1.00 67.91  ? 4505 LYS A O     1 
ATOM   21846 C  CB    . LYS A 1 4505 ? 259.679 227.864 257.458 1.00 56.16  ? 4505 LYS A CB    1 
ATOM   21847 C  CG    . LYS A 1 4505 ? 258.785 228.805 258.245 1.00 60.40  ? 4505 LYS A CG    1 
ATOM   21848 C  CD    . LYS A 1 4505 ? 259.470 230.133 258.496 1.00 57.03  ? 4505 LYS A CD    1 
ATOM   21849 C  CE    . LYS A 1 4505 ? 258.590 231.075 259.284 1.00 56.70  ? 4505 LYS A CE    1 
ATOM   21850 N  NZ    . LYS A 1 4505 ? 259.214 232.418 259.379 1.00 61.70  ? 4505 LYS A NZ    1 
ATOM   21851 N  N     . ASN A 1 4506 ? 261.517 228.966 254.974 1.00 59.57  ? 4506 ASN A N     1 
ATOM   21852 C  CA    . ASN A 1 4506 ? 262.388 230.075 254.610 1.00 59.92  ? 4506 ASN A CA    1 
ATOM   21853 C  C     . ASN A 1 4506 ? 262.501 230.269 253.102 1.00 59.58  ? 4506 ASN A C     1 
ATOM   21854 O  O     . ASN A 1 4506 ? 263.409 230.966 252.639 1.00 62.89  ? 4506 ASN A O     1 
ATOM   21855 C  CB    . ASN A 1 4506 ? 263.776 229.876 255.219 1.00 60.18  ? 4506 ASN A CB    1 
ATOM   21856 C  CG    . ASN A 1 4506 ? 263.743 229.818 256.731 1.00 64.20  ? 4506 ASN A CG    1 
ATOM   21857 O  OD1   . ASN A 1 4506 ? 262.865 230.400 257.367 1.00 66.15  ? 4506 ASN A OD1   1 
ATOM   21858 N  ND2   . ASN A 1 4506 ? 264.703 229.113 257.316 1.00 65.51  ? 4506 ASN A ND2   1 
ATOM   21859 N  N     . ILE A 1 4507 ? 261.607 229.668 252.325 1.00 54.57  ? 4507 ILE A N     1 
ATOM   21860 C  CA    . ILE A 1 4507 ? 261.596 229.840 250.877 1.00 56.51  ? 4507 ILE A CA    1 
ATOM   21861 C  C     . ILE A 1 4507 ? 260.480 230.813 250.519 1.00 57.33  ? 4507 ILE A C     1 
ATOM   21862 O  O     . ILE A 1 4507 ? 259.342 230.672 250.982 1.00 59.25  ? 4507 ILE A O     1 
ATOM   21863 C  CB    . ILE A 1 4507 ? 261.442 228.497 250.144 1.00 53.99  ? 4507 ILE A CB    1 
ATOM   21864 C  CG1   . ILE A 1 4507 ? 260.119 227.814 250.486 1.00 55.55  ? 4507 ILE A CG1   1 
ATOM   21865 C  CG2   . ILE A 1 4507 ? 262.601 227.575 250.476 1.00 59.48  ? 4507 ILE A CG2   1 
ATOM   21866 C  CD1   . ILE A 1 4507 ? 259.824 226.616 249.619 1.00 55.95  ? 4507 ILE A CD1   1 
ATOM   21867 N  N     . HIS A 1 4508 ? 260.816 231.826 249.724 1.00 47.73  ? 4508 HIS A N     1 
ATOM   21868 C  CA    . HIS A 1 4508 ? 259.841 232.822 249.303 1.00 43.66  ? 4508 HIS A CA    1 
ATOM   21869 C  C     . HIS A 1 4508 ? 259.081 232.297 248.094 1.00 48.96  ? 4508 HIS A C     1 
ATOM   21870 O  O     . HIS A 1 4508 ? 259.681 232.003 247.056 1.00 58.66  ? 4508 HIS A O     1 
ATOM   21871 C  CB    . HIS A 1 4508 ? 260.531 234.143 248.975 1.00 47.17  ? 4508 HIS A CB    1 
ATOM   21872 C  CG    . HIS A 1 4508 ? 261.558 234.554 249.982 1.00 50.68  ? 4508 HIS A CG    1 
ATOM   21873 N  ND1   . HIS A 1 4508 ? 261.333 234.499 251.340 1.00 53.85  ? 4508 HIS A ND1   1 
ATOM   21874 C  CD2   . HIS A 1 4508 ? 262.814 235.032 249.828 1.00 51.46  ? 4508 HIS A CD2   1 
ATOM   21875 C  CE1   . HIS A 1 4508 ? 262.408 234.923 251.980 1.00 48.87  ? 4508 HIS A CE1   1 
ATOM   21876 N  NE2   . HIS A 1 4508 ? 263.321 235.253 251.086 1.00 58.41  ? 4508 HIS A NE2   1 
ATOM   21877 N  N     . VAL A 1 4509 ? 257.768 232.181 248.227 1.00 41.74  ? 4509 VAL A N     1 
ATOM   21878 C  CA    . VAL A 1 4509 ? 256.936 231.622 247.182 1.00 45.38  ? 4509 VAL A CA    1 
ATOM   21879 C  C     . VAL A 1 4509 ? 256.302 232.758 246.395 1.00 41.76  ? 4509 VAL A C     1 
ATOM   21880 O  O     . VAL A 1 4509 ? 256.137 233.879 246.883 1.00 50.09  ? 4509 VAL A O     1 
ATOM   21881 C  CB    . VAL A 1 4509 ? 255.855 230.677 247.751 1.00 45.21  ? 4509 VAL A CB    1 
ATOM   21882 C  CG1   . VAL A 1 4509 ? 256.495 229.556 248.548 1.00 47.57  ? 4509 VAL A CG1   1 
ATOM   21883 C  CG2   . VAL A 1 4509 ? 254.875 231.451 248.604 1.00 45.28  ? 4509 VAL A CG2   1 
ATOM   21884 N  N     . CYS A 1 4510 ? 255.950 232.467 245.149 1.00 43.93  ? 4510 CYS A N     1 
ATOM   21885 C  CA    . CYS A 1 4510 ? 255.160 233.368 244.323 1.00 42.85  ? 4510 CYS A CA    1 
ATOM   21886 C  C     . CYS A 1 4510 ? 253.719 232.879 244.374 1.00 48.84  ? 4510 CYS A C     1 
ATOM   21887 O  O     . CYS A 1 4510 ? 253.411 231.789 243.884 1.00 53.58  ? 4510 CYS A O     1 
ATOM   21888 C  CB    . CYS A 1 4510 ? 255.688 233.407 242.891 1.00 40.14  ? 4510 CYS A CB    1 
ATOM   21889 S  SG    . CYS A 1 4510 ? 254.730 234.453 241.772 1.00 64.28  ? 4510 CYS A SG    1 
ATOM   21890 N  N     . LEU A 1 4511 ? 252.840 233.681 244.980 1.00 44.08  ? 4511 LEU A N     1 
ATOM   21891 C  CA    . LEU A 1 4511 ? 251.451 233.263 245.140 1.00 42.94  ? 4511 LEU A CA    1 
ATOM   21892 C  C     . LEU A 1 4511 ? 250.765 233.071 243.796 1.00 48.68  ? 4511 LEU A C     1 
ATOM   21893 O  O     . LEU A 1 4511 ? 249.821 232.280 243.690 1.00 51.33  ? 4511 LEU A O     1 
ATOM   21894 C  CB    . LEU A 1 4511 ? 250.689 234.283 245.983 1.00 48.28  ? 4511 LEU A CB    1 
ATOM   21895 C  CG    . LEU A 1 4511 ? 250.808 234.149 247.500 1.00 45.73  ? 4511 LEU A CG    1 
ATOM   21896 C  CD1   . LEU A 1 4511 ? 249.773 235.020 248.183 1.00 48.21  ? 4511 LEU A CD1   1 
ATOM   21897 C  CD2   . LEU A 1 4511 ? 250.661 232.702 247.927 1.00 44.47  ? 4511 LEU A CD2   1 
ATOM   21898 N  N     . GLY A 1 4512 ? 251.213 233.786 242.764 1.00 49.16  ? 4512 GLY A N     1 
ATOM   21899 C  CA    . GLY A 1 4512 ? 250.656 233.597 241.438 1.00 47.14  ? 4512 GLY A CA    1 
ATOM   21900 C  C     . GLY A 1 4512 ? 251.091 232.312 240.769 1.00 52.44  ? 4512 GLY A C     1 
ATOM   21901 O  O     . GLY A 1 4512 ? 250.404 231.838 239.859 1.00 61.94  ? 4512 GLY A O     1 
ATOM   21902 N  N     . GLY A 1 4513 ? 252.212 231.740 241.197 1.00 44.45  ? 4513 GLY A N     1 
ATOM   21903 C  CA    . GLY A 1 4513 ? 252.707 230.494 240.661 1.00 42.32  ? 4513 GLY A CA    1 
ATOM   21904 C  C     . GLY A 1 4513 ? 252.243 229.249 241.374 1.00 41.34  ? 4513 GLY A C     1 
ATOM   21905 O  O     . GLY A 1 4513 ? 252.621 228.143 240.977 1.00 47.28  ? 4513 GLY A O     1 
ATOM   21906 N  N     . LEU A 1 4514 ? 251.432 229.388 242.416 1.00 46.20  ? 4514 LEU A N     1 
ATOM   21907 C  CA    . LEU A 1 4514 ? 250.911 228.253 243.162 1.00 46.80  ? 4514 LEU A CA    1 
ATOM   21908 C  C     . LEU A 1 4514 ? 249.517 227.906 242.663 1.00 45.64  ? 4514 LEU A C     1 
ATOM   21909 O  O     . LEU A 1 4514 ? 248.746 228.789 242.276 1.00 51.12  ? 4514 LEU A O     1 
ATOM   21910 C  CB    . LEU A 1 4514 ? 250.869 228.553 244.661 1.00 44.19  ? 4514 LEU A CB    1 
ATOM   21911 C  CG    . LEU A 1 4514 ? 252.214 228.783 245.350 1.00 48.00  ? 4514 LEU A CG    1 
ATOM   21912 C  CD1   . LEU A 1 4514 ? 252.005 229.207 246.789 1.00 43.38  ? 4514 LEU A CD1   1 
ATOM   21913 C  CD2   . LEU A 1 4514 ? 253.073 227.536 245.278 1.00 45.65  ? 4514 LEU A CD2   1 
ATOM   21914 N  N     . PHE A 1 4515 ? 249.201 226.611 242.665 1.00 46.35  ? 4515 PHE A N     1 
ATOM   21915 C  CA    . PHE A 1 4515 ? 247.891 226.170 242.199 1.00 50.61  ? 4515 PHE A CA    1 
ATOM   21916 C  C     . PHE A 1 4515 ? 246.786 226.627 243.143 1.00 52.67  ? 4515 PHE A C     1 
ATOM   21917 O  O     . PHE A 1 4515 ? 245.695 226.998 242.695 1.00 54.80  ? 4515 PHE A O     1 
ATOM   21918 C  CB    . PHE A 1 4515 ? 247.878 224.650 242.038 1.00 50.62  ? 4515 PHE A CB    1 
ATOM   21919 C  CG    . PHE A 1 4515 ? 248.881 224.136 241.040 1.00 51.59  ? 4515 PHE A CG    1 
ATOM   21920 C  CD1   . PHE A 1 4515 ? 250.196 223.915 241.408 1.00 48.90  ? 4515 PHE A CD1   1 
ATOM   21921 C  CD2   . PHE A 1 4515 ? 248.507 223.871 239.736 1.00 52.02  ? 4515 PHE A CD2   1 
ATOM   21922 C  CE1   . PHE A 1 4515 ? 251.117 223.446 240.495 1.00 49.39  ? 4515 PHE A CE1   1 
ATOM   21923 C  CE2   . PHE A 1 4515 ? 249.427 223.399 238.821 1.00 54.46  ? 4515 PHE A CE2   1 
ATOM   21924 C  CZ    . PHE A 1 4515 ? 250.731 223.189 239.201 1.00 50.54  ? 4515 PHE A CZ    1 
ATOM   21925 N  N     . VAL A 1 4516 ? 247.043 226.600 244.448 1.00 48.20  ? 4516 VAL A N     1 
ATOM   21926 C  CA    . VAL A 1 4516 ? 246.077 227.043 245.452 1.00 45.79  ? 4516 VAL A CA    1 
ATOM   21927 C  C     . VAL A 1 4516 ? 246.753 227.966 246.463 1.00 46.76  ? 4516 VAL A C     1 
ATOM   21928 O  O     . VAL A 1 4516 ? 247.157 227.520 247.546 1.00 51.92  ? 4516 VAL A O     1 
ATOM   21929 C  CB    . VAL A 1 4516 ? 245.394 225.839 246.124 1.00 41.25  ? 4516 VAL A CB    1 
ATOM   21930 C  CG1   . VAL A 1 4516 ? 244.446 225.172 245.152 1.00 44.03  ? 4516 VAL A CG1   1 
ATOM   21931 C  CG2   . VAL A 1 4516 ? 246.426 224.810 246.545 1.00 45.89  ? 4516 VAL A CG2   1 
ATOM   21932 N  N     . PRO A 1 4517 ? 246.904 229.257 246.152 1.00 41.04  ? 4517 PRO A N     1 
ATOM   21933 C  CA    . PRO A 1 4517 ? 247.558 230.172 247.106 1.00 36.40  ? 4517 PRO A CA    1 
ATOM   21934 C  C     . PRO A 1 4517 ? 246.825 230.314 248.430 1.00 39.85  ? 4517 PRO A C     1 
ATOM   21935 O  O     . PRO A 1 4517 ? 247.473 230.503 249.470 1.00 48.72  ? 4517 PRO A O     1 
ATOM   21936 C  CB    . PRO A 1 4517 ? 247.601 231.499 246.338 1.00 43.01  ? 4517 PRO A CB    1 
ATOM   21937 C  CG    . PRO A 1 4517 ? 246.516 231.394 245.328 1.00 45.50  ? 4517 PRO A CG    1 
ATOM   21938 C  CD    . PRO A 1 4517 ? 246.434 229.952 244.944 1.00 38.99  ? 4517 PRO A CD    1 
ATOM   21939 N  N     . GLU A 1 4518 ? 245.492 230.243 248.426 1.00 43.47  ? 4518 GLU A N     1 
ATOM   21940 C  CA    . GLU A 1 4518 ? 244.748 230.310 249.679 1.00 39.81  ? 4518 GLU A CA    1 
ATOM   21941 C  C     . GLU A 1 4518 ? 245.094 229.142 250.591 1.00 43.07  ? 4518 GLU A C     1 
ATOM   21942 O  O     . GLU A 1 4518 ? 245.145 229.305 251.817 1.00 47.13  ? 4518 GLU A O     1 
ATOM   21943 C  CB    . GLU A 1 4518 ? 243.247 230.354 249.396 1.00 34.07  ? 4518 GLU A CB    1 
ATOM   21944 C  CG    . GLU A 1 4518 ? 242.708 229.127 248.688 1.00 46.13  ? 4518 GLU A CG    1 
ATOM   21945 C  CD    . GLU A 1 4518 ? 242.698 229.285 247.183 1.00 55.95  ? 4518 GLU A CD    1 
ATOM   21946 O  OE1   . GLU A 1 4518 ? 243.030 230.387 246.701 1.00 49.21  ? 4518 GLU A OE1   1 
ATOM   21947 O  OE2   . GLU A 1 4518 ? 242.361 228.308 246.482 1.00 58.43  ? 4518 GLU A OE2   1 
ATOM   21948 N  N     . ALA A 1 4519 ? 245.349 227.966 250.015 1.00 38.99  ? 4519 ALA A N     1 
ATOM   21949 C  CA    . ALA A 1 4519 ? 245.845 226.855 250.812 1.00 32.96  ? 4519 ALA A CA    1 
ATOM   21950 C  C     . ALA A 1 4519 ? 247.212 227.163 251.401 1.00 40.56  ? 4519 ALA A C     1 
ATOM   21951 O  O     . ALA A 1 4519 ? 247.505 226.738 252.520 1.00 52.48  ? 4519 ALA A O     1 
ATOM   21952 C  CB    . ALA A 1 4519 ? 245.901 225.582 249.973 1.00 41.55  ? 4519 ALA A CB    1 
ATOM   21953 N  N     . TYR A 1 4520 ? 248.059 227.899 250.676 1.00 38.80  ? 4520 TYR A N     1 
ATOM   21954 C  CA    . TYR A 1 4520 ? 249.342 228.304 251.243 1.00 30.79  ? 4520 TYR A CA    1 
ATOM   21955 C  C     . TYR A 1 4520 ? 249.152 229.236 252.430 1.00 37.22  ? 4520 TYR A C     1 
ATOM   21956 O  O     . TYR A 1 4520 ? 249.843 229.107 253.448 1.00 52.02  ? 4520 TYR A O     1 
ATOM   21957 C  CB    . TYR A 1 4520 ? 250.210 228.985 250.189 1.00 30.06  ? 4520 TYR A CB    1 
ATOM   21958 C  CG    . TYR A 1 4520 ? 251.483 229.555 250.767 1.00 37.44  ? 4520 TYR A CG    1 
ATOM   21959 C  CD1   . TYR A 1 4520 ? 252.518 228.723 251.164 1.00 42.86  ? 4520 TYR A CD1   1 
ATOM   21960 C  CD2   . TYR A 1 4520 ? 251.643 230.922 250.933 1.00 39.22  ? 4520 TYR A CD2   1 
ATOM   21961 C  CE1   . TYR A 1 4520 ? 253.678 229.235 251.699 1.00 39.06  ? 4520 TYR A CE1   1 
ATOM   21962 C  CE2   . TYR A 1 4520 ? 252.801 231.443 251.468 1.00 34.57  ? 4520 TYR A CE2   1 
ATOM   21963 C  CZ    . TYR A 1 4520 ? 253.815 230.595 251.848 1.00 37.76  ? 4520 TYR A CZ    1 
ATOM   21964 O  OH    . TYR A 1 4520 ? 254.972 231.110 252.380 1.00 41.63  ? 4520 TYR A OH    1 
ATOM   21965 N  N     . ILE A 1 4521 ? 248.239 230.201 252.308 1.00 37.42  ? 4521 ILE A N     1 
ATOM   21966 C  CA    . ILE A 1 4521 ? 247.983 231.111 253.421 1.00 31.53  ? 4521 ILE A CA    1 
ATOM   21967 C  C     . ILE A 1 4521 ? 247.474 230.336 254.629 1.00 35.94  ? 4521 ILE A C     1 
ATOM   21968 O  O     . ILE A 1 4521 ? 247.914 230.561 255.765 1.00 44.76  ? 4521 ILE A O     1 
ATOM   21969 C  CB    . ILE A 1 4521 ? 247.000 232.217 252.996 1.00 36.89  ? 4521 ILE A CB    1 
ATOM   21970 C  CG1   . ILE A 1 4521 ? 247.443 232.844 251.674 1.00 37.03  ? 4521 ILE A CG1   1 
ATOM   21971 C  CG2   . ILE A 1 4521 ? 246.894 233.278 254.074 1.00 39.17  ? 4521 ILE A CG2   1 
ATOM   21972 C  CD1   . ILE A 1 4521 ? 248.617 233.781 251.807 1.00 38.00  ? 4521 ILE A CD1   1 
ATOM   21973 N  N     . THR A 1 4522 ? 246.548 229.402 254.400 1.00 44.42  ? 4522 THR A N     1 
ATOM   21974 C  CA    . THR A 1 4522 ? 246.038 228.578 255.490 1.00 34.16  ? 4522 THR A CA    1 
ATOM   21975 C  C     . THR A 1 4522 ? 247.142 227.728 256.108 1.00 36.39  ? 4522 THR A C     1 
ATOM   21976 O  O     . THR A 1 4522 ? 247.192 227.559 257.330 1.00 42.53  ? 4522 THR A O     1 
ATOM   21977 C  CB    . THR A 1 4522 ? 244.897 227.694 254.987 1.00 40.60  ? 4522 THR A CB    1 
ATOM   21978 O  OG1   . THR A 1 4522 ? 243.869 228.515 254.421 1.00 44.94  ? 4522 THR A OG1   1 
ATOM   21979 C  CG2   . THR A 1 4522 ? 244.311 226.879 256.123 1.00 37.78  ? 4522 THR A CG2   1 
ATOM   21980 N  N     . ALA A 1 4523 ? 248.037 227.184 255.280 1.00 40.91  ? 4523 ALA A N     1 
ATOM   21981 C  CA    . ALA A 1 4523 ? 249.123 226.354 255.790 1.00 38.50  ? 4523 ALA A CA    1 
ATOM   21982 C  C     . ALA A 1 4523 ? 250.089 227.163 256.645 1.00 42.26  ? 4523 ALA A C     1 
ATOM   21983 O  O     . ALA A 1 4523 ? 250.559 226.684 257.680 1.00 43.95  ? 4523 ALA A O     1 
ATOM   21984 C  CB    . ALA A 1 4523 ? 249.862 225.688 254.631 1.00 36.80  ? 4523 ALA A CB    1 
ATOM   21985 N  N     . THR A 1 4524 ? 250.411 228.387 256.221 1.00 44.76  ? 4524 THR A N     1 
ATOM   21986 C  CA    . THR A 1 4524 ? 251.269 229.243 257.036 1.00 38.30  ? 4524 THR A CA    1 
ATOM   21987 C  C     . THR A 1 4524 ? 250.595 229.627 258.349 1.00 41.58  ? 4524 THR A C     1 
ATOM   21988 O  O     . THR A 1 4524 ? 251.245 229.635 259.404 1.00 52.83  ? 4524 THR A O     1 
ATOM   21989 C  CB    . THR A 1 4524 ? 251.661 230.496 256.256 1.00 31.62  ? 4524 THR A CB    1 
ATOM   21990 O  OG1   . THR A 1 4524 ? 250.481 231.172 255.809 1.00 40.18  ? 4524 THR A OG1   1 
ATOM   21991 C  CG2   . THR A 1 4524 ? 252.504 230.126 255.058 1.00 39.62  ? 4524 THR A CG2   1 
ATOM   21992 N  N     . ARG A 1 4525 ? 249.299 229.943 258.302 1.00 40.04  ? 4525 ARG A N     1 
ATOM   21993 C  CA    . ARG A 1 4525 ? 248.552 230.207 259.527 1.00 41.87  ? 4525 ARG A CA    1 
ATOM   21994 C  C     . ARG A 1 4525 ? 248.604 229.012 260.467 1.00 42.71  ? 4525 ARG A C     1 
ATOM   21995 O  O     . ARG A 1 4525 ? 248.818 229.164 261.676 1.00 44.81  ? 4525 ARG A O     1 
ATOM   21996 C  CB    . ARG A 1 4525 ? 247.105 230.541 259.175 1.00 43.45  ? 4525 ARG A CB    1 
ATOM   21997 C  CG    . ARG A 1 4525 ? 246.242 230.988 260.329 1.00 44.98  ? 4525 ARG A CG    1 
ATOM   21998 C  CD    . ARG A 1 4525 ? 244.782 230.842 259.953 1.00 41.81  ? 4525 ARG A CD    1 
ATOM   21999 N  NE    . ARG A 1 4525 ? 243.895 231.571 260.848 1.00 45.93  ? 4525 ARG A NE    1 
ATOM   22000 C  CZ    . ARG A 1 4525 ? 242.946 232.400 260.440 1.00 46.16  ? 4525 ARG A CZ    1 
ATOM   22001 N  NH1   . ARG A 1 4525 ? 242.736 232.630 259.155 1.00 46.63  ? 4525 ARG A NH1   1 
ATOM   22002 N  NH2   . ARG A 1 4525 ? 242.184 233.009 261.344 1.00 50.62  ? 4525 ARG A NH2   1 
ATOM   22003 N  N     . GLN A 1 4526 ? 248.411 227.813 259.921 1.00 49.20  ? 4526 GLN A N     1 
ATOM   22004 C  CA    . GLN A 1 4526 ? 248.426 226.593 260.717 1.00 38.92  ? 4526 GLN A CA    1 
ATOM   22005 C  C     . GLN A 1 4526 ? 249.808 226.329 261.302 1.00 38.13  ? 4526 GLN A C     1 
ATOM   22006 O  O     . GLN A 1 4526 ? 249.929 225.885 262.449 1.00 46.99  ? 4526 GLN A O     1 
ATOM   22007 C  CB    . GLN A 1 4526 ? 247.955 225.434 259.843 1.00 41.19  ? 4526 GLN A CB    1 
ATOM   22008 C  CG    . GLN A 1 4526 ? 247.827 224.113 260.537 1.00 51.06  ? 4526 GLN A CG    1 
ATOM   22009 C  CD    . GLN A 1 4526 ? 247.298 223.036 259.618 1.00 54.76  ? 4526 GLN A CD    1 
ATOM   22010 O  OE1   . GLN A 1 4526 ? 247.059 223.277 258.436 1.00 49.43  ? 4526 GLN A OE1   1 
ATOM   22011 N  NE2   . GLN A 1 4526 ? 247.106 221.840 260.158 1.00 60.19  ? 4526 GLN A NE2   1 
ATOM   22012 N  N     . TYR A 1 4527 ? 250.861 226.600 260.528 1.00 45.04  ? 4527 TYR A N     1 
ATOM   22013 C  CA    . TYR A 1 4527 ? 252.222 226.473 261.037 1.00 42.32  ? 4527 TYR A CA    1 
ATOM   22014 C  C     . TYR A 1 4527 ? 252.455 227.399 262.221 1.00 44.26  ? 4527 TYR A C     1 
ATOM   22015 O  O     . TYR A 1 4527 ? 253.005 226.982 263.246 1.00 47.44  ? 4527 TYR A O     1 
ATOM   22016 C  CB    . TYR A 1 4527 ? 253.225 226.770 259.921 1.00 38.35  ? 4527 TYR A CB    1 
ATOM   22017 C  CG    . TYR A 1 4527 ? 254.673 226.779 260.362 1.00 43.71  ? 4527 TYR A CG    1 
ATOM   22018 C  CD1   . TYR A 1 4527 ? 255.437 225.622 260.329 1.00 45.74  ? 4527 TYR A CD1   1 
ATOM   22019 C  CD2   . TYR A 1 4527 ? 255.281 227.951 260.793 1.00 43.49  ? 4527 TYR A CD2   1 
ATOM   22020 C  CE1   . TYR A 1 4527 ? 256.760 225.629 260.726 1.00 46.00  ? 4527 TYR A CE1   1 
ATOM   22021 C  CE2   . TYR A 1 4527 ? 256.599 227.966 261.192 1.00 47.33  ? 4527 TYR A CE2   1 
ATOM   22022 C  CZ    . TYR A 1 4527 ? 257.335 226.804 261.156 1.00 48.91  ? 4527 TYR A CZ    1 
ATOM   22023 O  OH    . TYR A 1 4527 ? 258.651 226.819 261.552 1.00 49.87  ? 4527 TYR A OH    1 
ATOM   22024 N  N     . VAL A 1 4528 ? 252.045 228.662 262.096 1.00 44.87  ? 4528 VAL A N     1 
ATOM   22025 C  CA    . VAL A 1 4528 ? 252.246 229.606 263.192 1.00 37.44  ? 4528 VAL A CA    1 
ATOM   22026 C  C     . VAL A 1 4528 ? 251.440 229.187 264.415 1.00 45.82  ? 4528 VAL A C     1 
ATOM   22027 O  O     . VAL A 1 4528 ? 251.925 229.264 265.549 1.00 52.63  ? 4528 VAL A O     1 
ATOM   22028 C  CB    . VAL A 1 4528 ? 251.899 231.035 262.743 1.00 41.20  ? 4528 VAL A CB    1 
ATOM   22029 C  CG1   . VAL A 1 4528 ? 251.899 231.976 263.932 1.00 39.24  ? 4528 VAL A CG1   1 
ATOM   22030 C  CG2   . VAL A 1 4528 ? 252.888 231.506 261.707 1.00 47.06  ? 4528 VAL A CG2   1 
ATOM   22031 N  N     . ALA A 1 4529 ? 250.202 228.733 264.208 1.00 50.35  ? 4529 ALA A N     1 
ATOM   22032 C  CA    . ALA A 1 4529 ? 249.372 228.320 265.335 1.00 44.29  ? 4529 ALA A CA    1 
ATOM   22033 C  C     . ALA A 1 4529 ? 249.965 227.115 266.054 1.00 49.25  ? 4529 ALA A C     1 
ATOM   22034 O  O     . ALA A 1 4529 ? 249.989 227.072 267.289 1.00 53.44  ? 4529 ALA A O     1 
ATOM   22035 C  CB    . ALA A 1 4529 ? 247.954 228.013 264.861 1.00 42.50  ? 4529 ALA A CB    1 
ATOM   22036 N  N     . GLN A 1 4530 ? 250.446 226.123 265.301 1.00 54.80  ? 4530 GLN A N     1 
ATOM   22037 C  CA    . GLN A 1 4530 ? 251.019 224.937 265.929 1.00 43.88  ? 4530 GLN A CA    1 
ATOM   22038 C  C     . GLN A 1 4530 ? 252.331 225.256 266.632 1.00 48.77  ? 4530 GLN A C     1 
ATOM   22039 O  O     . GLN A 1 4530 ? 252.595 224.741 267.724 1.00 52.76  ? 4530 GLN A O     1 
ATOM   22040 C  CB    . GLN A 1 4530 ? 251.224 223.837 264.890 1.00 43.91  ? 4530 GLN A CB    1 
ATOM   22041 C  CG    . GLN A 1 4530 ? 249.958 223.090 264.520 1.00 45.90  ? 4530 GLN A CG    1 
ATOM   22042 C  CD    . GLN A 1 4530 ? 250.162 222.140 263.361 1.00 53.19  ? 4530 GLN A CD    1 
ATOM   22043 O  OE1   . GLN A 1 4530 ? 251.253 221.607 263.166 1.00 54.49  ? 4530 GLN A OE1   1 
ATOM   22044 N  NE2   . GLN A 1 4530 ? 249.108 221.914 262.589 1.00 51.68  ? 4530 GLN A NE2   1 
ATOM   22045 N  N     . ALA A 1 4531 ? 253.171 226.094 266.018 1.00 52.87  ? 4531 ALA A N     1 
ATOM   22046 C  CA    . ALA A 1 4531 ? 254.473 226.397 266.601 1.00 51.65  ? 4531 ALA A CA    1 
ATOM   22047 C  C     . ALA A 1 4531 ? 254.336 227.117 267.937 1.00 56.16  ? 4531 ALA A C     1 
ATOM   22048 O  O     . ALA A 1 4531 ? 255.087 226.837 268.878 1.00 55.50  ? 4531 ALA A O     1 
ATOM   22049 C  CB    . ALA A 1 4531 ? 255.302 227.229 265.625 1.00 49.46  ? 4531 ALA A CB    1 
ATOM   22050 N  N     . ASN A 1 4532 ? 253.388 228.046 268.039 1.00 56.76  ? 4532 ASN A N     1 
ATOM   22051 C  CA    . ASN A 1 4532 ? 253.198 228.846 269.241 1.00 55.16  ? 4532 ASN A CA    1 
ATOM   22052 C  C     . ASN A 1 4532 ? 252.062 228.337 270.119 1.00 57.29  ? 4532 ASN A C     1 
ATOM   22053 O  O     . ASN A 1 4532 ? 251.725 228.989 271.112 1.00 61.31  ? 4532 ASN A O     1 
ATOM   22054 C  CB    . ASN A 1 4532 ? 252.951 230.305 268.861 1.00 55.47  ? 4532 ASN A CB    1 
ATOM   22055 C  CG    . ASN A 1 4532 ? 254.178 230.966 268.274 1.00 60.38  ? 4532 ASN A CG    1 
ATOM   22056 O  OD1   . ASN A 1 4532 ? 255.291 230.775 268.761 1.00 60.74  ? 4532 ASN A OD1   1 
ATOM   22057 N  ND2   . ASN A 1 4532 ? 253.982 231.746 267.220 1.00 61.58  ? 4532 ASN A ND2   1 
ATOM   22058 N  N     . SER A 1 4533 ? 251.465 227.195 269.773 1.00 58.63  ? 4533 SER A N     1 
ATOM   22059 C  CA    . SER A 1 4533 ? 250.379 226.593 270.550 1.00 58.37  ? 4533 SER A CA    1 
ATOM   22060 C  C     . SER A 1 4533 ? 249.201 227.552 270.709 1.00 62.58  ? 4533 SER A C     1 
ATOM   22061 O  O     . SER A 1 4533 ? 248.545 227.592 271.751 1.00 59.88  ? 4533 SER A O     1 
ATOM   22062 C  CB    . SER A 1 4533 ? 250.876 226.111 271.915 1.00 58.36  ? 4533 SER A CB    1 
ATOM   22063 O  OG    . SER A 1 4533 ? 251.817 225.063 271.772 1.00 67.00  ? 4533 SER A OG    1 
ATOM   22064 N  N     . TRP A 1 4534 ? 248.929 228.329 269.666 1.00 59.81  ? 4534 TRP A N     1 
ATOM   22065 C  CA    . TRP A 1 4534 ? 247.785 229.223 269.634 1.00 54.22  ? 4534 TRP A CA    1 
ATOM   22066 C  C     . TRP A 1 4534 ? 246.605 228.521 268.969 1.00 59.63  ? 4534 TRP A C     1 
ATOM   22067 O  O     . TRP A 1 4534 ? 246.691 227.367 268.543 1.00 62.13  ? 4534 TRP A O     1 
ATOM   22068 C  CB    . TRP A 1 4534 ? 248.134 230.520 268.903 1.00 55.93  ? 4534 TRP A CB    1 
ATOM   22069 C  CG    . TRP A 1 4534 ? 249.136 231.367 269.618 1.00 59.86  ? 4534 TRP A CG    1 
ATOM   22070 C  CD1   . TRP A 1 4534 ? 249.395 231.377 270.955 1.00 61.55  ? 4534 TRP A CD1   1 
ATOM   22071 C  CD2   . TRP A 1 4534 ? 250.018 232.329 269.031 1.00 61.24  ? 4534 TRP A CD2   1 
ATOM   22072 N  NE1   . TRP A 1 4534 ? 250.383 232.287 271.239 1.00 59.88  ? 4534 TRP A NE1   1 
ATOM   22073 C  CE2   . TRP A 1 4534 ? 250.782 232.885 270.074 1.00 59.27  ? 4534 TRP A CE2   1 
ATOM   22074 C  CE3   . TRP A 1 4534 ? 250.237 232.774 267.725 1.00 64.15  ? 4534 TRP A CE3   1 
ATOM   22075 C  CZ2   . TRP A 1 4534 ? 251.747 233.863 269.852 1.00 60.38  ? 4534 TRP A CZ2   1 
ATOM   22076 C  CZ3   . TRP A 1 4534 ? 251.195 233.746 267.507 1.00 61.29  ? 4534 TRP A CZ3   1 
ATOM   22077 C  CH2   . TRP A 1 4534 ? 251.938 234.278 268.564 1.00 60.49  ? 4534 TRP A CH2   1 
ATOM   22078 N  N     . SER A 1 4535 ? 245.486 229.229 268.883 1.00 54.85  ? 4535 SER A N     1 
ATOM   22079 C  CA    . SER A 1 4535 ? 244.300 228.729 268.205 1.00 53.89  ? 4535 SER A CA    1 
ATOM   22080 C  C     . SER A 1 4535 ? 244.181 229.392 266.841 1.00 61.45  ? 4535 SER A C     1 
ATOM   22081 O  O     . SER A 1 4535 ? 244.492 230.577 266.687 1.00 67.04  ? 4535 SER A O     1 
ATOM   22082 C  CB    . SER A 1 4535 ? 243.042 228.987 269.033 1.00 53.19  ? 4535 SER A CB    1 
ATOM   22083 O  OG    . SER A 1 4535 ? 241.968 228.183 268.583 1.00 57.32  ? 4535 SER A OG    1 
ATOM   22084 N  N     . LEU A 1 4536 ? 243.735 228.617 265.851 1.00 52.77  ? 4536 LEU A N     1 
ATOM   22085 C  CA    . LEU A 1 4536 ? 243.692 229.112 264.478 1.00 50.94  ? 4536 LEU A CA    1 
ATOM   22086 C  C     . LEU A 1 4536 ? 242.762 230.310 264.341 1.00 54.47  ? 4536 LEU A C     1 
ATOM   22087 O  O     . LEU A 1 4536 ? 243.096 231.290 263.665 1.00 50.89  ? 4536 LEU A O     1 
ATOM   22088 C  CB    . LEU A 1 4536 ? 243.252 227.994 263.534 1.00 54.68  ? 4536 LEU A CB    1 
ATOM   22089 C  CG    . LEU A 1 4536 ? 244.336 227.143 262.880 1.00 50.73  ? 4536 LEU A CG    1 
ATOM   22090 C  CD1   . LEU A 1 4536 ? 243.726 226.244 261.825 1.00 55.26  ? 4536 LEU A CD1   1 
ATOM   22091 C  CD2   . LEU A 1 4536 ? 245.396 228.024 262.270 1.00 50.49  ? 4536 LEU A CD2   1 
ATOM   22092 N  N     . GLU A 1 4537 ? 241.590 230.253 264.976 1.00 53.66  ? 4537 GLU A N     1 
ATOM   22093 C  CA    . GLU A 1 4537 ? 240.572 231.272 264.754 1.00 56.91  ? 4537 GLU A CA    1 
ATOM   22094 C  C     . GLU A 1 4537 ? 240.948 232.627 265.339 1.00 62.87  ? 4537 GLU A C     1 
ATOM   22095 O  O     . GLU A 1 4537 ? 240.332 233.633 264.975 1.00 58.96  ? 4537 GLU A O     1 
ATOM   22096 C  CB    . GLU A 1 4537 ? 239.236 230.808 265.334 1.00 51.14  ? 4537 GLU A CB    1 
ATOM   22097 C  CG    . GLU A 1 4537 ? 239.072 231.091 266.814 1.00 54.89  ? 4537 GLU A CG    1 
ATOM   22098 C  CD    . GLU A 1 4537 ? 239.509 229.927 267.674 1.00 58.55  ? 4537 GLU A CD    1 
ATOM   22099 O  OE1   . GLU A 1 4537 ? 239.939 228.902 267.108 1.00 59.43  ? 4537 GLU A OE1   1 
ATOM   22100 O  OE2   . GLU A 1 4537 ? 239.425 230.035 268.914 1.00 61.24  ? 4537 GLU A OE2   1 
ATOM   22101 N  N     . GLU A 1 4538 ? 241.940 232.683 266.228 1.00 61.78  ? 4538 GLU A N     1 
ATOM   22102 C  CA    . GLU A 1 4538 ? 242.335 233.927 266.876 1.00 58.69  ? 4538 GLU A CA    1 
ATOM   22103 C  C     . GLU A 1 4538 ? 243.664 234.457 266.343 1.00 64.67  ? 4538 GLU A C     1 
ATOM   22104 O  O     . GLU A 1 4538 ? 244.423 235.098 267.073 1.00 67.57  ? 4538 GLU A O     1 
ATOM   22105 C  CB    . GLU A 1 4538 ? 242.396 233.746 268.391 1.00 59.37  ? 4538 GLU A CB    1 
ATOM   22106 C  CG    . GLU A 1 4538 ? 243.413 232.726 268.869 1.00 65.04  ? 4538 GLU A CG    1 
ATOM   22107 C  CD    . GLU A 1 4538 ? 243.140 232.258 270.284 1.00 70.60  ? 4538 GLU A CD    1 
ATOM   22108 O  OE1   . GLU A 1 4538 ? 242.028 232.515 270.792 1.00 65.47  ? 4538 GLU A OE1   1 
ATOM   22109 O  OE2   . GLU A 1 4538 ? 244.039 231.639 270.891 1.00 67.73  ? 4538 GLU A OE2   1 
ATOM   22110 N  N     . LEU A 1 4539 ? 243.952 234.204 265.070 1.00 57.96  ? 4539 LEU A N     1 
ATOM   22111 C  CA    . LEU A 1 4539 ? 245.152 234.702 264.414 1.00 52.45  ? 4539 LEU A CA    1 
ATOM   22112 C  C     . LEU A 1 4539 ? 244.761 235.705 263.339 1.00 52.98  ? 4539 LEU A C     1 
ATOM   22113 O  O     . LEU A 1 4539 ? 243.830 235.458 262.565 1.00 58.64  ? 4539 LEU A O     1 
ATOM   22114 C  CB    . LEU A 1 4539 ? 245.957 233.559 263.794 1.00 53.11  ? 4539 LEU A CB    1 
ATOM   22115 C  CG    . LEU A 1 4539 ? 246.719 232.639 264.745 1.00 53.39  ? 4539 LEU A CG    1 
ATOM   22116 C  CD1   . LEU A 1 4539 ? 247.716 231.798 263.972 1.00 48.73  ? 4539 LEU A CD1   1 
ATOM   22117 C  CD2   . LEU A 1 4539 ? 247.418 233.453 265.812 1.00 55.21  ? 4539 LEU A CD2   1 
ATOM   22118 N  N     . CYS A 1 4540 ? 245.465 236.829 263.296 1.00 54.24  ? 4540 CYS A N     1 
ATOM   22119 C  CA    . CYS A 1 4540 ? 245.280 237.836 262.265 1.00 55.21  ? 4540 CYS A CA    1 
ATOM   22120 C  C     . CYS A 1 4540 ? 246.576 238.003 261.484 1.00 59.17  ? 4540 CYS A C     1 
ATOM   22121 O  O     . CYS A 1 4540 ? 247.655 237.604 261.927 1.00 62.15  ? 4540 CYS A O     1 
ATOM   22122 C  CB    . CYS A 1 4540 ? 244.831 239.175 262.863 1.00 53.75  ? 4540 CYS A CB    1 
ATOM   22123 S  SG    . CYS A 1 4540 ? 246.067 240.016 263.868 1.00 67.79  ? 4540 CYS A SG    1 
ATOM   22124 N  N     . LEU A 1 4541 ? 246.457 238.601 260.304 1.00 52.76  ? 4541 LEU A N     1 
ATOM   22125 C  CA    . LEU A 1 4541 ? 247.571 238.748 259.381 1.00 50.90  ? 4541 LEU A CA    1 
ATOM   22126 C  C     . LEU A 1 4541 ? 247.955 240.214 259.247 1.00 52.95  ? 4541 LEU A C     1 
ATOM   22127 O  O     . LEU A 1 4541 ? 247.088 241.085 259.128 1.00 59.67  ? 4541 LEU A O     1 
ATOM   22128 C  CB    . LEU A 1 4541 ? 247.214 238.177 258.007 1.00 52.02  ? 4541 LEU A CB    1 
ATOM   22129 C  CG    . LEU A 1 4541 ? 248.296 238.230 256.931 1.00 50.22  ? 4541 LEU A CG    1 
ATOM   22130 C  CD1   . LEU A 1 4541 ? 249.222 237.043 257.061 1.00 49.65  ? 4541 LEU A CD1   1 
ATOM   22131 C  CD2   . LEU A 1 4541 ? 247.663 238.265 255.556 1.00 53.21  ? 4541 LEU A CD2   1 
ATOM   22132 N  N     . GLU A 1 4542 ? 249.257 240.480 259.275 1.00 48.15  ? 4542 GLU A N     1 
ATOM   22133 C  CA    . GLU A 1 4542 ? 249.794 241.806 259.018 1.00 56.99  ? 4542 GLU A CA    1 
ATOM   22134 C  C     . GLU A 1 4542 ? 250.947 241.700 258.028 1.00 55.90  ? 4542 GLU A C     1 
ATOM   22135 O  O     . GLU A 1 4542 ? 251.745 240.759 258.074 1.00 59.78  ? 4542 GLU A O     1 
ATOM   22136 C  CB    . GLU A 1 4542 ? 250.241 242.490 260.317 1.00 50.22  ? 4542 GLU A CB    1 
ATOM   22137 C  CG    . GLU A 1 4542 ? 251.366 241.798 261.057 1.00 56.97  ? 4542 GLU A CG    1 
ATOM   22138 C  CD    . GLU A 1 4542 ? 251.670 242.456 262.387 1.00 64.38  ? 4542 GLU A CD    1 
ATOM   22139 O  OE1   . GLU A 1 4542 ? 250.982 243.438 262.736 1.00 62.86  ? 4542 GLU A OE1   1 
ATOM   22140 O  OE2   . GLU A 1 4542 ? 252.595 241.993 263.086 1.00 64.02  ? 4542 GLU A OE2   1 
ATOM   22141 N  N     . VAL A 1 4543 ? 251.021 242.675 257.127 1.00 50.67  ? 4543 VAL A N     1 
ATOM   22142 C  CA    . VAL A 1 4543 ? 251.879 242.616 255.950 1.00 50.59  ? 4543 VAL A CA    1 
ATOM   22143 C  C     . VAL A 1 4543 ? 252.950 243.690 256.058 1.00 56.41  ? 4543 VAL A C     1 
ATOM   22144 O  O     . VAL A 1 4543 ? 252.652 244.841 256.396 1.00 64.64  ? 4543 VAL A O     1 
ATOM   22145 C  CB    . VAL A 1 4543 ? 251.062 242.785 254.657 1.00 56.51  ? 4543 VAL A CB    1 
ATOM   22146 C  CG1   . VAL A 1 4543 ? 251.969 243.071 253.483 1.00 52.99  ? 4543 VAL A CG1   1 
ATOM   22147 C  CG2   . VAL A 1 4543 ? 250.245 241.536 254.400 1.00 61.39  ? 4543 VAL A CG2   1 
ATOM   22148 N  N     . ASN A 1 4544 ? 254.193 243.309 255.773 1.00 51.41  ? 4544 ASN A N     1 
ATOM   22149 C  CA    . ASN A 1 4544 ? 255.336 244.214 255.815 1.00 50.37  ? 4544 ASN A CA    1 
ATOM   22150 C  C     . ASN A 1 4544 ? 256.114 244.053 254.516 1.00 53.33  ? 4544 ASN A C     1 
ATOM   22151 O  O     . ASN A 1 4544 ? 256.749 243.017 254.296 1.00 60.91  ? 4544 ASN A O     1 
ATOM   22152 C  CB    . ASN A 1 4544 ? 256.212 243.921 257.032 1.00 50.83  ? 4544 ASN A CB    1 
ATOM   22153 C  CG    . ASN A 1 4544 ? 257.435 244.804 257.100 1.00 57.73  ? 4544 ASN A CG    1 
ATOM   22154 O  OD1   . ASN A 1 4544 ? 257.349 246.018 256.928 1.00 63.24  ? 4544 ASN A OD1   1 
ATOM   22155 N  ND2   . ASN A 1 4544 ? 258.582 244.200 257.376 1.00 56.40  ? 4544 ASN A ND2   1 
ATOM   22156 N  N     . VAL A 1 4545 ? 256.064 245.067 253.659 1.00 55.17  ? 4545 VAL A N     1 
ATOM   22157 C  CA    . VAL A 1 4545 ? 256.706 245.014 252.349 1.00 53.55  ? 4545 VAL A CA    1 
ATOM   22158 C  C     . VAL A 1 4545 ? 258.115 245.581 252.467 1.00 57.06  ? 4545 VAL A C     1 
ATOM   22159 O  O     . VAL A 1 4545 ? 258.293 246.762 252.785 1.00 56.68  ? 4545 VAL A O     1 
ATOM   22160 C  CB    . VAL A 1 4545 ? 255.893 245.785 251.300 1.00 52.89  ? 4545 VAL A CB    1 
ATOM   22161 C  CG1   . VAL A 1 4545 ? 256.575 245.708 249.947 1.00 53.22  ? 4545 VAL A CG1   1 
ATOM   22162 C  CG2   . VAL A 1 4545 ? 254.478 245.243 251.220 1.00 52.72  ? 4545 VAL A CG2   1 
ATOM   22163 N  N     . THR A 1 4546 ? 259.115 244.741 252.208 1.00 65.26  ? 4546 THR A N     1 
ATOM   22164 C  CA    . THR A 1 4546 ? 260.521 245.126 252.260 1.00 66.34  ? 4546 THR A CA    1 
ATOM   22165 C  C     . THR A 1 4546 ? 261.236 244.619 251.013 1.00 69.29  ? 4546 THR A C     1 
ATOM   22166 O  O     . THR A 1 4546 ? 260.655 243.936 250.166 1.00 69.89  ? 4546 THR A O     1 
ATOM   22167 C  CB    . THR A 1 4546 ? 261.217 244.579 253.514 1.00 70.02  ? 4546 THR A CB    1 
ATOM   22168 O  OG1   . THR A 1 4546 ? 261.564 243.205 253.307 1.00 66.91  ? 4546 THR A OG1   1 
ATOM   22169 C  CG2   . THR A 1 4546 ? 260.327 244.697 254.736 1.00 67.39  ? 4546 THR A CG2   1 
ATOM   22170 N  N     . THR A 1 4547 ? 262.517 244.964 250.912 1.00 80.63  ? 4547 THR A N     1 
ATOM   22171 C  CA    . THR A 1 4547 ? 263.362 244.468 249.835 1.00 79.07  ? 4547 THR A CA    1 
ATOM   22172 C  C     . THR A 1 4547 ? 263.663 242.985 250.037 1.00 77.07  ? 4547 THR A C     1 
ATOM   22173 O  O     . THR A 1 4547 ? 263.799 242.504 251.164 1.00 76.38  ? 4547 THR A O     1 
ATOM   22174 C  CB    . THR A 1 4547 ? 264.664 245.272 249.774 1.00 82.16  ? 4547 THR A CB    1 
ATOM   22175 O  OG1   . THR A 1 4547 ? 264.356 246.666 249.656 1.00 79.86  ? 4547 THR A OG1   1 
ATOM   22176 C  CG2   . THR A 1 4547 ? 265.511 244.855 248.580 1.00 79.86  ? 4547 THR A CG2   1 
ATOM   22177 N  N     . SER A 1 4548 ? 263.762 242.258 248.923 1.00 80.07  ? 4548 SER A N     1 
ATOM   22178 C  CA    . SER A 1 4548 ? 263.972 240.815 248.946 1.00 84.41  ? 4548 SER A CA    1 
ATOM   22179 C  C     . SER A 1 4548 ? 265.250 240.429 249.682 1.00 85.43  ? 4548 SER A C     1 
ATOM   22180 O  O     . SER A 1 4548 ? 265.220 239.585 250.582 1.00 84.63  ? 4548 SER A O     1 
ATOM   22181 C  CB    . SER A 1 4548 ? 264.006 240.264 247.518 1.00 79.82  ? 4548 SER A CB    1 
ATOM   22182 O  OG    . SER A 1 4548 ? 264.247 238.869 247.515 1.00 80.74  ? 4548 SER A OG    1 
ATOM   22183 N  N     . GLN A 1 4549 ? 266.379 241.031 249.301 1.00 92.21  ? 4549 GLN A N     1 
ATOM   22184 C  CA    . GLN A 1 4549 ? 267.642 240.711 249.959 1.00 92.73  ? 4549 GLN A CA    1 
ATOM   22185 C  C     . GLN A 1 4549 ? 267.682 241.273 251.376 1.00 90.65  ? 4549 GLN A C     1 
ATOM   22186 O  O     . GLN A 1 4549 ? 268.069 240.578 252.322 1.00 85.36  ? 4549 GLN A O     1 
ATOM   22187 C  CB    . GLN A 1 4549 ? 268.813 241.244 249.134 1.00 88.67  ? 4549 GLN A CB    1 
ATOM   22188 C  CG    . GLN A 1 4549 ? 270.163 241.123 249.825 1.00 89.77  ? 4549 GLN A CG    1 
ATOM   22189 C  CD    . GLN A 1 4549 ? 270.491 239.696 250.220 1.00 93.93  ? 4549 GLN A CD    1 
ATOM   22190 O  OE1   . GLN A 1 4549 ? 270.687 239.394 251.397 1.00 93.99  ? 4549 GLN A OE1   1 
ATOM   22191 N  NE2   . GLN A 1 4549 ? 270.550 238.808 249.234 1.00 91.02  ? 4549 GLN A NE2   1 
ATOM   22192 N  N     . GLY A 1 4550 ? 267.283 242.531 251.540 1.00 86.65  ? 4550 GLY A N     1 
ATOM   22193 C  CA    . GLY A 1 4550 ? 267.319 243.171 252.839 1.00 87.49  ? 4550 GLY A CA    1 
ATOM   22194 C  C     . GLY A 1 4550 ? 266.082 242.905 253.670 1.00 88.50  ? 4550 GLY A C     1 
ATOM   22195 O  O     . GLY A 1 4550 ? 265.279 243.813 253.906 1.00 86.65  ? 4550 GLY A O     1 
ATOM   22196 N  N     . ALA A 1 4551 ? 265.917 241.664 254.121 1.00 87.08  ? 4551 ALA A N     1 
ATOM   22197 C  CA    . ALA A 1 4551 ? 264.749 241.290 254.901 1.00 85.71  ? 4551 ALA A CA    1 
ATOM   22198 C  C     . ALA A 1 4551 ? 265.126 240.204 255.895 1.00 86.83  ? 4551 ALA A C     1 
ATOM   22199 O  O     . ALA A 1 4551 ? 266.055 239.425 255.666 1.00 86.81  ? 4551 ALA A O     1 
ATOM   22200 C  CB    . ALA A 1 4551 ? 263.606 240.804 254.005 1.00 84.47  ? 4551 ALA A CB    1 
ATOM   22201 N  N     . THR A 1 4552 ? 264.388 240.162 257.003 1.00 84.81  ? 4552 THR A N     1 
ATOM   22202 C  CA    . THR A 1 4552 ? 264.568 239.150 258.037 1.00 86.12  ? 4552 THR A CA    1 
ATOM   22203 C  C     . THR A 1 4552 ? 263.222 238.499 258.310 1.00 81.54  ? 4552 THR A C     1 
ATOM   22204 O  O     . THR A 1 4552 ? 262.244 239.194 258.603 1.00 81.02  ? 4552 THR A O     1 
ATOM   22205 C  CB    . THR A 1 4552 ? 265.137 239.760 259.321 1.00 87.24  ? 4552 THR A CB    1 
ATOM   22206 O  OG1   . THR A 1 4552 ? 264.259 240.790 259.792 1.00 87.55  ? 4552 THR A OG1   1 
ATOM   22207 C  CG2   . THR A 1 4552 ? 266.515 240.353 259.068 1.00 81.61  ? 4552 THR A CG2   1 
ATOM   22208 N  N     . LEU A 1 4553 ? 263.172 237.174 258.215 1.00 67.69  ? 4553 LEU A N     1 
ATOM   22209 C  CA    . LEU A 1 4553 ? 261.955 236.422 258.488 1.00 68.07  ? 4553 LEU A CA    1 
ATOM   22210 C  C     . LEU A 1 4553 ? 262.050 235.806 259.878 1.00 69.48  ? 4553 LEU A C     1 
ATOM   22211 O  O     . LEU A 1 4553 ? 262.945 234.996 260.142 1.00 71.33  ? 4553 LEU A O     1 
ATOM   22212 C  CB    . LEU A 1 4553 ? 261.739 235.336 257.435 1.00 65.83  ? 4553 LEU A CB    1 
ATOM   22213 C  CG    . LEU A 1 4553 ? 261.504 235.775 255.988 1.00 65.22  ? 4553 LEU A CG    1 
ATOM   22214 C  CD1   . LEU A 1 4553 ? 260.981 234.610 255.167 1.00 66.18  ? 4553 LEU A CD1   1 
ATOM   22215 C  CD2   . LEU A 1 4553 ? 260.543 236.945 255.924 1.00 61.79  ? 4553 LEU A CD2   1 
ATOM   22216 N  N     . ASP A 1 4554 ? 261.131 236.189 260.763 1.00 64.72  ? 4554 ASP A N     1 
ATOM   22217 C  CA    . ASP A 1 4554 ? 261.095 235.617 262.103 1.00 62.79  ? 4554 ASP A CA    1 
ATOM   22218 C  C     . ASP A 1 4554 ? 260.291 234.324 262.104 1.00 66.44  ? 4554 ASP A C     1 
ATOM   22219 O  O     . ASP A 1 4554 ? 259.975 233.785 261.040 1.00 68.43  ? 4554 ASP A O     1 
ATOM   22220 C  CB    . ASP A 1 4554 ? 260.529 236.624 263.110 1.00 63.04  ? 4554 ASP A CB    1 
ATOM   22221 C  CG    . ASP A 1 4554 ? 259.177 237.177 262.699 1.00 70.24  ? 4554 ASP A CG    1 
ATOM   22222 O  OD1   . ASP A 1 4554 ? 258.257 236.383 262.416 1.00 71.34  ? 4554 ASP A OD1   1 
ATOM   22223 O  OD2   . ASP A 1 4554 ? 259.034 238.416 262.663 1.00 71.71  ? 4554 ASP A OD2   1 
ATOM   22224 N  N     . ALA A 1 4555 ? 259.960 233.815 263.289 1.00 62.81  ? 4555 ALA A N     1 
ATOM   22225 C  CA    . ALA A 1 4555 ? 259.243 232.553 263.413 1.00 63.01  ? 4555 ALA A CA    1 
ATOM   22226 C  C     . ALA A 1 4555 ? 257.805 232.621 262.918 1.00 64.41  ? 4555 ALA A C     1 
ATOM   22227 O  O     . ALA A 1 4555 ? 257.188 231.570 262.717 1.00 63.31  ? 4555 ALA A O     1 
ATOM   22228 C  CB    . ALA A 1 4555 ? 259.253 232.082 264.871 1.00 61.97  ? 4555 ALA A CB    1 
ATOM   22229 N  N     . CYS A 1 4556 ? 257.257 233.818 262.716 1.00 60.24  ? 4556 CYS A N     1 
ATOM   22230 C  CA    . CYS A 1 4556 ? 255.877 233.974 262.283 1.00 55.15  ? 4556 CYS A CA    1 
ATOM   22231 C  C     . CYS A 1 4556 ? 255.743 234.676 260.940 1.00 57.38  ? 4556 CYS A C     1 
ATOM   22232 O  O     . CYS A 1 4556 ? 254.615 234.901 260.490 1.00 60.35  ? 4556 CYS A O     1 
ATOM   22233 C  CB    . CYS A 1 4556 ? 255.073 234.744 263.340 1.00 51.25  ? 4556 CYS A CB    1 
ATOM   22234 S  SG    . CYS A 1 4556 ? 255.154 234.037 265.000 1.00 70.09  ? 4556 CYS A SG    1 
ATOM   22235 N  N     . SER A 1 4557 ? 256.849 235.021 260.288 1.00 53.94  ? 4557 SER A N     1 
ATOM   22236 C  CA    . SER A 1 4557 ? 256.829 235.782 259.047 1.00 51.51  ? 4557 SER A CA    1 
ATOM   22237 C  C     . SER A 1 4557 ? 257.196 234.880 257.877 1.00 51.34  ? 4557 SER A C     1 
ATOM   22238 O  O     . SER A 1 4557 ? 258.163 234.116 257.956 1.00 57.30  ? 4557 SER A O     1 
ATOM   22239 C  CB    . SER A 1 4557 ? 257.795 236.965 259.128 1.00 53.38  ? 4557 SER A CB    1 
ATOM   22240 O  OG    . SER A 1 4557 ? 257.933 237.598 257.871 1.00 60.99  ? 4557 SER A OG    1 
ATOM   22241 N  N     . PHE A 1 4558 ? 256.419 234.966 256.800 1.00 41.51  ? 4558 PHE A N     1 
ATOM   22242 C  CA    . PHE A 1 4558 ? 256.655 234.200 255.584 1.00 45.68  ? 4558 PHE A CA    1 
ATOM   22243 C  C     . PHE A 1 4558 ? 256.808 235.154 254.411 1.00 47.28  ? 4558 PHE A C     1 
ATOM   22244 O  O     . PHE A 1 4558 ? 255.969 236.038 254.212 1.00 53.16  ? 4558 PHE A O     1 
ATOM   22245 C  CB    . PHE A 1 4558 ? 255.515 233.216 255.309 1.00 44.32  ? 4558 PHE A CB    1 
ATOM   22246 C  CG    . PHE A 1 4558 ? 255.255 232.258 256.432 1.00 49.53  ? 4558 PHE A CG    1 
ATOM   22247 C  CD1   . PHE A 1 4558 ? 254.480 232.631 257.513 1.00 45.61  ? 4558 PHE A CD1   1 
ATOM   22248 C  CD2   . PHE A 1 4558 ? 255.790 230.983 256.405 1.00 50.47  ? 4558 PHE A CD2   1 
ATOM   22249 C  CE1   . PHE A 1 4558 ? 254.243 231.751 258.544 1.00 44.93  ? 4558 PHE A CE1   1 
ATOM   22250 C  CE2   . PHE A 1 4558 ? 255.556 230.100 257.435 1.00 50.69  ? 4558 PHE A CE2   1 
ATOM   22251 C  CZ    . PHE A 1 4558 ? 254.780 230.486 258.506 1.00 47.65  ? 4558 PHE A CZ    1 
ATOM   22252 N  N     . GLY A 1 4559 ? 257.873 234.972 253.633 1.00 44.71  ? 4559 GLY A N     1 
ATOM   22253 C  CA    . GLY A 1 4559 ? 258.112 235.837 252.492 1.00 41.65  ? 4559 GLY A CA    1 
ATOM   22254 C  C     . GLY A 1 4559 ? 257.299 235.410 251.280 1.00 43.62  ? 4559 GLY A C     1 
ATOM   22255 O  O     . GLY A 1 4559 ? 257.142 234.225 250.993 1.00 45.84  ? 4559 GLY A O     1 
ATOM   22256 N  N     . VAL A 1 4560 ? 256.776 236.404 250.568 1.00 46.09  ? 4560 VAL A N     1 
ATOM   22257 C  CA    . VAL A 1 4560 ? 255.992 236.192 249.358 1.00 39.59  ? 4560 VAL A CA    1 
ATOM   22258 C  C     . VAL A 1 4560 ? 256.462 237.190 248.311 1.00 40.85  ? 4560 VAL A C     1 
ATOM   22259 O  O     . VAL A 1 4560 ? 256.623 238.378 248.610 1.00 48.72  ? 4560 VAL A O     1 
ATOM   22260 C  CB    . VAL A 1 4560 ? 254.480 236.343 249.621 1.00 35.32  ? 4560 VAL A CB    1 
ATOM   22261 C  CG1   . VAL A 1 4560 ? 253.725 236.533 248.321 1.00 43.62  ? 4560 VAL A CG1   1 
ATOM   22262 C  CG2   . VAL A 1 4560 ? 253.952 235.131 250.360 1.00 44.08  ? 4560 VAL A CG2   1 
ATOM   22263 N  N     . THR A 1 4561 ? 256.690 236.710 247.094 1.00 37.73  ? 4561 THR A N     1 
ATOM   22264 C  CA    . THR A 1 4561 ? 257.135 237.544 245.990 1.00 37.24  ? 4561 THR A CA    1 
ATOM   22265 C  C     . THR A 1 4561 ? 256.058 237.600 244.915 1.00 43.42  ? 4561 THR A C     1 
ATOM   22266 O  O     . THR A 1 4561 ? 255.080 236.849 244.936 1.00 40.79  ? 4561 THR A O     1 
ATOM   22267 C  CB    . THR A 1 4561 ? 258.446 237.019 245.393 1.00 39.60  ? 4561 THR A CB    1 
ATOM   22268 O  OG1   . THR A 1 4561 ? 258.214 235.750 244.773 1.00 43.69  ? 4561 THR A OG1   1 
ATOM   22269 C  CG2   . THR A 1 4561 ? 259.495 236.859 246.476 1.00 45.93  ? 4561 THR A CG2   1 
ATOM   22270 N  N     . GLY A 1 4562 ? 256.247 238.517 243.970 1.00 49.70  ? 4562 GLY A N     1 
ATOM   22271 C  CA    . GLY A 1 4562 ? 255.378 238.626 242.820 1.00 45.07  ? 4562 GLY A CA    1 
ATOM   22272 C  C     . GLY A 1 4562 ? 254.103 239.408 243.030 1.00 44.29  ? 4562 GLY A C     1 
ATOM   22273 O  O     . GLY A 1 4562 ? 253.310 239.522 242.088 1.00 49.69  ? 4562 GLY A O     1 
ATOM   22274 N  N     . LEU A 1 4563 ? 253.873 239.951 244.222 1.00 47.99  ? 4563 LEU A N     1 
ATOM   22275 C  CA    . LEU A 1 4563 ? 252.658 240.715 244.470 1.00 39.02  ? 4563 LEU A CA    1 
ATOM   22276 C  C     . LEU A 1 4563 ? 252.759 242.087 243.819 1.00 37.52  ? 4563 LEU A C     1 
ATOM   22277 O  O     . LEU A 1 4563 ? 253.707 242.837 244.068 1.00 43.68  ? 4563 LEU A O     1 
ATOM   22278 C  CB    . LEU A 1 4563 ? 252.417 240.853 245.971 1.00 39.50  ? 4563 LEU A CB    1 
ATOM   22279 C  CG    . LEU A 1 4563 ? 252.045 239.575 246.720 1.00 39.88  ? 4563 LEU A CG    1 
ATOM   22280 C  CD1   . LEU A 1 4563 ? 251.640 239.903 248.140 1.00 42.99  ? 4563 LEU A CD1   1 
ATOM   22281 C  CD2   . LEU A 1 4563 ? 250.925 238.848 246.005 1.00 41.88  ? 4563 LEU A CD2   1 
ATOM   22282 N  N     . LYS A 1 4564 ? 251.778 242.416 242.985 1.00 41.21  ? 4564 LYS A N     1 
ATOM   22283 C  CA    . LYS A 1 4564 ? 251.755 243.667 242.241 1.00 38.62  ? 4564 LYS A CA    1 
ATOM   22284 C  C     . LYS A 1 4564 ? 250.714 244.596 242.844 1.00 40.07  ? 4564 LYS A C     1 
ATOM   22285 O  O     . LYS A 1 4564 ? 249.562 244.197 243.039 1.00 52.66  ? 4564 LYS A O     1 
ATOM   22286 C  CB    . LYS A 1 4564 ? 251.447 243.418 240.763 1.00 39.95  ? 4564 LYS A CB    1 
ATOM   22287 C  CG    . LYS A 1 4564 ? 252.443 242.514 240.063 1.00 44.30  ? 4564 LYS A CG    1 
ATOM   22288 C  CD    . LYS A 1 4564 ? 253.701 243.273 239.691 1.00 43.99  ? 4564 LYS A CD    1 
ATOM   22289 C  CE    . LYS A 1 4564 ? 254.627 242.426 238.841 1.00 44.24  ? 4564 LYS A CE    1 
ATOM   22290 N  NZ    . LYS A 1 4564 ? 255.087 241.214 239.568 1.00 45.99  ? 4564 LYS A NZ    1 
ATOM   22291 N  N     . LEU A 1 4565 ? 251.117 245.828 243.131 1.00 29.56  ? 4565 LEU A N     1 
ATOM   22292 C  CA    . LEU A 1 4565 ? 250.226 246.832 243.698 1.00 35.88  ? 4565 LEU A CA    1 
ATOM   22293 C  C     . LEU A 1 4565 ? 249.668 247.686 242.568 1.00 41.81  ? 4565 LEU A C     1 
ATOM   22294 O  O     . LEU A 1 4565 ? 250.431 248.285 241.804 1.00 53.46  ? 4565 LEU A O     1 
ATOM   22295 C  CB    . LEU A 1 4565 ? 250.960 247.698 244.719 1.00 38.28  ? 4565 LEU A CB    1 
ATOM   22296 C  CG    . LEU A 1 4565 ? 250.095 248.686 245.498 1.00 36.92  ? 4565 LEU A CG    1 
ATOM   22297 C  CD1   . LEU A 1 4565 ? 248.901 247.981 246.108 1.00 38.38  ? 4565 LEU A CD1   1 
ATOM   22298 C  CD2   . LEU A 1 4565 ? 250.919 249.361 246.570 1.00 42.61  ? 4565 LEU A CD2   1 
ATOM   22299 N  N     . GLN A 1 4566 ? 248.344 247.746 242.469 1.00 37.99  ? 4566 GLN A N     1 
ATOM   22300 C  CA    . GLN A 1 4566 ? 247.670 248.434 241.377 1.00 38.93  ? 4566 GLN A CA    1 
ATOM   22301 C  C     . GLN A 1 4566 ? 247.307 249.848 241.807 1.00 43.66  ? 4566 GLN A C     1 
ATOM   22302 O  O     . GLN A 1 4566 ? 246.540 250.035 242.755 1.00 48.14  ? 4566 GLN A O     1 
ATOM   22303 C  CB    . GLN A 1 4566 ? 246.419 247.671 240.947 1.00 38.97  ? 4566 GLN A CB    1 
ATOM   22304 C  CG    . GLN A 1 4566 ? 246.652 246.198 240.685 1.00 43.41  ? 4566 GLN A CG    1 
ATOM   22305 C  CD    . GLN A 1 4566 ? 247.625 245.954 239.551 1.00 44.61  ? 4566 GLN A CD    1 
ATOM   22306 O  OE1   . GLN A 1 4566 ? 248.633 245.271 239.720 1.00 47.62  ? 4566 GLN A OE1   1 
ATOM   22307 N  NE2   . GLN A 1 4566 ? 247.327 246.512 238.387 1.00 45.17  ? 4566 GLN A NE2   1 
ATOM   22308 N  N     . GLY A 1 4567 ? 247.852 250.837 241.103 1.00 44.19  ? 4567 GLY A N     1 
ATOM   22309 C  CA    . GLY A 1 4567 ? 247.477 252.216 241.335 1.00 37.66  ? 4567 GLY A CA    1 
ATOM   22310 C  C     . GLY A 1 4567 ? 247.992 252.820 242.617 1.00 38.41  ? 4567 GLY A C     1 
ATOM   22311 O  O     . GLY A 1 4567 ? 247.418 253.798 243.100 1.00 51.71  ? 4567 GLY A O     1 
ATOM   22312 N  N     . ALA A 1 4568 ? 249.060 252.271 243.186 1.00 39.15  ? 4568 ALA A N     1 
ATOM   22313 C  CA    . ALA A 1 4568 ? 249.631 252.816 244.407 1.00 35.30  ? 4568 ALA A CA    1 
ATOM   22314 C  C     . ALA A 1 4568 ? 251.088 252.392 244.503 1.00 42.97  ? 4568 ALA A C     1 
ATOM   22315 O  O     . ALA A 1 4568 ? 251.527 251.457 243.829 1.00 52.52  ? 4568 ALA A O     1 
ATOM   22316 C  CB    . ALA A 1 4568 ? 248.853 252.362 245.646 1.00 30.38  ? 4568 ALA A CB    1 
ATOM   22317 N  N     . THR A 1 4569 ? 251.833 253.100 245.347 1.00 45.28  ? 4569 THR A N     1 
ATOM   22318 C  CA    . THR A 1 4569 ? 253.225 252.790 245.627 1.00 45.34  ? 4569 THR A CA    1 
ATOM   22319 C  C     . THR A 1 4569 ? 253.414 252.579 247.121 1.00 50.27  ? 4569 THR A C     1 
ATOM   22320 O  O     . THR A 1 4569 ? 252.765 253.232 247.942 1.00 55.37  ? 4569 THR A O     1 
ATOM   22321 C  CB    . THR A 1 4569 ? 254.164 253.901 245.146 1.00 49.65  ? 4569 THR A CB    1 
ATOM   22322 O  OG1   . THR A 1 4569 ? 253.826 255.131 245.796 1.00 50.08  ? 4569 THR A OG1   1 
ATOM   22323 C  CG2   . THR A 1 4569 ? 254.061 254.078 243.646 1.00 54.89  ? 4569 THR A CG2   1 
ATOM   22324 N  N     . CYS A 1 4570 ? 254.308 251.660 247.467 1.00 63.34  ? 4570 CYS A N     1 
ATOM   22325 C  CA    . CYS A 1 4570 ? 254.609 251.333 248.856 1.00 57.93  ? 4570 CYS A CA    1 
ATOM   22326 C  C     . CYS A 1 4570 ? 256.035 251.773 249.160 1.00 61.16  ? 4570 CYS A C     1 
ATOM   22327 O  O     . CYS A 1 4570 ? 256.994 251.184 248.653 1.00 61.09  ? 4570 CYS A O     1 
ATOM   22328 C  CB    . CYS A 1 4570 ? 254.428 249.840 249.117 1.00 55.40  ? 4570 CYS A CB    1 
ATOM   22329 S  SG    . CYS A 1 4570 ? 254.304 249.403 250.861 1.00 69.94  ? 4570 CYS A SG    1 
ATOM   22330 N  N     . ASN A 1 4571 ? 256.169 252.809 249.984 1.00 68.50  ? 4571 ASN A N     1 
ATOM   22331 C  CA    . ASN A 1 4571 ? 257.463 253.272 250.464 1.00 69.93  ? 4571 ASN A CA    1 
ATOM   22332 C  C     . ASN A 1 4571 ? 257.429 253.299 251.983 1.00 70.33  ? 4571 ASN A C     1 
ATOM   22333 O  O     . ASN A 1 4571 ? 256.537 253.915 252.574 1.00 73.96  ? 4571 ASN A O     1 
ATOM   22334 C  CB    . ASN A 1 4571 ? 257.807 254.657 249.905 1.00 71.94  ? 4571 ASN A CB    1 
ATOM   22335 C  CG    . ASN A 1 4571 ? 256.699 255.668 250.123 1.00 75.42  ? 4571 ASN A CG    1 
ATOM   22336 O  OD1   . ASN A 1 4571 ? 255.630 255.576 249.521 1.00 72.14  ? 4571 ASN A OD1   1 
ATOM   22337 N  ND2   . ASN A 1 4571 ? 256.952 256.645 250.988 1.00 69.77  ? 4571 ASN A ND2   1 
ATOM   22338 N  N     . ASN A 1 4572 ? 258.395 252.623 252.607 1.00 70.88  ? 4572 ASN A N     1 
ATOM   22339 C  CA    . ASN A 1 4572 ? 258.452 252.490 254.062 1.00 70.79  ? 4572 ASN A CA    1 
ATOM   22340 C  C     . ASN A 1 4572 ? 257.154 251.902 254.608 1.00 71.51  ? 4572 ASN A C     1 
ATOM   22341 O  O     . ASN A 1 4572 ? 256.658 252.303 255.663 1.00 74.03  ? 4572 ASN A O     1 
ATOM   22342 C  CB    . ASN A 1 4572 ? 258.768 253.830 254.727 1.00 72.47  ? 4572 ASN A CB    1 
ATOM   22343 C  CG    . ASN A 1 4572 ? 260.137 254.356 254.347 1.00 78.55  ? 4572 ASN A CG    1 
ATOM   22344 O  OD1   . ASN A 1 4572 ? 260.257 255.392 253.693 1.00 74.50  ? 4572 ASN A OD1   1 
ATOM   22345 N  ND2   . ASN A 1 4572 ? 261.179 253.641 254.753 1.00 79.64  ? 4572 ASN A ND2   1 
ATOM   22346 N  N     . ASN A 1 4573 ? 256.599 250.940 253.868 1.00 66.24  ? 4573 ASN A N     1 
ATOM   22347 C  CA    . ASN A 1 4573 ? 255.375 250.233 254.246 1.00 64.29  ? 4573 ASN A CA    1 
ATOM   22348 C  C     . ASN A 1 4573 ? 254.189 251.187 254.383 1.00 65.73  ? 4573 ASN A C     1 
ATOM   22349 O  O     . ASN A 1 4573 ? 253.268 250.946 255.166 1.00 66.54  ? 4573 ASN A O     1 
ATOM   22350 C  CB    . ASN A 1 4573 ? 255.578 249.426 255.532 1.00 64.71  ? 4573 ASN A CB    1 
ATOM   22351 C  CG    . ASN A 1 4573 ? 254.566 248.310 255.688 1.00 66.85  ? 4573 ASN A CG    1 
ATOM   22352 O  OD1   . ASN A 1 4573 ? 253.711 248.106 254.828 1.00 70.19  ? 4573 ASN A OD1   1 
ATOM   22353 N  ND2   . ASN A 1 4573 ? 254.656 247.582 256.793 1.00 67.07  ? 4573 ASN A ND2   1 
ATOM   22354 N  N     . LYS A 1 4574 ? 254.203 252.280 253.621 1.00 64.80  ? 4574 LYS A N     1 
ATOM   22355 C  CA    . LYS A 1 4574 ? 253.107 253.237 253.586 1.00 57.22  ? 4574 LYS A CA    1 
ATOM   22356 C  C     . LYS A 1 4574 ? 252.675 253.452 252.145 1.00 62.00  ? 4574 LYS A C     1 
ATOM   22357 O  O     . LYS A 1 4574 ? 253.514 253.578 251.249 1.00 65.59  ? 4574 LYS A O     1 
ATOM   22358 C  CB    . LYS A 1 4574 ? 253.499 254.575 254.217 1.00 58.32  ? 4574 LYS A CB    1 
ATOM   22359 C  CG    . LYS A 1 4574 ? 253.766 254.508 255.707 1.00 60.38  ? 4574 LYS A CG    1 
ATOM   22360 C  CD    . LYS A 1 4574 ? 254.083 255.883 256.263 1.00 62.78  ? 4574 LYS A CD    1 
ATOM   22361 C  CE    . LYS A 1 4574 ? 254.685 255.793 257.653 1.00 63.85  ? 4574 LYS A CE    1 
ATOM   22362 N  NZ    . LYS A 1 4574 ? 253.936 254.846 258.522 1.00 65.04  ? 4574 LYS A NZ    1 
ATOM   22363 N  N     . LEU A 1 4575 ? 251.365 253.500 251.928 1.00 53.32  ? 4575 LEU A N     1 
ATOM   22364 C  CA    . LEU A 1 4575 ? 250.805 253.576 250.587 1.00 50.62  ? 4575 LEU A CA    1 
ATOM   22365 C  C     . LEU A 1 4575 ? 250.624 255.019 250.139 1.00 52.04  ? 4575 LEU A C     1 
ATOM   22366 O  O     . LEU A 1 4575 ? 250.245 255.888 250.929 1.00 64.06  ? 4575 LEU A O     1 
ATOM   22367 C  CB    . LEU A 1 4575 ? 249.460 252.856 250.525 1.00 51.72  ? 4575 LEU A CB    1 
ATOM   22368 C  CG    . LEU A 1 4575 ? 249.455 251.336 250.638 1.00 54.05  ? 4575 LEU A CG    1 
ATOM   22369 C  CD1   . LEU A 1 4575 ? 248.174 250.806 250.041 1.00 53.50  ? 4575 LEU A CD1   1 
ATOM   22370 C  CD2   . LEU A 1 4575 ? 250.661 250.732 249.946 1.00 50.54  ? 4575 LEU A CD2   1 
ATOM   22371 N  N     . SER A 1 4576 ? 250.896 255.263 248.860 1.00 44.20  ? 4576 SER A N     1 
ATOM   22372 C  CA    . SER A 1 4576 ? 250.620 256.540 248.222 1.00 46.72  ? 4576 SER A CA    1 
ATOM   22373 C  C     . SER A 1 4576 ? 250.078 256.276 246.827 1.00 50.08  ? 4576 SER A C     1 
ATOM   22374 O  O     . SER A 1 4576 ? 250.527 255.350 246.148 1.00 61.18  ? 4576 SER A O     1 
ATOM   22375 C  CB    . SER A 1 4576 ? 251.876 257.413 248.146 1.00 54.44  ? 4576 SER A CB    1 
ATOM   22376 O  OG    . SER A 1 4576 ? 252.421 257.633 249.434 1.00 59.04  ? 4576 SER A OG    1 
ATOM   22377 N  N     . LEU A 1 4577 ? 249.112 257.085 246.405 1.00 48.36  ? 4577 LEU A N     1 
ATOM   22378 C  CA    . LEU A 1 4577 ? 248.537 256.928 245.078 1.00 46.67  ? 4577 LEU A CA    1 
ATOM   22379 C  C     . LEU A 1 4577 ? 249.558 257.288 244.005 1.00 51.46  ? 4577 LEU A C     1 
ATOM   22380 O  O     . LEU A 1 4577 ? 250.426 258.142 244.202 1.00 54.22  ? 4577 LEU A O     1 
ATOM   22381 C  CB    . LEU A 1 4577 ? 247.293 257.799 244.928 1.00 42.10  ? 4577 LEU A CB    1 
ATOM   22382 C  CG    . LEU A 1 4577 ? 246.088 257.418 245.783 1.00 40.94  ? 4577 LEU A CG    1 
ATOM   22383 C  CD1   . LEU A 1 4577 ? 245.028 258.497 245.698 1.00 47.10  ? 4577 LEU A CD1   1 
ATOM   22384 C  CD2   . LEU A 1 4577 ? 245.525 256.077 245.354 1.00 40.75  ? 4577 LEU A CD2   1 
ATOM   22385 N  N     . SER A 1 4578 ? 249.446 256.627 242.856 1.00 46.77  ? 4578 SER A N     1 
ATOM   22386 C  CA    . SER A 1 4578 ? 250.384 256.844 241.766 1.00 47.41  ? 4578 SER A CA    1 
ATOM   22387 C  C     . SER A 1 4578 ? 249.663 256.690 240.437 1.00 52.64  ? 4578 SER A C     1 
ATOM   22388 O  O     . SER A 1 4578 ? 248.601 256.070 240.350 1.00 58.28  ? 4578 SER A O     1 
ATOM   22389 C  CB    . SER A 1 4578 ? 251.566 255.873 241.839 1.00 50.30  ? 4578 SER A CB    1 
ATOM   22390 O  OG    . SER A 1 4578 ? 251.226 254.617 241.282 1.00 50.36  ? 4578 SER A OG    1 
ATOM   22391 N  N     . ASN A 1 4579 ? 250.260 257.266 239.396 1.00 57.93  ? 4579 ASN A N     1 
ATOM   22392 C  CA    . ASN A 1 4579 ? 249.726 257.181 238.045 1.00 57.63  ? 4579 ASN A CA    1 
ATOM   22393 C  C     . ASN A 1 4579 ? 250.234 255.965 237.283 1.00 59.84  ? 4579 ASN A C     1 
ATOM   22394 O  O     . ASN A 1 4579 ? 249.815 255.749 236.142 1.00 65.62  ? 4579 ASN A O     1 
ATOM   22395 C  CB    . ASN A 1 4579 ? 250.060 258.454 237.265 1.00 57.06  ? 4579 ASN A CB    1 
ATOM   22396 C  CG    . ASN A 1 4579 ? 249.371 259.676 237.830 1.00 62.49  ? 4579 ASN A CG    1 
ATOM   22397 O  OD1   . ASN A 1 4579 ? 249.987 260.727 238.000 1.00 64.29  ? 4579 ASN A OD1   1 
ATOM   22398 N  ND2   . ASN A 1 4579 ? 248.085 259.541 238.133 1.00 56.84  ? 4579 ASN A ND2   1 
ATOM   22399 N  N     . ALA A 1 4580 ? 251.125 255.178 237.876 1.00 54.35  ? 4580 ALA A N     1 
ATOM   22400 C  CA    . ALA A 1 4580 ? 251.553 253.935 237.257 1.00 53.64  ? 4580 ALA A CA    1 
ATOM   22401 C  C     . ALA A 1 4580 ? 250.438 252.899 237.328 1.00 59.69  ? 4580 ALA A C     1 
ATOM   22402 O  O     . ALA A 1 4580 ? 249.674 252.841 238.294 1.00 60.45  ? 4580 ALA A O     1 
ATOM   22403 C  CB    . ALA A 1 4580 ? 252.810 253.402 237.941 1.00 55.51  ? 4580 ALA A CB    1 
ATOM   22404 N  N     . ILE A 1 4581 ? 250.345 252.077 236.282 1.00 54.90  ? 4581 ILE A N     1 
ATOM   22405 C  CA    . ILE A 1 4581 ? 249.290 251.069 236.222 1.00 55.30  ? 4581 ILE A CA    1 
ATOM   22406 C  C     . ILE A 1 4581 ? 249.450 250.064 237.355 1.00 54.22  ? 4581 ILE A C     1 
ATOM   22407 O  O     . ILE A 1 4581 ? 248.489 249.740 238.063 1.00 52.91  ? 4581 ILE A O     1 
ATOM   22408 C  CB    . ILE A 1 4581 ? 249.287 250.376 234.848 1.00 54.60  ? 4581 ILE A CB    1 
ATOM   22409 C  CG1   . ILE A 1 4581 ? 248.779 251.335 233.771 1.00 54.33  ? 4581 ILE A CG1   1 
ATOM   22410 C  CG2   . ILE A 1 4581 ? 248.434 249.121 234.886 1.00 50.84  ? 4581 ILE A CG2   1 
ATOM   22411 C  CD1   . ILE A 1 4581 ? 247.305 251.635 233.869 1.00 54.53  ? 4581 ILE A CD1   1 
ATOM   22412 N  N     . SER A 1 4582 ? 250.668 249.565 237.552 1.00 53.74  ? 4582 SER A N     1 
ATOM   22413 C  CA    . SER A 1 4582 ? 250.937 248.608 238.614 1.00 50.99  ? 4582 SER A CA    1 
ATOM   22414 C  C     . SER A 1 4582 ? 252.351 248.816 239.131 1.00 50.76  ? 4582 SER A C     1 
ATOM   22415 O  O     . SER A 1 4582 ? 253.265 249.115 238.358 1.00 54.07  ? 4582 SER A O     1 
ATOM   22416 C  CB    . SER A 1 4582 ? 250.762 247.164 238.132 1.00 52.34  ? 4582 SER A CB    1 
ATOM   22417 O  OG    . SER A 1 4582 ? 251.805 246.790 237.251 1.00 56.64  ? 4582 SER A OG    1 
ATOM   22418 N  N     . THR A 1 4583 ? 252.521 248.651 240.439 1.00 49.94  ? 4583 THR A N     1 
ATOM   22419 C  CA    . THR A 1 4583 ? 253.816 248.764 241.093 1.00 47.19  ? 4583 THR A CA    1 
ATOM   22420 C  C     . THR A 1 4583 ? 254.154 247.431 241.743 1.00 50.46  ? 4583 THR A C     1 
ATOM   22421 O  O     . THR A 1 4583 ? 253.342 246.880 242.493 1.00 60.64  ? 4583 THR A O     1 
ATOM   22422 C  CB    . THR A 1 4583 ? 253.811 249.882 242.139 1.00 47.53  ? 4583 THR A CB    1 
ATOM   22423 O  OG1   . THR A 1 4583 ? 253.795 251.154 241.479 1.00 48.06  ? 4583 THR A OG1   1 
ATOM   22424 C  CG2   . THR A 1 4583 ? 255.040 249.796 243.026 1.00 48.31  ? 4583 THR A CG2   1 
ATOM   22425 N  N     . ALA A 1 4584 ? 255.343 246.915 241.452 1.00 44.96  ? 4584 ALA A N     1 
ATOM   22426 C  CA    . ALA A 1 4584 ? 255.761 245.628 241.987 1.00 42.17  ? 4584 ALA A CA    1 
ATOM   22427 C  C     . ALA A 1 4584 ? 256.185 245.771 243.442 1.00 44.34  ? 4584 ALA A C     1 
ATOM   22428 O  O     . ALA A 1 4584 ? 256.940 246.683 243.792 1.00 51.69  ? 4584 ALA A O     1 
ATOM   22429 C  CB    . ALA A 1 4584 ? 256.906 245.053 241.157 1.00 47.31  ? 4584 ALA A CB    1 
ATOM   22430 N  N     . LEU A 1 4585 ? 255.694 244.871 244.288 1.00 44.35  ? 4585 LEU A N     1 
ATOM   22431 C  CA    . LEU A 1 4585 ? 256.143 244.794 245.670 1.00 43.62  ? 4585 LEU A CA    1 
ATOM   22432 C  C     . LEU A 1 4585 ? 257.277 243.783 245.762 1.00 52.67  ? 4585 LEU A C     1 
ATOM   22433 O  O     . LEU A 1 4585 ? 257.051 242.596 245.492 1.00 57.34  ? 4585 LEU A O     1 
ATOM   22434 C  CB    . LEU A 1 4585 ? 255.001 244.391 246.586 1.00 40.95  ? 4585 LEU A CB    1 
ATOM   22435 C  CG    . LEU A 1 4585 ? 253.749 245.270 246.520 1.00 44.40  ? 4585 LEU A CG    1 
ATOM   22436 C  CD1   . LEU A 1 4585 ? 252.661 244.735 247.433 1.00 37.51  ? 4585 LEU A CD1   1 
ATOM   22437 C  CD2   . LEU A 1 4585 ? 254.083 246.708 246.873 1.00 45.85  ? 4585 LEU A CD2   1 
ATOM   22438 N  N     . PRO A 1 4586 ? 258.497 244.197 246.122 1.00 49.22  ? 4586 PRO A N     1 
ATOM   22439 C  CA    . PRO A 1 4586 ? 259.651 243.290 246.029 1.00 50.78  ? 4586 PRO A CA    1 
ATOM   22440 C  C     . PRO A 1 4586 ? 259.503 242.022 246.856 1.00 55.78  ? 4586 PRO A C     1 
ATOM   22441 O  O     . PRO A 1 4586 ? 259.571 240.914 246.315 1.00 53.47  ? 4586 PRO A O     1 
ATOM   22442 C  CB    . PRO A 1 4586 ? 260.818 244.152 246.532 1.00 54.02  ? 4586 PRO A CB    1 
ATOM   22443 C  CG    . PRO A 1 4586 ? 260.186 245.280 247.277 1.00 55.28  ? 4586 PRO A CG    1 
ATOM   22444 C  CD    . PRO A 1 4586 ? 258.868 245.526 246.630 1.00 48.61  ? 4586 PRO A CD    1 
ATOM   22445 N  N     . LEU A 1 4587 ? 259.302 242.168 248.162 1.00 54.29  ? 4587 LEU A N     1 
ATOM   22446 C  CA    . LEU A 1 4587 ? 259.071 241.028 249.038 1.00 45.86  ? 4587 LEU A CA    1 
ATOM   22447 C  C     . LEU A 1 4587 ? 258.019 241.404 250.064 1.00 49.81  ? 4587 LEU A C     1 
ATOM   22448 O  O     . LEU A 1 4587 ? 258.171 242.399 250.777 1.00 56.28  ? 4587 LEU A O     1 
ATOM   22449 C  CB    . LEU A 1 4587 ? 260.356 240.582 249.742 1.00 49.29  ? 4587 LEU A CB    1 
ATOM   22450 C  CG    . LEU A 1 4587 ? 260.189 239.385 250.682 1.00 51.40  ? 4587 LEU A CG    1 
ATOM   22451 C  CD1   . LEU A 1 4587 ? 260.083 238.098 249.893 1.00 48.01  ? 4587 LEU A CD1   1 
ATOM   22452 C  CD2   . LEU A 1 4587 ? 261.330 239.306 251.669 1.00 57.48  ? 4587 LEU A CD2   1 
ATOM   22453 N  N     . THR A 1 4588 ? 256.961 240.606 250.138 1.00 47.64  ? 4588 THR A N     1 
ATOM   22454 C  CA    . THR A 1 4588 ? 255.866 240.821 251.072 1.00 41.61  ? 4588 THR A CA    1 
ATOM   22455 C  C     . THR A 1 4588 ? 255.964 239.786 252.183 1.00 44.84  ? 4588 THR A C     1 
ATOM   22456 O  O     . THR A 1 4588 ? 255.925 238.581 251.917 1.00 54.90  ? 4588 THR A O     1 
ATOM   22457 C  CB    . THR A 1 4588 ? 254.519 240.726 250.359 1.00 45.13  ? 4588 THR A CB    1 
ATOM   22458 O  OG1   . THR A 1 4588 ? 254.334 241.881 249.534 1.00 52.85  ? 4588 THR A OG1   1 
ATOM   22459 C  CG2   . THR A 1 4588 ? 253.392 240.639 251.358 1.00 49.36  ? 4588 THR A CG2   1 
ATOM   22460 N  N     . GLN A 1 4589 ? 256.092 240.256 253.418 1.00 42.49  ? 4589 GLN A N     1 
ATOM   22461 C  CA    . GLN A 1 4589 ? 256.228 239.387 254.579 1.00 40.57  ? 4589 GLN A CA    1 
ATOM   22462 C  C     . GLN A 1 4589 ? 254.878 239.261 255.268 1.00 43.91  ? 4589 GLN A C     1 
ATOM   22463 O  O     . GLN A 1 4589 ? 254.309 240.262 255.714 1.00 57.26  ? 4589 GLN A O     1 
ATOM   22464 C  CB    . GLN A 1 4589 ? 257.273 239.933 255.548 1.00 43.75  ? 4589 GLN A CB    1 
ATOM   22465 C  CG    . GLN A 1 4589 ? 258.679 239.939 254.996 1.00 49.96  ? 4589 GLN A CG    1 
ATOM   22466 C  CD    . GLN A 1 4589 ? 259.658 240.601 255.937 1.00 56.27  ? 4589 GLN A CD    1 
ATOM   22467 O  OE1   . GLN A 1 4589 ? 260.405 241.495 255.544 1.00 57.74  ? 4589 GLN A OE1   1 
ATOM   22468 N  NE2   . GLN A 1 4589 ? 259.652 240.172 257.192 1.00 55.16  ? 4589 GLN A NE2   1 
ATOM   22469 N  N     . LEU A 1 4590 ? 254.375 238.035 255.359 1.00 43.46  ? 4590 LEU A N     1 
ATOM   22470 C  CA    . LEU A 1 4590 ? 253.104 237.759 256.018 1.00 43.08  ? 4590 LEU A CA    1 
ATOM   22471 C  C     . LEU A 1 4590 ? 253.386 237.264 257.431 1.00 47.93  ? 4590 LEU A C     1 
ATOM   22472 O  O     . LEU A 1 4590 ? 253.830 236.128 257.620 1.00 59.16  ? 4590 LEU A O     1 
ATOM   22473 C  CB    . LEU A 1 4590 ? 252.301 236.731 255.229 1.00 48.24  ? 4590 LEU A CB    1 
ATOM   22474 C  CG    . LEU A 1 4590 ? 252.226 236.931 253.718 1.00 49.76  ? 4590 LEU A CG    1 
ATOM   22475 C  CD1   . LEU A 1 4590 ? 251.553 235.738 253.069 1.00 50.72  ? 4590 LEU A CD1   1 
ATOM   22476 C  CD2   . LEU A 1 4590 ? 251.476 238.208 253.396 1.00 48.75  ? 4590 LEU A CD2   1 
ATOM   22477 N  N     . ARG A 1 4591 ? 253.123 238.110 258.421 1.00 48.79  ? 4591 ARG A N     1 
ATOM   22478 C  CA    . ARG A 1 4591 ? 253.311 237.762 259.821 1.00 47.96  ? 4591 ARG A CA    1 
ATOM   22479 C  C     . ARG A 1 4591 ? 251.961 237.452 260.447 1.00 49.32  ? 4591 ARG A C     1 
ATOM   22480 O  O     . ARG A 1 4591 ? 251.016 238.235 260.313 1.00 60.32  ? 4591 ARG A O     1 
ATOM   22481 C  CB    . ARG A 1 4591 ? 253.998 238.891 260.589 1.00 50.56  ? 4591 ARG A CB    1 
ATOM   22482 C  CG    . ARG A 1 4591 ? 254.320 238.534 262.032 1.00 55.47  ? 4591 ARG A CG    1 
ATOM   22483 C  CD    . ARG A 1 4591 ? 255.646 239.123 262.475 1.00 52.95  ? 4591 ARG A CD    1 
ATOM   22484 N  NE    . ARG A 1 4591 ? 255.857 240.458 261.932 1.00 61.95  ? 4591 ARG A NE    1 
ATOM   22485 C  CZ    . ARG A 1 4591 ? 255.686 241.580 262.618 1.00 63.65  ? 4591 ARG A CZ    1 
ATOM   22486 N  NH1   . ARG A 1 4591 ? 255.305 241.563 263.885 1.00 57.99  ? 4591 ARG A NH1   1 
ATOM   22487 N  NH2   . ARG A 1 4591 ? 255.900 242.747 262.018 1.00 55.69  ? 4591 ARG A NH2   1 
ATOM   22488 N  N     . TRP A 1 4592 ? 251.876 236.316 261.130 1.00 43.89  ? 4592 TRP A N     1 
ATOM   22489 C  CA    . TRP A 1 4592 ? 250.665 235.908 261.826 1.00 41.19  ? 4592 TRP A CA    1 
ATOM   22490 C  C     . TRP A 1 4592 ? 250.813 236.248 263.302 1.00 51.25  ? 4592 TRP A C     1 
ATOM   22491 O  O     . TRP A 1 4592 ? 251.757 235.796 263.956 1.00 58.56  ? 4592 TRP A O     1 
ATOM   22492 C  CB    . TRP A 1 4592 ? 250.402 234.416 261.636 1.00 44.70  ? 4592 TRP A CB    1 
ATOM   22493 C  CG    . TRP A 1 4592 ? 249.964 234.073 260.254 1.00 45.30  ? 4592 TRP A CG    1 
ATOM   22494 C  CD1   . TRP A 1 4592 ? 250.737 233.573 259.252 1.00 44.04  ? 4592 TRP A CD1   1 
ATOM   22495 C  CD2   . TRP A 1 4592 ? 248.647 234.216 259.713 1.00 46.02  ? 4592 TRP A CD2   1 
ATOM   22496 N  NE1   . TRP A 1 4592 ? 249.984 233.391 258.120 1.00 42.07  ? 4592 TRP A NE1   1 
ATOM   22497 C  CE2   . TRP A 1 4592 ? 248.696 233.780 258.378 1.00 42.85  ? 4592 TRP A CE2   1 
ATOM   22498 C  CE3   . TRP A 1 4592 ? 247.432 234.671 260.229 1.00 44.84  ? 4592 TRP A CE3   1 
ATOM   22499 C  CZ2   . TRP A 1 4592 ? 247.578 233.781 257.552 1.00 43.56  ? 4592 TRP A CZ2   1 
ATOM   22500 C  CZ3   . TRP A 1 4592 ? 246.324 234.673 259.408 1.00 44.33  ? 4592 TRP A CZ3   1 
ATOM   22501 C  CH2   . TRP A 1 4592 ? 246.403 234.231 258.085 1.00 45.45  ? 4592 TRP A CH2   1 
ATOM   22502 N  N     . VAL A 1 4593 ? 249.883 237.049 263.819 1.00 53.94  ? 4593 VAL A N     1 
ATOM   22503 C  CA    . VAL A 1 4593 ? 249.913 237.497 265.202 1.00 57.86  ? 4593 VAL A CA    1 
ATOM   22504 C  C     . VAL A 1 4593 ? 248.531 237.310 265.809 1.00 61.57  ? 4593 VAL A C     1 
ATOM   22505 O  O     . VAL A 1 4593 ? 247.529 237.174 265.105 1.00 61.15  ? 4593 VAL A O     1 
ATOM   22506 C  CB    . VAL A 1 4593 ? 250.366 238.967 265.328 1.00 56.19  ? 4593 VAL A CB    1 
ATOM   22507 C  CG1   . VAL A 1 4593 ? 251.847 239.092 265.029 1.00 58.20  ? 4593 VAL A CG1   1 
ATOM   22508 C  CG2   . VAL A 1 4593 ? 249.567 239.844 264.388 1.00 51.31  ? 4593 VAL A CG2   1 
ATOM   22509 N  N     . LYS A 1 4594 ? 248.492 237.296 267.138 1.00 68.40  ? 4594 LYS A N     1 
ATOM   22510 C  CA    . LYS A 1 4594 ? 247.231 237.142 267.847 1.00 66.01  ? 4594 LYS A CA    1 
ATOM   22511 C  C     . LYS A 1 4594 ? 246.338 238.355 267.624 1.00 67.22  ? 4594 LYS A C     1 
ATOM   22512 O  O     . LYS A 1 4594 ? 246.813 239.491 267.543 1.00 67.70  ? 4594 LYS A O     1 
ATOM   22513 C  CB    . LYS A 1 4594 ? 247.480 236.944 269.340 1.00 67.63  ? 4594 LYS A CB    1 
ATOM   22514 C  CG    . LYS A 1 4594 ? 248.328 235.732 269.674 1.00 67.01  ? 4594 LYS A CG    1 
ATOM   22515 C  CD    . LYS A 1 4594 ? 248.097 235.278 271.105 1.00 68.79  ? 4594 LYS A CD    1 
ATOM   22516 C  CE    . LYS A 1 4594 ? 246.627 235.001 271.364 1.00 68.00  ? 4594 LYS A CE    1 
ATOM   22517 N  NZ    . LYS A 1 4594 ? 246.056 234.067 270.358 1.00 70.13  ? 4594 LYS A NZ    1 
ATOM   22518 N  N     . GLN A 1 4595 ? 245.037 238.106 267.519 1.00 73.31  ? 4595 GLN A N     1 
ATOM   22519 C  CA    . GLN A 1 4595 ? 244.080 239.188 267.344 1.00 77.52  ? 4595 GLN A CA    1 
ATOM   22520 C  C     . GLN A 1 4595 ? 244.031 240.059 268.592 1.00 83.14  ? 4595 GLN A C     1 
ATOM   22521 O  O     . GLN A 1 4595 ? 244.064 239.560 269.720 1.00 83.08  ? 4595 GLN A O     1 
ATOM   22522 C  CB    . GLN A 1 4595 ? 242.693 238.624 267.040 1.00 76.99  ? 4595 GLN A CB    1 
ATOM   22523 C  CG    . GLN A 1 4595 ? 242.413 238.436 265.562 1.00 78.35  ? 4595 GLN A CG    1 
ATOM   22524 C  CD    . GLN A 1 4595 ? 241.831 239.677 264.917 1.00 84.23  ? 4595 GLN A CD    1 
ATOM   22525 O  OE1   . GLN A 1 4595 ? 241.597 240.685 265.584 1.00 84.47  ? 4595 GLN A OE1   1 
ATOM   22526 N  NE2   . GLN A 1 4595 ? 241.599 239.612 263.611 1.00 79.83  ? 4595 GLN A NE2   1 
ATOM   22527 N  N     . THR A 1 4596 ? 243.955 241.375 268.385 1.00 91.35  ? 4596 THR A N     1 
ATOM   22528 C  CA    . THR A 1 4596 ? 243.917 242.327 269.485 1.00 89.50  ? 4596 THR A CA    1 
ATOM   22529 C  C     . THR A 1 4596 ? 242.537 242.908 269.746 1.00 89.87  ? 4596 THR A C     1 
ATOM   22530 O  O     . THR A 1 4596 ? 242.259 243.295 270.885 1.00 89.32  ? 4596 THR A O     1 
ATOM   22531 C  CB    . THR A 1 4596 ? 244.895 243.482 269.227 1.00 91.60  ? 4596 THR A CB    1 
ATOM   22532 O  OG1   . THR A 1 4596 ? 244.514 244.176 268.034 1.00 90.99  ? 4596 THR A OG1   1 
ATOM   22533 C  CG2   . THR A 1 4596 ? 246.310 242.952 269.065 1.00 90.04  ? 4596 THR A CG2   1 
ATOM   22534 N  N     . ASN A 1 4597 ? 241.674 242.975 268.729 1.00 94.83  ? 4597 ASN A N     1 
ATOM   22535 C  CA    . ASN A 1 4597 ? 240.313 243.497 268.869 1.00 94.46  ? 4597 ASN A CA    1 
ATOM   22536 C  C     . ASN A 1 4597 ? 240.312 244.921 269.422 1.00 93.61  ? 4597 ASN A C     1 
ATOM   22537 O  O     . ASN A 1 4597 ? 239.570 245.247 270.351 1.00 91.87  ? 4597 ASN A O     1 
ATOM   22538 C  CB    . ASN A 1 4597 ? 239.454 242.575 269.737 1.00 93.87  ? 4597 ASN A CB    1 
ATOM   22539 C  CG    . ASN A 1 4597 ? 239.273 241.200 269.125 1.00 95.04  ? 4597 ASN A CG    1 
ATOM   22540 O  OD1   . ASN A 1 4597 ? 239.751 240.201 269.662 1.00 94.34  ? 4597 ASN A OD1   1 
ATOM   22541 N  ND2   . ASN A 1 4597 ? 238.581 241.143 267.993 1.00 94.53  ? 4597 ASN A ND2   1 
ATOM   22542 N  N     . THR A 1 4598 ? 241.156 245.778 268.847 1.00 98.21  ? 4598 THR A N     1 
ATOM   22543 C  CA    . THR A 1 4598 ? 241.255 247.177 269.242 1.00 99.29  ? 4598 THR A CA    1 
ATOM   22544 C  C     . THR A 1 4598 ? 240.914 248.117 268.089 1.00 100.65 ? 4598 THR A C     1 
ATOM   22545 O  O     . THR A 1 4598 ? 241.499 249.197 267.969 1.00 99.55  ? 4598 THR A O     1 
ATOM   22546 C  CB    . THR A 1 4598 ? 242.652 247.487 269.780 1.00 99.12  ? 4598 THR A CB    1 
ATOM   22547 O  OG1   . THR A 1 4598 ? 243.634 247.150 268.792 1.00 99.17  ? 4598 THR A OG1   1 
ATOM   22548 C  CG2   . THR A 1 4598 ? 242.923 246.689 271.047 1.00 96.47  ? 4598 THR A CG2   1 
ATOM   22549 N  N     . GLU A 1 4599 ? 239.975 247.714 267.240 1.00 107.72 ? 4599 GLU A N     1 
ATOM   22550 C  CA    . GLU A 1 4599 ? 239.548 248.482 266.062 1.00 107.33 ? 4599 GLU A CA    1 
ATOM   22551 C  C     . GLU A 1 4599 ? 240.763 248.686 265.152 1.00 106.42 ? 4599 GLU A C     1 
ATOM   22552 O  O     . GLU A 1 4599 ? 241.704 247.881 265.163 1.00 106.94 ? 4599 GLU A O     1 
ATOM   22553 C  CB    . GLU A 1 4599 ? 238.858 249.764 266.497 1.00 105.80 ? 4599 GLU A CB    1 
ATOM   22554 C  CG    . GLU A 1 4599 ? 237.523 249.546 267.189 1.00 105.73 ? 4599 GLU A CG    1 
ATOM   22555 C  CD    . GLU A 1 4599 ? 236.874 250.846 267.620 1.00 108.06 ? 4599 GLU A CD    1 
ATOM   22556 O  OE1   . GLU A 1 4599 ? 237.524 251.906 267.495 1.00 108.57 ? 4599 GLU A OE1   1 
ATOM   22557 O  OE2   . GLU A 1 4599 ? 235.714 250.809 268.083 1.00 106.62 ? 4599 GLU A OE2   1 
ATOM   22558 N  N     . LYS A 1 4600 ? 240.759 249.755 264.359 1.00 90.42  ? 4600 LYS A N     1 
ATOM   22559 C  CA    . LYS A 1 4600 ? 241.860 250.034 263.451 1.00 89.88  ? 4600 LYS A CA    1 
ATOM   22560 C  C     . LYS A 1 4600 ? 241.993 251.539 263.275 1.00 88.85  ? 4600 LYS A C     1 
ATOM   22561 O  O     . LYS A 1 4600 ? 241.044 252.297 263.494 1.00 88.86  ? 4600 LYS A O     1 
ATOM   22562 C  CB    . LYS A 1 4600 ? 241.662 249.342 262.095 1.00 85.17  ? 4600 LYS A CB    1 
ATOM   22563 C  CG    . LYS A 1 4600 ? 240.786 250.108 261.119 1.00 89.30  ? 4600 LYS A CG    1 
ATOM   22564 C  CD    . LYS A 1 4600 ? 240.807 249.464 259.741 1.00 90.22  ? 4600 LYS A CD    1 
ATOM   22565 C  CE    . LYS A 1 4600 ? 240.277 250.413 258.678 1.00 88.03  ? 4600 LYS A CE    1 
ATOM   22566 N  NZ    . LYS A 1 4600 ? 240.288 249.795 257.325 1.00 84.10  ? 4600 LYS A NZ    1 
ATOM   22567 N  N     . LYS A 1 4601 ? 243.188 251.962 262.876 1.00 77.27  ? 4601 LYS A N     1 
ATOM   22568 C  CA    . LYS A 1 4601 ? 243.474 253.377 262.713 1.00 78.84  ? 4601 LYS A CA    1 
ATOM   22569 C  C     . LYS A 1 4601 ? 242.712 253.950 261.521 1.00 80.34  ? 4601 LYS A C     1 
ATOM   22570 O  O     . LYS A 1 4601 ? 242.273 253.229 260.621 1.00 77.12  ? 4601 LYS A O     1 
ATOM   22571 C  CB    . LYS A 1 4601 ? 244.974 253.602 262.530 1.00 77.94  ? 4601 LYS A CB    1 
ATOM   22572 C  CG    . LYS A 1 4601 ? 245.831 253.037 263.648 1.00 78.87  ? 4601 LYS A CG    1 
ATOM   22573 C  CD    . LYS A 1 4601 ? 247.312 253.160 263.323 1.00 80.85  ? 4601 LYS A CD    1 
ATOM   22574 C  CE    . LYS A 1 4601 ? 247.669 254.570 262.882 1.00 79.76  ? 4601 LYS A CE    1 
ATOM   22575 N  NZ    . LYS A 1 4601 ? 248.974 255.014 263.444 1.00 77.72  ? 4601 LYS A NZ    1 
ATOM   22576 N  N     . ALA A 1 4602 ? 242.553 255.276 261.529 1.00 73.94  ? 4602 ALA A N     1 
ATOM   22577 C  CA    . ALA A 1 4602 ? 241.883 255.945 260.420 1.00 73.37  ? 4602 ALA A CA    1 
ATOM   22578 C  C     . ALA A 1 4602 ? 242.762 255.996 259.178 1.00 76.15  ? 4602 ALA A C     1 
ATOM   22579 O  O     . ALA A 1 4602 ? 242.260 256.228 258.073 1.00 71.19  ? 4602 ALA A O     1 
ATOM   22580 C  CB    . ALA A 1 4602 ? 241.465 257.356 260.832 1.00 69.54  ? 4602 ALA A CB    1 
ATOM   22581 N  N     . SER A 1 4603 ? 244.066 255.788 259.337 1.00 72.29  ? 4603 SER A N     1 
ATOM   22582 C  CA    . SER A 1 4603 ? 245.004 255.791 258.223 1.00 66.64  ? 4603 SER A CA    1 
ATOM   22583 C  C     . SER A 1 4603 ? 245.219 254.407 257.628 1.00 66.13  ? 4603 SER A C     1 
ATOM   22584 O  O     . SER A 1 4603 ? 246.077 254.252 256.753 1.00 66.83  ? 4603 SER A O     1 
ATOM   22585 C  CB    . SER A 1 4603 ? 246.349 256.370 258.669 1.00 66.81  ? 4603 SER A CB    1 
ATOM   22586 O  OG    . SER A 1 4603 ? 246.750 255.819 259.911 1.00 67.26  ? 4603 SER A OG    1 
ATOM   22587 N  N     . VAL A 1 4604 ? 244.477 253.405 258.082 1.00 61.10  ? 4604 VAL A N     1 
ATOM   22588 C  CA    . VAL A 1 4604 ? 244.635 252.037 257.605 1.00 62.26  ? 4604 VAL A CA    1 
ATOM   22589 C  C     . VAL A 1 4604 ? 243.611 251.771 256.512 1.00 62.56  ? 4604 VAL A C     1 
ATOM   22590 O  O     . VAL A 1 4604 ? 242.417 252.038 256.687 1.00 64.87  ? 4604 VAL A O     1 
ATOM   22591 C  CB    . VAL A 1 4604 ? 244.486 251.035 258.761 1.00 62.53  ? 4604 VAL A CB    1 
ATOM   22592 C  CG1   . VAL A 1 4604 ? 244.208 249.642 258.226 1.00 62.44  ? 4604 VAL A CG1   1 
ATOM   22593 C  CG2   . VAL A 1 4604 ? 245.736 251.037 259.621 1.00 62.44  ? 4604 VAL A CG2   1 
ATOM   22594 N  N     . VAL A 1 4605 ? 244.078 251.250 255.381 1.00 54.31  ? 4605 VAL A N     1 
ATOM   22595 C  CA    . VAL A 1 4605 ? 243.217 250.885 254.265 1.00 49.82  ? 4605 VAL A CA    1 
ATOM   22596 C  C     . VAL A 1 4605 ? 243.246 249.371 254.113 1.00 46.44  ? 4605 VAL A C     1 
ATOM   22597 O  O     . VAL A 1 4605 ? 244.267 248.721 254.360 1.00 53.36  ? 4605 VAL A O     1 
ATOM   22598 C  CB    . VAL A 1 4605 ? 243.651 251.587 252.958 1.00 47.01  ? 4605 VAL A CB    1 
ATOM   22599 C  CG1   . VAL A 1 4605 ? 245.017 251.101 252.512 1.00 53.51  ? 4605 VAL A CG1   1 
ATOM   22600 C  CG2   . VAL A 1 4605 ? 242.626 251.378 251.864 1.00 53.89  ? 4605 VAL A CG2   1 
ATOM   22601 N  N     . THR A 1 4606 ? 242.107 248.804 253.727 1.00 40.95  ? 4606 THR A N     1 
ATOM   22602 C  CA    . THR A 1 4606 ? 241.981 247.372 253.485 1.00 38.57  ? 4606 THR A CA    1 
ATOM   22603 C  C     . THR A 1 4606 ? 241.915 247.142 251.983 1.00 51.55  ? 4606 THR A C     1 
ATOM   22604 O  O     . THR A 1 4606 ? 240.969 247.587 251.325 1.00 60.83  ? 4606 THR A O     1 
ATOM   22605 C  CB    . THR A 1 4606 ? 240.742 246.800 254.172 1.00 48.63  ? 4606 THR A CB    1 
ATOM   22606 O  OG1   . THR A 1 4606 ? 240.851 246.986 255.588 1.00 58.00  ? 4606 THR A OG1   1 
ATOM   22607 C  CG2   . THR A 1 4606 ? 240.612 245.318 253.876 1.00 44.76  ? 4606 THR A CG2   1 
ATOM   22608 N  N     . LEU A 1 4607 ? 242.914 246.444 251.447 1.00 44.03  ? 4607 LEU A N     1 
ATOM   22609 C  CA    . LEU A 1 4607 ? 243.041 246.249 250.014 1.00 38.42  ? 4607 LEU A CA    1 
ATOM   22610 C  C     . LEU A 1 4607 ? 242.773 244.803 249.647 1.00 38.18  ? 4607 LEU A C     1 
ATOM   22611 O  O     . LEU A 1 4607 ? 243.316 243.896 250.289 1.00 50.35  ? 4607 LEU A O     1 
ATOM   22612 C  CB    . LEU A 1 4607 ? 244.441 246.644 249.540 1.00 40.46  ? 4607 LEU A CB    1 
ATOM   22613 C  CG    . LEU A 1 4607 ? 244.820 248.120 249.577 1.00 36.68  ? 4607 LEU A CG    1 
ATOM   22614 C  CD1   . LEU A 1 4607 ? 246.011 248.345 248.675 1.00 44.16  ? 4607 LEU A CD1   1 
ATOM   22615 C  CD2   . LEU A 1 4607 ? 243.652 248.987 249.151 1.00 41.50  ? 4607 LEU A CD2   1 
ATOM   22616 N  N     . PRO A 1 4608 ? 241.949 244.545 248.636 1.00 37.20  ? 4608 PRO A N     1 
ATOM   22617 C  CA    . PRO A 1 4608 ? 241.774 243.170 248.166 1.00 36.44  ? 4608 PRO A CA    1 
ATOM   22618 C  C     . PRO A 1 4608 ? 243.031 242.656 247.489 1.00 37.16  ? 4608 PRO A C     1 
ATOM   22619 O  O     . PRO A 1 4608 ? 243.807 243.416 246.905 1.00 49.19  ? 4608 PRO A O     1 
ATOM   22620 C  CB    . PRO A 1 4608 ? 240.616 243.283 247.171 1.00 38.04  ? 4608 PRO A CB    1 
ATOM   22621 C  CG    . PRO A 1 4608 ? 240.675 244.686 246.693 1.00 39.28  ? 4608 PRO A CG    1 
ATOM   22622 C  CD    . PRO A 1 4608 ? 241.162 245.507 247.848 1.00 42.78  ? 4608 PRO A CD    1 
ATOM   22623 N  N     . VAL A 1 4609 ? 243.229 241.346 247.572 1.00 41.04  ? 4609 VAL A N     1 
ATOM   22624 C  CA    . VAL A 1 4609 ? 244.317 240.670 246.874 1.00 40.70  ? 4609 VAL A CA    1 
ATOM   22625 C  C     . VAL A 1 4609 ? 243.673 239.671 245.925 1.00 39.35  ? 4609 VAL A C     1 
ATOM   22626 O  O     . VAL A 1 4609 ? 243.150 238.636 246.353 1.00 48.07  ? 4609 VAL A O     1 
ATOM   22627 C  CB    . VAL A 1 4609 ? 245.296 239.983 247.832 1.00 36.08  ? 4609 VAL A CB    1 
ATOM   22628 C  CG1   . VAL A 1 4609 ? 246.436 239.356 247.053 1.00 35.07  ? 4609 VAL A CG1   1 
ATOM   22629 C  CG2   . VAL A 1 4609 ? 245.829 240.979 248.842 1.00 30.99  ? 4609 VAL A CG2   1 
ATOM   22630 N  N     . TYR A 1 4610 ? 243.703 239.979 244.635 1.00 37.59  ? 4610 TYR A N     1 
ATOM   22631 C  CA    . TYR A 1 4610 ? 243.160 239.105 243.611 1.00 39.55  ? 4610 TYR A CA    1 
ATOM   22632 C  C     . TYR A 1 4610 ? 244.271 238.269 242.991 1.00 41.79  ? 4610 TYR A C     1 
ATOM   22633 O  O     . TYR A 1 4610 ? 245.450 238.624 243.037 1.00 51.25  ? 4610 TYR A O     1 
ATOM   22634 C  CB    . TYR A 1 4610 ? 242.447 239.918 242.533 1.00 42.71  ? 4610 TYR A CB    1 
ATOM   22635 C  CG    . TYR A 1 4610 ? 241.344 240.799 243.065 1.00 35.14  ? 4610 TYR A CG    1 
ATOM   22636 C  CD1   . TYR A 1 4610 ? 240.166 240.252 243.546 1.00 42.08  ? 4610 TYR A CD1   1 
ATOM   22637 C  CD2   . TYR A 1 4610 ? 241.484 242.177 243.093 1.00 39.77  ? 4610 TYR A CD2   1 
ATOM   22638 C  CE1   . TYR A 1 4610 ? 239.156 241.049 244.036 1.00 44.08  ? 4610 TYR A CE1   1 
ATOM   22639 C  CE2   . TYR A 1 4610 ? 240.480 242.984 243.582 1.00 46.86  ? 4610 TYR A CE2   1 
ATOM   22640 C  CZ    . TYR A 1 4610 ? 239.317 242.414 244.052 1.00 49.24  ? 4610 TYR A CZ    1 
ATOM   22641 O  OH    . TYR A 1 4610 ? 238.310 243.213 244.538 1.00 50.07  ? 4610 TYR A OH    1 
ATOM   22642 N  N     . LEU A 1 4611 ? 243.879 237.138 242.407 1.00 42.16  ? 4611 LEU A N     1 
ATOM   22643 C  CA    . LEU A 1 4611 ? 244.869 236.241 241.823 1.00 43.38  ? 4611 LEU A CA    1 
ATOM   22644 C  C     . LEU A 1 4611 ? 245.422 236.803 240.519 1.00 45.64  ? 4611 LEU A C     1 
ATOM   22645 O  O     . LEU A 1 4611 ? 246.621 236.683 240.246 1.00 52.07  ? 4611 LEU A O     1 
ATOM   22646 C  CB    . LEU A 1 4611 ? 244.254 234.855 241.614 1.00 45.50  ? 4611 LEU A CB    1 
ATOM   22647 C  CG    . LEU A 1 4611 ? 245.142 233.686 241.178 1.00 43.79  ? 4611 LEU A CG    1 
ATOM   22648 C  CD1   . LEU A 1 4611 ? 244.527 232.390 241.663 1.00 46.83  ? 4611 LEU A CD1   1 
ATOM   22649 C  CD2   . LEU A 1 4611 ? 245.332 233.631 239.671 1.00 50.29  ? 4611 LEU A CD2   1 
ATOM   22650 N  N     . ASN A 1 4612 ? 244.570 237.422 239.704 1.00 50.36  ? 4612 ASN A N     1 
ATOM   22651 C  CA    . ASN A 1 4612 ? 244.975 237.949 238.409 1.00 46.81  ? 4612 ASN A CA    1 
ATOM   22652 C  C     . ASN A 1 4612 ? 244.236 239.256 238.151 1.00 50.32  ? 4612 ASN A C     1 
ATOM   22653 O  O     . ASN A 1 4612 ? 243.428 239.710 238.966 1.00 49.84  ? 4612 ASN A O     1 
ATOM   22654 C  CB    . ASN A 1 4612 ? 244.724 236.923 237.297 1.00 44.02  ? 4612 ASN A CB    1 
ATOM   22655 C  CG    . ASN A 1 4612 ? 243.335 236.323 237.359 1.00 49.17  ? 4612 ASN A CG    1 
ATOM   22656 O  OD1   . ASN A 1 4612 ? 242.477 236.788 238.107 1.00 56.64  ? 4612 ASN A OD1   1 
ATOM   22657 N  ND2   . ASN A 1 4612 ? 243.112 235.272 236.584 1.00 50.85  ? 4612 ASN A ND2   1 
ATOM   22658 N  N     . PHE A 1 4613 ? 244.520 239.864 236.996 1.00 52.75  ? 4613 PHE A N     1 
ATOM   22659 C  CA    . PHE A 1 4613 ? 243.984 241.183 236.680 1.00 47.97  ? 4613 PHE A CA    1 
ATOM   22660 C  C     . PHE A 1 4613 ? 242.474 241.179 236.492 1.00 46.97  ? 4613 PHE A C     1 
ATOM   22661 O  O     . PHE A 1 4613 ? 241.853 242.243 236.567 1.00 50.40  ? 4613 PHE A O     1 
ATOM   22662 C  CB    . PHE A 1 4613 ? 244.659 241.736 235.423 1.00 44.45  ? 4613 PHE A CB    1 
ATOM   22663 C  CG    . PHE A 1 4613 ? 244.511 240.855 234.215 1.00 50.56  ? 4613 PHE A CG    1 
ATOM   22664 C  CD1   . PHE A 1 4613 ? 243.373 240.915 233.428 1.00 51.68  ? 4613 PHE A CD1   1 
ATOM   22665 C  CD2   . PHE A 1 4613 ? 245.510 239.965 233.867 1.00 52.23  ? 4613 PHE A CD2   1 
ATOM   22666 C  CE1   . PHE A 1 4613 ? 243.235 240.105 232.322 1.00 49.63  ? 4613 PHE A CE1   1 
ATOM   22667 C  CE2   . PHE A 1 4613 ? 245.376 239.155 232.759 1.00 55.14  ? 4613 PHE A CE2   1 
ATOM   22668 C  CZ    . PHE A 1 4613 ? 244.237 239.226 231.987 1.00 49.29  ? 4613 PHE A CZ    1 
ATOM   22669 N  N     . THR A 1 4614 ? 241.873 240.015 236.240 1.00 46.73  ? 4614 THR A N     1 
ATOM   22670 C  CA    . THR A 1 4614 ? 240.432 239.947 236.035 1.00 43.31  ? 4614 THR A CA    1 
ATOM   22671 C  C     . THR A 1 4614 ? 239.651 240.283 237.296 1.00 42.87  ? 4614 THR A C     1 
ATOM   22672 O  O     . THR A 1 4614 ? 238.464 240.612 237.202 1.00 47.47  ? 4614 THR A O     1 
ATOM   22673 C  CB    . THR A 1 4614 ? 240.038 238.558 235.537 1.00 45.53  ? 4614 THR A CB    1 
ATOM   22674 O  OG1   . THR A 1 4614 ? 240.462 237.571 236.485 1.00 50.95  ? 4614 THR A OG1   1 
ATOM   22675 C  CG2   . THR A 1 4614 ? 240.693 238.273 234.200 1.00 47.19  ? 4614 THR A CG2   1 
ATOM   22676 N  N     . ARG A 1 4615 ? 240.288 240.206 238.465 1.00 39.72  ? 4615 ARG A N     1 
ATOM   22677 C  CA    . ARG A 1 4615 ? 239.661 240.537 239.744 1.00 42.59  ? 4615 ARG A CA    1 
ATOM   22678 C  C     . ARG A 1 4615 ? 238.419 239.690 240.004 1.00 52.46  ? 4615 ARG A C     1 
ATOM   22679 O  O     . ARG A 1 4615 ? 237.465 240.146 240.638 1.00 52.43  ? 4615 ARG A O     1 
ATOM   22680 C  CB    . ARG A 1 4615 ? 239.322 242.027 239.822 1.00 37.93  ? 4615 ARG A CB    1 
ATOM   22681 C  CG    . ARG A 1 4615 ? 240.517 242.942 239.617 1.00 37.65  ? 4615 ARG A CG    1 
ATOM   22682 C  CD    . ARG A 1 4615 ? 240.291 244.285 240.280 1.00 44.23  ? 4615 ARG A CD    1 
ATOM   22683 N  NE    . ARG A 1 4615 ? 241.389 245.213 240.042 1.00 40.10  ? 4615 ARG A NE    1 
ATOM   22684 C  CZ    . ARG A 1 4615 ? 241.540 246.366 240.677 1.00 35.53  ? 4615 ARG A CZ    1 
ATOM   22685 N  NH1   . ARG A 1 4615 ? 240.677 246.767 241.594 1.00 38.23  ? 4615 ARG A NH1   1 
ATOM   22686 N  NH2   . ARG A 1 4615 ? 242.582 247.137 240.383 1.00 36.56  ? 4615 ARG A NH2   1 
ATOM   22687 N  N     . ALA A 1 4616 ? 238.427 238.447 239.524 1.00 53.93  ? 4616 ALA A N     1 
ATOM   22688 C  CA    . ALA A 1 4616 ? 237.295 237.546 239.687 1.00 50.47  ? 4616 ALA A CA    1 
ATOM   22689 C  C     . ALA A 1 4616 ? 237.393 236.674 240.930 1.00 59.86  ? 4616 ALA A C     1 
ATOM   22690 O  O     . ALA A 1 4616 ? 236.361 236.193 241.410 1.00 61.74  ? 4616 ALA A O     1 
ATOM   22691 C  CB    . ALA A 1 4616 ? 237.151 236.645 238.456 1.00 48.09  ? 4616 ALA A CB    1 
ATOM   22692 N  N     . ASP A 1 4617 ? 238.595 236.462 241.457 1.00 60.47  ? 4617 ASP A N     1 
ATOM   22693 C  CA    . ASP A 1 4617 ? 238.810 235.648 242.644 1.00 53.39  ? 4617 ASP A CA    1 
ATOM   22694 C  C     . ASP A 1 4617 ? 239.595 236.444 243.675 1.00 47.01  ? 4617 ASP A C     1 
ATOM   22695 O  O     . ASP A 1 4617 ? 240.510 237.193 243.323 1.00 52.88  ? 4617 ASP A O     1 
ATOM   22696 C  CB    . ASP A 1 4617 ? 239.542 234.350 242.296 1.00 55.98  ? 4617 ASP A CB    1 
ATOM   22697 C  CG    . ASP A 1 4617 ? 240.724 234.573 241.372 1.00 62.56  ? 4617 ASP A CG    1 
ATOM   22698 O  OD1   . ASP A 1 4617 ? 241.177 233.593 240.750 1.00 59.61  ? 4617 ASP A OD1   1 
ATOM   22699 O  OD2   . ASP A 1 4617 ? 241.186 235.723 241.237 1.00 60.71  ? 4617 ASP A OD2   1 
ATOM   22700 N  N     . LEU A 1 4618 ? 239.233 236.287 244.942 1.00 40.13  ? 4618 LEU A N     1 
ATOM   22701 C  CA    . LEU A 1 4618 ? 239.884 236.986 246.039 1.00 37.76  ? 4618 LEU A CA    1 
ATOM   22702 C  C     . LEU A 1 4618 ? 240.612 235.977 246.914 1.00 47.21  ? 4618 LEU A C     1 
ATOM   22703 O  O     . LEU A 1 4618 ? 239.990 235.058 247.456 1.00 50.34  ? 4618 LEU A O     1 
ATOM   22704 C  CB    . LEU A 1 4618 ? 238.865 237.774 246.863 1.00 34.87  ? 4618 LEU A CB    1 
ATOM   22705 C  CG    . LEU A 1 4618 ? 239.393 238.453 248.123 1.00 44.64  ? 4618 LEU A CG    1 
ATOM   22706 C  CD1   . LEU A 1 4618 ? 239.964 239.810 247.780 1.00 42.44  ? 4618 LEU A CD1   1 
ATOM   22707 C  CD2   . LEU A 1 4618 ? 238.293 238.580 249.160 1.00 48.93  ? 4618 LEU A CD2   1 
ATOM   22708 N  N     . ILE A 1 4619 ? 241.924 236.151 247.053 1.00 40.30  ? 4619 ILE A N     1 
ATOM   22709 C  CA    . ILE A 1 4619 ? 242.738 235.232 247.839 1.00 36.40  ? 4619 ILE A CA    1 
ATOM   22710 C  C     . ILE A 1 4619 ? 242.639 235.609 249.310 1.00 43.23  ? 4619 ILE A C     1 
ATOM   22711 O  O     . ILE A 1 4619 ? 242.198 234.807 250.140 1.00 51.64  ? 4619 ILE A O     1 
ATOM   22712 C  CB    . ILE A 1 4619 ? 244.202 235.233 247.364 1.00 39.60  ? 4619 ILE A CB    1 
ATOM   22713 C  CG1   . ILE A 1 4619 ? 244.269 235.056 245.847 1.00 38.14  ? 4619 ILE A CG1   1 
ATOM   22714 C  CG2   . ILE A 1 4619 ? 244.990 234.141 248.064 1.00 44.40  ? 4619 ILE A CG2   1 
ATOM   22715 C  CD1   . ILE A 1 4619 ? 243.667 233.764 245.358 1.00 43.26  ? 4619 ILE A CD1   1 
ATOM   22716 N  N     . PHE A 1 4620 ? 243.043 236.830 249.640 1.00 37.40  ? 4620 PHE A N     1 
ATOM   22717 C  CA    . PHE A 1 4620 ? 242.971 237.337 251.004 1.00 39.07  ? 4620 PHE A CA    1 
ATOM   22718 C  C     . PHE A 1 4620 ? 242.964 238.860 250.935 1.00 40.96  ? 4620 PHE A C     1 
ATOM   22719 O  O     . PHE A 1 4620 ? 242.900 239.446 249.851 1.00 47.56  ? 4620 PHE A O     1 
ATOM   22720 C  CB    . PHE A 1 4620 ? 244.117 236.785 251.863 1.00 41.15  ? 4620 PHE A CB    1 
ATOM   22721 C  CG    . PHE A 1 4620 ? 245.485 237.253 251.446 1.00 39.74  ? 4620 PHE A CG    1 
ATOM   22722 C  CD1   . PHE A 1 4620 ? 246.060 236.814 250.266 1.00 41.79  ? 4620 PHE A CD1   1 
ATOM   22723 C  CD2   . PHE A 1 4620 ? 246.209 238.111 252.253 1.00 38.26  ? 4620 PHE A CD2   1 
ATOM   22724 C  CE1   . PHE A 1 4620 ? 247.318 237.239 249.892 1.00 43.53  ? 4620 PHE A CE1   1 
ATOM   22725 C  CE2   . PHE A 1 4620 ? 247.469 238.535 251.884 1.00 39.11  ? 4620 PHE A CE2   1 
ATOM   22726 C  CZ    . PHE A 1 4620 ? 248.022 238.099 250.703 1.00 35.17  ? 4620 PHE A CZ    1 
ATOM   22727 N  N     . THR A 1 4621 ? 243.008 239.506 252.096 1.00 38.47  ? 4621 THR A N     1 
ATOM   22728 C  CA    . THR A 1 4621 ? 243.008 240.958 252.175 1.00 36.34  ? 4621 THR A CA    1 
ATOM   22729 C  C     . THR A 1 4621 ? 244.178 241.423 253.026 1.00 44.99  ? 4621 THR A C     1 
ATOM   22730 O  O     . THR A 1 4621 ? 244.621 240.722 253.939 1.00 52.88  ? 4621 THR A O     1 
ATOM   22731 C  CB    . THR A 1 4621 ? 241.699 241.501 252.761 1.00 38.39  ? 4621 THR A CB    1 
ATOM   22732 O  OG1   . THR A 1 4621 ? 241.509 240.972 254.078 1.00 54.68  ? 4621 THR A OG1   1 
ATOM   22733 C  CG2   . THR A 1 4621 ? 240.520 241.113 251.888 1.00 37.55  ? 4621 THR A CG2   1 
ATOM   22734 N  N     . VAL A 1 4622 ? 244.674 242.616 252.716 1.00 43.71  ? 4622 VAL A N     1 
ATOM   22735 C  CA    . VAL A 1 4622 ? 245.803 243.211 253.416 1.00 45.42  ? 4622 VAL A CA    1 
ATOM   22736 C  C     . VAL A 1 4622 ? 245.372 244.557 253.978 1.00 50.58  ? 4622 VAL A C     1 
ATOM   22737 O  O     . VAL A 1 4622 ? 244.673 245.327 253.310 1.00 53.68  ? 4622 VAL A O     1 
ATOM   22738 C  CB    . VAL A 1 4622 ? 247.031 243.364 252.494 1.00 46.76  ? 4622 VAL A CB    1 
ATOM   22739 C  CG1   . VAL A 1 4622 ? 247.555 242.005 252.093 1.00 46.15  ? 4622 VAL A CG1   1 
ATOM   22740 C  CG2   . VAL A 1 4622 ? 246.678 244.166 251.257 1.00 52.22  ? 4622 VAL A CG2   1 
ATOM   22741 N  N     . ASP A 1 4623 ? 245.769 244.827 255.216 1.00 55.76  ? 4623 ASP A N     1 
ATOM   22742 C  CA    . ASP A 1 4623 ? 245.497 246.102 255.869 1.00 47.45  ? 4623 ASP A CA    1 
ATOM   22743 C  C     . ASP A 1 4623 ? 246.762 246.943 255.771 1.00 51.03  ? 4623 ASP A C     1 
ATOM   22744 O  O     . ASP A 1 4623 ? 247.730 246.720 256.502 1.00 57.09  ? 4623 ASP A O     1 
ATOM   22745 C  CB    . ASP A 1 4623 ? 245.068 245.897 257.318 1.00 53.29  ? 4623 ASP A CB    1 
ATOM   22746 C  CG    . ASP A 1 4623 ? 243.660 245.351 257.435 1.00 61.61  ? 4623 ASP A CG    1 
ATOM   22747 O  OD1   . ASP A 1 4623 ? 243.167 244.759 256.453 1.00 58.19  ? 4623 ASP A OD1   1 
ATOM   22748 O  OD2   . ASP A 1 4623 ? 243.045 245.515 258.509 1.00 64.40  ? 4623 ASP A OD2   1 
ATOM   22749 N  N     . PHE A 1 4624 ? 246.754 247.907 254.859 1.00 59.30  ? 4624 PHE A N     1 
ATOM   22750 C  CA    . PHE A 1 4624 ? 247.888 248.788 254.636 1.00 51.84  ? 4624 PHE A CA    1 
ATOM   22751 C  C     . PHE A 1 4624 ? 247.637 250.139 255.289 1.00 53.05  ? 4624 PHE A C     1 
ATOM   22752 O  O     . PHE A 1 4624 ? 246.496 250.586 255.416 1.00 63.71  ? 4624 PHE A O     1 
ATOM   22753 C  CB    . PHE A 1 4624 ? 248.143 248.979 253.141 1.00 54.25  ? 4624 PHE A CB    1 
ATOM   22754 C  CG    . PHE A 1 4624 ? 249.166 248.042 252.573 1.00 58.09  ? 4624 PHE A CG    1 
ATOM   22755 C  CD1   . PHE A 1 4624 ? 250.511 248.220 252.840 1.00 60.11  ? 4624 PHE A CD1   1 
ATOM   22756 C  CD2   . PHE A 1 4624 ? 248.784 246.991 251.760 1.00 55.36  ? 4624 PHE A CD2   1 
ATOM   22757 C  CE1   . PHE A 1 4624 ? 251.454 247.362 252.313 1.00 58.44  ? 4624 PHE A CE1   1 
ATOM   22758 C  CE2   . PHE A 1 4624 ? 249.721 246.132 251.229 1.00 49.85  ? 4624 PHE A CE2   1 
ATOM   22759 C  CZ    . PHE A 1 4624 ? 251.057 246.317 251.506 1.00 56.90  ? 4624 PHE A CZ    1 
ATOM   22760 N  N     . GLU A 1 4625 ? 248.719 250.788 255.701 1.00 55.20  ? 4625 GLU A N     1 
ATOM   22761 C  CA    . GLU A 1 4625 ? 248.661 252.113 256.303 1.00 55.73  ? 4625 GLU A CA    1 
ATOM   22762 C  C     . GLU A 1 4625 ? 249.046 253.132 255.240 1.00 60.64  ? 4625 GLU A C     1 
ATOM   22763 O  O     . GLU A 1 4625 ? 250.150 253.078 254.692 1.00 65.68  ? 4625 GLU A O     1 
ATOM   22764 C  CB    . GLU A 1 4625 ? 249.587 252.198 257.513 1.00 57.51  ? 4625 GLU A CB    1 
ATOM   22765 C  CG    . GLU A 1 4625 ? 249.881 253.610 257.968 1.00 59.97  ? 4625 GLU A CG    1 
ATOM   22766 C  CD    . GLU A 1 4625 ? 251.017 253.671 258.964 1.00 67.62  ? 4625 GLU A CD    1 
ATOM   22767 O  OE1   . GLU A 1 4625 ? 251.247 252.665 259.666 1.00 65.90  ? 4625 GLU A OE1   1 
ATOM   22768 O  OE2   . GLU A 1 4625 ? 251.678 254.727 259.047 1.00 68.94  ? 4625 GLU A OE2   1 
ATOM   22769 N  N     . ILE A 1 4626 ? 248.138 254.053 254.943 1.00 60.77  ? 4626 ILE A N     1 
ATOM   22770 C  CA    . ILE A 1 4626 ? 248.398 255.063 253.926 1.00 59.06  ? 4626 ILE A CA    1 
ATOM   22771 C  C     . ILE A 1 4626 ? 249.181 256.214 254.540 1.00 60.26  ? 4626 ILE A C     1 
ATOM   22772 O  O     . ILE A 1 4626 ? 249.058 256.521 255.731 1.00 61.07  ? 4626 ILE A O     1 
ATOM   22773 C  CB    . ILE A 1 4626 ? 247.084 255.553 253.287 1.00 57.26  ? 4626 ILE A CB    1 
ATOM   22774 C  CG1   . ILE A 1 4626 ? 246.247 256.334 254.295 1.00 56.06  ? 4626 ILE A CG1   1 
ATOM   22775 C  CG2   . ILE A 1 4626 ? 246.291 254.386 252.753 1.00 60.10  ? 4626 ILE A CG2   1 
ATOM   22776 C  CD1   . ILE A 1 4626 ? 245.048 257.001 253.682 1.00 55.47  ? 4626 ILE A CD1   1 
ATOM   22777 N  N     . ALA A 1 4627 ? 250.004 256.855 253.715 1.00 57.70  ? 4627 ALA A N     1 
ATOM   22778 C  CA    . ALA A 1 4627 ? 250.780 257.995 254.168 1.00 61.60  ? 4627 ALA A CA    1 
ATOM   22779 C  C     . ALA A 1 4627 ? 249.863 259.188 254.425 1.00 66.95  ? 4627 ALA A C     1 
ATOM   22780 O  O     . ALA A 1 4627 ? 248.688 259.200 254.050 1.00 68.75  ? 4627 ALA A O     1 
ATOM   22781 C  CB    . ALA A 1 4627 ? 251.852 258.353 253.140 1.00 59.22  ? 4627 ALA A CB    1 
ATOM   22782 N  N     . THR A 1 4628 ? 250.414 260.202 255.086 1.00 74.01  ? 4628 THR A N     1 
ATOM   22783 C  CA    . THR A 1 4628 ? 249.650 261.411 255.349 1.00 72.88  ? 4628 THR A CA    1 
ATOM   22784 C  C     . THR A 1 4628 ? 249.314 262.116 254.039 1.00 76.11  ? 4628 THR A C     1 
ATOM   22785 O  O     . THR A 1 4628 ? 249.906 261.848 252.989 1.00 74.55  ? 4628 THR A O     1 
ATOM   22786 C  CB    . THR A 1 4628 ? 250.427 262.352 256.270 1.00 72.65  ? 4628 THR A CB    1 
ATOM   22787 O  OG1   . THR A 1 4628 ? 251.649 262.746 255.633 1.00 74.20  ? 4628 THR A OG1   1 
ATOM   22788 C  CG2   . THR A 1 4628 ? 250.745 261.662 257.587 1.00 70.72  ? 4628 THR A CG2   1 
ATOM   22789 N  N     . LYS A 1 4629 ? 248.332 263.016 254.110 1.00 77.73  ? 4629 LYS A N     1 
ATOM   22790 C  CA    . LYS A 1 4629 ? 247.797 263.760 252.972 1.00 76.52  ? 4629 LYS A CA    1 
ATOM   22791 C  C     . LYS A 1 4629 ? 247.076 262.851 251.983 1.00 77.31  ? 4629 LYS A C     1 
ATOM   22792 O  O     . LYS A 1 4629 ? 246.757 263.281 250.868 1.00 77.65  ? 4629 LYS A O     1 
ATOM   22793 C  CB    . LYS A 1 4629 ? 248.895 264.560 252.257 1.00 79.91  ? 4629 LYS A CB    1 
ATOM   22794 C  CG    . LYS A 1 4629 ? 248.419 265.760 251.450 1.00 82.05  ? 4629 LYS A CG    1 
ATOM   22795 C  CD    . LYS A 1 4629 ? 249.578 266.397 250.698 1.00 80.93  ? 4629 LYS A CD    1 
ATOM   22796 C  CE    . LYS A 1 4629 ? 249.112 267.549 249.825 1.00 80.00  ? 4629 LYS A CE    1 
ATOM   22797 N  NZ    . LYS A 1 4629 ? 250.240 268.154 249.063 1.00 80.40  ? 4629 LYS A NZ    1 
ATOM   22798 N  N     . GLU A 1 4630 ? 246.802 261.606 252.361 1.00 68.77  ? 4630 GLU A N     1 
ATOM   22799 C  CA    . GLU A 1 4630 ? 246.089 260.657 251.520 1.00 65.49  ? 4630 GLU A CA    1 
ATOM   22800 C  C     . GLU A 1 4630 ? 244.699 260.415 252.091 1.00 69.77  ? 4630 GLU A C     1 
ATOM   22801 O  O     . GLU A 1 4630 ? 244.512 260.400 253.311 1.00 71.26  ? 4630 GLU A O     1 
ATOM   22802 C  CB    . GLU A 1 4630 ? 246.845 259.329 251.416 1.00 66.62  ? 4630 GLU A CB    1 
ATOM   22803 C  CG    . GLU A 1 4630 ? 248.178 259.414 250.689 1.00 68.56  ? 4630 GLU A CG    1 
ATOM   22804 C  CD    . GLU A 1 4630 ? 248.026 259.482 249.183 1.00 71.36  ? 4630 GLU A CD    1 
ATOM   22805 O  OE1   . GLU A 1 4630 ? 246.882 259.400 248.692 1.00 74.70  ? 4630 GLU A OE1   1 
ATOM   22806 O  OE2   . GLU A 1 4630 ? 249.054 259.619 248.488 1.00 65.74  ? 4630 GLU A OE2   1 
ATOM   22807 N  N     . ASP A 1 4631 ? 243.726 260.234 251.201 1.00 65.15  ? 4631 ASP A N     1 
ATOM   22808 C  CA    . ASP A 1 4631 ? 242.348 260.003 251.601 1.00 58.93  ? 4631 ASP A CA    1 
ATOM   22809 C  C     . ASP A 1 4631 ? 241.981 258.559 251.305 1.00 58.19  ? 4631 ASP A C     1 
ATOM   22810 O  O     . ASP A 1 4631 ? 242.053 258.146 250.137 1.00 64.22  ? 4631 ASP A O     1 
ATOM   22811 C  CB    . ASP A 1 4631 ? 241.415 260.951 250.856 1.00 58.06  ? 4631 ASP A CB    1 
ATOM   22812 C  CG    . ASP A 1 4631 ? 240.008 260.955 251.419 1.00 68.27  ? 4631 ASP A CG    1 
ATOM   22813 O  OD1   . ASP A 1 4631 ? 239.787 260.362 252.495 1.00 69.86  ? 4631 ASP A OD1   1 
ATOM   22814 O  OD2   . ASP A 1 4631 ? 239.118 261.558 250.783 1.00 67.50  ? 4631 ASP A OD2   1 
ATOM   22815 N  N     . PRO A 1 4632 ? 241.611 257.755 252.305 1.00 51.93  ? 4632 PRO A N     1 
ATOM   22816 C  CA    . PRO A 1 4632 ? 241.236 256.358 252.018 1.00 55.35  ? 4632 PRO A CA    1 
ATOM   22817 C  C     . PRO A 1 4632 ? 240.069 256.232 251.056 1.00 54.43  ? 4632 PRO A C     1 
ATOM   22818 O  O     . PRO A 1 4632 ? 239.987 255.242 250.315 1.00 63.05  ? 4632 PRO A O     1 
ATOM   22819 C  CB    . PRO A 1 4632 ? 240.893 255.793 253.405 1.00 52.87  ? 4632 PRO A CB    1 
ATOM   22820 C  CG    . PRO A 1 4632 ? 240.681 256.987 254.277 1.00 55.33  ? 4632 PRO A CG    1 
ATOM   22821 C  CD    . PRO A 1 4632 ? 241.577 258.052 253.744 1.00 52.69  ? 4632 PRO A CD    1 
ATOM   22822 N  N     . ARG A 1 4633 ? 239.161 257.208 251.040 1.00 47.39  ? 4633 ARG A N     1 
ATOM   22823 C  CA    . ARG A 1 4633 ? 238.089 257.193 250.053 1.00 48.14  ? 4633 ARG A CA    1 
ATOM   22824 C  C     . ARG A 1 4633 ? 238.647 257.292 248.640 1.00 50.19  ? 4633 ARG A C     1 
ATOM   22825 O  O     . ARG A 1 4633 ? 238.104 256.690 247.709 1.00 55.45  ? 4633 ARG A O     1 
ATOM   22826 C  CB    . ARG A 1 4633 ? 237.108 258.332 250.321 1.00 57.03  ? 4633 ARG A CB    1 
ATOM   22827 C  CG    . ARG A 1 4633 ? 236.333 258.193 251.615 1.00 56.17  ? 4633 ARG A CG    1 
ATOM   22828 C  CD    . ARG A 1 4633 ? 235.403 259.373 251.812 1.00 59.65  ? 4633 ARG A CD    1 
ATOM   22829 N  NE    . ARG A 1 4633 ? 236.138 260.611 252.040 1.00 60.34  ? 4633 ARG A NE    1 
ATOM   22830 C  CZ    . ARG A 1 4633 ? 235.579 261.811 252.107 1.00 63.94  ? 4633 ARG A CZ    1 
ATOM   22831 N  NH1   . ARG A 1 4633 ? 234.272 261.973 251.980 1.00 58.18  ? 4633 ARG A NH1   1 
ATOM   22832 N  NH2   . ARG A 1 4633 ? 236.350 262.876 252.308 1.00 59.64  ? 4633 ARG A NH2   1 
ATOM   22833 N  N     . SER A 1 4634 ? 239.729 258.052 248.459 1.00 49.37  ? 4634 SER A N     1 
ATOM   22834 C  CA    . SER A 1 4634 ? 240.367 258.117 247.148 1.00 45.22  ? 4634 SER A CA    1 
ATOM   22835 C  C     . SER A 1 4634 ? 240.982 256.776 246.772 1.00 42.78  ? 4634 SER A C     1 
ATOM   22836 O  O     . SER A 1 4634 ? 241.012 256.407 245.593 1.00 56.08  ? 4634 SER A O     1 
ATOM   22837 C  CB    . SER A 1 4634 ? 241.424 259.219 247.130 1.00 48.10  ? 4634 SER A CB    1 
ATOM   22838 O  OG    . SER A 1 4634 ? 242.553 258.852 247.902 1.00 56.91  ? 4634 SER A OG    1 
ATOM   22839 N  N     . PHE A 1 4635 ? 241.489 256.036 247.760 1.00 38.90  ? 4635 PHE A N     1 
ATOM   22840 C  CA    . PHE A 1 4635 ? 241.965 254.682 247.496 1.00 42.29  ? 4635 PHE A CA    1 
ATOM   22841 C  C     . PHE A 1 4635 ? 240.823 253.772 247.072 1.00 41.43  ? 4635 PHE A C     1 
ATOM   22842 O  O     . PHE A 1 4635 ? 240.991 252.921 246.192 1.00 45.50  ? 4635 PHE A O     1 
ATOM   22843 C  CB    . PHE A 1 4635 ? 242.671 254.119 248.729 1.00 38.08  ? 4635 PHE A CB    1 
ATOM   22844 C  CG    . PHE A 1 4635 ? 244.093 254.569 248.869 1.00 42.07  ? 4635 PHE A CG    1 
ATOM   22845 C  CD1   . PHE A 1 4635 ? 244.392 255.885 249.163 1.00 46.75  ? 4635 PHE A CD1   1 
ATOM   22846 C  CD2   . PHE A 1 4635 ? 245.132 253.674 248.703 1.00 42.25  ? 4635 PHE A CD2   1 
ATOM   22847 C  CE1   . PHE A 1 4635 ? 245.698 256.298 249.288 1.00 45.17  ? 4635 PHE A CE1   1 
ATOM   22848 C  CE2   . PHE A 1 4635 ? 246.441 254.083 248.826 1.00 41.60  ? 4635 PHE A CE2   1 
ATOM   22849 C  CZ    . PHE A 1 4635 ? 246.723 255.396 249.120 1.00 41.77  ? 4635 PHE A CZ    1 
ATOM   22850 N  N     . TYR A 1 4636 ? 239.657 253.927 247.697 1.00 41.88  ? 4636 TYR A N     1 
ATOM   22851 C  CA    . TYR A 1 4636 ? 238.507 253.110 247.322 1.00 32.73  ? 4636 TYR A CA    1 
ATOM   22852 C  C     . TYR A 1 4636 ? 238.018 253.453 245.919 1.00 42.97  ? 4636 TYR A C     1 
ATOM   22853 O  O     . TYR A 1 4636 ? 237.671 252.562 245.136 1.00 48.42  ? 4636 TYR A O     1 
ATOM   22854 C  CB    . TYR A 1 4636 ? 237.382 253.287 248.343 1.00 39.47  ? 4636 TYR A CB    1 
ATOM   22855 C  CG    . TYR A 1 4636 ? 237.758 252.881 249.751 1.00 41.82  ? 4636 TYR A CG    1 
ATOM   22856 C  CD1   . TYR A 1 4636 ? 238.869 252.087 249.994 1.00 39.44  ? 4636 TYR A CD1   1 
ATOM   22857 C  CD2   . TYR A 1 4636 ? 237.005 253.301 250.837 1.00 44.53  ? 4636 TYR A CD2   1 
ATOM   22858 C  CE1   . TYR A 1 4636 ? 239.216 251.719 251.273 1.00 41.83  ? 4636 TYR A CE1   1 
ATOM   22859 C  CE2   . TYR A 1 4636 ? 237.346 252.937 252.124 1.00 46.67  ? 4636 TYR A CE2   1 
ATOM   22860 C  CZ    . TYR A 1 4636 ? 238.454 252.146 252.335 1.00 49.62  ? 4636 TYR A CZ    1 
ATOM   22861 O  OH    . TYR A 1 4636 ? 238.803 251.776 253.612 1.00 51.90  ? 4636 TYR A OH    1 
ATOM   22862 N  N     . GLU A 1 4637 ? 237.989 254.745 245.583 1.00 41.63  ? 4637 GLU A N     1 
ATOM   22863 C  CA    . GLU A 1 4637 ? 237.438 255.174 244.301 1.00 32.52  ? 4637 GLU A CA    1 
ATOM   22864 C  C     . GLU A 1 4637 ? 238.332 254.790 243.131 1.00 30.15  ? 4637 GLU A C     1 
ATOM   22865 O  O     . GLU A 1 4637 ? 237.828 254.481 242.047 1.00 42.36  ? 4637 GLU A O     1 
ATOM   22866 C  CB    . GLU A 1 4637 ? 237.208 256.684 244.307 1.00 37.27  ? 4637 GLU A CB    1 
ATOM   22867 C  CG    . GLU A 1 4637 ? 236.148 257.147 245.286 1.00 44.28  ? 4637 GLU A CG    1 
ATOM   22868 C  CD    . GLU A 1 4637 ? 235.935 258.644 245.243 1.00 49.93  ? 4637 GLU A CD    1 
ATOM   22869 O  OE1   . GLU A 1 4637 ? 236.590 259.314 244.418 1.00 44.40  ? 4637 GLU A OE1   1 
ATOM   22870 O  OE2   . GLU A 1 4637 ? 235.118 259.154 246.037 1.00 54.82  ? 4637 GLU A OE2   1 
ATOM   22871 N  N     . ARG A 1 4638 ? 239.646 254.806 243.322 1.00 27.76  ? 4638 ARG A N     1 
ATOM   22872 C  CA    . ARG A 1 4638 ? 240.588 254.546 242.245 1.00 31.37  ? 4638 ARG A CA    1 
ATOM   22873 C  C     . ARG A 1 4638 ? 240.841 253.061 242.029 1.00 41.48  ? 4638 ARG A C     1 
ATOM   22874 O  O     . ARG A 1 4638 ? 241.665 252.703 241.183 1.00 44.78  ? 4638 ARG A O     1 
ATOM   22875 C  CB    . ARG A 1 4638 ? 241.908 255.270 242.517 1.00 30.54  ? 4638 ARG A CB    1 
ATOM   22876 C  CG    . ARG A 1 4638 ? 241.789 256.779 242.450 1.00 39.65  ? 4638 ARG A CG    1 
ATOM   22877 C  CD    . ARG A 1 4638 ? 243.098 257.464 242.770 1.00 40.97  ? 4638 ARG A CD    1 
ATOM   22878 N  NE    . ARG A 1 4638 ? 244.191 256.978 241.938 1.00 42.36  ? 4638 ARG A NE    1 
ATOM   22879 C  CZ    . ARG A 1 4638 ? 244.942 257.751 241.167 1.00 36.92  ? 4638 ARG A CZ    1 
ATOM   22880 N  NH1   . ARG A 1 4638 ? 244.738 259.055 241.089 1.00 36.35  ? 4638 ARG A NH1   1 
ATOM   22881 N  NH2   . ARG A 1 4638 ? 245.923 257.202 240.458 1.00 45.06  ? 4638 ARG A NH2   1 
ATOM   22882 N  N     . GLY A 1 4639 ? 240.160 252.196 242.773 1.00 40.51  ? 4639 GLY A N     1 
ATOM   22883 C  CA    . GLY A 1 4639 ? 240.291 250.762 242.569 1.00 30.84  ? 4639 GLY A CA    1 
ATOM   22884 C  C     . GLY A 1 4639 ? 241.657 250.210 242.906 1.00 37.69  ? 4639 GLY A C     1 
ATOM   22885 O  O     . GLY A 1 4639 ? 242.181 249.364 242.171 1.00 41.76  ? 4639 GLY A O     1 
ATOM   22886 N  N     . VAL A 1 4640 ? 242.250 250.671 244.006 1.00 33.45  ? 4640 VAL A N     1 
ATOM   22887 C  CA    . VAL A 1 4640 ? 243.557 250.174 244.414 1.00 32.88  ? 4640 VAL A CA    1 
ATOM   22888 C  C     . VAL A 1 4640 ? 243.409 248.762 244.961 1.00 34.46  ? 4640 VAL A C     1 
ATOM   22889 O  O     . VAL A 1 4640 ? 242.565 248.498 245.827 1.00 42.91  ? 4640 VAL A O     1 
ATOM   22890 C  CB    . VAL A 1 4640 ? 244.190 251.112 245.451 1.00 29.73  ? 4640 VAL A CB    1 
ATOM   22891 C  CG1   . VAL A 1 4640 ? 245.584 250.638 245.810 1.00 26.07  ? 4640 VAL A CG1   1 
ATOM   22892 C  CG2   . VAL A 1 4640 ? 244.224 252.534 244.925 1.00 36.18  ? 4640 VAL A CG2   1 
ATOM   22893 N  N     . ALA A 1 4641 ? 244.229 247.846 244.456 1.00 32.99  ? 4641 ALA A N     1 
ATOM   22894 C  CA    . ALA A 1 4641 ? 244.198 246.457 244.885 1.00 30.24  ? 4641 ALA A CA    1 
ATOM   22895 C  C     . ALA A 1 4641 ? 245.579 245.853 244.676 1.00 35.08  ? 4641 ALA A C     1 
ATOM   22896 O  O     . ALA A 1 4641 ? 246.481 246.491 244.128 1.00 45.28  ? 4641 ALA A O     1 
ATOM   22897 C  CB    . ALA A 1 4641 ? 243.124 245.670 244.132 1.00 25.83  ? 4641 ALA A CB    1 
ATOM   22898 N  N     . VAL A 1 4642 ? 245.738 244.610 245.120 1.00 30.73  ? 4642 VAL A N     1 
ATOM   22899 C  CA    . VAL A 1 4642 ? 246.987 243.869 244.992 1.00 29.06  ? 4642 VAL A CA    1 
ATOM   22900 C  C     . VAL A 1 4642 ? 246.723 242.640 244.135 1.00 39.67  ? 4642 VAL A C     1 
ATOM   22901 O  O     . VAL A 1 4642 ? 245.714 241.953 244.324 1.00 46.90  ? 4642 VAL A O     1 
ATOM   22902 C  CB    . VAL A 1 4642 ? 247.556 243.470 246.367 1.00 33.39  ? 4642 VAL A CB    1 
ATOM   22903 C  CG1   . VAL A 1 4642 ? 248.949 242.896 246.219 1.00 29.75  ? 4642 VAL A CG1   1 
ATOM   22904 C  CG2   . VAL A 1 4642 ? 247.570 244.665 247.303 1.00 39.90  ? 4642 VAL A CG2   1 
ATOM   22905 N  N     . LEU A 1 4643 ? 247.617 242.373 243.190 1.00 35.57  ? 4643 LEU A N     1 
ATOM   22906 C  CA    . LEU A 1 4643 ? 247.496 241.230 242.296 1.00 34.75  ? 4643 LEU A CA    1 
ATOM   22907 C  C     . LEU A 1 4643 ? 248.607 240.228 242.575 1.00 41.40  ? 4643 LEU A C     1 
ATOM   22908 O  O     . LEU A 1 4643 ? 249.752 240.610 242.830 1.00 45.43  ? 4643 LEU A O     1 
ATOM   22909 C  CB    . LEU A 1 4643 ? 247.551 241.666 240.831 1.00 43.70  ? 4643 LEU A CB    1 
ATOM   22910 C  CG    . LEU A 1 4643 ? 246.426 242.566 240.319 1.00 47.87  ? 4643 LEU A CG    1 
ATOM   22911 C  CD1   . LEU A 1 4643 ? 246.514 242.690 238.811 1.00 43.38  ? 4643 LEU A CD1   1 
ATOM   22912 C  CD2   . LEU A 1 4643 ? 245.066 242.038 240.735 1.00 39.77  ? 4643 LEU A CD2   1 
ATOM   22913 N  N     . CYS A 1 4644 ? 248.259 238.941 242.529 1.00 42.78  ? 4644 CYS A N     1 
ATOM   22914 C  CA    . CYS A 1 4644 ? 249.256 237.898 242.739 1.00 40.78  ? 4644 CYS A CA    1 
ATOM   22915 C  C     . CYS A 1 4644 ? 250.158 237.726 241.523 1.00 48.99  ? 4644 CYS A C     1 
ATOM   22916 O  O     . CYS A 1 4644 ? 251.351 237.443 241.675 1.00 55.48  ? 4644 CYS A O     1 
ATOM   22917 C  CB    . CYS A 1 4644 ? 248.573 236.575 243.080 1.00 37.65  ? 4644 CYS A CB    1 
ATOM   22918 S  SG    . CYS A 1 4644 ? 247.697 236.567 244.657 1.00 61.44  ? 4644 CYS A SG    1 
ATOM   22919 N  N     . THR A 1 4645 ? 249.615 237.889 240.321 1.00 48.58  ? 4645 THR A N     1 
ATOM   22920 C  CA    . THR A 1 4645 ? 250.399 237.729 239.102 1.00 51.40  ? 4645 THR A CA    1 
ATOM   22921 C  C     . THR A 1 4645 ? 249.984 238.742 238.041 1.00 51.22  ? 4645 THR A C     1 
ATOM   22922 O  O     . THR A 1 4645 ? 248.948 239.394 238.162 1.00 55.90  ? 4645 THR A O     1 
ATOM   22923 C  CB    . THR A 1 4645 ? 250.262 236.308 238.522 1.00 55.11  ? 4645 THR A CB    1 
ATOM   22924 O  OG1   . THR A 1 4645 ? 251.176 236.145 237.431 1.00 62.58  ? 4645 THR A OG1   1 
ATOM   22925 C  CG2   . THR A 1 4645 ? 248.851 236.067 238.023 1.00 48.68  ? 4645 THR A CG2   1 
HETATM 22926 P  PB    . AOV B 2 .    ? 218.706 228.848 249.072 1.00 36.55  ? 4701 AOV A PB    1 
HETATM 22927 O  O1B   . AOV B 2 .    ? 220.015 229.484 248.912 1.00 53.77  ? 4701 AOV A O1B   1 
HETATM 22928 O  O2B   . AOV B 2 .    ? 217.564 229.755 249.047 1.00 58.05  ? 4701 AOV A O2B   1 
HETATM 22929 O  O3B   . AOV B 2 .    ? 218.386 227.894 247.838 1.00 59.31  ? 4701 AOV A O3B   1 
HETATM 22930 P  PA    . AOV B 2 .    ? 218.001 227.973 251.638 1.00 35.34  ? 4701 AOV A PA    1 
HETATM 22931 O  O1A   . AOV B 2 .    ? 217.319 229.258 251.690 1.00 50.95  ? 4701 AOV A O1A   1 
HETATM 22932 O  O2A   . AOV B 2 .    ? 217.086 226.786 251.679 1.00 55.06  ? 4701 AOV A O2A   1 
HETATM 22933 O  O3A   . AOV B 2 .    ? 218.879 227.953 250.358 1.00 53.12  ? 4701 AOV A O3A   1 
HETATM 22934 O  "O5'" . AOV B 2 .    ? 219.029 228.018 252.814 1.00 50.34  ? 4701 AOV A "O5'" 1 
HETATM 22935 C  "C5'" . AOV B 2 .    ? 219.927 226.955 253.005 1.00 50.42  ? 4701 AOV A "C5'" 1 
HETATM 22936 C  "C4'" . AOV B 2 .    ? 219.989 226.626 254.460 1.00 44.20  ? 4701 AOV A "C4'" 1 
HETATM 22937 O  "O4'" . AOV B 2 .    ? 220.515 227.715 255.173 1.00 52.52  ? 4701 AOV A "O4'" 1 
HETATM 22938 C  "C3'" . AOV B 2 .    ? 218.614 226.362 255.002 1.00 46.50  ? 4701 AOV A "C3'" 1 
HETATM 22939 O  "O3'" . AOV B 2 .    ? 218.693 225.214 255.813 1.00 56.64  ? 4701 AOV A "O3'" 1 
HETATM 22940 C  "C2'" . AOV B 2 .    ? 218.340 227.524 255.880 1.00 49.21  ? 4701 AOV A "C2'" 1 
HETATM 22941 O  "O2'" . AOV B 2 .    ? 217.530 227.110 256.962 1.00 42.42  ? 4701 AOV A "O2'" 1 
HETATM 22942 C  "C1'" . AOV B 2 .    ? 219.719 227.889 256.316 1.00 52.43  ? 4701 AOV A "C1'" 1 
HETATM 22943 N  N9    . AOV B 2 .    ? 219.655 229.293 256.664 1.00 48.58  ? 4701 AOV A N9    1 
HETATM 22944 C  C8    . AOV B 2 .    ? 219.804 230.273 255.804 1.00 47.60  ? 4701 AOV A C8    1 
HETATM 22945 N  N7    . AOV B 2 .    ? 219.681 231.461 256.428 1.00 53.95  ? 4701 AOV A N7    1 
HETATM 22946 C  C5    . AOV B 2 .    ? 219.440 231.251 257.721 1.00 49.91  ? 4701 AOV A C5    1 
HETATM 22947 C  C6    . AOV B 2 .    ? 219.209 232.061 258.928 1.00 45.25  ? 4701 AOV A C6    1 
HETATM 22948 N  N6    . AOV B 2 .    ? 219.203 233.394 258.899 1.00 48.61  ? 4701 AOV A N6    1 
HETATM 22949 N  N1    . AOV B 2 .    ? 218.992 231.433 260.077 1.00 49.24  ? 4701 AOV A N1    1 
HETATM 22950 C  C2    . AOV B 2 .    ? 218.981 230.111 260.161 1.00 48.39  ? 4701 AOV A C2    1 
HETATM 22951 N  N3    . AOV B 2 .    ? 219.185 229.325 259.102 1.00 56.77  ? 4701 AOV A N3    1 
HETATM 22952 C  C4    . AOV B 2 .    ? 219.419 229.808 257.866 1.00 53.14  ? 4701 AOV A C4    1 
HETATM 22953 V  VG    . AOV B 2 .    ? 219.782 227.306 246.560 1.00 61.75  ? 4701 AOV A VG    1 
HETATM 22954 O  O1G   . AOV B 2 .    ? 220.568 225.868 247.838 1.00 44.06  ? 4701 AOV A O1G   1 
HETATM 22955 O  O2G   . AOV B 2 .    ? 221.183 226.662 245.246 1.00 47.31  ? 4701 AOV A O2G   1 
HETATM 22956 O  O3G   . AOV B 2 .    ? 218.363 226.570 245.260 1.00 58.67  ? 4701 AOV A O3G   1 
HETATM 22957 O  O4G   . AOV B 2 .    ? 220.540 229.245 246.351 1.00 60.49  ? 4701 AOV A O4G   1 
HETATM 22958 P  PG    . ATP C 3 .    ? 228.755 200.523 240.590 1.00 45.31  ? 4702 ATP A PG    1 
HETATM 22959 O  O1G   . ATP C 3 .    ? 228.858 201.994 240.630 1.00 57.10  ? 4702 ATP A O1G   1 
HETATM 22960 O  O2G   . ATP C 3 .    ? 227.368 200.057 240.765 1.00 56.50  ? 4702 ATP A O2G   1 
HETATM 22961 O  O3G   . ATP C 3 .    ? 229.394 199.947 239.397 1.00 55.12  ? 4702 ATP A O3G   1 
HETATM 22962 P  PB    . ATP C 3 .    ? 229.032 199.760 243.330 1.00 27.78  ? 4702 ATP A PB    1 
HETATM 22963 O  O1B   . ATP C 3 .    ? 229.643 200.705 244.270 1.00 62.47  ? 4702 ATP A O1B   1 
HETATM 22964 O  O2B   . ATP C 3 .    ? 227.564 199.651 243.239 1.00 54.57  ? 4702 ATP A O2B   1 
HETATM 22965 O  O3B   . ATP C 3 .    ? 229.570 200.039 241.863 1.00 40.50  ? 4702 ATP A O3B   1 
HETATM 22966 P  PA    . ATP C 3 .    ? 229.096 196.940 244.246 1.00 28.41  ? 4702 ATP A PA    1 
HETATM 22967 O  O1A   . ATP C 3 .    ? 227.703 196.729 243.799 1.00 53.93  ? 4702 ATP A O1A   1 
HETATM 22968 O  O2A   . ATP C 3 .    ? 229.350 196.833 245.698 1.00 54.25  ? 4702 ATP A O2A   1 
HETATM 22969 O  O3A   . ATP C 3 .    ? 229.632 198.333 243.695 1.00 38.57  ? 4702 ATP A O3A   1 
HETATM 22970 O  "O5'" . ATP C 3 .    ? 230.065 195.946 243.472 1.00 52.84  ? 4702 ATP A "O5'" 1 
HETATM 22971 C  "C5'" . ATP C 3 .    ? 231.367 195.654 244.015 1.00 48.06  ? 4702 ATP A "C5'" 1 
HETATM 22972 C  "C4'" . ATP C 3 .    ? 231.643 194.192 243.798 1.00 51.15  ? 4702 ATP A "C4'" 1 
HETATM 22973 O  "O4'" . ATP C 3 .    ? 232.242 193.638 244.992 1.00 57.52  ? 4702 ATP A "O4'" 1 
HETATM 22974 C  "C3'" . ATP C 3 .    ? 230.401 193.335 243.568 1.00 49.10  ? 4702 ATP A "C3'" 1 
HETATM 22975 O  "O3'" . ATP C 3 .    ? 230.709 192.100 242.943 1.00 59.93  ? 4702 ATP A "O3'" 1 
HETATM 22976 C  "C2'" . ATP C 3 .    ? 229.958 193.071 244.999 1.00 45.82  ? 4702 ATP A "C2'" 1 
HETATM 22977 O  "O2'" . ATP C 3 .    ? 229.147 191.924 245.057 1.00 50.28  ? 4702 ATP A "O2'" 1 
HETATM 22978 C  "C1'" . ATP C 3 .    ? 231.297 192.872 245.696 1.00 48.63  ? 4702 ATP A "C1'" 1 
HETATM 22979 N  N9    . ATP C 3 .    ? 231.257 193.333 247.065 1.00 51.05  ? 4702 ATP A N9    1 
HETATM 22980 C  C8    . ATP C 3 .    ? 230.620 194.436 247.567 1.00 47.43  ? 4702 ATP A C8    1 
HETATM 22981 N  N7    . ATP C 3 .    ? 230.748 194.547 248.865 1.00 45.59  ? 4702 ATP A N7    1 
HETATM 22982 C  C5    . ATP C 3 .    ? 231.508 193.447 249.234 1.00 51.21  ? 4702 ATP A C5    1 
HETATM 22983 C  C6    . ATP C 3 .    ? 231.988 192.989 250.469 1.00 52.60  ? 4702 ATP A C6    1 
HETATM 22984 N  N6    . ATP C 3 .    ? 231.768 193.600 251.624 1.00 45.82  ? 4702 ATP A N6    1 
HETATM 22985 N  N1    . ATP C 3 .    ? 232.713 191.850 250.466 1.00 55.76  ? 4702 ATP A N1    1 
HETATM 22986 C  C2    . ATP C 3 .    ? 232.926 191.221 249.309 1.00 44.11  ? 4702 ATP A C2    1 
HETATM 22987 N  N3    . ATP C 3 .    ? 232.533 191.563 248.092 1.00 44.82  ? 4702 ATP A N3    1 
HETATM 22988 C  C4    . ATP C 3 .    ? 231.819 192.693 248.128 1.00 51.49  ? 4702 ATP A C4    1 
HETATM 22989 P  PB    . ADP D 4 .    ? 232.828 193.113 211.572 1.00 39.02  ? 4703 ADP A PB    1 
HETATM 22990 O  O1B   . ADP D 4 .    ? 231.700 192.554 212.398 1.00 26.67  ? 4703 ADP A O1B   1 
HETATM 22991 O  O2B   . ADP D 4 .    ? 232.449 194.376 210.845 1.00 50.64  ? 4703 ADP A O2B   1 
HETATM 22992 O  O3B   . ADP D 4 .    ? 234.107 193.253 212.352 1.00 38.19  ? 4703 ADP A O3B   1 
HETATM 22993 P  PA    . ADP D 4 .    ? 232.185 191.110 209.511 1.00 45.43  ? 4703 ADP A PA    1 
HETATM 22994 O  O1A   . ADP D 4 .    ? 231.936 189.811 210.201 1.00 37.49  ? 4703 ADP A O1A   1 
HETATM 22995 O  O2A   . ADP D 4 .    ? 231.004 191.926 209.104 1.00 47.48  ? 4703 ADP A O2A   1 
HETATM 22996 O  O3A   . ADP D 4 .    ? 233.134 192.015 210.432 1.00 40.31  ? 4703 ADP A O3A   1 
HETATM 22997 O  "O5'" . ADP D 4 .    ? 233.127 190.868 208.238 1.00 37.51  ? 4703 ADP A "O5'" 1 
HETATM 22998 C  "C5'" . ADP D 4 .    ? 234.427 190.267 208.445 1.00 28.66  ? 4703 ADP A "C5'" 1 
HETATM 22999 C  "C4'" . ADP D 4 .    ? 235.091 190.053 207.109 1.00 34.58  ? 4703 ADP A "C4'" 1 
HETATM 23000 O  "O4'" . ADP D 4 .    ? 236.327 189.319 207.312 1.00 40.84  ? 4703 ADP A "O4'" 1 
HETATM 23001 C  "C3'" . ADP D 4 .    ? 234.294 189.228 206.091 1.00 39.62  ? 4703 ADP A "C3'" 1 
HETATM 23002 O  "O3'" . ADP D 4 .    ? 234.579 189.646 204.764 1.00 40.34  ? 4703 ADP A "O3'" 1 
HETATM 23003 C  "C2'" . ADP D 4 .    ? 234.836 187.821 206.344 1.00 36.99  ? 4703 ADP A "C2'" 1 
HETATM 23004 O  "O2'" . ADP D 4 .    ? 234.614 186.935 205.269 1.00 53.30  ? 4703 ADP A "O2'" 1 
HETATM 23005 C  "C1'" . ADP D 4 .    ? 236.312 188.139 206.544 1.00 32.33  ? 4703 ADP A "C1'" 1 
HETATM 23006 N  N9    . ADP D 4 .    ? 237.044 187.113 207.275 1.00 32.58  ? 4703 ADP A N9    1 
HETATM 23007 C  C8    . ADP D 4 .    ? 238.011 187.326 208.225 1.00 36.67  ? 4703 ADP A C8    1 
HETATM 23008 N  N7    . ADP D 4 .    ? 238.505 186.220 208.720 1.00 42.14  ? 4703 ADP A N7    1 
HETATM 23009 C  C5    . ADP D 4 .    ? 237.831 185.211 208.049 1.00 37.98  ? 4703 ADP A C5    1 
HETATM 23010 C  C6    . ADP D 4 .    ? 237.910 183.808 208.128 1.00 34.60  ? 4703 ADP A C6    1 
HETATM 23011 N  N6    . ADP D 4 .    ? 238.733 183.159 208.945 1.00 37.57  ? 4703 ADP A N6    1 
HETATM 23012 N  N1    . ADP D 4 .    ? 237.096 183.091 207.318 1.00 37.45  ? 4703 ADP A N1    1 
HETATM 23013 C  C2    . ADP D 4 .    ? 236.270 183.750 206.498 1.00 33.66  ? 4703 ADP A C2    1 
HETATM 23014 N  N3    . ADP D 4 .    ? 236.111 185.060 206.339 1.00 36.36  ? 4703 ADP A N3    1 
HETATM 23015 C  C4    . ADP D 4 .    ? 236.928 185.748 207.152 1.00 37.45  ? 4703 ADP A C4    1 
HETATM 23016 P  PB    . ADP E 4 .    ? 221.697 214.314 190.030 1.00 45.75  ? 4704 ADP A PB    1 
HETATM 23017 O  O1B   . ADP E 4 .    ? 222.916 213.932 189.236 1.00 51.93  ? 4704 ADP A O1B   1 
HETATM 23018 O  O2B   . ADP E 4 .    ? 220.980 213.121 190.604 1.00 51.30  ? 4704 ADP A O2B   1 
HETATM 23019 O  O3B   . ADP E 4 .    ? 221.983 215.373 191.062 1.00 50.24  ? 4704 ADP A O3B   1 
HETATM 23020 P  PA    . ADP E 4 .    ? 219.776 214.418 187.783 1.00 50.42  ? 4704 ADP A PA    1 
HETATM 23021 O  O1A   . ADP E 4 .    ? 220.600 213.504 186.941 1.00 34.19  ? 4704 ADP A O1A   1 
HETATM 23022 O  O2A   . ADP E 4 .    ? 218.490 213.907 188.340 1.00 52.06  ? 4704 ADP A O2A   1 
HETATM 23023 O  O3A   . ADP E 4 .    ? 220.677 214.985 188.981 1.00 47.87  ? 4704 ADP A O3A   1 
HETATM 23024 O  "O5'" . ADP E 4 .    ? 219.502 215.773 186.975 1.00 49.40  ? 4704 ADP A "O5'" 1 
HETATM 23025 C  "C5'" . ADP E 4 .    ? 218.757 215.709 185.736 1.00 47.53  ? 4704 ADP A "C5'" 1 
HETATM 23026 C  "C4'" . ADP E 4 .    ? 219.377 216.666 184.751 1.00 36.70  ? 4704 ADP A "C4'" 1 
HETATM 23027 O  "O4'" . ADP E 4 .    ? 220.735 216.238 184.478 1.00 36.23  ? 4704 ADP A "O4'" 1 
HETATM 23028 C  "C3'" . ADP E 4 .    ? 218.688 216.776 183.381 1.00 44.11  ? 4704 ADP A "C3'" 1 
HETATM 23029 O  "O3'" . ADP E 4 .    ? 218.459 218.140 183.054 1.00 55.74  ? 4704 ADP A "O3'" 1 
HETATM 23030 C  "C2'" . ADP E 4 .    ? 219.697 216.138 182.420 1.00 47.95  ? 4704 ADP A "C2'" 1 
HETATM 23031 O  "O2'" . ADP E 4 .    ? 219.638 216.676 181.116 1.00 57.25  ? 4704 ADP A "O2'" 1 
HETATM 23032 C  "C1'" . ADP E 4 .    ? 221.012 216.453 183.119 1.00 41.46  ? 4704 ADP A "C1'" 1 
HETATM 23033 N  N9    . ADP E 4 .    ? 222.106 215.572 182.731 1.00 46.92  ? 4704 ADP A N9    1 
HETATM 23034 C  C8    . ADP E 4 .    ? 222.919 214.860 183.576 1.00 49.18  ? 4704 ADP A C8    1 
HETATM 23035 N  N7    . ADP E 4 .    ? 223.826 214.154 182.951 1.00 49.65  ? 4704 ADP A N7    1 
HETATM 23036 C  C5    . ADP E 4 .    ? 223.612 214.428 181.609 1.00 40.19  ? 4704 ADP A C5    1 
HETATM 23037 C  C6    . ADP E 4 .    ? 224.257 213.986 180.438 1.00 42.58  ? 4704 ADP A C6    1 
HETATM 23038 N  N6    . ADP E 4 .    ? 225.286 213.143 180.434 1.00 43.34  ? 4704 ADP A N6    1 
HETATM 23039 N  N1    . ADP E 4 .    ? 223.794 214.454 179.256 1.00 44.42  ? 4704 ADP A N1    1 
HETATM 23040 C  C2    . ADP E 4 .    ? 222.759 215.302 179.267 1.00 46.24  ? 4704 ADP A C2    1 
HETATM 23041 N  N3    . ADP E 4 .    ? 222.076 215.784 180.301 1.00 48.53  ? 4704 ADP A N3    1 
HETATM 23042 C  C4    . ADP E 4 .    ? 222.556 215.305 181.459 1.00 43.44  ? 4704 ADP A C4    1 
HETATM 23043 MG MG    . MG  F 5 .    ? 225.703 200.208 242.740 1.00 22.84  ? 4705 MG  A MG    1 
HETATM 23044 MG MG    . MG  G 5 .    ? 216.149 228.111 247.553 1.00 30.18  ? 4706 MG  A MG    1 
# 
